data_9C0M
# 
_entry.id   9C0M 
# 
_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   9C0M         pdb_00009c0m 10.2210/pdb9c0m/pdb 
WWPDB D_1000284406 ?            ?                   
# 
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                        9C0M 
_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    78 ? ?                                    ? ? 
# 
_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   ?   ?   ?   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 45  HOH HOH A . 
F 3 HOH 2  402 47  HOH HOH A . 
F 3 HOH 3  403 26  HOH HOH A . 
F 3 HOH 4  404 114 HOH HOH A . 
F 3 HOH 5  405 4   HOH HOH A . 
F 3 HOH 6  406 154 HOH HOH A . 
F 3 HOH 7  407 35  HOH HOH A . 
F 3 HOH 8  408 37  HOH HOH A . 
F 3 HOH 9  409 46  HOH HOH A . 
F 3 HOH 10 410 61  HOH HOH A . 
F 3 HOH 11 411 13  HOH HOH A . 
F 3 HOH 12 412 11  HOH HOH A . 
F 3 HOH 13 413 9   HOH HOH A . 
F 3 HOH 14 414 147 HOH HOH A . 
F 3 HOH 15 415 48  HOH HOH A . 
F 3 HOH 16 416 12  HOH HOH A . 
F 3 HOH 17 417 50  HOH HOH A . 
F 3 HOH 18 418 36  HOH HOH A . 
F 3 HOH 19 419 8   HOH HOH A . 
F 3 HOH 20 420 33  HOH HOH A . 
F 3 HOH 21 421 56  HOH HOH A . 
F 3 HOH 22 422 43  HOH HOH A . 
F 3 HOH 23 423 30  HOH HOH A . 
F 3 HOH 24 424 111 HOH HOH A . 
F 3 HOH 25 425 82  HOH HOH A . 
F 3 HOH 26 426 52  HOH HOH A . 
F 3 HOH 27 427 118 HOH HOH A . 
F 3 HOH 28 428 78  HOH HOH A . 
F 3 HOH 29 429 101 HOH HOH A . 
F 3 HOH 30 430 95  HOH HOH A . 
F 3 HOH 31 431 21  HOH HOH A . 
F 3 HOH 32 432 22  HOH HOH A . 
F 3 HOH 33 433 104 HOH HOH A . 
F 3 HOH 34 434 6   HOH HOH A . 
F 3 HOH 35 435 5   HOH HOH A . 
F 3 HOH 36 436 72  HOH HOH A . 
F 3 HOH 37 437 17  HOH HOH A . 
F 3 HOH 38 438 149 HOH HOH A . 
F 3 HOH 39 439 15  HOH HOH A . 
F 3 HOH 40 440 68  HOH HOH A . 
F 3 HOH 41 441 98  HOH HOH A . 
F 3 HOH 42 442 152 HOH HOH A . 
F 3 HOH 43 443 20  HOH HOH A . 
F 3 HOH 44 444 28  HOH HOH A . 
F 3 HOH 45 445 40  HOH HOH A . 
F 3 HOH 46 446 24  HOH HOH A . 
F 3 HOH 47 447 19  HOH HOH A . 
F 3 HOH 48 448 18  HOH HOH A . 
F 3 HOH 49 449 16  HOH HOH A . 
F 3 HOH 50 450 65  HOH HOH A . 
F 3 HOH 51 451 59  HOH HOH A . 
F 3 HOH 52 452 10  HOH HOH A . 
F 3 HOH 53 453 103 HOH HOH A . 
F 3 HOH 54 454 38  HOH HOH A . 
F 3 HOH 55 455 91  HOH HOH A . 
F 3 HOH 56 456 77  HOH HOH A . 
F 3 HOH 57 457 53  HOH HOH A . 
F 3 HOH 58 458 54  HOH HOH A . 
F 3 HOH 59 459 64  HOH HOH A . 
F 3 HOH 60 460 32  HOH HOH A . 
F 3 HOH 61 461 109 HOH HOH A . 
F 3 HOH 62 462 151 HOH HOH A . 
F 3 HOH 63 463 148 HOH HOH A . 
F 3 HOH 64 464 106 HOH HOH A . 
F 3 HOH 65 465 51  HOH HOH A . 
F 3 HOH 66 466 122 HOH HOH A . 
F 3 HOH 67 467 55  HOH HOH A . 
F 3 HOH 68 468 150 HOH HOH A . 
F 3 HOH 69 469 119 HOH HOH A . 
F 3 HOH 70 470 100 HOH HOH A . 
F 3 HOH 71 471 107 HOH HOH A . 
F 3 HOH 72 472 41  HOH HOH A . 
F 3 HOH 73 473 23  HOH HOH A . 
F 3 HOH 74 474 63  HOH HOH A . 
F 3 HOH 75 475 42  HOH HOH A . 
F 3 HOH 76 476 115 HOH HOH A . 
F 3 HOH 77 477 138 HOH HOH A . 
F 3 HOH 78 478 70  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                     9C0M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.285 
_cell.length_a_esd                 ? 
_cell.length_b                     62.285 
_cell.length_b_esd                 ? 
_cell.length_c                     164.094 
_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                         9C0M 
_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                   9C0M 
_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             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.20 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;2 uL 12 mg/mL FphH (10mM HEPES pH 7.5, 100mM NaCl) were mixed with 1.5 uL of reservoir solution and 0.5 uL crystals seeds in reservoir solution. Sitting drop reservoir contained 100mM Calcium acetate hydrate, 100mM Tris pH 7.5 and 12.5 % w/v PEG 4000.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     295 
_diffrn.ambient_temp_details             'Room temperature' 
_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         2024-03-13 
_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   0.979 
_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                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C0M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.50 
_reflns.d_resolution_low                               49.61 
_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                                     11665 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.95 
_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                                0.119 
_reflns.pdbx_Rpim_I_all                                0.049 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       66796 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.108 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.50 
_reflns_shell.d_res_low                                     2.60 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           5779 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1129 
_reflns_shell.percent_possible_obs                          86.1 
_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                               5.1 
_reflns_shell.pdbx_chi_squared                              1.15 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.316 
_reflns_shell.pdbx_Rpim_I_all                               0.549 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.500 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.190 
_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                                 9C0M 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             49.61 
_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                     11523 
_refine.ls_number_reflns_R_free                  542 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.30 
_refine.ls_percent_reflns_R_free                 4.70 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1765 
_refine.ls_R_factor_R_free                       0.2159 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1744 
_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                          1.33 
_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                 24.14 
_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                            0.30 
_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        1950 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             78 
_refine_hist.number_atoms_total               2032 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        49.61 
# 
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' ? 0.008 ? 1996 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.871 ? 2700 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.748 ? 260  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050 ? 283  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 356  ? 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' 2.50 2.75  . . 129 2507 92.00  . . . . 0.2623 . . . . . . . . . . . 0.3270 
'X-RAY DIFFRACTION' 2.75 3.15  . . 146 2738 100.00 . . . . 0.2260 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 3.15 3.97  . . 127 2768 98.00  . . . . 0.1753 . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 3.97 49.61 . . 140 2968 99.00  . . . . 0.1491 . . . . . . . . . . . 0.1767 
# 
_struct.entry_id                     9C0M 
_struct.title                        
'FphH, Staphylococcus aureus fluorophosphonate-binding serine hydrolases H, apo form 2 at room temperature' 
_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        9C0M 
_struct_keywords.text            
;FphH, Staphylococcus aureus, S. aureus, fluorophosphonate-binding, serine hydrolases, lipase, room temperature, humidity, humidifier, 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              9C0M 
_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 9C0M GLY A 1 ? UNP A0A0D6HZA6 ? ? 'expression tag' -2 1 
1 9C0M PRO A 2 ? UNP A0A0D6HZA6 ? ? 'expression tag' -1 2 
1 9C0M 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  ? GLY A 86  ? SER A 64  GLY A 83  1 ? 20 
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 ? ASP A 156 ? ASP A 144 ASP A 153 1 ? 10 
HELX_P HELX_P8  AA8 PRO A 160 ? GLU A 176 ? PRO A 157 GLU A 173 1 ? 17 
HELX_P HELX_P9  AA9 GLN A 177 ? VAL A 181 ? GLN A 174 VAL A 178 5 ? 5  
HELX_P HELX_P10 AB1 GLN A 199 ? VAL A 208 ? GLN A 196 VAL A 205 1 ? 10 
HELX_P HELX_P11 AB2 VAL A 224 ? ASP A 228 ? VAL A 221 ASP A 225 5 ? 5  
HELX_P HELX_P12 AB3 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 GLU 176 O   ? ? ? 1_555 E CA  . CA ? ? A GLU 173 A CA  304 1_555 ? ? ? ? ? ? ? 2.491 ? ? 
metalc2  metalc ? ? A ASP 179 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 176 A CA  304 1_555 ? ? ? ? ? ? ? 2.664 ? ? 
metalc3  metalc ? ? A ASP 179 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 176 A CA  304 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc4  metalc ? ? A ASP 209 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 206 A CA  302 1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc5  metalc ? ? A ASP 212 OD1 ? ? ? 1_555 B CA  . CA ? ? A ASP 209 A CA  301 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc6  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 421 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc7  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 435 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc8  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 435 8_555 ? ? ? ? ? ? ? 2.234 ? ? 
metalc9  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 436 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc10 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 436 8_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc11 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 449 1_555 ? ? ? ? ? ? ? 2.407 ? ? 
metalc12 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 453 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc13 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 417 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc14 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 438 8_555 ? ? ? ? ? ? ? 2.547 ? ? 
metalc15 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 463 1_555 ? ? ? ? ? ? ? 2.515 ? ? 
metalc16 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 466 1_555 ? ? ? ? ? ? ? 2.612 ? ? 
metalc17 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 467 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc18 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 468 8_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc19 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 403 1_555 ? ? ? ? ? ? ? 2.483 ? ? 
metalc20 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 423 1_555 ? ? ? ? ? ? ? 2.755 ? ? 
metalc21 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 458 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc22 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 462 6_545 ? ? ? ? ? ? ? 2.707 ? ? 
metalc23 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 469 1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc24 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 474 6_545 ? ? ? ? ? ? ? 2.853 ? ? 
metalc25 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 441 1_555 ? ? ? ? ? ? ? 2.656 ? ? 
metalc26 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 464 1_555 ? ? ? ? ? ? ? 2.568 ? ? 
# 
_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  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_555 110.7 ? 
2  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 73.3  ? 
3  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 50.2  ? 
4  O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 441 ? 1_555 127.2 ? 
5  OD1 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 441 ? 1_555 95.9  ? 
6  OD2 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 441 ? 1_555 146.0 ? 
7  O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 1_555 79.3  ? 
8  OD1 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 1_555 169.8 ? 
9  OD2 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 1_555 138.2 ? 
10 O   ? F HOH .   ? A HOH 441 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 1_555 75.7  ? 
11 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 417 ? 1_555 68.4  ? 
12 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 438 ? 8_555 129.9 ? 
13 O   ? F HOH .   ? A HOH 417 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 438 ? 8_555 126.8 ? 
14 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 1_555 80.9  ? 
15 O   ? F HOH .   ? A HOH 417 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 1_555 75.3  ? 
16 O   ? F HOH .   ? A HOH 438 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 1_555 63.0  ? 
17 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 82.0  ? 
18 O   ? F HOH .   ? A HOH 417 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 67.6  ? 
19 O   ? F HOH .   ? A HOH 438 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 147.0 ? 
20 O   ? F HOH .   ? A HOH 463 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 142.7 ? 
21 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 467 ? 1_555 88.7  ? 
22 O   ? F HOH .   ? A HOH 417 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 467 ? 1_555 152.5 ? 
23 O   ? F HOH .   ? A HOH 438 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 467 ? 1_555 57.4  ? 
24 O   ? F HOH .   ? A HOH 463 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 467 ? 1_555 86.6  ? 
25 O   ? F HOH .   ? A HOH 466 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 467 ? 1_555 125.9 ? 
26 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 130.4 ? 
27 O   ? F HOH .   ? A HOH 417 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 63.2  ? 
28 O   ? F HOH .   ? A HOH 438 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 76.2  ? 
29 O   ? F HOH .   ? A HOH 463 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 77.4  ? 
30 O   ? F HOH .   ? A HOH 466 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 89.1  ? 
31 O   ? F HOH .   ? A HOH 467 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 468 ? 8_555 133.1 ? 
32 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 72.5  ? 
33 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 435 ? 1_555 75.4  ? 
34 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 435 ? 1_555 144.9 ? 
35 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 435 ? 8_555 75.9  ? 
36 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 435 ? 8_555 144.6 ? 
37 O   ? F HOH .   ? A HOH 435 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 435 ? 8_555 2.0   ? 
38 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 1_555 77.8  ? 
39 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 1_555 79.4  ? 
40 O   ? F HOH .   ? A HOH 435 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 1_555 80.5  ? 
41 O   ? F HOH .   ? A HOH 435 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 1_555 78.7  ? 
42 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 8_555 148.8 ? 
43 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 8_555 124.7 ? 
44 O   ? F HOH .   ? A HOH 435 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 8_555 79.3  ? 
45 O   ? F HOH .   ? A HOH 435 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 8_555 78.2  ? 
46 O   ? F HOH .   ? A HOH 436 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 436 ? 8_555 80.4  ? 
47 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 76.8  ? 
48 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 94.1  ? 
49 O   ? F HOH .   ? A HOH 435 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 91.8  ? 
50 O   ? F HOH .   ? A HOH 435 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 93.8  ? 
51 O   ? F HOH .   ? A HOH 436 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 154.5 ? 
52 O   ? F HOH .   ? A HOH 436 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 1_555 122.2 ? 
53 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 133.6 ? 
54 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 62.6  ? 
55 O   ? F HOH .   ? A HOH 435 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 151.0 ? 
56 O   ? F HOH .   ? A HOH 435 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 150.5 ? 
57 O   ? F HOH .   ? A HOH 436 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 103.8 ? 
58 O   ? F HOH .   ? A HOH 436 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 73.4  ? 
59 O   ? F HOH .   ? A HOH 449 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 453 ? 1_555 94.7  ? 
60 O   ? F HOH .   ? A HOH 403 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 423 ? 1_555 107.6 ? 
61 O   ? F HOH .   ? A HOH 403 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 458 ? 1_555 43.1  ? 
62 O   ? F HOH .   ? A HOH 423 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 458 ? 1_555 126.8 ? 
63 O   ? F HOH .   ? A HOH 403 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 462 ? 6_545 67.7  ? 
64 O   ? F HOH .   ? A HOH 423 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 462 ? 6_545 57.2  ? 
65 O   ? F HOH .   ? A HOH 458 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 462 ? 6_545 69.6  ? 
66 O   ? F HOH .   ? A HOH 403 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 469 ? 1_555 119.6 ? 
67 O   ? F HOH .   ? A HOH 423 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 469 ? 1_555 104.5 ? 
68 O   ? F HOH .   ? A HOH 458 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 469 ? 1_555 76.6  ? 
69 O   ? F HOH .   ? A HOH 462 ? 6_545 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 469 ? 1_555 90.3  ? 
70 O   ? F HOH .   ? A HOH 403 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 474 ? 6_545 133.7 ? 
71 O   ? F HOH .   ? A HOH 423 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 474 ? 6_545 45.2  ? 
72 O   ? F HOH .   ? A HOH 458 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 474 ? 6_545 115.5 ? 
73 O   ? F HOH .   ? A HOH 462 ? 6_545 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 474 ? 6_545 66.0  ? 
74 O   ? F HOH .   ? A HOH 469 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 474 ? 6_545 59.6  ? 
# 
_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 14  ? N PHE A 11  O SER A 48  ? O SER A 45  
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                   9C0M 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    403 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    458 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.87 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 448 ? ? 1_555 O A HOH 452 ? ? 6_545 2.08 
2 1 O A HOH 423 ? ? 1_555 O A HOH 474 ? ? 6_545 2.16 
# 
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  ? ? -129.45 -106.46 
2 1 THR A 25  ? ? 58.15   15.60   
3 1 SER A 63  ? ? -107.92 -165.81 
4 1 SER A 93  ? ? 57.64   -122.33 
5 1 LYS A 121 ? ? -66.85  96.49   
6 1 ASP A 243 ? ? -108.98 68.36   
# 
_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     435 
_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 21.7443 -9.9794 16.9060 0.3770 ? -0.0123 ? 0.0076  ? 0.6720 ? 0.1008 ? 0.3360 ? 5.1826 ? 0.1014  ? 
-0.7978 ? 6.0604 ? -1.0296 ? 4.7395 ? -0.0297 ? 1.0851  ? 0.3141 ? -0.6972 ? -0.0529 ? -0.1127 ? -0.3707 ? 0.1684  ? 0.0995  ? 
2 'X-RAY DIFFRACTION' ? refined 12.5799 -5.4153 24.3888 0.3255 ? 0.0508  ? -0.0056 ? 0.4779 ? 0.1243 ? 0.4086 ? 6.9022 ? 1.6469  ? 
-0.0596 ? 5.5621 ? 1.0798  ? 7.3526 ? -0.0778 ? 0.5187  ? 0.9047 ? -0.1200 ? 0.0455  ? 0.6251  ? -0.9246 ? -0.5393 ? -0.0221 ? 
3 'X-RAY DIFFRACTION' ? refined 27.3669 14.1811 9.7148  1.4721 ? -0.1001 ? 0.1969  ? 1.2310 ? 0.5464 ? 1.4544 ? 3.8503 ? 1.4254  ? 
-2.1428 ? 6.4711 ? -2.1127 ? 8.6729 ? 0.2806  ? 0.3963  ? 1.1637 ? -0.1113 ? -0.7180 ? -0.6142 ? -2.0845 ? 1.4401  ? 0.2261  ? 
4 'X-RAY DIFFRACTION' ? refined 15.4820 -3.1192 31.0451 0.4156 ? -0.0367 ? 0.0276  ? 0.3694 ? 0.0538 ? 0.3870 ? 6.4239 ? -0.2916 ? 
-1.4101 ? 5.3467 ? -0.5497 ? 5.7624 ? 0.2422  ? -0.0255 ? 0.8112 ? 0.1906  ? -0.0905 ? 0.0447  ? -0.8891 ? 0.1169  ? -0.0814 ? 
# 
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 5 through 85 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 86 through 124 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 125 through 157 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 158 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 
7 1 Y 1 A LYS 4  ? A LYS 7 
# 
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                    9C0M 
_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]   0.016055 
_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]   0.016055 
_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]   0.006094 
_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   . LEU A 1 8   ? 33.770 -2.481  9.616  1.00 80.45  ? 5   LEU A N   1 
ATOM   2    C  CA  . LEU A 1 8   ? 32.374 -2.321  10.041 1.00 80.63  ? 5   LEU A CA  1 
ATOM   3    C  C   . LEU A 1 8   ? 31.789 -3.629  10.552 1.00 80.85  ? 5   LEU A C   1 
ATOM   4    O  O   . LEU A 1 8   ? 31.969 -4.666  9.922  1.00 82.62  ? 5   LEU A O   1 
ATOM   5    C  CB  . LEU A 1 8   ? 31.515 -1.790  8.892  1.00 87.47  ? 5   LEU A CB  1 
ATOM   6    C  CG  . LEU A 1 8   ? 31.487 -0.265  8.751  1.00 90.10  ? 5   LEU A CG  1 
ATOM   7    C  CD1 . LEU A 1 8   ? 30.337 0.190   7.876  1.00 85.03  ? 5   LEU A CD1 1 
ATOM   8    C  CD2 . LEU A 1 8   ? 31.403 0.384   10.117 1.00 90.48  ? 5   LEU A CD2 1 
ATOM   9    N  N   . PRO A 1 9   ? 31.064 -3.558  11.671 1.00 80.50  ? 6   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 9   ? 30.651 -4.774  12.393 1.00 73.90  ? 6   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 9   ? 29.633 -5.626  11.637 1.00 71.90  ? 6   PRO A C   1 
ATOM   12   O  O   . PRO A 1 9   ? 28.974 -5.171  10.703 1.00 73.91  ? 6   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 9   ? 30.041 -4.219  13.687 1.00 71.30  ? 6   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 9   ? 30.656 -2.861  13.844 1.00 73.91  ? 6   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 9   ? 30.789 -2.336  12.446 1.00 79.63  ? 6   PRO A CD  1 
ATOM   16   N  N   . LYS A 1 10  ? 29.517 -6.884  12.070 1.00 69.33  ? 7   LYS A N   1 
ATOM   17   C  CA  . LYS A 1 10  ? 28.664 -7.918  11.491 1.00 67.46  ? 7   LYS A CA  1 
ATOM   18   C  C   . LYS A 1 10  ? 28.072 -8.788  12.596 1.00 64.92  ? 7   LYS A C   1 
ATOM   19   O  O   . LYS A 1 10  ? 28.598 -8.823  13.714 1.00 64.72  ? 7   LYS A O   1 
ATOM   20   C  CB  . LYS A 1 10  ? 29.440 -8.796  10.494 1.00 71.77  ? 7   LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 10  ? 30.540 -8.055  9.716  1.00 87.56  ? 7   LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 10  ? 31.123 -8.853  8.541  1.00 100.28 ? 7   LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 10  ? 32.172 -9.876  9.005  1.00 110.10 ? 7   LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 10  ? 33.425 -9.264  9.550  1.00 110.67 ? 7   LYS A NZ  1 
ATOM   25   N  N   . PRO A 1 11  ? 26.974 -9.496  12.318 1.00 66.18  ? 8   PRO A N   1 
ATOM   26   C  CA  . PRO A 1 11  ? 26.350 -10.321 13.364 1.00 60.68  ? 8   PRO A CA  1 
ATOM   27   C  C   . PRO A 1 11  ? 27.263 -11.457 13.799 1.00 58.74  ? 8   PRO A C   1 
ATOM   28   O  O   . PRO A 1 11  ? 28.211 -11.829 13.107 1.00 56.00  ? 8   PRO A O   1 
ATOM   29   C  CB  . PRO A 1 11  ? 25.083 -10.863 12.689 1.00 55.03  ? 8   PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 11  ? 24.806 -9.927  11.596 1.00 59.77  ? 8   PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 11  ? 26.150 -9.461  11.097 1.00 61.33  ? 8   PRO A CD  1 
ATOM   32   N  N   . PHE A 1 12  ? 26.975 -12.015 14.975 1.00 55.70  ? 9   PHE A N   1 
ATOM   33   C  CA  . PHE A 1 12  ? 27.767 -13.144 15.440 1.00 56.34  ? 9   PHE A CA  1 
ATOM   34   C  C   . PHE A 1 12  ? 26.852 -14.214 16.022 1.00 50.14  ? 9   PHE A C   1 
ATOM   35   O  O   . PHE A 1 12  ? 25.709 -13.956 16.400 1.00 51.91  ? 9   PHE A O   1 
ATOM   36   C  CB  . PHE A 1 12  ? 28.856 -12.710 16.450 1.00 53.37  ? 9   PHE A CB  1 
ATOM   37   C  CG  . PHE A 1 12  ? 28.310 -12.081 17.711 1.00 58.56  ? 9   PHE A CG  1 
ATOM   38   C  CD1 . PHE A 1 12  ? 27.716 -12.863 18.707 1.00 52.74  ? 9   PHE A CD1 1 
ATOM   39   C  CD2 . PHE A 1 12  ? 28.384 -10.704 17.902 1.00 56.47  ? 9   PHE A CD2 1 
ATOM   40   C  CE1 . PHE A 1 12  ? 27.211 -12.288 19.860 1.00 50.62  ? 9   PHE A CE1 1 
ATOM   41   C  CE2 . PHE A 1 12  ? 27.873 -10.130 19.061 1.00 56.31  ? 9   PHE A CE2 1 
ATOM   42   C  CZ  . PHE A 1 12  ? 27.291 -10.925 20.035 1.00 47.67  ? 9   PHE A CZ  1 
ATOM   43   N  N   . PHE A 1 13  ? 27.396 -15.424 16.101 1.00 53.77  ? 10  PHE A N   1 
ATOM   44   C  CA  . PHE A 1 13  ? 26.667 -16.612 16.533 1.00 55.58  ? 10  PHE A CA  1 
ATOM   45   C  C   . PHE A 1 13  ? 27.667 -17.496 17.274 1.00 54.02  ? 10  PHE A C   1 
ATOM   46   O  O   . PHE A 1 13  ? 28.592 -18.024 16.653 1.00 59.00  ? 10  PHE A O   1 
ATOM   47   C  CB  . PHE A 1 13  ? 26.067 -17.326 15.315 1.00 51.71  ? 10  PHE A CB  1 
ATOM   48   C  CG  . PHE A 1 13  ? 25.123 -18.455 15.650 1.00 55.63  ? 10  PHE A CG  1 
ATOM   49   C  CD1 . PHE A 1 13  ? 24.455 -18.499 16.860 1.00 56.06  ? 10  PHE A CD1 1 
ATOM   50   C  CD2 . PHE A 1 13  ? 24.913 -19.490 14.738 1.00 63.40  ? 10  PHE A CD2 1 
ATOM   51   C  CE1 . PHE A 1 13  ? 23.583 -19.556 17.159 1.00 62.83  ? 10  PHE A CE1 1 
ATOM   52   C  CE2 . PHE A 1 13  ? 24.053 -20.555 15.036 1.00 64.43  ? 10  PHE A CE2 1 
ATOM   53   C  CZ  . PHE A 1 13  ? 23.386 -20.583 16.248 1.00 62.09  ? 10  PHE A CZ  1 
ATOM   54   N  N   . PHE A 1 14  ? 27.515 -17.634 18.594 1.00 55.48  ? 11  PHE A N   1 
ATOM   55   C  CA  . PHE A 1 14  ? 28.381 -18.491 19.417 1.00 55.20  ? 11  PHE A CA  1 
ATOM   56   C  C   . PHE A 1 14  ? 27.575 -19.699 19.893 1.00 52.74  ? 11  PHE A C   1 
ATOM   57   O  O   . PHE A 1 14  ? 26.683 -19.562 20.740 1.00 50.40  ? 11  PHE A O   1 
ATOM   58   C  CB  . PHE A 1 14  ? 28.948 -17.735 20.621 1.00 53.51  ? 11  PHE A CB  1 
ATOM   59   C  CG  . PHE A 1 14  ? 29.661 -16.456 20.273 1.00 54.65  ? 11  PHE A CG  1 
ATOM   60   C  CD1 . PHE A 1 14  ? 30.377 -16.336 19.092 1.00 51.76  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 . PHE A 1 14  ? 29.617 -15.372 21.142 1.00 51.77  ? 11  PHE A CD2 1 
ATOM   62   C  CE1 . PHE A 1 14  ? 31.044 -15.156 18.779 1.00 52.72  ? 11  PHE A CE1 1 
ATOM   63   C  CE2 . PHE A 1 14  ? 30.273 -14.181 20.832 1.00 53.96  ? 11  PHE A CE2 1 
ATOM   64   C  CZ  . PHE A 1 14  ? 30.991 -14.075 19.644 1.00 55.20  ? 11  PHE A CZ  1 
ATOM   65   N  N   . GLU A 1 15  ? 27.896 -20.876 19.365 1.00 53.63  ? 12  GLU A N   1 
ATOM   66   C  CA  . GLU A 1 15  ? 27.158 -22.098 19.673 1.00 58.22  ? 12  GLU A CA  1 
ATOM   67   C  C   . GLU A 1 15  ? 27.829 -22.841 20.826 1.00 57.29  ? 12  GLU A C   1 
ATOM   68   O  O   . GLU A 1 15  ? 28.967 -23.293 20.697 1.00 61.57  ? 12  GLU A O   1 
ATOM   69   C  CB  . GLU A 1 15  ? 27.083 -23.006 18.444 1.00 59.40  ? 12  GLU A CB  1 
ATOM   70   C  CG  . GLU A 1 15  ? 26.264 -22.414 17.297 1.00 69.25  ? 12  GLU A CG  1 
ATOM   71   C  CD  . GLU A 1 15  ? 25.802 -23.453 16.285 1.00 76.91  ? 12  GLU A CD  1 
ATOM   72   O  OE1 . GLU A 1 15  ? 24.730 -24.073 16.521 1.00 80.31  ? 12  GLU A OE1 1 
ATOM   73   O  OE2 . GLU A 1 15  ? 26.505 -23.646 15.264 1.00 74.78  ? 12  GLU A OE2 1 
ATOM   74   N  N   . GLU A 1 16  ? 27.113 -22.998 21.935 1.00 57.52  ? 13  GLU A N   1 
ATOM   75   C  CA  . GLU A 1 16  ? 27.587 -23.817 23.045 1.00 55.08  ? 13  GLU A CA  1 
ATOM   76   C  C   . GLU A 1 16  ? 26.511 -24.815 23.476 1.00 62.13  ? 13  GLU A C   1 
ATOM   77   O  O   . GLU A 1 16  ? 26.244 -25.791 22.763 1.00 65.46  ? 13  GLU A O   1 
ATOM   78   C  CB  . GLU A 1 16  ? 28.005 -22.924 24.206 1.00 56.90  ? 13  GLU A CB  1 
ATOM   79   C  CG  . GLU A 1 16  ? 29.173 -21.988 23.866 1.00 59.41  ? 13  GLU A CG  1 
ATOM   80   C  CD  . GLU A 1 16  ? 30.500 -22.713 23.775 1.00 62.87  ? 13  GLU A CD  1 
ATOM   81   O  OE1 . GLU A 1 16  ? 31.256 -22.472 22.803 1.00 66.07  ? 13  GLU A OE1 1 
ATOM   82   O  OE2 . GLU A 1 16  ? 30.780 -23.543 24.670 1.00 67.57  ? 13  GLU A OE2 1 
ATOM   83   N  N   . GLY A 1 17  ? 25.871 -24.582 24.618 1.00 56.57  ? 14  GLY A N   1 
ATOM   84   C  CA  . GLY A 1 17  ? 24.808 -25.451 25.071 1.00 61.22  ? 14  GLY A CA  1 
ATOM   85   C  C   . GLY A 1 17  ? 23.468 -25.152 24.409 1.00 62.91  ? 14  GLY A C   1 
ATOM   86   O  O   . GLY A 1 17  ? 23.353 -24.366 23.468 1.00 59.54  ? 14  GLY A O   1 
ATOM   87   N  N   . LYS A 1 18  ? 22.428 -25.787 24.953 1.00 63.53  ? 15  LYS A N   1 
ATOM   88   C  CA  . LYS A 1 18  ? 21.086 -25.763 24.390 1.00 63.09  ? 15  LYS A CA  1 
ATOM   89   C  C   . LYS A 1 18  ? 20.249 -24.591 24.879 1.00 62.61  ? 15  LYS A C   1 
ATOM   90   O  O   . LYS A 1 18  ? 19.170 -24.332 24.319 1.00 64.24  ? 15  LYS A O   1 
ATOM   91   C  CB  . LYS A 1 18  ? 20.354 -27.072 24.723 1.00 68.39  ? 15  LYS A CB  1 
ATOM   92   C  CG  . LYS A 1 18  ? 20.734 -28.274 23.841 1.00 78.28  ? 15  LYS A CG  1 
ATOM   93   C  CD  . LYS A 1 18  ? 19.971 -28.275 22.512 1.00 85.37  ? 15  LYS A CD  1 
ATOM   94   C  CE  . LYS A 1 18  ? 20.585 -29.244 21.487 1.00 90.70  ? 15  LYS A CE  1 
ATOM   95   N  NZ  . LYS A 1 18  ? 21.076 -28.559 20.234 1.00 89.77  ? 15  LYS A NZ  1 
ATOM   96   N  N   . ARG A 1 19  ? 20.689 -23.894 25.916 1.00 58.51  ? 16  ARG A N   1 
ATOM   97   C  CA  . ARG A 1 19  ? 20.012 -22.683 26.350 1.00 59.71  ? 16  ARG A CA  1 
ATOM   98   C  C   . ARG A 1 19  ? 20.557 -21.515 25.532 1.00 56.32  ? 16  ARG A C   1 
ATOM   99   O  O   . ARG A 1 19  ? 21.772 -21.330 25.455 1.00 51.80  ? 16  ARG A O   1 
ATOM   100  C  CB  . ARG A 1 19  ? 20.232 -22.445 27.845 1.00 58.13  ? 16  ARG A CB  1 
ATOM   101  C  CG  . ARG A 1 19  ? 20.164 -23.681 28.731 1.00 58.76  ? 16  ARG A CG  1 
ATOM   102  C  CD  . ARG A 1 19  ? 20.526 -23.302 30.177 1.00 58.72  ? 16  ARG A CD  1 
ATOM   103  N  NE  . ARG A 1 19  ? 20.394 -24.405 31.120 1.00 67.89  ? 16  ARG A NE  1 
ATOM   104  C  CZ  . ARG A 1 19  ? 20.652 -24.330 32.423 1.00 70.68  ? 16  ARG A CZ  1 
ATOM   105  N  NH1 . ARG A 1 19  ? 21.107 -23.215 32.987 1.00 57.98  ? 16  ARG A NH1 1 
ATOM   106  N  NH2 . ARG A 1 19  ? 20.450 -25.403 33.183 1.00 67.14  ? 16  ARG A NH2 1 
ATOM   107  N  N   . ALA A 1 20  ? 19.673 -20.728 24.920 1.00 53.84  ? 17  ALA A N   1 
ATOM   108  C  CA  . ALA A 1 20  ? 20.121 -19.708 23.980 1.00 55.11  ? 17  ALA A CA  1 
ATOM   109  C  C   . ALA A 1 20  ? 19.622 -18.335 24.397 1.00 51.74  ? 17  ALA A C   1 
ATOM   110  O  O   . ALA A 1 20  ? 18.554 -18.202 25.016 1.00 44.89  ? 17  ALA A O   1 
ATOM   111  C  CB  . ALA A 1 20  ? 19.669 -20.017 22.536 1.00 47.73  ? 17  ALA A CB  1 
ATOM   112  N  N   . VAL A 1 21  ? 20.413 -17.317 24.043 1.00 43.42  ? 18  VAL A N   1 
ATOM   113  C  CA  . VAL A 1 21  ? 20.077 -15.917 24.286 1.00 50.78  ? 18  VAL A CA  1 
ATOM   114  C  C   . VAL A 1 21  ? 20.140 -15.150 22.968 1.00 51.36  ? 18  VAL A C   1 
ATOM   115  O  O   . VAL A 1 21  ? 21.134 -15.245 22.232 1.00 47.20  ? 18  VAL A O   1 
ATOM   116  C  CB  . VAL A 1 21  ? 21.017 -15.252 25.318 1.00 48.72  ? 18  VAL A CB  1 
ATOM   117  C  CG1 . VAL A 1 21  ? 20.466 -13.898 25.713 1.00 43.45  ? 18  VAL A CG1 1 
ATOM   118  C  CG2 . VAL A 1 21  ? 21.198 -16.135 26.530 1.00 48.26  ? 18  VAL A CG2 1 
ATOM   119  N  N   . LEU A 1 22  ? 19.100 -14.350 22.708 1.00 45.98  ? 19  LEU A N   1 
ATOM   120  C  CA  . LEU A 1 22  ? 19.021 -13.453 21.562 1.00 46.38  ? 19  LEU A CA  1 
ATOM   121  C  C   . LEU A 1 22  ? 19.319 -12.029 22.042 1.00 47.98  ? 19  LEU A C   1 
ATOM   122  O  O   . LEU A 1 22  ? 18.658 -11.524 22.959 1.00 47.21  ? 19  LEU A O   1 
ATOM   123  C  CB  . LEU A 1 22  ? 17.637 -13.558 20.901 1.00 44.81  ? 19  LEU A CB  1 
ATOM   124  C  CG  . LEU A 1 22  ? 17.332 -12.646 19.702 1.00 51.14  ? 19  LEU A CG  1 
ATOM   125  C  CD1 . LEU A 1 22  ? 18.221 -13.016 18.507 1.00 44.90  ? 19  LEU A CD1 1 
ATOM   126  C  CD2 . LEU A 1 22  ? 15.849 -12.679 19.330 1.00 42.74  ? 19  LEU A CD2 1 
ATOM   127  N  N   . LEU A 1 23  ? 20.313 -11.389 21.424 1.00 46.50  ? 20  LEU A N   1 
ATOM   128  C  CA  . LEU A 1 23  ? 20.815 -10.078 21.834 1.00 47.29  ? 20  LEU A CA  1 
ATOM   129  C  C   . LEU A 1 23  ? 20.468 -9.009  20.791 1.00 48.15  ? 20  LEU A C   1 
ATOM   130  O  O   . LEU A 1 23  ? 20.829 -9.140  19.611 1.00 53.35  ? 20  LEU A O   1 
ATOM   131  C  CB  . LEU A 1 23  ? 22.340 -10.124 22.045 1.00 50.69  ? 20  LEU A CB  1 
ATOM   132  C  CG  . LEU A 1 23  ? 22.934 -11.146 23.022 1.00 49.19  ? 20  LEU A CG  1 
ATOM   133  C  CD1 . LEU A 1 23  ? 24.467 -11.277 22.892 1.00 51.91  ? 20  LEU A CD1 1 
ATOM   134  C  CD2 . LEU A 1 23  ? 22.547 -10.794 24.456 1.00 48.51  ? 20  LEU A CD2 1 
ATOM   135  N  N   . LEU A 1 24  ? 19.817 -7.933  21.242 1.00 42.82  ? 21  LEU A N   1 
ATOM   136  C  CA  . LEU A 1 24  ? 19.344 -6.845  20.397 1.00 50.34  ? 21  LEU A CA  1 
ATOM   137  C  C   . LEU A 1 24  ? 20.011 -5.526  20.798 1.00 53.08  ? 21  LEU A C   1 
ATOM   138  O  O   . LEU A 1 24  ? 19.969 -5.144  21.970 1.00 51.18  ? 21  LEU A O   1 
ATOM   139  C  CB  . LEU A 1 24  ? 17.818 -6.747  20.495 1.00 47.88  ? 21  LEU A CB  1 
ATOM   140  C  CG  . LEU A 1 24  ? 17.085 -8.080  20.282 1.00 47.68  ? 21  LEU A CG  1 
ATOM   141  C  CD1 . LEU A 1 24  ? 15.615 -7.942  20.594 1.00 45.56  ? 21  LEU A CD1 1 
ATOM   142  C  CD2 . LEU A 1 24  ? 17.260 -8.570  18.859 1.00 47.49  ? 21  LEU A CD2 1 
ATOM   143  N  N   . HIS A 1 25  ? 20.610 -4.820  19.821 1.00 52.88  ? 22  HIS A N   1 
ATOM   144  C  CA  . HIS A 1 25  ? 21.336 -3.577  20.072 1.00 53.66  ? 22  HIS A CA  1 
ATOM   145  C  C   . HIS A 1 25  ? 20.416 -2.351  19.969 1.00 55.53  ? 22  HIS A C   1 
ATOM   146  O  O   . HIS A 1 25  ? 19.214 -2.460  19.715 1.00 51.30  ? 22  HIS A O   1 
ATOM   147  C  CB  . HIS A 1 25  ? 22.543 -3.443  19.129 1.00 52.96  ? 22  HIS A CB  1 
ATOM   148  C  CG  . HIS A 1 25  ? 22.195 -3.355  17.676 1.00 58.31  ? 22  HIS A CG  1 
ATOM   149  N  ND1 . HIS A 1 25  ? 21.743 -2.193  17.082 1.00 61.29  ? 22  HIS A ND1 1 
ATOM   150  C  CD2 . HIS A 1 25  ? 22.268 -4.275  16.684 1.00 63.31  ? 22  HIS A CD2 1 
ATOM   151  C  CE1 . HIS A 1 25  ? 21.524 -2.410  15.797 1.00 59.79  ? 22  HIS A CE1 1 
ATOM   152  N  NE2 . HIS A 1 25  ? 21.828 -3.667  15.530 1.00 64.06  ? 22  HIS A NE2 1 
ATOM   153  N  N   . GLY A 1 26  ? 20.996 -1.159  20.164 1.00 54.80  ? 23  GLY A N   1 
ATOM   154  C  CA  . GLY A 1 26  ? 20.243 0.077   20.186 1.00 57.35  ? 23  GLY A CA  1 
ATOM   155  C  C   . GLY A 1 26  ? 20.290 0.856   18.868 1.00 66.70  ? 23  GLY A C   1 
ATOM   156  O  O   . GLY A 1 26  ? 20.995 0.508   17.917 1.00 62.67  ? 23  GLY A O   1 
ATOM   157  N  N   . PHE A 1 27  ? 19.507 1.945   18.839 1.00 65.57  ? 24  PHE A N   1 
ATOM   158  C  CA  . PHE A 1 27  ? 19.414 2.817   17.669 1.00 65.42  ? 24  PHE A CA  1 
ATOM   159  C  C   . PHE A 1 27  ? 20.784 3.397   17.332 1.00 75.99  ? 24  PHE A C   1 
ATOM   160  O  O   . PHE A 1 27  ? 21.471 3.934   18.204 1.00 77.49  ? 24  PHE A O   1 
ATOM   161  C  CB  . PHE A 1 27  ? 18.396 3.936   17.944 1.00 73.62  ? 24  PHE A CB  1 
ATOM   162  C  CG  . PHE A 1 27  ? 18.253 4.959   16.838 1.00 75.29  ? 24  PHE A CG  1 
ATOM   163  C  CD1 . PHE A 1 27  ? 18.041 4.577   15.524 1.00 80.21  ? 24  PHE A CD1 1 
ATOM   164  C  CD2 . PHE A 1 27  ? 18.277 6.314   17.132 1.00 81.21  ? 24  PHE A CD2 1 
ATOM   165  C  CE1 . PHE A 1 27  ? 17.895 5.541   14.510 1.00 86.45  ? 24  PHE A CE1 1 
ATOM   166  C  CE2 . PHE A 1 27  ? 18.132 7.280   16.126 1.00 85.88  ? 24  PHE A CE2 1 
ATOM   167  C  CZ  . PHE A 1 27  ? 17.941 6.888   14.817 1.00 85.78  ? 24  PHE A CZ  1 
ATOM   168  N  N   . THR A 1 28  ? 21.179 3.272   16.055 1.00 73.98  ? 25  THR A N   1 
ATOM   169  C  CA  . THR A 1 28  ? 22.513 3.590   15.524 1.00 76.12  ? 25  THR A CA  1 
ATOM   170  C  C   . THR A 1 28  ? 23.648 2.804   16.202 1.00 71.30  ? 25  THR A C   1 
ATOM   171  O  O   . THR A 1 28  ? 24.825 3.147   16.045 1.00 70.87  ? 25  THR A O   1 
ATOM   172  C  CB  . THR A 1 28  ? 22.814 5.105   15.558 1.00 80.03  ? 25  THR A CB  1 
ATOM   173  O  OG1 . THR A 1 28  ? 23.391 5.479   16.817 1.00 72.48  ? 25  THR A OG1 1 
ATOM   174  C  CG2 . THR A 1 28  ? 21.545 5.934   15.280 1.00 83.09  ? 25  THR A CG2 1 
ATOM   175  N  N   . GLY A 1 29  ? 23.335 1.732   16.930 1.00 68.09  ? 26  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 29  ? 24.341 0.821   17.437 1.00 64.76  ? 26  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 29  ? 24.591 -0.346  16.493 1.00 64.59  ? 26  GLY A C   1 
ATOM   178  O  O   . GLY A 1 29  ? 24.089 -0.400  15.368 1.00 64.75  ? 26  GLY A O   1 
ATOM   179  N  N   . ASN A 1 30  ? 25.394 -1.298  16.967 1.00 61.66  ? 27  ASN A N   1 
ATOM   180  C  CA  . ASN A 1 30  ? 25.666 -2.492  16.182 1.00 62.15  ? 27  ASN A CA  1 
ATOM   181  C  C   . ASN A 1 30  ? 26.050 -3.624  17.125 1.00 63.15  ? 27  ASN A C   1 
ATOM   182  O  O   . ASN A 1 30  ? 25.974 -3.491  18.350 1.00 64.00  ? 27  ASN A O   1 
ATOM   183  C  CB  . ASN A 1 30  ? 26.741 -2.227  15.136 1.00 64.50  ? 27  ASN A CB  1 
ATOM   184  C  CG  . ASN A 1 30  ? 27.888 -1.440  15.688 1.00 64.67  ? 27  ASN A CG  1 
ATOM   185  O  OD1 . ASN A 1 30  ? 28.549 -1.866  16.633 1.00 66.71  ? 27  ASN A OD1 1 
ATOM   186  N  ND2 . ASN A 1 30  ? 28.126 -0.268  15.115 1.00 71.81  ? 27  ASN A ND2 1 
ATOM   187  N  N   . SER A 1 31  ? 26.435 -4.762  16.542 1.00 60.59  ? 28  SER A N   1 
ATOM   188  C  CA  . SER A 1 31  ? 26.627 -5.964  17.345 1.00 56.91  ? 28  SER A CA  1 
ATOM   189  C  C   . SER A 1 31  ? 27.791 -5.813  18.310 1.00 57.29  ? 28  SER A C   1 
ATOM   190  O  O   . SER A 1 31  ? 27.787 -6.432  19.375 1.00 55.50  ? 28  SER A O   1 
ATOM   191  C  CB  . SER A 1 31  ? 26.839 -7.172  16.435 1.00 57.71  ? 28  SER A CB  1 
ATOM   192  O  OG  . SER A 1 31  ? 28.086 -7.085  15.759 1.00 64.28  ? 28  SER A OG  1 
ATOM   193  N  N   . SER A 1 32  ? 28.779 -4.981  17.977 1.00 58.25  ? 29  SER A N   1 
ATOM   194  C  CA  . SER A 1 32  ? 29.927 -4.827  18.859 1.00 61.86  ? 29  SER A CA  1 
ATOM   195  C  C   . SER A 1 32  ? 29.536 -4.225  20.205 1.00 62.29  ? 29  SER A C   1 
ATOM   196  O  O   . SER A 1 32  ? 30.290 -4.358  21.179 1.00 53.93  ? 29  SER A O   1 
ATOM   197  C  CB  . SER A 1 32  ? 31.011 -3.985  18.179 1.00 62.49  ? 29  SER A CB  1 
ATOM   198  O  OG  . SER A 1 32  ? 30.747 -2.601  18.328 1.00 69.72  ? 29  SER A OG  1 
ATOM   199  N  N   . ASP A 1 33  ? 28.358 -3.605  20.289 1.00 61.60  ? 30  ASP A N   1 
ATOM   200  C  CA  . ASP A 1 33  ? 27.865 -3.116  21.570 1.00 58.72  ? 30  ASP A CA  1 
ATOM   201  C  C   . ASP A 1 33  ? 27.498 -4.243  22.519 1.00 56.52  ? 30  ASP A C   1 
ATOM   202  O  O   . ASP A 1 33  ? 27.468 -4.014  23.731 1.00 54.87  ? 30  ASP A O   1 
ATOM   203  C  CB  . ASP A 1 33  ? 26.651 -2.207  21.361 1.00 57.56  ? 30  ASP A CB  1 
ATOM   204  C  CG  . ASP A 1 33  ? 27.030 -0.879  20.768 1.00 63.62  ? 30  ASP A CG  1 
ATOM   205  O  OD1 . ASP A 1 33  ? 28.152 -0.406  21.048 1.00 66.99  ? 30  ASP A OD1 1 
ATOM   206  O  OD2 . ASP A 1 33  ? 26.219 -0.310  20.008 1.00 70.03  ? 30  ASP A OD2 1 
ATOM   207  N  N   . VAL A 1 34  ? 27.220 -5.446  22.006 1.00 56.98  ? 31  VAL A N   1 
ATOM   208  C  CA  . VAL A 1 34  ? 26.821 -6.580  22.835 1.00 55.81  ? 31  VAL A CA  1 
ATOM   209  C  C   . VAL A 1 34  ? 27.788 -7.759  22.717 1.00 54.27  ? 31  VAL A C   1 
ATOM   210  O  O   . VAL A 1 34  ? 27.465 -8.870  23.148 1.00 52.57  ? 31  VAL A O   1 
ATOM   211  C  CB  . VAL A 1 34  ? 25.377 -7.024  22.517 1.00 53.58  ? 31  VAL A CB  1 
ATOM   212  C  CG1 . VAL A 1 34  ? 24.395 -5.962  22.952 1.00 51.73  ? 31  VAL A CG1 1 
ATOM   213  C  CG2 . VAL A 1 34  ? 25.192 -7.349  21.027 1.00 50.10  ? 31  VAL A CG2 1 
ATOM   214  N  N   . ARG A 1 35  ? 28.975 -7.539  22.153 1.00 52.03  ? 32  ARG A N   1 
ATOM   215  C  CA  . ARG A 1 35  ? 29.853 -8.659  21.840 1.00 54.04  ? 32  ARG A CA  1 
ATOM   216  C  C   . ARG A 1 35  ? 30.494 -9.223  23.097 1.00 53.63  ? 32  ARG A C   1 
ATOM   217  O  O   . ARG A 1 35  ? 30.496 -10.440 23.308 1.00 54.12  ? 32  ARG A O   1 
ATOM   218  C  CB  . ARG A 1 35  ? 30.925 -8.228  20.839 1.00 51.75  ? 32  ARG A CB  1 
ATOM   219  C  CG  . ARG A 1 35  ? 31.537 -9.408  20.123 1.00 56.22  ? 32  ARG A CG  1 
ATOM   220  C  CD  . ARG A 1 35  ? 32.658 -9.000  19.214 1.00 54.48  ? 32  ARG A CD  1 
ATOM   221  N  NE  . ARG A 1 35  ? 33.275 -10.150 18.558 1.00 60.53  ? 32  ARG A NE  1 
ATOM   222  C  CZ  . ARG A 1 35  ? 32.890 -10.642 17.385 1.00 61.04  ? 32  ARG A CZ  1 
ATOM   223  N  NH1 . ARG A 1 35  ? 31.845 -10.142 16.736 1.00 57.53  ? 32  ARG A NH1 1 
ATOM   224  N  NH2 . ARG A 1 35  ? 33.577 -11.650 16.845 1.00 55.98  ? 32  ARG A NH2 1 
ATOM   225  N  N   . GLN A 1 36  ? 31.062 -8.352  23.935 1.00 52.33  ? 33  GLN A N   1 
ATOM   226  C  CA  . GLN A 1 36  ? 31.604 -8.794  25.214 1.00 54.43  ? 33  GLN A CA  1 
ATOM   227  C  C   . GLN A 1 36  ? 30.586 -9.570  26.031 1.00 48.12  ? 33  GLN A C   1 
ATOM   228  O  O   . GLN A 1 36  ? 30.917 -10.601 26.618 1.00 47.61  ? 33  GLN A O   1 
ATOM   229  C  CB  . GLN A 1 36  ? 32.110 -7.601  26.008 1.00 58.01  ? 33  GLN A CB  1 
ATOM   230  C  CG  . GLN A 1 36  ? 33.450 -7.137  25.548 1.00 58.95  ? 33  GLN A CG  1 
ATOM   231  C  CD  . GLN A 1 36  ? 33.736 -5.722  25.987 1.00 74.61  ? 33  GLN A CD  1 
ATOM   232  O  OE1 . GLN A 1 36  ? 33.078 -4.778  25.542 1.00 75.08  ? 33  GLN A OE1 1 
ATOM   233  N  NE2 . GLN A 1 36  ? 34.723 -5.561  26.877 1.00 79.12  ? 33  GLN A NE2 1 
ATOM   234  N  N   . LEU A 1 37  ? 29.336 -9.108  26.069 1.00 53.28  ? 34  LEU A N   1 
ATOM   235  C  CA  . LEU A 1 37  ? 28.309 -9.899  26.743 1.00 51.05  ? 34  LEU A CA  1 
ATOM   236  C  C   . LEU A 1 37  ? 28.147 -11.266 26.083 1.00 48.74  ? 34  LEU A C   1 
ATOM   237  O  O   . LEU A 1 37  ? 27.970 -12.279 26.778 1.00 45.23  ? 34  LEU A O   1 
ATOM   238  C  CB  . LEU A 1 37  ? 26.987 -9.141  26.776 1.00 47.39  ? 34  LEU A CB  1 
ATOM   239  C  CG  . LEU A 1 37  ? 25.722 -9.888  27.210 1.00 47.70  ? 34  LEU A CG  1 
ATOM   240  C  CD1 . LEU A 1 37  ? 25.795 -10.342 28.655 1.00 45.22  ? 34  LEU A CD1 1 
ATOM   241  C  CD2 . LEU A 1 37  ? 24.502 -9.003  26.989 1.00 47.35  ? 34  LEU A CD2 1 
ATOM   242  N  N   . GLY A 1 38  ? 28.233 -11.324 24.748 1.00 46.13  ? 35  GLY A N   1 
ATOM   243  C  CA  . GLY A 1 38  ? 28.212 -12.621 24.077 1.00 47.61  ? 35  GLY A CA  1 
ATOM   244  C  C   . GLY A 1 38  ? 29.374 -13.511 24.487 1.00 50.92  ? 35  GLY A C   1 
ATOM   245  O  O   . GLY A 1 38  ? 29.211 -14.713 24.698 1.00 47.25  ? 35  GLY A O   1 
ATOM   246  N  N   . ARG A 1 39  ? 30.566 -12.935 24.611 1.00 49.93  ? 36  ARG A N   1 
ATOM   247  C  CA  . ARG A 1 39  ? 31.706 -13.744 25.018 1.00 55.23  ? 36  ARG A CA  1 
ATOM   248  C  C   . ARG A 1 39  ? 31.566 -14.214 26.460 1.00 53.95  ? 36  ARG A C   1 
ATOM   249  O  O   . ARG A 1 39  ? 31.997 -15.327 26.791 1.00 46.72  ? 36  ARG A O   1 
ATOM   250  C  CB  . ARG A 1 39  ? 33.000 -12.956 24.827 1.00 55.03  ? 36  ARG A CB  1 
ATOM   251  C  CG  . ARG A 1 39  ? 33.401 -12.829 23.378 1.00 55.30  ? 36  ARG A CG  1 
ATOM   252  C  CD  . ARG A 1 39  ? 33.794 -14.160 22.802 1.00 53.86  ? 36  ARG A CD  1 
ATOM   253  N  NE  . ARG A 1 39  ? 34.448 -13.997 21.512 1.00 59.31  ? 36  ARG A NE  1 
ATOM   254  C  CZ  . ARG A 1 39  ? 34.357 -14.876 20.526 1.00 53.24  ? 36  ARG A CZ  1 
ATOM   255  N  NH1 . ARG A 1 39  ? 33.657 -15.994 20.668 1.00 48.14  ? 36  ARG A NH1 1 
ATOM   256  N  NH2 . ARG A 1 39  ? 34.965 -14.618 19.369 1.00 50.63  ? 36  ARG A NH2 1 
ATOM   257  N  N   . PHE A 1 40  ? 30.964 -13.388 27.326 1.00 53.82  ? 37  PHE A N   1 
ATOM   258  C  CA  . PHE A 1 40  ? 30.791 -13.787 28.718 1.00 52.83  ? 37  PHE A CA  1 
ATOM   259  C  C   . PHE A 1 40  ? 29.805 -14.944 28.824 1.00 52.56  ? 37  PHE A C   1 
ATOM   260  O  O   . PHE A 1 40  ? 30.059 -15.928 29.535 1.00 52.24  ? 37  PHE A O   1 
ATOM   261  C  CB  . PHE A 1 40  ? 30.332 -12.591 29.560 1.00 50.00  ? 37  PHE A CB  1 
ATOM   262  C  CG  . PHE A 1 40  ? 29.993 -12.944 30.988 1.00 51.03  ? 37  PHE A CG  1 
ATOM   263  C  CD1 . PHE A 1 40  ? 30.959 -12.888 31.982 1.00 60.38  ? 37  PHE A CD1 1 
ATOM   264  C  CD2 . PHE A 1 40  ? 28.714 -13.347 31.335 1.00 51.99  ? 37  PHE A CD2 1 
ATOM   265  C  CE1 . PHE A 1 40  ? 30.656 -13.225 33.302 1.00 63.34  ? 37  PHE A CE1 1 
ATOM   266  C  CE2 . PHE A 1 40  ? 28.400 -13.688 32.663 1.00 58.03  ? 37  PHE A CE2 1 
ATOM   267  C  CZ  . PHE A 1 40  ? 29.367 -13.628 33.643 1.00 59.19  ? 37  PHE A CZ  1 
ATOM   268  N  N   . LEU A 1 41  ? 28.676 -14.847 28.118 1.00 49.95  ? 38  LEU A N   1 
ATOM   269  C  CA  . LEU A 1 41  ? 27.698 -15.933 28.138 1.00 49.00  ? 38  LEU A CA  1 
ATOM   270  C  C   . LEU A 1 41  ? 28.289 -17.226 27.575 1.00 52.71  ? 38  LEU A C   1 
ATOM   271  O  O   . LEU A 1 41  ? 27.955 -18.321 28.049 1.00 49.60  ? 38  LEU A O   1 
ATOM   272  C  CB  . LEU A 1 41  ? 26.439 -15.534 27.363 1.00 45.32  ? 38  LEU A CB  1 
ATOM   273  C  CG  . LEU A 1 41  ? 25.582 -14.404 27.948 1.00 49.20  ? 38  LEU A CG  1 
ATOM   274  C  CD1 . LEU A 1 41  ? 24.485 -14.017 26.997 1.00 46.32  ? 38  LEU A CD1 1 
ATOM   275  C  CD2 . LEU A 1 41  ? 24.990 -14.788 29.291 1.00 43.87  ? 38  LEU A CD2 1 
ATOM   276  N  N   . GLN A 1 42  ? 29.155 -17.125 26.553 1.00 50.30  ? 39  GLN A N   1 
ATOM   277  C  CA  . GLN A 1 42  ? 29.702 -18.332 25.944 1.00 47.19  ? 39  GLN A CA  1 
ATOM   278  C  C   . GLN A 1 42  ? 30.552 -19.071 26.956 1.00 56.85  ? 39  GLN A C   1 
ATOM   279  O  O   . GLN A 1 42  ? 30.477 -20.302 27.085 1.00 54.99  ? 39  GLN A O   1 
ATOM   280  C  CB  . GLN A 1 42  ? 30.526 -17.972 24.702 1.00 49.44  ? 39  GLN A CB  1 
ATOM   281  C  CG  . GLN A 1 42  ? 31.487 -19.059 24.217 1.00 48.90  ? 39  GLN A CG  1 
ATOM   282  C  CD  . GLN A 1 42  ? 32.248 -18.656 22.950 1.00 56.53  ? 39  GLN A CD  1 
ATOM   283  O  OE1 . GLN A 1 42  ? 32.922 -17.622 22.916 1.00 60.52  ? 39  GLN A OE1 1 
ATOM   284  N  NE2 . GLN A 1 42  ? 32.144 -19.474 21.902 1.00 49.11  ? 39  GLN A NE2 1 
ATOM   285  N  N   . LYS A 1 43  ? 31.348 -18.319 27.712 1.00 56.12  ? 40  LYS A N   1 
ATOM   286  C  CA  . LYS A 1 43  ? 32.209 -18.906 28.716 1.00 55.08  ? 40  LYS A CA  1 
ATOM   287  C  C   . LYS A 1 43  ? 31.401 -19.567 29.827 1.00 55.67  ? 40  LYS A C   1 
ATOM   288  O  O   . LYS A 1 43  ? 31.888 -20.515 30.452 1.00 54.83  ? 40  LYS A O   1 
ATOM   289  C  CB  . LYS A 1 43  ? 33.154 -17.818 29.215 1.00 53.59  ? 40  LYS A CB  1 
ATOM   290  C  CG  . LYS A 1 43  ? 33.813 -18.075 30.503 1.00 66.39  ? 40  LYS A CG  1 
ATOM   291  C  CD  . LYS A 1 43  ? 33.684 -16.835 31.380 1.00 81.29  ? 40  LYS A CD  1 
ATOM   292  C  CE  . LYS A 1 43  ? 34.723 -15.777 30.996 1.00 83.62  ? 40  LYS A CE  1 
ATOM   293  N  NZ  . LYS A 1 43  ? 34.999 -14.852 32.138 1.00 90.80  ? 40  LYS A NZ  1 
ATOM   294  N  N   . LYS A 1 44  ? 30.158 -19.138 30.040 1.00 51.15  ? 41  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 44  ? 29.251 -19.836 30.949 1.00 53.24  ? 41  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 44  ? 28.486 -20.974 30.277 1.00 54.45  ? 41  LYS A C   1 
ATOM   297  O  O   . LYS A 1 44  ? 27.725 -21.665 30.954 1.00 55.00  ? 41  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 44  ? 28.231 -18.867 31.571 1.00 51.51  ? 41  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 44  ? 28.820 -17.754 32.454 1.00 57.14  ? 41  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 44  ? 29.771 -18.286 33.523 1.00 49.61  ? 41  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 44  ? 30.111 -17.198 34.541 1.00 55.06  ? 41  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 44  ? 31.200 -17.604 35.516 1.00 59.95  ? 41  LYS A NZ  1 
ATOM   303  N  N   . GLY A 1 45  ? 28.648 -21.184 28.974 1.00 56.42  ? 42  GLY A N   1 
ATOM   304  C  CA  . GLY A 1 45  ? 28.001 -22.285 28.293 1.00 51.53  ? 42  GLY A CA  1 
ATOM   305  C  C   . GLY A 1 45  ? 26.674 -21.960 27.655 1.00 54.05  ? 42  GLY A C   1 
ATOM   306  O  O   . GLY A 1 45  ? 25.973 -22.884 27.214 1.00 56.79  ? 42  GLY A O   1 
ATOM   307  N  N   . TYR A 1 46  ? 26.297 -20.684 27.597 1.00 54.51  ? 43  TYR A N   1 
ATOM   308  C  CA  . TYR A 1 46  ? 25.095 -20.263 26.891 1.00 51.24  ? 43  TYR A CA  1 
ATOM   309  C  C   . TYR A 1 46  ? 25.419 -19.954 25.429 1.00 52.76  ? 43  TYR A C   1 
ATOM   310  O  O   . TYR A 1 46  ? 26.453 -19.350 25.120 1.00 46.89  ? 43  TYR A O   1 
ATOM   311  C  CB  . TYR A 1 46  ? 24.484 -19.038 27.568 1.00 45.59  ? 43  TYR A CB  1 
ATOM   312  C  CG  . TYR A 1 46  ? 23.709 -19.367 28.835 1.00 55.69  ? 43  TYR A CG  1 
ATOM   313  C  CD1 . TYR A 1 46  ? 24.371 -19.584 30.038 1.00 51.39  ? 43  TYR A CD1 1 
ATOM   314  C  CD2 . TYR A 1 46  ? 22.314 -19.473 28.827 1.00 52.37  ? 43  TYR A CD2 1 
ATOM   315  C  CE1 . TYR A 1 46  ? 23.687 -19.888 31.185 1.00 52.17  ? 43  TYR A CE1 1 
ATOM   316  C  CE2 . TYR A 1 46  ? 21.619 -19.776 29.987 1.00 55.59  ? 43  TYR A CE2 1 
ATOM   317  C  CZ  . TYR A 1 46  ? 22.315 -19.983 31.161 1.00 52.75  ? 43  TYR A CZ  1 
ATOM   318  O  OH  . TYR A 1 46  ? 21.659 -20.262 32.328 1.00 50.40  ? 43  TYR A OH  1 
ATOM   319  N  N   . THR A 1 47  ? 24.544 -20.411 24.537 1.00 51.13  ? 44  THR A N   1 
ATOM   320  C  CA  . THR A 1 47  ? 24.588 -20.050 23.126 1.00 49.49  ? 44  THR A CA  1 
ATOM   321  C  C   . THR A 1 47  ? 23.998 -18.655 22.965 1.00 50.99  ? 44  THR A C   1 
ATOM   322  O  O   . THR A 1 47  ? 23.024 -18.304 23.636 1.00 48.96  ? 44  THR A O   1 
ATOM   323  C  CB  . THR A 1 47  ? 23.792 -21.078 22.305 1.00 50.87  ? 44  THR A CB  1 
ATOM   324  O  OG1 . THR A 1 47  ? 24.537 -22.299 22.185 1.00 55.31  ? 44  THR A OG1 1 
ATOM   325  C  CG2 . THR A 1 47  ? 23.426 -20.569 20.916 1.00 51.10  ? 44  THR A CG2 1 
ATOM   326  N  N   . SER A 1 48  ? 24.584 -17.842 22.086 1.00 50.89  ? 45  SER A N   1 
ATOM   327  C  CA  . SER A 1 48  ? 24.010 -16.520 21.878 1.00 51.83  ? 45  SER A CA  1 
ATOM   328  C  C   . SER A 1 48  ? 24.080 -16.122 20.407 1.00 50.81  ? 45  SER A C   1 
ATOM   329  O  O   . SER A 1 48  ? 24.940 -16.595 19.657 1.00 52.77  ? 45  SER A O   1 
ATOM   330  C  CB  . SER A 1 48  ? 24.689 -15.461 22.777 1.00 49.87  ? 45  SER A CB  1 
ATOM   331  O  OG  . SER A 1 48  ? 26.003 -15.174 22.345 1.00 54.64  ? 45  SER A OG  1 
ATOM   332  N  N   . TYR A 1 49  ? 23.136 -15.260 20.000 1.00 51.14  ? 46  TYR A N   1 
ATOM   333  C  CA  . TYR A 1 49  ? 23.008 -14.806 18.617 1.00 50.78  ? 46  TYR A CA  1 
ATOM   334  C  C   . TYR A 1 49  ? 22.637 -13.328 18.588 1.00 51.33  ? 46  TYR A C   1 
ATOM   335  O  O   . TYR A 1 49  ? 21.737 -12.899 19.315 1.00 48.75  ? 46  TYR A O   1 
ATOM   336  C  CB  . TYR A 1 49  ? 21.962 -15.631 17.857 1.00 46.81  ? 46  TYR A CB  1 
ATOM   337  C  CG  . TYR A 1 49  ? 21.766 -15.156 16.440 1.00 53.29  ? 46  TYR A CG  1 
ATOM   338  C  CD1 . TYR A 1 49  ? 22.831 -15.138 15.536 1.00 55.28  ? 46  TYR A CD1 1 
ATOM   339  C  CD2 . TYR A 1 49  ? 20.529 -14.689 16.008 1.00 54.96  ? 46  TYR A CD2 1 
ATOM   340  C  CE1 . TYR A 1 49  ? 22.656 -14.687 14.237 1.00 51.89  ? 46  TYR A CE1 1 
ATOM   341  C  CE2 . TYR A 1 49  ? 20.344 -14.244 14.710 1.00 56.45  ? 46  TYR A CE2 1 
ATOM   342  C  CZ  . TYR A 1 49  ? 21.411 -14.243 13.828 1.00 55.45  ? 46  TYR A CZ  1 
ATOM   343  O  OH  . TYR A 1 49  ? 21.219 -13.793 12.535 1.00 57.91  ? 46  TYR A OH  1 
ATOM   344  N  N   . ALA A 1 50  ? 23.318 -12.556 17.741 1.00 49.65  ? 47  ALA A N   1 
ATOM   345  C  CA  . ALA A 1 50  ? 23.194 -11.099 17.720 1.00 49.38  ? 47  ALA A CA  1 
ATOM   346  C  C   . ALA A 1 50  ? 23.016 -10.614 16.288 1.00 56.88  ? 47  ALA A C   1 
ATOM   347  O  O   . ALA A 1 50  ? 24.011 -10.464 15.557 1.00 56.25  ? 47  ALA A O   1 
ATOM   348  C  CB  . ALA A 1 50  ? 24.418 -10.437 18.340 1.00 46.24  ? 47  ALA A CB  1 
ATOM   349  N  N   . PRO A 1 51  ? 21.788 -10.355 15.854 1.00 55.72  ? 48  PRO A N   1 
ATOM   350  C  CA  . PRO A 1 51  ? 21.567 -9.801  14.513 1.00 58.69  ? 48  PRO A CA  1 
ATOM   351  C  C   . PRO A 1 51  ? 21.772 -8.284  14.497 1.00 56.83  ? 48  PRO A C   1 
ATOM   352  O  O   . PRO A 1 51  ? 21.941 -7.646  15.531 1.00 61.19  ? 48  PRO A O   1 
ATOM   353  C  CB  . PRO A 1 51  ? 20.109 -10.190 14.225 1.00 54.34  ? 48  PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 51  ? 19.468 -10.240 15.586 1.00 54.97  ? 48  PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 51  ? 20.530 -10.709 16.540 1.00 49.07  ? 48  PRO A CD  1 
ATOM   356  N  N   . GLN A 1 52  ? 21.752 -7.703  13.294 1.00 60.02  ? 49  GLN A N   1 
ATOM   357  C  CA  . GLN A 1 52  ? 21.888 -6.258  13.120 1.00 62.08  ? 49  GLN A CA  1 
ATOM   358  C  C   . GLN A 1 52  ? 20.711 -5.713  12.333 1.00 62.76  ? 49  GLN A C   1 
ATOM   359  O  O   . GLN A 1 52  ? 20.229 -6.363  11.402 1.00 67.08  ? 49  GLN A O   1 
ATOM   360  C  CB  . GLN A 1 52  ? 23.192 -5.902  12.396 1.00 62.37  ? 49  GLN A CB  1 
ATOM   361  C  CG  . GLN A 1 52  ? 24.428 -6.267  13.220 1.00 64.25  ? 49  GLN A CG  1 
ATOM   362  C  CD  . GLN A 1 52  ? 25.708 -5.616  12.721 1.00 69.00  ? 49  GLN A CD  1 
ATOM   363  O  OE1 . GLN A 1 52  ? 26.555 -5.210  13.529 1.00 66.96  ? 49  GLN A OE1 1 
ATOM   364  N  NE2 . GLN A 1 52  ? 25.867 -5.522  11.393 1.00 67.20  ? 49  GLN A NE2 1 
ATOM   365  N  N   . TYR A 1 53  ? 20.250 -4.516  12.693 1.00 65.83  ? 50  TYR A N   1 
ATOM   366  C  CA  . TYR A 1 53  ? 19.105 -3.977  11.977 1.00 67.96  ? 50  TYR A CA  1 
ATOM   367  C  C   . TYR A 1 53  ? 19.523 -3.445  10.621 1.00 71.98  ? 50  TYR A C   1 
ATOM   368  O  O   . TYR A 1 53  ? 20.694 -3.169  10.361 1.00 72.27  ? 50  TYR A O   1 
ATOM   369  C  CB  . TYR A 1 53  ? 18.419 -2.849  12.741 1.00 71.94  ? 50  TYR A CB  1 
ATOM   370  C  CG  . TYR A 1 53  ? 18.063 -3.155  14.168 1.00 66.99  ? 50  TYR A CG  1 
ATOM   371  C  CD1 . TYR A 1 53  ? 17.299 -4.259  14.507 1.00 67.42  ? 50  TYR A CD1 1 
ATOM   372  C  CD2 . TYR A 1 53  ? 18.469 -2.312  15.181 1.00 68.21  ? 50  TYR A CD2 1 
ATOM   373  C  CE1 . TYR A 1 53  ? 16.968 -4.523  15.854 1.00 63.52  ? 50  TYR A CE1 1 
ATOM   374  C  CE2 . TYR A 1 53  ? 18.168 -2.568  16.505 1.00 65.16  ? 50  TYR A CE2 1 
ATOM   375  C  CZ  . TYR A 1 53  ? 17.414 -3.661  16.842 1.00 62.91  ? 50  TYR A CZ  1 
ATOM   376  O  OH  . TYR A 1 53  ? 17.125 -3.857  18.176 1.00 59.15  ? 50  TYR A OH  1 
ATOM   377  N  N   . GLU A 1 54  ? 18.525 -3.274  9.763  1.00 77.30  ? 51  GLU A N   1 
ATOM   378  C  CA  . GLU A 1 54  ? 18.748 -2.741  8.431  1.00 77.67  ? 51  GLU A CA  1 
ATOM   379  C  C   . GLU A 1 54  ? 19.196 -1.286  8.532  1.00 81.12  ? 51  GLU A C   1 
ATOM   380  O  O   . GLU A 1 54  ? 18.741 -0.544  9.406  1.00 80.09  ? 51  GLU A O   1 
ATOM   381  C  CB  . GLU A 1 54  ? 17.462 -2.895  7.608  1.00 81.42  ? 51  GLU A CB  1 
ATOM   382  C  CG  . GLU A 1 54  ? 17.547 -2.524  6.133  1.00 81.70  ? 51  GLU A CG  1 
ATOM   383  C  CD  . GLU A 1 54  ? 16.165 -2.522  5.459  1.00 95.67  ? 51  GLU A CD  1 
ATOM   384  O  OE1 . GLU A 1 54  ? 15.423 -1.515  5.569  1.00 90.15  ? 51  GLU A OE1 1 
ATOM   385  O  OE2 . GLU A 1 54  ? 15.812 -3.547  4.823  1.00 103.22 ? 51  GLU A OE2 1 
ATOM   386  N  N   . GLY A 1 55  ? 20.134 -0.892  7.661  1.00 84.40  ? 52  GLY A N   1 
ATOM   387  C  CA  . GLY A 1 55  ? 20.751 0.426   7.713  1.00 86.35  ? 52  GLY A CA  1 
ATOM   388  C  C   . GLY A 1 55  ? 21.866 0.603   8.733  1.00 83.52  ? 52  GLY A C   1 
ATOM   389  O  O   . GLY A 1 55  ? 22.579 1.621   8.681  1.00 83.27  ? 52  GLY A O   1 
ATOM   390  N  N   . HIS A 1 56  ? 22.040 -0.337  9.658  1.00 79.28  ? 53  HIS A N   1 
ATOM   391  C  CA  . HIS A 1 56  ? 23.034 -0.220  10.713 1.00 80.13  ? 53  HIS A CA  1 
ATOM   392  C  C   . HIS A 1 56  ? 24.349 -0.885  10.298 1.00 78.46  ? 53  HIS A C   1 
ATOM   393  O  O   . HIS A 1 56  ? 24.406 -1.673  9.348  1.00 78.34  ? 53  HIS A O   1 
ATOM   394  C  CB  . HIS A 1 56  ? 22.498 -0.823  12.018 1.00 72.16  ? 53  HIS A CB  1 
ATOM   395  C  CG  . HIS A 1 56  ? 21.426 0.004   12.663 1.00 74.24  ? 53  HIS A CG  1 
ATOM   396  N  ND1 . HIS A 1 56  ? 20.213 0.260   12.053 1.00 78.99  ? 53  HIS A ND1 1 
ATOM   397  C  CD2 . HIS A 1 56  ? 21.389 0.644   13.856 1.00 66.65  ? 53  HIS A CD2 1 
ATOM   398  C  CE1 . HIS A 1 56  ? 19.475 1.020   12.844 1.00 76.56  ? 53  HIS A CE1 1 
ATOM   399  N  NE2 . HIS A 1 56  ? 20.167 1.271   13.942 1.00 69.57  ? 53  HIS A NE2 1 
ATOM   400  N  N   . ALA A 1 57  ? 25.416 -0.547  11.027 1.00 75.60  ? 54  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 57  ? 26.780 -0.901  10.637 1.00 77.37  ? 54  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 57  ? 27.042 -0.512  9.175  1.00 88.99  ? 54  ALA A C   1 
ATOM   403  O  O   . ALA A 1 57  ? 27.620 -1.274  8.393  1.00 86.06  ? 54  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 57  ? 27.051 -2.387  10.877 1.00 74.11  ? 54  ALA A CB  1 
ATOM   405  N  N   . ALA A 1 58  ? 26.612 0.702   8.823  1.00 90.93  ? 55  ALA A N   1 
ATOM   406  C  CA  . ALA A 1 58  ? 26.551 1.169   7.444  1.00 88.40  ? 55  ALA A CA  1 
ATOM   407  C  C   . ALA A 1 58  ? 26.561 2.691   7.461  1.00 95.01  ? 55  ALA A C   1 
ATOM   408  O  O   . ALA A 1 58  ? 26.460 3.306   8.531  1.00 96.30  ? 55  ALA A O   1 
ATOM   409  C  CB  . ALA A 1 58  ? 25.294 0.637   6.735  1.00 87.22  ? 55  ALA A CB  1 
ATOM   410  N  N   . PRO A 1 59  ? 26.716 3.331   6.301  1.00 100.90 ? 56  PRO A N   1 
ATOM   411  C  CA  . PRO A 1 59  ? 26.562 4.802   6.227  1.00 103.76 ? 56  PRO A CA  1 
ATOM   412  C  C   . PRO A 1 59  ? 25.215 5.240   6.770  1.00 106.32 ? 56  PRO A C   1 
ATOM   413  O  O   . PRO A 1 59  ? 24.198 4.569   6.533  1.00 104.78 ? 56  PRO A O   1 
ATOM   414  C  CB  . PRO A 1 59  ? 26.676 5.105   4.728  1.00 96.81  ? 56  PRO A CB  1 
ATOM   415  C  CG  . PRO A 1 59  ? 27.368 3.939   4.132  1.00 100.92 ? 56  PRO A CG  1 
ATOM   416  C  CD  . PRO A 1 59  ? 27.379 2.786   5.104  1.00 97.79  ? 56  PRO A CD  1 
ATOM   417  N  N   . PRO A 1 60  ? 25.165 6.367   7.491  1.00 107.93 ? 57  PRO A N   1 
ATOM   418  C  CA  . PRO A 1 60  ? 23.918 6.746   8.181  1.00 109.23 ? 57  PRO A CA  1 
ATOM   419  C  C   . PRO A 1 60  ? 22.748 7.028   7.249  1.00 111.76 ? 57  PRO A C   1 
ATOM   420  O  O   . PRO A 1 60  ? 21.596 6.905   7.688  1.00 111.93 ? 57  PRO A O   1 
ATOM   421  C  CB  . PRO A 1 60  ? 24.322 7.997   8.978  1.00 108.67 ? 57  PRO A CB  1 
ATOM   422  C  CG  . PRO A 1 60  ? 25.524 8.538   8.278  1.00 107.69 ? 57  PRO A CG  1 
ATOM   423  C  CD  . PRO A 1 60  ? 26.244 7.344   7.714  1.00 106.14 ? 57  PRO A CD  1 
ATOM   424  N  N   . ASP A 1 61  ? 23.004 7.394   5.986  1.00 113.52 ? 58  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 61  ? 21.930 7.565   5.008  1.00 113.15 ? 58  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 61  ? 21.081 6.310   4.882  1.00 111.41 ? 58  ASP A C   1 
ATOM   427  O  O   . ASP A 1 61  ? 19.882 6.402   4.595  1.00 115.58 ? 58  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 61  ? 22.513 7.925   3.641  1.00 116.97 ? 58  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 61  ? 23.047 9.330   3.591  1.00 126.37 ? 58  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 61  ? 22.244 10.289  3.630  1.00 128.22 ? 58  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 61  ? 24.285 9.473   3.541  1.00 134.62 ? 58  ASP A OD2 1 
ATOM   432  N  N   . GLU A 1 62  ? 21.681 5.131   5.078  1.00 110.98 ? 59  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 62  ? 20.917 3.889   5.009  1.00 109.62 ? 59  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 62  ? 19.822 3.834   6.071  1.00 108.84 ? 59  GLU A C   1 
ATOM   435  O  O   . GLU A 1 62  ? 18.739 3.295   5.812  1.00 110.21 ? 59  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 62  ? 21.855 2.688   5.142  1.00 106.76 ? 59  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 62  ? 22.953 2.653   4.088  1.00 106.90 ? 59  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 62  ? 22.498 2.005   2.791  1.00 115.55 ? 59  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 62  ? 21.991 0.863   2.846  1.00 122.60 ? 59  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 62  ? 22.651 2.634   1.718  1.00 117.59 ? 59  GLU A OE2 1 
ATOM   441  N  N   . ILE A 1 63  ? 20.074 4.394   7.258  1.00 103.89 ? 60  ILE A N   1 
ATOM   442  C  CA  . ILE A 1 63  ? 19.052 4.420   8.302  1.00 98.28  ? 60  ILE A CA  1 
ATOM   443  C  C   . ILE A 1 63  ? 17.863 5.270   7.872  1.00 105.36 ? 60  ILE A C   1 
ATOM   444  O  O   . ILE A 1 63  ? 16.704 4.913   8.119  1.00 102.25 ? 60  ILE A O   1 
ATOM   445  C  CB  . ILE A 1 63  ? 19.659 4.923   9.621  1.00 97.14  ? 60  ILE A CB  1 
ATOM   446  C  CG1 . ILE A 1 63  ? 20.704 3.920   10.121 1.00 94.92  ? 60  ILE A CG1 1 
ATOM   447  C  CG2 . ILE A 1 63  ? 18.567 5.154   10.648 1.00 95.73  ? 60  ILE A CG2 1 
ATOM   448  C  CD1 . ILE A 1 63  ? 21.335 4.279   11.448 1.00 91.80  ? 60  ILE A CD1 1 
ATOM   449  N  N   . LEU A 1 64  ? 18.133 6.401   7.210  1.00 107.60 ? 61  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 64  ? 17.082 7.316   6.775  1.00 109.24 ? 61  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 64  ? 16.176 6.699   5.718  1.00 111.14 ? 61  LEU A C   1 
ATOM   452  O  O   . LEU A 1 64  ? 15.018 7.116   5.585  1.00 105.83 ? 61  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 64  ? 17.703 8.605   6.226  1.00 112.63 ? 61  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 64  ? 18.022 9.733   7.209  1.00 113.71 ? 61  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 64  ? 18.114 11.036  6.464  1.00 108.92 ? 61  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 64  ? 16.976 9.818   8.312  1.00 113.53 ? 61  LEU A CD2 1 
ATOM   457  N  N   . LYS A 1 65  ? 16.680 5.730   4.959  1.00 110.37 ? 62  LYS A N   1 
ATOM   458  C  CA  . LYS A 1 65  ? 15.903 5.041   3.939  1.00 109.19 ? 62  LYS A CA  1 
ATOM   459  C  C   . LYS A 1 65  ? 15.106 3.885   4.518  1.00 102.40 ? 62  LYS A C   1 
ATOM   460  O  O   . LYS A 1 65  ? 14.393 3.198   3.777  1.00 102.98 ? 62  LYS A O   1 
ATOM   461  C  CB  . LYS A 1 65  ? 16.829 4.522   2.830  1.00 113.82 ? 62  LYS A CB  1 
ATOM   462  C  CG  . LYS A 1 65  ? 17.601 5.592   2.058  1.00 110.06 ? 62  LYS A CG  1 
ATOM   463  C  CD  . LYS A 1 65  ? 16.774 6.178   0.929  1.00 125.36 ? 62  LYS A CD  1 
ATOM   464  C  CE  . LYS A 1 65  ? 17.160 7.630   0.624  1.00 130.34 ? 62  LYS A CE  1 
ATOM   465  N  NZ  . LYS A 1 65  ? 17.541 8.381   1.862  1.00 133.88 ? 62  LYS A NZ  1 
ATOM   466  N  N   . SER A 1 66  ? 15.219 3.654   5.817  1.00 103.55 ? 63  SER A N   1 
ATOM   467  C  CA  . SER A 1 66  ? 14.640 2.504   6.475  1.00 96.90  ? 63  SER A CA  1 
ATOM   468  C  C   . SER A 1 66  ? 13.449 2.940   7.321  1.00 98.19  ? 63  SER A C   1 
ATOM   469  O  O   . SER A 1 66  ? 12.935 4.063   7.190  1.00 98.93  ? 63  SER A O   1 
ATOM   470  C  CB  . SER A 1 66  ? 15.709 1.798   7.312  1.00 92.88  ? 63  SER A CB  1 
ATOM   471  O  OG  . SER A 1 66  ? 15.404 0.426   7.488  1.00 87.70  ? 63  SER A OG  1 
ATOM   472  N  N   . SER A 1 67  ? 13.011 2.039   8.202  1.00 90.59  ? 64  SER A N   1 
ATOM   473  C  CA  . SER A 1 67  ? 11.892 2.297   9.064  1.00 86.40  ? 64  SER A CA  1 
ATOM   474  C  C   . SER A 1 67  ? 12.091 1.471   10.321 1.00 86.22  ? 64  SER A C   1 
ATOM   475  O  O   . SER A 1 67  ? 12.650 0.365   10.241 1.00 89.24  ? 64  SER A O   1 
ATOM   476  C  CB  . SER A 1 67  ? 10.572 1.930   8.386  1.00 94.27  ? 64  SER A CB  1 
ATOM   477  O  OG  . SER A 1 67  ? 9.502  1.921   9.311  1.00 99.57  ? 64  SER A OG  1 
ATOM   478  N  N   . PRO A 1 68  ? 11.700 1.986   11.492 1.00 92.60  ? 65  PRO A N   1 
ATOM   479  C  CA  . PRO A 1 68  ? 11.726 1.147   12.705 1.00 88.18  ? 65  PRO A CA  1 
ATOM   480  C  C   . PRO A 1 68  ? 10.899 -0.115  12.596 1.00 83.09  ? 65  PRO A C   1 
ATOM   481  O  O   . PRO A 1 68  ? 11.139 -1.055  13.354 1.00 77.12  ? 65  PRO A O   1 
ATOM   482  C  CB  . PRO A 1 68  ? 11.173 2.072   13.801 1.00 87.63  ? 65  PRO A CB  1 
ATOM   483  C  CG  . PRO A 1 68  ? 11.083 3.468   13.185 1.00 90.90  ? 65  PRO A CG  1 
ATOM   484  C  CD  . PRO A 1 68  ? 11.682 3.423   11.811 1.00 95.06  ? 65  PRO A CD  1 
ATOM   485  N  N   . PHE A 1 69  ? 9.931  -0.171  11.683 1.00 85.34  ? 66  PHE A N   1 
ATOM   486  C  CA  . PHE A 1 69  ? 9.088  -1.356  11.586 1.00 83.77  ? 66  PHE A CA  1 
ATOM   487  C  C   . PHE A 1 69  ? 9.809  -2.496  10.878 1.00 82.71  ? 66  PHE A C   1 
ATOM   488  O  O   . PHE A 1 69  ? 9.508  -3.668  11.136 1.00 85.23  ? 66  PHE A O   1 
ATOM   489  C  CB  . PHE A 1 69  ? 7.775  -0.996  10.880 1.00 93.13  ? 66  PHE A CB  1 
ATOM   490  C  CG  . PHE A 1 69  ? 7.016  0.128   11.555 1.00 98.09  ? 66  PHE A CG  1 
ATOM   491  C  CD1 . PHE A 1 69  ? 6.838  0.130   12.939 1.00 92.36  ? 66  PHE A CD1 1 
ATOM   492  C  CD2 . PHE A 1 69  ? 6.517  1.205   10.810 1.00 100.73 ? 66  PHE A CD2 1 
ATOM   493  C  CE1 . PHE A 1 69  ? 6.152  1.161   13.576 1.00 96.94  ? 66  PHE A CE1 1 
ATOM   494  C  CE2 . PHE A 1 69  ? 5.827  2.250   11.438 1.00 102.09 ? 66  PHE A CE2 1 
ATOM   495  C  CZ  . PHE A 1 69  ? 5.646  2.227   12.828 1.00 107.16 ? 66  PHE A CZ  1 
ATOM   496  N  N   . VAL A 1 70  ? 10.759 -2.177  9.989  1.00 86.91  ? 67  VAL A N   1 
ATOM   497  C  CA  . VAL A 1 70  ? 11.689 -3.189  9.487  1.00 78.48  ? 67  VAL A CA  1 
ATOM   498  C  C   . VAL A 1 70  ? 12.537 -3.719  10.628 1.00 76.89  ? 67  VAL A C   1 
ATOM   499  O  O   . VAL A 1 70  ? 12.663 -4.932  10.831 1.00 75.22  ? 67  VAL A O   1 
ATOM   500  C  CB  . VAL A 1 70  ? 12.573 -2.604  8.371  1.00 79.90  ? 67  VAL A CB  1 
ATOM   501  C  CG1 . VAL A 1 70  ? 13.486 -3.675  7.794  1.00 71.19  ? 67  VAL A CG1 1 
ATOM   502  C  CG2 . VAL A 1 70  ? 11.717 -1.945  7.291  1.00 76.92  ? 67  VAL A CG2 1 
ATOM   503  N  N   . TRP A 1 71  ? 13.116 -2.805  11.405 1.00 77.31  ? 68  TRP A N   1 
ATOM   504  C  CA  . TRP A 1 71  ? 14.020 -3.182  12.485 1.00 70.49  ? 68  TRP A CA  1 
ATOM   505  C  C   . TRP A 1 71  ? 13.386 -4.185  13.451 1.00 71.89  ? 68  TRP A C   1 
ATOM   506  O  O   . TRP A 1 71  ? 14.090 -5.040  14.009 1.00 62.45  ? 68  TRP A O   1 
ATOM   507  C  CB  . TRP A 1 71  ? 14.472 -1.913  13.219 1.00 75.11  ? 68  TRP A CB  1 
ATOM   508  C  CG  . TRP A 1 71  ? 15.049 -0.861  12.284 1.00 79.72  ? 68  TRP A CG  1 
ATOM   509  C  CD1 . TRP A 1 71  ? 15.548 -1.071  11.030 1.00 80.47  ? 68  TRP A CD1 1 
ATOM   510  C  CD2 . TRP A 1 71  ? 15.191 0.546   12.539 1.00 82.85  ? 68  TRP A CD2 1 
ATOM   511  N  NE1 . TRP A 1 71  ? 15.977 0.112   10.484 1.00 84.89  ? 68  TRP A NE1 1 
ATOM   512  C  CE2 . TRP A 1 71  ? 15.777 1.122   11.389 1.00 85.15  ? 68  TRP A CE2 1 
ATOM   513  C  CE3 . TRP A 1 71  ? 14.886 1.374   13.627 1.00 82.25  ? 68  TRP A CE3 1 
ATOM   514  C  CZ2 . TRP A 1 71  ? 16.055 2.496   11.290 1.00 82.26  ? 68  TRP A CZ2 1 
ATOM   515  C  CZ3 . TRP A 1 71  ? 15.159 2.740   13.525 1.00 82.00  ? 68  TRP A CZ3 1 
ATOM   516  C  CH2 . TRP A 1 71  ? 15.740 3.283   12.367 1.00 81.94  ? 68  TRP A CH2 1 
ATOM   517  N  N   . PHE A 1 72  ? 12.064 -4.110  13.674 1.00 72.01  ? 69  PHE A N   1 
ATOM   518  C  CA  . PHE A 1 72  ? 11.447 -5.115  14.541 1.00 66.59  ? 69  PHE A CA  1 
ATOM   519  C  C   . PHE A 1 72  ? 11.443 -6.488  13.873 1.00 67.81  ? 69  PHE A C   1 
ATOM   520  O  O   . PHE A 1 72  ? 11.708 -7.501  14.535 1.00 60.58  ? 69  PHE A O   1 
ATOM   521  C  CB  . PHE A 1 72  ? 10.028 -4.708  14.952 1.00 62.74  ? 69  PHE A CB  1 
ATOM   522  C  CG  . PHE A 1 72  ? 9.366  -5.691  15.910 1.00 67.38  ? 69  PHE A CG  1 
ATOM   523  C  CD1 . PHE A 1 72  ? 9.936  -5.975  17.153 1.00 60.48  ? 69  PHE A CD1 1 
ATOM   524  C  CD2 . PHE A 1 72  ? 8.174  -6.332  15.571 1.00 63.54  ? 69  PHE A CD2 1 
ATOM   525  C  CE1 . PHE A 1 72  ? 9.339  -6.877  18.034 1.00 56.45  ? 69  PHE A CE1 1 
ATOM   526  C  CE2 . PHE A 1 72  ? 7.573  -7.233  16.460 1.00 61.66  ? 69  PHE A CE2 1 
ATOM   527  C  CZ  . PHE A 1 72  ? 8.172  -7.503  17.694 1.00 55.93  ? 69  PHE A CZ  1 
ATOM   528  N  N   . LYS A 1 73  ? 11.173 -6.538  12.558 1.00 65.73  ? 70  LYS A N   1 
ATOM   529  C  CA  . LYS A 1 73  ? 11.210 -7.810  11.843 1.00 62.52  ? 70  LYS A CA  1 
ATOM   530  C  C   . LYS A 1 73  ? 12.604 -8.425  11.863 1.00 63.47  ? 70  LYS A C   1 
ATOM   531  O  O   . LYS A 1 73  ? 12.743 -9.653  11.938 1.00 64.70  ? 70  LYS A O   1 
ATOM   532  C  CB  . LYS A 1 73  ? 10.738 -7.629  10.405 1.00 73.15  ? 70  LYS A CB  1 
ATOM   533  C  CG  . LYS A 1 73  ? 10.509 -8.948  9.662  1.00 80.61  ? 70  LYS A CG  1 
ATOM   534  C  CD  . LYS A 1 73  ? 11.234 -8.943  8.294  1.00 94.53  ? 70  LYS A CD  1 
ATOM   535  C  CE  . LYS A 1 73  ? 10.686 -10.005 7.300  1.00 98.97  ? 70  LYS A CE  1 
ATOM   536  N  NZ  . LYS A 1 73  ? 10.073 -11.206 7.955  1.00 104.34 ? 70  LYS A NZ  1 
ATOM   537  N  N   . ASP A 1 74  ? 13.653 -7.595  11.789 1.00 62.28  ? 71  ASP A N   1 
ATOM   538  C  CA  . ASP A 1 74  ? 15.004 -8.129  11.924 1.00 65.11  ? 71  ASP A CA  1 
ATOM   539  C  C   . ASP A 1 74  ? 15.182 -8.839  13.261 1.00 66.05  ? 71  ASP A C   1 
ATOM   540  O  O   . ASP A 1 74  ? 15.926 -9.826  13.345 1.00 64.54  ? 71  ASP A O   1 
ATOM   541  C  CB  . ASP A 1 74  ? 16.043 -7.015  11.763 1.00 64.63  ? 71  ASP A CB  1 
ATOM   542  C  CG  . ASP A 1 74  ? 16.044 -6.428  10.372 1.00 71.00  ? 71  ASP A CG  1 
ATOM   543  O  OD1 . ASP A 1 74  ? 15.778 -7.177  9.401  1.00 70.31  ? 71  ASP A OD1 1 
ATOM   544  O  OD2 . ASP A 1 74  ? 16.292 -5.211  10.249 1.00 72.39  ? 71  ASP A OD2 1 
ATOM   545  N  N   . ALA A 1 75  ? 14.480 -8.376  14.305 1.00 61.75  ? 72  ALA A N   1 
ATOM   546  C  CA  . ALA A 1 75  ? 14.525 -9.062  15.591 1.00 59.63  ? 72  ALA A CA  1 
ATOM   547  C  C   . ALA A 1 75  ? 13.744 -10.370 15.551 1.00 61.40  ? 72  ALA A C   1 
ATOM   548  O  O   . ALA A 1 75  ? 14.203 -11.387 16.087 1.00 55.31  ? 72  ALA A O   1 
ATOM   549  C  CB  . ALA A 1 75  ? 13.998 -8.147  16.699 1.00 53.72  ? 72  ALA A CB  1 
ATOM   550  N  N   . LEU A 1 76  ? 12.558 -10.370 14.931 1.00 57.07  ? 73  LEU A N   1 
ATOM   551  C  CA  . LEU A 1 76  ? 11.791 -11.609 14.882 1.00 55.71  ? 73  LEU A CA  1 
ATOM   552  C  C   . LEU A 1 76  ? 12.528 -12.660 14.065 1.00 58.66  ? 73  LEU A C   1 
ATOM   553  O  O   . LEU A 1 76  ? 12.576 -13.836 14.444 1.00 57.62  ? 73  LEU A O   1 
ATOM   554  C  CB  . LEU A 1 76  ? 10.395 -11.353 14.310 1.00 62.89  ? 73  LEU A CB  1 
ATOM   555  C  CG  . LEU A 1 76  ? 9.389  -10.526 15.131 1.00 61.72  ? 73  LEU A CG  1 
ATOM   556  C  CD1 . LEU A 1 76  ? 8.113  -10.407 14.376 1.00 53.93  ? 73  LEU A CD1 1 
ATOM   557  C  CD2 . LEU A 1 76  ? 9.108  -11.102 16.522 1.00 56.33  ? 73  LEU A CD2 1 
ATOM   558  N  N   . ASP A 1 77  ? 13.130 -12.246 12.949 1.00 62.65  ? 74  ASP A N   1 
ATOM   559  C  CA  . ASP A 1 77  ? 13.956 -13.154 12.162 1.00 60.25  ? 74  ASP A CA  1 
ATOM   560  C  C   . ASP A 1 77  ? 15.127 -13.691 12.974 1.00 59.51  ? 74  ASP A C   1 
ATOM   561  O  O   . ASP A 1 77  ? 15.573 -14.821 12.748 1.00 59.59  ? 74  ASP A O   1 
ATOM   562  C  CB  . ASP A 1 77  ? 14.449 -12.438 10.914 1.00 59.24  ? 74  ASP A CB  1 
ATOM   563  C  CG  . ASP A 1 77  ? 13.362 -12.266 9.902  1.00 68.89  ? 74  ASP A CG  1 
ATOM   564  O  OD1 . ASP A 1 77  ? 12.384 -13.045 9.951  1.00 76.45  ? 74  ASP A OD1 1 
ATOM   565  O  OD2 . ASP A 1 77  ? 13.457 -11.346 9.067  1.00 80.31  ? 74  ASP A OD2 1 
ATOM   566  N  N   . GLY A 1 78  ? 15.630 -12.907 13.927 1.00 56.45  ? 75  GLY A N   1 
ATOM   567  C  CA  . GLY A 1 78  ? 16.656 -13.424 14.816 1.00 54.57  ? 75  GLY A CA  1 
ATOM   568  C  C   . GLY A 1 78  ? 16.166 -14.617 15.610 1.00 58.90  ? 75  GLY A C   1 
ATOM   569  O  O   . GLY A 1 78  ? 16.841 -15.652 15.676 1.00 58.37  ? 75  GLY A O   1 
ATOM   570  N  N   . TYR A 1 79  ? 14.965 -14.496 16.205 1.00 55.38  ? 76  TYR A N   1 
ATOM   571  C  CA  . TYR A 1 79  ? 14.417 -15.581 17.015 1.00 53.61  ? 76  TYR A CA  1 
ATOM   572  C  C   . TYR A 1 79  ? 14.163 -16.816 16.165 1.00 57.65  ? 76  TYR A C   1 
ATOM   573  O  O   . TYR A 1 79  ? 14.528 -17.935 16.551 1.00 54.65  ? 76  TYR A O   1 
ATOM   574  C  CB  . TYR A 1 79  ? 13.130 -15.126 17.713 1.00 54.82  ? 76  TYR A CB  1 
ATOM   575  C  CG  . TYR A 1 79  ? 12.362 -16.208 18.485 1.00 56.32  ? 76  TYR A CG  1 
ATOM   576  C  CD1 . TYR A 1 79  ? 11.526 -17.127 17.826 1.00 54.30  ? 76  TYR A CD1 1 
ATOM   577  C  CD2 . TYR A 1 79  ? 12.440 -16.286 19.865 1.00 49.11  ? 76  TYR A CD2 1 
ATOM   578  C  CE1 . TYR A 1 79  ? 10.826 -18.096 18.521 1.00 50.49  ? 76  TYR A CE1 1 
ATOM   579  C  CE2 . TYR A 1 79  ? 11.738 -17.243 20.566 1.00 49.12  ? 76  TYR A CE2 1 
ATOM   580  C  CZ  . TYR A 1 79  ? 10.936 -18.139 19.901 1.00 52.99  ? 76  TYR A CZ  1 
ATOM   581  O  OH  . TYR A 1 79  ? 10.253 -19.084 20.634 1.00 52.06  ? 76  TYR A OH  1 
ATOM   582  N  N   . ASP A 1 80  ? 13.532 -16.628 14.998 1.00 56.36  ? 77  ASP A N   1 
ATOM   583  C  CA  . ASP A 1 80  ? 13.243 -17.761 14.126 1.00 55.93  ? 77  ASP A CA  1 
ATOM   584  C  C   . ASP A 1 80  ? 14.525 -18.441 13.653 1.00 58.59  ? 77  ASP A C   1 
ATOM   585  O  O   . ASP A 1 80  ? 14.520 -19.649 13.380 1.00 61.80  ? 77  ASP A O   1 
ATOM   586  C  CB  . ASP A 1 80  ? 12.411 -17.312 12.915 1.00 54.85  ? 77  ASP A CB  1 
ATOM   587  C  CG  . ASP A 1 80  ? 11.021 -16.793 13.293 1.00 61.49  ? 77  ASP A CG  1 
ATOM   588  O  OD1 . ASP A 1 80  ? 10.610 -16.954 14.466 1.00 55.52  ? 77  ASP A OD1 1 
ATOM   589  O  OD2 . ASP A 1 80  ? 10.333 -16.233 12.396 1.00 65.39  ? 77  ASP A OD2 1 
ATOM   590  N  N   . TYR A 1 81  ? 15.624 -17.685 13.531 1.00 57.29  ? 78  TYR A N   1 
ATOM   591  C  CA  . TYR A 1 81  ? 16.898 -18.281 13.136 1.00 60.57  ? 78  TYR A CA  1 
ATOM   592  C  C   . TYR A 1 81  ? 17.402 -19.239 14.204 1.00 63.69  ? 78  TYR A C   1 
ATOM   593  O  O   . TYR A 1 81  ? 17.856 -20.349 13.893 1.00 66.53  ? 78  TYR A O   1 
ATOM   594  C  CB  . TYR A 1 81  ? 17.944 -17.195 12.883 1.00 62.36  ? 78  TYR A CB  1 
ATOM   595  C  CG  . TYR A 1 81  ? 19.290 -17.726 12.450 1.00 59.47  ? 78  TYR A CG  1 
ATOM   596  C  CD1 . TYR A 1 81  ? 19.453 -18.290 11.191 1.00 68.30  ? 78  TYR A CD1 1 
ATOM   597  C  CD2 . TYR A 1 81  ? 20.394 -17.664 13.291 1.00 60.65  ? 78  TYR A CD2 1 
ATOM   598  C  CE1 . TYR A 1 81  ? 20.684 -18.777 10.762 1.00 70.93  ? 78  TYR A CE1 1 
ATOM   599  C  CE2 . TYR A 1 81  ? 21.638 -18.163 12.881 1.00 65.62  ? 78  TYR A CE2 1 
ATOM   600  C  CZ  . TYR A 1 81  ? 21.772 -18.713 11.607 1.00 71.71  ? 78  TYR A CZ  1 
ATOM   601  O  OH  . TYR A 1 81  ? 22.979 -19.212 11.163 1.00 73.79  ? 78  TYR A OH  1 
ATOM   602  N  N   . LEU A 1 82  ? 17.334 -18.818 15.471 1.00 57.78  ? 79  LEU A N   1 
ATOM   603  C  CA  . LEU A 1 82  ? 17.755 -19.689 16.558 1.00 61.99  ? 79  LEU A CA  1 
ATOM   604  C  C   . LEU A 1 82  ? 16.950 -20.981 16.557 1.00 61.79  ? 79  LEU A C   1 
ATOM   605  O  O   . LEU A 1 82  ? 17.510 -22.066 16.734 1.00 61.42  ? 79  LEU A O   1 
ATOM   606  C  CB  . LEU A 1 82  ? 17.622 -18.959 17.893 1.00 55.08  ? 79  LEU A CB  1 
ATOM   607  C  CG  . LEU A 1 82  ? 18.772 -18.005 18.183 1.00 53.44  ? 79  LEU A CG  1 
ATOM   608  C  CD1 . LEU A 1 82  ? 18.372 -16.990 19.232 1.00 53.09  ? 79  LEU A CD1 1 
ATOM   609  C  CD2 . LEU A 1 82  ? 20.003 -18.779 18.642 1.00 54.08  ? 79  LEU A CD2 1 
ATOM   610  N  N   . VAL A 1 83  ? 15.637 -20.885 16.337 1.00 59.53  ? 80  VAL A N   1 
ATOM   611  C  CA  . VAL A 1 83  ? 14.789 -22.074 16.340 1.00 66.32  ? 80  VAL A CA  1 
ATOM   612  C  C   . VAL A 1 83  ? 15.111 -22.970 15.144 1.00 69.19  ? 80  VAL A C   1 
ATOM   613  O  O   . VAL A 1 83  ? 15.151 -24.202 15.260 1.00 64.39  ? 80  VAL A O   1 
ATOM   614  C  CB  . VAL A 1 83  ? 13.304 -21.660 16.358 1.00 65.05  ? 80  VAL A CB  1 
ATOM   615  C  CG1 . VAL A 1 83  ? 12.404 -22.888 16.254 1.00 58.26  ? 80  VAL A CG1 1 
ATOM   616  C  CG2 . VAL A 1 83  ? 12.988 -20.863 17.619 1.00 60.52  ? 80  VAL A CG2 1 
ATOM   617  N  N   . GLU A 1 84  ? 15.332 -22.366 13.975 1.00 73.35  ? 81  GLU A N   1 
ATOM   618  C  CA  . GLU A 1 84  ? 15.768 -23.129 12.813 1.00 73.44  ? 81  GLU A CA  1 
ATOM   619  C  C   . GLU A 1 84  ? 17.040 -23.925 13.117 1.00 74.19  ? 81  GLU A C   1 
ATOM   620  O  O   . GLU A 1 84  ? 17.143 -25.103 12.755 1.00 75.52  ? 81  GLU A O   1 
ATOM   621  C  CB  . GLU A 1 84  ? 15.983 -22.177 11.639 1.00 74.83  ? 81  GLU A CB  1 
ATOM   622  C  CG  . GLU A 1 84  ? 16.395 -22.843 10.359 1.00 83.30  ? 81  GLU A CG  1 
ATOM   623  C  CD  . GLU A 1 84  ? 15.249 -22.963 9.375  1.00 103.61 ? 81  GLU A CD  1 
ATOM   624  O  OE1 . GLU A 1 84  ? 15.508 -23.102 8.148  1.00 109.47 ? 81  GLU A OE1 1 
ATOM   625  O  OE2 . GLU A 1 84  ? 14.083 -22.907 9.830  1.00 106.94 ? 81  GLU A OE2 1 
ATOM   626  N  N   . GLN A 1 85  ? 18.003 -23.309 13.811 1.00 68.07  ? 82  GLN A N   1 
ATOM   627  C  CA  . GLN A 1 85  ? 19.290 -23.924 14.132 1.00 67.87  ? 82  GLN A CA  1 
ATOM   628  C  C   . GLN A 1 85  ? 19.215 -24.983 15.232 1.00 68.09  ? 82  GLN A C   1 
ATOM   629  O  O   . GLN A 1 85  ? 20.218 -25.660 15.470 1.00 69.95  ? 82  GLN A O   1 
ATOM   630  C  CB  . GLN A 1 85  ? 20.286 -22.842 14.563 1.00 66.29  ? 82  GLN A CB  1 
ATOM   631  C  CG  . GLN A 1 85  ? 20.846 -22.021 13.426 1.00 66.09  ? 82  GLN A CG  1 
ATOM   632  C  CD  . GLN A 1 85  ? 21.476 -22.866 12.344 1.00 70.18  ? 82  GLN A CD  1 
ATOM   633  O  OE1 . GLN A 1 85  ? 21.197 -22.663 11.167 1.00 71.18  ? 82  GLN A OE1 1 
ATOM   634  N  NE2 . GLN A 1 85  ? 22.401 -23.765 12.729 1.00 79.92  ? 82  GLN A NE2 1 
ATOM   635  N  N   . GLY A 1 86  ? 18.091 -25.116 15.935 1.00 64.19  ? 83  GLY A N   1 
ATOM   636  C  CA  . GLY A 1 86  ? 17.917 -26.214 16.866 1.00 64.32  ? 83  GLY A CA  1 
ATOM   637  C  C   . GLY A 1 86  ? 17.673 -25.832 18.314 1.00 67.92  ? 83  GLY A C   1 
ATOM   638  O  O   . GLY A 1 86  ? 17.847 -26.672 19.201 1.00 72.05  ? 83  GLY A O   1 
ATOM   639  N  N   . TYR A 1 87  ? 17.239 -24.594 18.570 1.00 67.87  ? 84  TYR A N   1 
ATOM   640  C  CA  . TYR A 1 87  ? 17.162 -24.022 19.916 1.00 62.53  ? 84  TYR A CA  1 
ATOM   641  C  C   . TYR A 1 87  ? 15.717 -23.613 20.256 1.00 63.83  ? 84  TYR A C   1 
ATOM   642  O  O   . TYR A 1 87  ? 15.271 -22.527 19.870 1.00 65.89  ? 84  TYR A O   1 
ATOM   643  C  CB  . TYR A 1 87  ? 18.132 -22.844 20.025 1.00 58.40  ? 84  TYR A CB  1 
ATOM   644  C  CG  . TYR A 1 87  ? 19.574 -23.234 19.757 1.00 61.04  ? 84  TYR A CG  1 
ATOM   645  C  CD1 . TYR A 1 87  ? 20.362 -23.811 20.749 1.00 63.94  ? 84  TYR A CD1 1 
ATOM   646  C  CD2 . TYR A 1 87  ? 20.145 -23.042 18.513 1.00 64.11  ? 84  TYR A CD2 1 
ATOM   647  C  CE1 . TYR A 1 87  ? 21.688 -24.186 20.500 1.00 58.85  ? 84  TYR A CE1 1 
ATOM   648  C  CE2 . TYR A 1 87  ? 21.465 -23.416 18.258 1.00 65.89  ? 84  TYR A CE2 1 
ATOM   649  C  CZ  . TYR A 1 87  ? 22.228 -23.986 19.260 1.00 62.11  ? 84  TYR A CZ  1 
ATOM   650  O  OH  . TYR A 1 87  ? 23.530 -24.368 19.003 1.00 65.81  ? 84  TYR A OH  1 
ATOM   651  N  N   . ASP A 1 88  ? 15.001 -24.482 21.002 1.00 62.61  ? 85  ASP A N   1 
ATOM   652  C  CA  . ASP A 1 88  ? 13.633 -24.208 21.468 1.00 65.95  ? 85  ASP A CA  1 
ATOM   653  C  C   . ASP A 1 88  ? 13.572 -23.093 22.509 1.00 61.39  ? 85  ASP A C   1 
ATOM   654  O  O   . ASP A 1 88  ? 12.579 -22.357 22.586 1.00 58.71  ? 85  ASP A O   1 
ATOM   655  C  CB  . ASP A 1 88  ? 13.022 -25.439 22.136 1.00 63.88  ? 85  ASP A CB  1 
ATOM   656  C  CG  . ASP A 1 88  ? 13.056 -26.654 21.290 1.00 77.90  ? 85  ASP A CG  1 
ATOM   657  O  OD1 . ASP A 1 88  ? 12.528 -26.609 20.155 1.00 81.98  ? 85  ASP A OD1 1 
ATOM   658  O  OD2 . ASP A 1 88  ? 13.595 -27.672 21.785 1.00 87.01  ? 85  ASP A OD2 1 
ATOM   659  N  N   . GLU A 1 89  ? 14.562 -23.027 23.390 1.00 59.79  ? 86  GLU A N   1 
ATOM   660  C  CA  . GLU A 1 89  ? 14.432 -22.318 24.655 1.00 58.70  ? 86  GLU A CA  1 
ATOM   661  C  C   . GLU A 1 89  ? 15.335 -21.099 24.621 1.00 53.10  ? 86  GLU A C   1 
ATOM   662  O  O   . GLU A 1 89  ? 16.558 -21.228 24.680 1.00 54.77  ? 86  GLU A O   1 
ATOM   663  C  CB  . GLU A 1 89  ? 14.757 -23.252 25.821 1.00 59.58  ? 86  GLU A CB  1 
ATOM   664  C  CG  . GLU A 1 89  ? 14.184 -24.645 25.581 1.00 65.57  ? 86  GLU A CG  1 
ATOM   665  C  CD  . GLU A 1 89  ? 14.222 -25.576 26.785 1.00 70.71  ? 86  GLU A CD  1 
ATOM   666  O  OE1 . GLU A 1 89  ? 14.249 -25.096 27.937 1.00 66.33  ? 86  GLU A OE1 1 
ATOM   667  O  OE2 . GLU A 1 89  ? 14.215 -26.809 26.554 1.00 81.29  ? 86  GLU A OE2 1 
ATOM   668  N  N   . ILE A 1 90  ? 14.719 -19.919 24.559 1.00 52.54  ? 87  ILE A N   1 
ATOM   669  C  CA  . ILE A 1 90  ? 15.386 -18.680 24.195 1.00 51.05  ? 87  ILE A CA  1 
ATOM   670  C  C   . ILE A 1 90  ? 14.970 -17.586 25.163 1.00 51.21  ? 87  ILE A C   1 
ATOM   671  O  O   . ILE A 1 90  ? 13.775 -17.383 25.398 1.00 49.26  ? 87  ILE A O   1 
ATOM   672  C  CB  . ILE A 1 90  ? 15.040 -18.263 22.754 1.00 50.66  ? 87  ILE A CB  1 
ATOM   673  C  CG1 . ILE A 1 90  ? 15.549 -19.310 21.766 1.00 48.15  ? 87  ILE A CG1 1 
ATOM   674  C  CG2 . ILE A 1 90  ? 15.565 -16.847 22.456 1.00 45.82  ? 87  ILE A CG2 1 
ATOM   675  C  CD1 . ILE A 1 90  ? 14.792 -19.303 20.448 1.00 54.87  ? 87  ILE A CD1 1 
ATOM   676  N  N   . VAL A 1 91  ? 15.959 -16.893 25.728 1.00 46.94  ? 88  VAL A N   1 
ATOM   677  C  CA  . VAL A 1 91  ? 15.774 -15.624 26.410 1.00 43.50  ? 88  VAL A CA  1 
ATOM   678  C  C   . VAL A 1 91  ? 16.117 -14.520 25.419 1.00 46.12  ? 88  VAL A C   1 
ATOM   679  O  O   . VAL A 1 91  ? 16.994 -14.681 24.564 1.00 46.49  ? 88  VAL A O   1 
ATOM   680  C  CB  . VAL A 1 91  ? 16.667 -15.566 27.665 1.00 45.67  ? 88  VAL A CB  1 
ATOM   681  C  CG1 . VAL A 1 91  ? 16.776 -14.145 28.222 1.00 41.18  ? 88  VAL A CG1 1 
ATOM   682  C  CG2 . VAL A 1 91  ? 16.158 -16.528 28.703 1.00 45.77  ? 88  VAL A CG2 1 
ATOM   683  N  N   . VAL A 1 92  ? 15.404 -13.402 25.492 1.00 46.88  ? 89  VAL A N   1 
ATOM   684  C  CA  . VAL A 1 92  ? 15.692 -12.228 24.668 1.00 47.83  ? 89  VAL A CA  1 
ATOM   685  C  C   . VAL A 1 92  ? 16.203 -11.110 25.578 1.00 41.89  ? 89  VAL A C   1 
ATOM   686  O  O   . VAL A 1 92  ? 15.596 -10.809 26.609 1.00 44.75  ? 89  VAL A O   1 
ATOM   687  C  CB  . VAL A 1 92  ? 14.446 -11.797 23.870 1.00 43.53  ? 89  VAL A CB  1 
ATOM   688  C  CG1 . VAL A 1 92  ? 13.289 -11.460 24.812 1.00 43.03  ? 89  VAL A CG1 1 
ATOM   689  C  CG2 . VAL A 1 92  ? 14.755 -10.638 22.957 1.00 43.60  ? 89  VAL A CG2 1 
ATOM   690  N  N   . ALA A 1 93  ? 17.321 -10.507 25.203 1.00 39.78  ? 90  ALA A N   1 
ATOM   691  C  CA  . ALA A 1 93  ? 17.960 -9.438  25.970 1.00 49.96  ? 90  ALA A CA  1 
ATOM   692  C  C   . ALA A 1 93  ? 18.251 -8.264  25.037 1.00 51.31  ? 90  ALA A C   1 
ATOM   693  O  O   . ALA A 1 93  ? 18.873 -8.455  23.990 1.00 49.50  ? 90  ALA A O   1 
ATOM   694  C  CB  . ALA A 1 93  ? 19.267 -9.933  26.607 1.00 39.84  ? 90  ALA A CB  1 
ATOM   695  N  N   . GLY A 1 94  ? 17.823 -7.062  25.404 1.00 51.54  ? 91  GLY A N   1 
ATOM   696  C  CA  . GLY A 1 94  ? 17.821 -5.937  24.474 1.00 48.64  ? 91  GLY A CA  1 
ATOM   697  C  C   . GLY A 1 94  ? 18.348 -4.668  25.111 1.00 52.23  ? 91  GLY A C   1 
ATOM   698  O  O   . GLY A 1 94  ? 18.056 -4.379  26.270 1.00 48.06  ? 91  GLY A O   1 
ATOM   699  N  N   . LEU A 1 95  ? 19.142 -3.929  24.335 1.00 54.38  ? 92  LEU A N   1 
ATOM   700  C  CA  . LEU A 1 95  ? 19.849 -2.742  24.799 1.00 54.60  ? 92  LEU A CA  1 
ATOM   701  C  C   . LEU A 1 95  ? 19.203 -1.489  24.212 1.00 56.82  ? 92  LEU A C   1 
ATOM   702  O  O   . LEU A 1 95  ? 19.075 -1.360  22.984 1.00 51.91  ? 92  LEU A O   1 
ATOM   703  C  CB  . LEU A 1 95  ? 21.333 -2.802  24.411 1.00 49.54  ? 92  LEU A CB  1 
ATOM   704  C  CG  . LEU A 1 95  ? 22.188 -1.541  24.664 1.00 55.06  ? 92  LEU A CG  1 
ATOM   705  C  CD1 . LEU A 1 95  ? 22.180 -1.154  26.142 1.00 53.40  ? 92  LEU A CD1 1 
ATOM   706  C  CD2 . LEU A 1 95  ? 23.628 -1.704  24.201 1.00 53.29  ? 92  LEU A CD2 1 
ATOM   707  N  N   . SER A 1 96  ? 18.814 -0.563  25.094 1.00 51.26  ? 93  SER A N   1 
ATOM   708  C  CA  . SER A 1 96  ? 18.232 0.716   24.699 1.00 55.24  ? 93  SER A CA  1 
ATOM   709  C  C   . SER A 1 96  ? 16.992 0.426   23.854 1.00 58.51  ? 93  SER A C   1 
ATOM   710  O  O   . SER A 1 96  ? 16.077 -0.257  24.346 1.00 56.93  ? 93  SER A O   1 
ATOM   711  C  CB  . SER A 1 96  ? 19.339 1.536   24.037 1.00 58.05  ? 93  SER A CB  1 
ATOM   712  O  OG  . SER A 1 96  ? 18.924 2.871   23.779 1.00 62.35  ? 93  SER A OG  1 
ATOM   713  N  N   . LEU A 1 97  ? 16.904 0.907   22.614 1.00 59.24  ? 94  LEU A N   1 
ATOM   714  C  CA  . LEU A 1 97  ? 15.794 0.543   21.734 1.00 60.18  ? 94  LEU A CA  1 
ATOM   715  C  C   . LEU A 1 97  ? 15.588 -0.975  21.662 1.00 57.66  ? 94  LEU A C   1 
ATOM   716  O  O   . LEU A 1 97  ? 14.448 -1.457  21.699 1.00 56.71  ? 94  LEU A O   1 
ATOM   717  C  CB  . LEU A 1 97  ? 16.036 1.125   20.337 1.00 54.13  ? 94  LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 97  ? 15.029 0.648   19.276 1.00 64.38  ? 94  LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 97  ? 13.671 1.316   19.440 1.00 57.83  ? 94  LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 97  ? 15.555 0.900   17.872 1.00 67.68  ? 94  LEU A CD2 1 
ATOM   721  N  N   . GLY A 1 98  ? 16.675 -1.749  21.567 1.00 53.38  ? 95  GLY A N   1 
ATOM   722  C  CA  . GLY A 1 98  ? 16.528 -3.197  21.555 1.00 50.70  ? 95  GLY A CA  1 
ATOM   723  C  C   . GLY A 1 98  ? 15.780 -3.732  22.764 1.00 54.85  ? 95  GLY A C   1 
ATOM   724  O  O   . GLY A 1 98  ? 15.105 -4.763  22.684 1.00 49.65  ? 95  GLY A O   1 
ATOM   725  N  N   . GLY A 1 99  ? 15.892 -3.055  23.906 1.00 55.14  ? 96  GLY A N   1 
ATOM   726  C  CA  . GLY A 1 99  ? 15.121 -3.469  25.062 1.00 48.03  ? 96  GLY A CA  1 
ATOM   727  C  C   . GLY A 1 99  ? 13.637 -3.270  24.866 1.00 49.69  ? 96  GLY A C   1 
ATOM   728  O  O   . GLY A 1 99  ? 12.834 -4.067  25.353 1.00 50.80  ? 96  GLY A O   1 
ATOM   729  N  N   . ASP A 1 100 ? 13.244 -2.206  24.160 1.00 54.80  ? 97  ASP A N   1 
ATOM   730  C  CA  . ASP A 1 100 ? 11.839 -2.074  23.785 1.00 58.78  ? 97  ASP A CA  1 
ATOM   731  C  C   . ASP A 1 100 ? 11.401 -3.210  22.865 1.00 58.40  ? 97  ASP A C   1 
ATOM   732  O  O   . ASP A 1 100 ? 10.297 -3.754  23.028 1.00 57.96  ? 97  ASP A O   1 
ATOM   733  C  CB  . ASP A 1 100 ? 11.574 -0.714  23.127 1.00 55.21  ? 97  ASP A CB  1 
ATOM   734  C  CG  . ASP A 1 100 ? 11.423 0.402   24.145 1.00 55.85  ? 97  ASP A CG  1 
ATOM   735  O  OD1 . ASP A 1 100 ? 10.362 1.031   24.172 1.00 64.44  ? 97  ASP A OD1 1 
ATOM   736  O  OD2 . ASP A 1 100 ? 12.349 0.634   24.939 1.00 62.93  ? 97  ASP A OD2 1 
ATOM   737  N  N   . PHE A 1 101 ? 12.249 -3.577  21.887 1.00 53.25  ? 98  PHE A N   1 
ATOM   738  C  CA  . PHE A 1 101 ? 11.916 -4.670  20.973 1.00 54.50  ? 98  PHE A CA  1 
ATOM   739  C  C   . PHE A 1 101 ? 11.798 -6.004  21.708 1.00 57.17  ? 98  PHE A C   1 
ATOM   740  O  O   . PHE A 1 101 ? 10.958 -6.847  21.356 1.00 52.90  ? 98  PHE A O   1 
ATOM   741  C  CB  . PHE A 1 101 ? 12.972 -4.769  19.878 1.00 54.92  ? 98  PHE A CB  1 
ATOM   742  C  CG  . PHE A 1 101 ? 12.837 -3.729  18.808 1.00 61.24  ? 98  PHE A CG  1 
ATOM   743  C  CD1 . PHE A 1 101 ? 11.666 -3.005  18.666 1.00 63.50  ? 98  PHE A CD1 1 
ATOM   744  C  CD2 . PHE A 1 101 ? 13.872 -3.491  17.927 1.00 62.14  ? 98  PHE A CD2 1 
ATOM   745  C  CE1 . PHE A 1 101 ? 11.543 -2.049  17.662 1.00 67.22  ? 98  PHE A CE1 1 
ATOM   746  C  CE2 . PHE A 1 101 ? 13.758 -2.539  16.923 1.00 61.69  ? 98  PHE A CE2 1 
ATOM   747  C  CZ  . PHE A 1 101 ? 12.598 -1.817  16.792 1.00 67.69  ? 98  PHE A CZ  1 
ATOM   748  N  N   . ALA A 1 102 ? 12.641 -6.218  22.724 1.00 52.22  ? 99  ALA A N   1 
ATOM   749  C  CA  . ALA A 1 102 ? 12.579 -7.456  23.487 1.00 51.00  ? 99  ALA A CA  1 
ATOM   750  C  C   . ALA A 1 102 ? 11.221 -7.607  24.163 1.00 50.68  ? 99  ALA A C   1 
ATOM   751  O  O   . ALA A 1 102 ? 10.621 -8.686  24.128 1.00 45.26  ? 99  ALA A O   1 
ATOM   752  C  CB  . ALA A 1 102 ? 13.720 -7.497  24.507 1.00 47.05  ? 99  ALA A CB  1 
ATOM   753  N  N   . LEU A 1 103 ? 10.715 -6.527  24.767 1.00 52.68  ? 100 LEU A N   1 
ATOM   754  C  CA  . LEU A 1 103 ? 9.384  -6.555  25.369 1.00 54.43  ? 100 LEU A CA  1 
ATOM   755  C  C   . LEU A 1 103 ? 8.335  -6.968  24.346 1.00 53.38  ? 100 LEU A C   1 
ATOM   756  O  O   . LEU A 1 103 ? 7.517  -7.862  24.604 1.00 51.47  ? 100 LEU A O   1 
ATOM   757  C  CB  . LEU A 1 103 ? 9.032  -5.180  25.958 1.00 53.67  ? 100 LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 103 ? 9.800  -4.698  27.195 1.00 58.18  ? 100 LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 103 ? 9.639  -3.170  27.385 1.00 51.10  ? 100 LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 103 ? 9.374  -5.462  28.452 1.00 45.22  ? 100 LEU A CD2 1 
ATOM   761  N  N   . LYS A 1 104 ? 8.346  -6.310  23.179 1.00 52.94  ? 101 LYS A N   1 
ATOM   762  C  CA  . LYS A 1 104 ? 7.358  -6.565  22.139 1.00 49.89  ? 101 LYS A CA  1 
ATOM   763  C  C   . LYS A 1 104 ? 7.519  -7.962  21.560 1.00 51.89  ? 101 LYS A C   1 
ATOM   764  O  O   . LYS A 1 104 ? 6.524  -8.626  21.239 1.00 54.19  ? 101 LYS A O   1 
ATOM   765  C  CB  . LYS A 1 104 ? 7.485  -5.523  21.029 1.00 53.94  ? 101 LYS A CB  1 
ATOM   766  C  CG  . LYS A 1 104 ? 6.319  -5.560  20.051 1.00 60.41  ? 101 LYS A CG  1 
ATOM   767  C  CD  . LYS A 1 104 ? 6.480  -4.579  18.895 1.00 58.20  ? 101 LYS A CD  1 
ATOM   768  C  CE  . LYS A 1 104 ? 5.317  -4.687  17.899 1.00 66.58  ? 101 LYS A CE  1 
ATOM   769  N  NZ  . LYS A 1 104 ? 4.052  -3.923  18.248 1.00 74.06  ? 101 LYS A NZ  1 
ATOM   770  N  N   . LEU A 1 105 ? 8.761  -8.427  21.431 1.00 47.92  ? 102 LEU A N   1 
ATOM   771  C  CA  . LEU A 1 105 ? 9.005  -9.752  20.880 1.00 50.68  ? 102 LEU A CA  1 
ATOM   772  C  C   . LEU A 1 105 ? 8.400  -10.841 21.760 1.00 54.18  ? 102 LEU A C   1 
ATOM   773  O  O   . LEU A 1 105 ? 7.896  -11.857 21.258 1.00 54.10  ? 102 LEU A O   1 
ATOM   774  C  CB  . LEU A 1 105 ? 10.505 -9.972  20.725 1.00 53.04  ? 102 LEU A CB  1 
ATOM   775  C  CG  . LEU A 1 105 ? 10.887 -11.267 20.015 1.00 57.15  ? 102 LEU A CG  1 
ATOM   776  C  CD1 . LEU A 1 105 ? 12.032 -11.020 19.029 1.00 52.53  ? 102 LEU A CD1 1 
ATOM   777  C  CD2 . LEU A 1 105 ? 11.237 -12.347 21.046 1.00 54.48  ? 102 LEU A CD2 1 
ATOM   778  N  N   . SER A 1 106 ? 8.459  -10.657 23.079 1.00 51.20  ? 103 SER A N   1 
ATOM   779  C  CA  . SER A 1 106 ? 7.889  -11.629 24.003 1.00 53.12  ? 103 SER A CA  1 
ATOM   780  C  C   . SER A 1 106 ? 6.384  -11.813 23.787 1.00 52.82  ? 103 SER A C   1 
ATOM   781  O  O   . SER A 1 106 ? 5.839  -12.873 24.133 1.00 44.45  ? 103 SER A O   1 
ATOM   782  C  CB  . SER A 1 106 ? 8.174  -11.193 25.446 1.00 46.80  ? 103 SER A CB  1 
ATOM   783  O  OG  . SER A 1 106 ? 7.135  -10.334 25.908 1.00 52.32  ? 103 SER A OG  1 
ATOM   784  N  N   . LEU A 1 107 ? 5.704  -10.805 23.229 1.00 51.80  ? 104 LEU A N   1 
ATOM   785  C  CA  . LEU A 1 107 ? 4.292  -10.915 22.891 1.00 53.24  ? 104 LEU A CA  1 
ATOM   786  C  C   . LEU A 1 107 ? 4.046  -11.657 21.576 1.00 52.41  ? 104 LEU A C   1 
ATOM   787  O  O   . LEU A 1 107 ? 2.890  -11.961 21.261 1.00 48.71  ? 104 LEU A O   1 
ATOM   788  C  CB  . LEU A 1 107 ? 3.674  -9.519  22.811 1.00 51.98  ? 104 LEU A CB  1 
ATOM   789  C  CG  . LEU A 1 107 ? 3.853  -8.535  23.968 1.00 52.98  ? 104 LEU A CG  1 
ATOM   790  C  CD1 . LEU A 1 107 ? 3.218  -7.196  23.607 1.00 52.94  ? 104 LEU A CD1 1 
ATOM   791  C  CD2 . LEU A 1 107 ? 3.250  -9.064  25.259 1.00 57.02  ? 104 LEU A CD2 1 
ATOM   792  N  N   . ASN A 1 108 ? 5.104  -11.948 20.804 1.00 55.00  ? 105 ASN A N   1 
ATOM   793  C  CA  . ASN A 1 108 ? 4.983  -12.572 19.492 1.00 56.72  ? 105 ASN A CA  1 
ATOM   794  C  C   . ASN A 1 108 ? 5.672  -13.924 19.371 1.00 57.11  ? 105 ASN A C   1 
ATOM   795  O  O   . ASN A 1 108 ? 5.386  -14.649 18.408 1.00 56.14  ? 105 ASN A O   1 
ATOM   796  C  CB  . ASN A 1 108 ? 5.543  -11.643 18.397 1.00 53.92  ? 105 ASN A CB  1 
ATOM   797  C  CG  . ASN A 1 108 ? 4.681  -10.400 18.194 1.00 57.55  ? 105 ASN A CG  1 
ATOM   798  O  OD1 . ASN A 1 108 ? 3.765  -10.384 17.357 1.00 54.17  ? 105 ASN A OD1 1 
ATOM   799  N  ND2 . ASN A 1 108 ? 4.970  -9.354  18.968 1.00 53.25  ? 105 ASN A ND2 1 
ATOM   800  N  N   . ARG A 1 109 ? 6.561  -14.282 20.303 1.00 49.67  ? 106 ARG A N   1 
ATOM   801  C  CA  . ARG A 1 109 ? 7.204  -15.587 20.319 1.00 51.54  ? 106 ARG A CA  1 
ATOM   802  C  C   . ARG A 1 109 ? 7.292  -16.085 21.756 1.00 54.04  ? 106 ARG A C   1 
ATOM   803  O  O   . ARG A 1 109 ? 7.281  -15.295 22.702 1.00 56.64  ? 106 ARG A O   1 
ATOM   804  C  CB  . ARG A 1 109 ? 8.613  -15.525 19.721 1.00 54.89  ? 106 ARG A CB  1 
ATOM   805  C  CG  . ARG A 1 109 ? 8.679  -14.939 18.359 1.00 50.43  ? 106 ARG A CG  1 
ATOM   806  C  CD  . ARG A 1 109 ? 8.068  -15.906 17.379 1.00 56.30  ? 106 ARG A CD  1 
ATOM   807  N  NE  . ARG A 1 109 ? 8.480  -15.606 16.016 1.00 56.56  ? 106 ARG A NE  1 
ATOM   808  C  CZ  . ARG A 1 109 ? 7.753  -14.910 15.156 1.00 61.36  ? 106 ARG A CZ  1 
ATOM   809  N  NH1 . ARG A 1 109 ? 6.543  -14.456 15.479 1.00 59.50  ? 106 ARG A NH1 1 
ATOM   810  N  NH2 . ARG A 1 109 ? 8.243  -14.673 13.941 1.00 55.37  ? 106 ARG A NH2 1 
ATOM   811  N  N   . ASP A 1 110 ? 7.399  -17.409 21.910 1.00 52.89  ? 107 ASP A N   1 
ATOM   812  C  CA  . ASP A 1 110 ? 7.597  -18.043 23.214 1.00 49.35  ? 107 ASP A CA  1 
ATOM   813  C  C   . ASP A 1 110 ? 9.036  -17.818 23.698 1.00 51.33  ? 107 ASP A C   1 
ATOM   814  O  O   . ASP A 1 110 ? 9.985  -18.382 23.135 1.00 49.03  ? 107 ASP A O   1 
ATOM   815  C  CB  . ASP A 1 110 ? 7.307  -19.535 23.098 1.00 47.22  ? 107 ASP A CB  1 
ATOM   816  C  CG  . ASP A 1 110 ? 5.849  -19.853 22.699 1.00 58.81  ? 107 ASP A CG  1 
ATOM   817  O  OD1 . ASP A 1 110 ? 4.877  -19.181 23.132 1.00 58.51  ? 107 ASP A OD1 1 
ATOM   818  O  OD2 . ASP A 1 110 ? 5.668  -20.829 21.940 1.00 66.24  ? 107 ASP A OD2 1 
ATOM   819  N  N   . VAL A 1 111 ? 9.219  -17.014 24.755 1.00 48.52  ? 108 VAL A N   1 
ATOM   820  C  CA  . VAL A 1 111 ? 10.537 -16.850 25.366 1.00 48.18  ? 108 VAL A CA  1 
ATOM   821  C  C   . VAL A 1 111 ? 10.513 -17.373 26.799 1.00 49.84  ? 108 VAL A C   1 
ATOM   822  O  O   . VAL A 1 111 ? 9.469  -17.433 27.457 1.00 48.52  ? 108 VAL A O   1 
ATOM   823  C  CB  . VAL A 1 111 ? 11.042 -15.387 25.347 1.00 48.25  ? 108 VAL A CB  1 
ATOM   824  C  CG1 . VAL A 1 111 ? 11.140 -14.859 23.907 1.00 44.93  ? 108 VAL A CG1 1 
ATOM   825  C  CG2 . VAL A 1 111 ? 10.176 -14.486 26.247 1.00 39.26  ? 108 VAL A CG2 1 
ATOM   826  N  N   . LYS A 1 112 ? 11.691 -17.757 27.285 1.00 51.06  ? 109 LYS A N   1 
ATOM   827  C  CA  . LYS A 1 112 ? 11.838 -18.168 28.673 1.00 47.00  ? 109 LYS A CA  1 
ATOM   828  C  C   . LYS A 1 112 ? 11.936 -16.983 29.617 1.00 47.22  ? 109 LYS A C   1 
ATOM   829  O  O   . LYS A 1 112 ? 11.666 -17.149 30.813 1.00 48.08  ? 109 LYS A O   1 
ATOM   830  C  CB  . LYS A 1 112 ? 13.099 -19.013 28.849 1.00 52.34  ? 109 LYS A CB  1 
ATOM   831  C  CG  . LYS A 1 112 ? 13.115 -20.291 28.088 1.00 56.02  ? 109 LYS A CG  1 
ATOM   832  C  CD  . LYS A 1 112 ? 11.991 -21.174 28.549 1.00 64.83  ? 109 LYS A CD  1 
ATOM   833  C  CE  . LYS A 1 112 ? 12.402 -21.945 29.781 1.00 66.41  ? 109 LYS A CE  1 
ATOM   834  N  NZ  . LYS A 1 112 ? 11.700 -23.246 29.834 1.00 74.55  ? 109 LYS A NZ  1 
ATOM   835  N  N   . GLY A 1 113 ? 12.370 -15.821 29.115 1.00 41.80  ? 110 GLY A N   1 
ATOM   836  C  CA  . GLY A 1 113 ? 12.591 -14.639 29.948 1.00 40.14  ? 110 GLY A CA  1 
ATOM   837  C  C   . GLY A 1 113 ? 13.016 -13.447 29.096 1.00 43.55  ? 110 GLY A C   1 
ATOM   838  O  O   . GLY A 1 113 ? 13.449 -13.596 27.946 1.00 42.19  ? 110 GLY A O   1 
ATOM   839  N  N   . ILE A 1 114 ? 12.897 -12.253 29.702 1.00 41.33  ? 111 ILE A N   1 
ATOM   840  C  CA  . ILE A 1 114 ? 13.212 -10.962 29.087 1.00 41.91  ? 111 ILE A CA  1 
ATOM   841  C  C   . ILE A 1 114 ? 14.259 -10.223 29.916 1.00 44.53  ? 111 ILE A C   1 
ATOM   842  O  O   . ILE A 1 114 ? 14.218 -10.239 31.154 1.00 43.78  ? 111 ILE A O   1 
ATOM   843  C  CB  . ILE A 1 114 ? 11.953 -10.077 28.969 1.00 44.29  ? 111 ILE A CB  1 
ATOM   844  C  CG1 . ILE A 1 114 ? 10.842 -10.795 28.217 1.00 46.33  ? 111 ILE A CG1 1 
ATOM   845  C  CG2 . ILE A 1 114 ? 12.284 -8.754  28.328 1.00 43.82  ? 111 ILE A CG2 1 
ATOM   846  C  CD1 . ILE A 1 114 ? 9.476  -10.506 28.781 1.00 47.55  ? 111 ILE A CD1 1 
ATOM   847  N  N   . VAL A 1 115 ? 15.175 -9.539  29.233 1.00 43.69  ? 112 VAL A N   1 
ATOM   848  C  CA  . VAL A 1 115 ? 16.117 -8.612  29.869 1.00 49.88  ? 112 VAL A CA  1 
ATOM   849  C  C   . VAL A 1 115 ? 16.125 -7.300  29.089 1.00 50.15  ? 112 VAL A C   1 
ATOM   850  O  O   . VAL A 1 115 ? 16.592 -7.261  27.936 1.00 47.42  ? 112 VAL A O   1 
ATOM   851  C  CB  . VAL A 1 115 ? 17.536 -9.174  29.940 1.00 45.24  ? 112 VAL A CB  1 
ATOM   852  C  CG1 . VAL A 1 115 ? 18.399 -8.207  30.738 1.00 44.30  ? 112 VAL A CG1 1 
ATOM   853  C  CG2 . VAL A 1 115 ? 17.525 -10.568 30.535 1.00 40.52  ? 112 VAL A CG2 1 
ATOM   854  N  N   . THR A 1 116 ? 15.640 -6.223  29.714 1.00 46.26  ? 113 THR A N   1 
ATOM   855  C  CA  . THR A 1 116 ? 15.730 -4.896  29.119 1.00 45.37  ? 113 THR A CA  1 
ATOM   856  C  C   . THR A 1 116 ? 16.855 -4.127  29.798 1.00 48.57  ? 113 THR A C   1 
ATOM   857  O  O   . THR A 1 116 ? 17.005 -4.167  31.021 1.00 51.76  ? 113 THR A O   1 
ATOM   858  C  CB  . THR A 1 116 ? 14.398 -4.137  29.219 1.00 44.89  ? 113 THR A CB  1 
ATOM   859  O  OG1 . THR A 1 116 ? 14.171 -3.683  30.559 1.00 49.54  ? 113 THR A OG1 1 
ATOM   860  C  CG2 . THR A 1 116 ? 13.236 -5.034  28.805 1.00 47.51  ? 113 THR A CG2 1 
ATOM   861  N  N   . MET A 1 117 ? 17.663 -3.449  28.994 1.00 54.51  ? 114 MET A N   1 
ATOM   862  C  CA  . MET A 1 117 ? 18.815 -2.681  29.465 1.00 54.50  ? 114 MET A CA  1 
ATOM   863  C  C   . MET A 1 117 ? 18.693 -1.233  28.986 1.00 52.00  ? 114 MET A C   1 
ATOM   864  O  O   . MET A 1 117 ? 18.866 -0.946  27.796 1.00 50.87  ? 114 MET A O   1 
ATOM   865  C  CB  . MET A 1 117 ? 20.115 -3.307  28.961 1.00 51.26  ? 114 MET A CB  1 
ATOM   866  C  CG  . MET A 1 117 ? 20.666 -4.404  29.832 1.00 52.07  ? 114 MET A CG  1 
ATOM   867  S  SD  . MET A 1 117 ? 21.892 -5.458  29.032 1.00 55.48  ? 114 MET A SD  1 
ATOM   868  C  CE  . MET A 1 117 ? 21.205 -5.766  27.412 1.00 51.92  ? 114 MET A CE  1 
ATOM   869  N  N   . CYS A 1 118 ? 18.437 -0.327  29.917 1.00 51.33  ? 115 CYS A N   1 
ATOM   870  C  CA  . CYS A 1 118 ? 18.276 1.089   29.625 1.00 54.68  ? 115 CYS A CA  1 
ATOM   871  C  C   . CYS A 1 118 ? 17.269 1.313   28.496 1.00 60.31  ? 115 CYS A C   1 
ATOM   872  O  O   . CYS A 1 118 ? 17.511 2.079   27.559 1.00 65.22  ? 115 CYS A O   1 
ATOM   873  C  CB  . CYS A 1 118 ? 19.623 1.730   29.298 1.00 60.96  ? 115 CYS A CB  1 
ATOM   874  S  SG  . CYS A 1 118 ? 20.901 1.501   30.563 1.00 62.62  ? 115 CYS A SG  1 
ATOM   875  N  N   . ALA A 1 119 ? 16.106 0.646   28.603 1.00 55.02  ? 116 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 119 ? 15.097 0.769   27.561 1.00 57.17  ? 116 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 119 ? 14.184 1.942   27.870 1.00 62.02  ? 116 ALA A C   1 
ATOM   878  O  O   . ALA A 1 119 ? 13.671 2.033   28.989 1.00 66.22  ? 116 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 119 ? 14.264 -0.506  27.448 1.00 56.16  ? 116 ALA A CB  1 
ATOM   880  N  N   . PRO A 1 120 ? 13.952 2.840   26.916 1.00 67.32  ? 117 PRO A N   1 
ATOM   881  C  CA  . PRO A 1 120 ? 13.097 4.009   27.170 1.00 67.24  ? 117 PRO A CA  1 
ATOM   882  C  C   . PRO A 1 120 ? 11.602 3.707   27.109 1.00 65.18  ? 117 PRO A C   1 
ATOM   883  O  O   . PRO A 1 120 ? 11.153 2.802   26.404 1.00 65.36  ? 117 PRO A O   1 
ATOM   884  C  CB  . PRO A 1 120 ? 13.487 4.965   26.037 1.00 70.81  ? 117 PRO A CB  1 
ATOM   885  C  CG  . PRO A 1 120 ? 13.930 4.051   24.933 1.00 66.54  ? 117 PRO A CG  1 
ATOM   886  C  CD  . PRO A 1 120 ? 14.669 2.947   25.631 1.00 59.52  ? 117 PRO A CD  1 
ATOM   887  N  N   . MET A 1 121 ? 10.831 4.520   27.842 1.00 62.91  ? 118 MET A N   1 
ATOM   888  C  CA  . MET A 1 121 ? 9.371  4.466   27.854 1.00 71.90  ? 118 MET A CA  1 
ATOM   889  C  C   . MET A 1 121 ? 8.844  5.844   27.474 1.00 77.85  ? 118 MET A C   1 
ATOM   890  O  O   . MET A 1 121 ? 8.890  6.780   28.284 1.00 83.30  ? 118 MET A O   1 
ATOM   891  C  CB  . MET A 1 121 ? 8.826  4.063   29.222 1.00 63.20  ? 118 MET A CB  1 
ATOM   892  C  CG  . MET A 1 121 ? 8.850  2.587   29.500 1.00 72.54  ? 118 MET A CG  1 
ATOM   893  S  SD  . MET A 1 121 ? 7.718  1.619   28.480 1.00 70.54  ? 118 MET A SD  1 
ATOM   894  C  CE  . MET A 1 121 ? 8.949  0.581   27.646 1.00 56.32  ? 118 MET A CE  1 
ATOM   895  N  N   . GLY A 1 122 ? 8.317  5.961   26.259 1.00 81.64  ? 119 GLY A N   1 
ATOM   896  C  CA  . GLY A 1 122 ? 7.891  7.280   25.781 1.00 93.95  ? 119 GLY A CA  1 
ATOM   897  C  C   . GLY A 1 122 ? 8.674  7.652   24.534 1.00 104.58 ? 119 GLY A C   1 
ATOM   898  O  O   . GLY A 1 122 ? 9.895  7.521   24.466 1.00 104.83 ? 119 GLY A O   1 
ATOM   899  N  N   . GLY A 1 123 ? 7.949  8.133   23.529 1.00 124.43 ? 120 GLY A N   1 
ATOM   900  C  CA  . GLY A 1 123 ? 8.562  8.498   22.266 1.00 128.91 ? 120 GLY A CA  1 
ATOM   901  C  C   . GLY A 1 123 ? 9.134  9.900   22.215 1.00 142.45 ? 120 GLY A C   1 
ATOM   902  O  O   . GLY A 1 123 ? 9.165  10.505  21.140 1.00 150.70 ? 120 GLY A O   1 
ATOM   903  N  N   . LYS A 1 124 ? 9.590  10.428  23.356 1.00 138.83 ? 121 LYS A N   1 
ATOM   904  C  CA  . LYS A 1 124 ? 10.274 11.717  23.380 1.00 148.43 ? 121 LYS A CA  1 
ATOM   905  C  C   . LYS A 1 124 ? 11.614 11.627  22.653 1.00 160.82 ? 121 LYS A C   1 
ATOM   906  O  O   . LYS A 1 124 ? 12.622 11.209  23.238 1.00 151.00 ? 121 LYS A O   1 
ATOM   907  C  CB  . LYS A 1 124 ? 10.490 12.196  24.816 1.00 138.72 ? 121 LYS A CB  1 
ATOM   908  C  CG  . LYS A 1 124 ? 11.351 13.447  24.896 1.00 148.03 ? 121 LYS A CG  1 
ATOM   909  C  CD  . LYS A 1 124 ? 11.910 13.668  26.284 1.00 143.36 ? 121 LYS A CD  1 
ATOM   910  C  CE  . LYS A 1 124 ? 12.818 14.885  26.292 1.00 146.98 ? 121 LYS A CE  1 
ATOM   911  N  NZ  . LYS A 1 124 ? 13.387 15.145  27.641 1.00 149.63 ? 121 LYS A NZ  1 
ATOM   912  N  N   . THR A 1 125 ? 11.634 12.022  21.378 1.00 176.52 ? 122 THR A N   1 
ATOM   913  C  CA  . THR A 1 125 ? 12.826 11.944  20.541 1.00 176.22 ? 122 THR A CA  1 
ATOM   914  C  C   . THR A 1 125 ? 13.584 13.261  20.460 1.00 179.89 ? 122 THR A C   1 
ATOM   915  O  O   . THR A 1 125 ? 14.634 13.316  19.812 1.00 179.68 ? 122 THR A O   1 
ATOM   916  C  CB  . THR A 1 125 ? 12.461 11.489  19.119 1.00 173.25 ? 122 THR A CB  1 
ATOM   917  O  OG1 . THR A 1 125 ? 11.360 12.269  18.630 1.00 180.04 ? 122 THR A OG1 1 
ATOM   918  C  CG2 . THR A 1 125 ? 12.094 10.006  19.092 1.00 165.08 ? 122 THR A CG2 1 
ATOM   919  N  N   . GLU A 1 126 ? 13.087 14.316  21.095 1.00 180.80 ? 123 GLU A N   1 
ATOM   920  C  CA  . GLU A 1 126 ? 13.729 15.615  20.979 1.00 185.48 ? 123 GLU A CA  1 
ATOM   921  C  C   . GLU A 1 126 ? 14.869 15.741  21.986 1.00 179.95 ? 123 GLU A C   1 
ATOM   922  O  O   . GLU A 1 126 ? 14.935 15.027  22.991 1.00 175.15 ? 123 GLU A O   1 
ATOM   923  C  CB  . GLU A 1 126 ? 12.712 16.746  21.175 1.00 191.34 ? 123 GLU A CB  1 
ATOM   924  C  CG  . GLU A 1 126 ? 11.730 16.945  20.016 1.00 196.32 ? 123 GLU A CG  1 
ATOM   925  C  CD  . GLU A 1 126 ? 10.901 15.705  19.715 1.00 199.17 ? 123 GLU A CD  1 
ATOM   926  O  OE1 . GLU A 1 126 ? 10.224 15.202  20.637 1.00 198.27 ? 123 GLU A OE1 1 
ATOM   927  O  OE2 . GLU A 1 126 ? 10.922 15.232  18.558 1.00 199.85 ? 123 GLU A OE2 1 
ATOM   928  N  N   . GLY A 1 127 ? 15.779 16.665  21.696 1.00 163.08 ? 124 GLY A N   1 
ATOM   929  C  CA  . GLY A 1 127 ? 16.945 16.858  22.530 1.00 148.22 ? 124 GLY A CA  1 
ATOM   930  C  C   . GLY A 1 127 ? 17.959 15.744  22.382 1.00 136.30 ? 124 GLY A C   1 
ATOM   931  O  O   . GLY A 1 127 ? 18.796 15.779  21.476 1.00 134.22 ? 124 GLY A O   1 
ATOM   932  N  N   . ALA A 1 128 ? 17.874 14.732  23.249 1.00 133.41 ? 125 ALA A N   1 
ATOM   933  C  CA  . ALA A 1 128 ? 18.952 13.753  23.358 1.00 123.96 ? 125 ALA A CA  1 
ATOM   934  C  C   . ALA A 1 128 ? 19.016 12.837  22.143 1.00 123.39 ? 125 ALA A C   1 
ATOM   935  O  O   . ALA A 1 128 ? 20.104 12.570  21.622 1.00 121.19 ? 125 ALA A O   1 
ATOM   936  C  CB  . ALA A 1 128 ? 18.785 12.935  24.637 1.00 116.20 ? 125 ALA A CB  1 
ATOM   937  N  N   . ILE A 1 129 ? 17.873 12.328  21.685 1.00 125.55 ? 126 ILE A N   1 
ATOM   938  C  CA  . ILE A 1 129 ? 17.900 11.398  20.560 1.00 122.86 ? 126 ILE A CA  1 
ATOM   939  C  C   . ILE A 1 129 ? 18.301 12.115  19.277 1.00 126.77 ? 126 ILE A C   1 
ATOM   940  O  O   . ILE A 1 129 ? 18.944 11.525  18.398 1.00 121.80 ? 126 ILE A O   1 
ATOM   941  C  CB  . ILE A 1 129 ? 16.534 10.699  20.424 1.00 121.75 ? 126 ILE A CB  1 
ATOM   942  C  CG1 . ILE A 1 129 ? 16.228 9.881   21.680 1.00 119.75 ? 126 ILE A CG1 1 
ATOM   943  C  CG2 . ILE A 1 129 ? 16.491 9.817   19.184 1.00 115.76 ? 126 ILE A CG2 1 
ATOM   944  C  CD1 . ILE A 1 129 ? 17.436 9.212   22.303 1.00 107.22 ? 126 ILE A CD1 1 
ATOM   945  N  N   . TYR A 1 130 ? 17.963 13.399  19.163 1.00 129.49 ? 127 TYR A N   1 
ATOM   946  C  CA  . TYR A 1 130 ? 18.188 14.137  17.926 1.00 127.75 ? 127 TYR A CA  1 
ATOM   947  C  C   . TYR A 1 130 ? 19.672 14.400  17.697 1.00 124.83 ? 127 TYR A C   1 
ATOM   948  O  O   . TYR A 1 130 ? 20.244 13.958  16.696 1.00 123.84 ? 127 TYR A O   1 
ATOM   949  C  CB  . TYR A 1 130 ? 17.394 15.443  17.964 1.00 136.16 ? 127 TYR A CB  1 
ATOM   950  C  CG  . TYR A 1 130 ? 17.535 16.304  16.736 1.00 136.19 ? 127 TYR A CG  1 
ATOM   951  C  CD1 . TYR A 1 130 ? 16.706 16.122  15.636 1.00 135.32 ? 127 TYR A CD1 1 
ATOM   952  C  CD2 . TYR A 1 130 ? 18.485 17.317  16.685 1.00 138.51 ? 127 TYR A CD2 1 
ATOM   953  C  CE1 . TYR A 1 130 ? 16.829 16.915  14.511 1.00 139.30 ? 127 TYR A CE1 1 
ATOM   954  C  CE2 . TYR A 1 130 ? 18.617 18.119  15.569 1.00 140.22 ? 127 TYR A CE2 1 
ATOM   955  C  CZ  . TYR A 1 130 ? 17.786 17.917  14.483 1.00 143.92 ? 127 TYR A CZ  1 
ATOM   956  O  OH  . TYR A 1 130 ? 17.920 18.721  13.366 1.00 145.73 ? 127 TYR A OH  1 
ATOM   957  N  N   . GLU A 1 131 ? 20.315 15.123  18.618 1.00 126.34 ? 128 GLU A N   1 
ATOM   958  C  CA  . GLU A 1 131 ? 21.747 15.397  18.498 1.00 125.62 ? 128 GLU A CA  1 
ATOM   959  C  C   . GLU A 1 131 ? 22.572 14.135  18.268 1.00 126.33 ? 128 GLU A C   1 
ATOM   960  O  O   . GLU A 1 131 ? 23.615 14.194  17.605 1.00 125.99 ? 128 GLU A O   1 
ATOM   961  C  CB  . GLU A 1 131 ? 22.238 16.151  19.744 1.00 127.30 ? 128 GLU A CB  1 
ATOM   962  C  CG  . GLU A 1 131 ? 21.999 15.479  21.132 1.00 137.75 ? 128 GLU A CG  1 
ATOM   963  C  CD  . GLU A 1 131 ? 22.841 14.221  21.465 1.00 138.83 ? 128 GLU A CD  1 
ATOM   964  O  OE1 . GLU A 1 131 ? 22.507 13.515  22.444 1.00 137.21 ? 128 GLU A OE1 1 
ATOM   965  O  OE2 . GLU A 1 131 ? 23.889 13.980  20.820 1.00 139.46 ? 128 GLU A OE2 1 
ATOM   966  N  N   . GLY A 1 132 ? 22.111 12.990  18.782 1.00 126.70 ? 129 GLY A N   1 
ATOM   967  C  CA  . GLY A 1 132 ? 22.909 11.776  18.715 1.00 119.29 ? 129 GLY A CA  1 
ATOM   968  C  C   . GLY A 1 132 ? 22.968 11.188  17.321 1.00 116.79 ? 129 GLY A C   1 
ATOM   969  O  O   . GLY A 1 132 ? 24.029 10.747  16.868 1.00 114.86 ? 129 GLY A O   1 
ATOM   970  N  N   . PHE A 1 133 ? 21.825 11.151  16.633 1.00 113.32 ? 130 PHE A N   1 
ATOM   971  C  CA  . PHE A 1 133 ? 21.813 10.827  15.211 1.00 107.74 ? 130 PHE A CA  1 
ATOM   972  C  C   . PHE A 1 133 ? 22.730 11.771  14.429 1.00 111.90 ? 130 PHE A C   1 
ATOM   973  O  O   . PHE A 1 133 ? 23.435 11.339  13.508 1.00 114.76 ? 130 PHE A O   1 
ATOM   974  C  CB  . PHE A 1 133 ? 20.368 10.884  14.703 1.00 104.13 ? 130 PHE A CB  1 
ATOM   975  C  CG  . PHE A 1 133 ? 20.087 10.012  13.511 1.00 99.55  ? 130 PHE A CG  1 
ATOM   976  C  CD1 . PHE A 1 133 ? 20.961 9.008   13.137 1.00 99.30  ? 130 PHE A CD1 1 
ATOM   977  C  CD2 . PHE A 1 133 ? 18.928 10.197  12.767 1.00 105.14 ? 130 PHE A CD2 1 
ATOM   978  C  CE1 . PHE A 1 133 ? 20.689 8.209   12.031 1.00 101.50 ? 130 PHE A CE1 1 
ATOM   979  C  CE2 . PHE A 1 133 ? 18.648 9.405   11.667 1.00 104.22 ? 130 PHE A CE2 1 
ATOM   980  C  CZ  . PHE A 1 133 ? 19.528 8.412   11.297 1.00 102.83 ? 130 PHE A CZ  1 
ATOM   981  N  N   . LEU A 1 134 ? 22.766 13.058  14.811 1.00 116.58 ? 131 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 134 ? 23.633 14.032  14.139 1.00 117.15 ? 131 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 134 ? 25.107 13.708  14.364 1.00 119.44 ? 131 LEU A C   1 
ATOM   984  O  O   . LEU A 1 134 ? 25.907 13.698  13.419 1.00 113.13 ? 131 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 134 ? 23.328 15.446  14.642 1.00 108.50 ? 131 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 134 ? 22.168 16.194  13.996 1.00 112.93 ? 131 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 134 ? 22.043 17.585  14.599 1.00 120.48 ? 131 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 134 ? 22.352 16.262  12.488 1.00 116.86 ? 131 LEU A CD2 1 
ATOM   989  N  N   . GLU A 1 135 ? 25.482 13.463  15.621 1.00 118.47 ? 132 GLU A N   1 
ATOM   990  C  CA  . GLU A 1 135 ? 26.850 13.072  15.941 1.00 118.15 ? 132 GLU A CA  1 
ATOM   991  C  C   . GLU A 1 135 ? 27.207 11.731  15.318 1.00 116.17 ? 132 GLU A C   1 
ATOM   992  O  O   . GLU A 1 135 ? 28.362 11.510  14.933 1.00 118.57 ? 132 GLU A O   1 
ATOM   993  C  CB  . GLU A 1 135 ? 27.028 13.019  17.454 1.00 123.24 ? 132 GLU A CB  1 
ATOM   994  C  CG  . GLU A 1 135 ? 27.476 14.318  18.068 1.00 130.18 ? 132 GLU A CG  1 
ATOM   995  C  CD  . GLU A 1 135 ? 28.654 14.118  18.999 1.00 141.97 ? 132 GLU A CD  1 
ATOM   996  O  OE1 . GLU A 1 135 ? 28.878 14.983  19.875 1.00 148.62 ? 132 GLU A OE1 1 
ATOM   997  O  OE2 . GLU A 1 135 ? 29.345 13.082  18.867 1.00 140.00 ? 132 GLU A OE2 1 
ATOM   998  N  N   . TYR A 1 136 ? 26.237 10.815  15.229 1.00 107.66 ? 133 TYR A N   1 
ATOM   999  C  CA  . TYR A 1 136 ? 26.487 9.540   14.564 1.00 105.79 ? 133 TYR A CA  1 
ATOM   1000 C  C   . TYR A 1 136 ? 26.981 9.762   13.138 1.00 109.55 ? 133 TYR A C   1 
ATOM   1001 O  O   . TYR A 1 136 ? 27.935 9.111   12.691 1.00 107.58 ? 133 TYR A O   1 
ATOM   1002 C  CB  . TYR A 1 136 ? 25.220 8.678   14.590 1.00 97.94  ? 133 TYR A CB  1 
ATOM   1003 C  CG  . TYR A 1 136 ? 25.304 7.381   13.803 1.00 88.67  ? 133 TYR A CG  1 
ATOM   1004 C  CD1 . TYR A 1 136 ? 26.022 6.290   14.280 1.00 87.73  ? 133 TYR A CD1 1 
ATOM   1005 C  CD2 . TYR A 1 136 ? 24.648 7.245   12.588 1.00 96.26  ? 133 TYR A CD2 1 
ATOM   1006 C  CE1 . TYR A 1 136 ? 26.094 5.104   13.556 1.00 86.22  ? 133 TYR A CE1 1 
ATOM   1007 C  CE2 . TYR A 1 136 ? 24.713 6.068   11.859 1.00 94.99  ? 133 TYR A CE2 1 
ATOM   1008 C  CZ  . TYR A 1 136 ? 25.432 5.002   12.345 1.00 90.67  ? 133 TYR A CZ  1 
ATOM   1009 O  OH  . TYR A 1 136 ? 25.479 3.842   11.602 1.00 92.94  ? 133 TYR A OH  1 
ATOM   1010 N  N   . ALA A 1 137 ? 26.373 10.711  12.426 1.00 115.08 ? 134 ALA A N   1 
ATOM   1011 C  CA  . ALA A 1 137 ? 26.795 11.009  11.066 1.00 110.10 ? 134 ALA A CA  1 
ATOM   1012 C  C   . ALA A 1 137 ? 28.083 11.827  11.026 1.00 121.10 ? 134 ALA A C   1 
ATOM   1013 O  O   . ALA A 1 137 ? 28.876 11.664  10.093 1.00 120.38 ? 134 ALA A O   1 
ATOM   1014 C  CB  . ALA A 1 137 ? 25.669 11.728  10.329 1.00 113.43 ? 134 ALA A CB  1 
ATOM   1015 N  N   . ARG A 1 138 ? 28.318 12.691  12.021 1.00 123.74 ? 135 ARG A N   1 
ATOM   1016 C  CA  . ARG A 1 138 ? 29.564 13.460  12.071 1.00 125.44 ? 135 ARG A CA  1 
ATOM   1017 C  C   . ARG A 1 138 ? 30.775 12.540  12.151 1.00 126.77 ? 135 ARG A C   1 
ATOM   1018 O  O   . ARG A 1 138 ? 31.654 12.570  11.282 1.00 129.19 ? 135 ARG A O   1 
ATOM   1019 C  CB  . ARG A 1 138 ? 29.559 14.423  13.265 1.00 129.03 ? 135 ARG A CB  1 
ATOM   1020 C  CG  . ARG A 1 138 ? 28.820 15.734  13.037 1.00 133.15 ? 135 ARG A CG  1 
ATOM   1021 C  CD  . ARG A 1 138 ? 29.403 16.871  13.875 1.00 142.29 ? 135 ARG A CD  1 
ATOM   1022 N  NE  . ARG A 1 138 ? 28.647 18.110  13.728 1.00 147.13 ? 135 ARG A NE  1 
ATOM   1023 C  CZ  . ARG A 1 138 ? 28.556 18.813  12.606 1.00 148.43 ? 135 ARG A CZ  1 
ATOM   1024 N  NH1 . ARG A 1 138 ? 29.193 18.451  11.506 1.00 147.87 ? 135 ARG A NH1 1 
ATOM   1025 N  NH2 . ARG A 1 138 ? 27.814 19.916  12.592 1.00 150.17 ? 135 ARG A NH2 1 
ATOM   1026 N  N   . ASN A 1 139 ? 30.845 11.724  13.205 1.00 123.70 ? 136 ASN A N   1 
ATOM   1027 C  CA  . ASN A 1 139 ? 31.983 10.828  13.373 1.00 127.21 ? 136 ASN A CA  1 
ATOM   1028 C  C   . ASN A 1 139 ? 32.071 9.811   12.247 1.00 127.42 ? 136 ASN A C   1 
ATOM   1029 O  O   . ASN A 1 139 ? 33.172 9.340   11.927 1.00 133.50 ? 136 ASN A O   1 
ATOM   1030 C  CB  . ASN A 1 139 ? 31.901 10.119  14.726 1.00 134.17 ? 136 ASN A CB  1 
ATOM   1031 C  CG  . ASN A 1 139 ? 31.836 11.088  15.887 1.00 135.72 ? 136 ASN A CG  1 
ATOM   1032 O  OD1 . ASN A 1 139 ? 31.206 12.143  15.795 1.00 132.46 ? 136 ASN A OD1 1 
ATOM   1033 N  ND2 . ASN A 1 139 ? 32.484 10.731  16.993 1.00 134.66 ? 136 ASN A ND2 1 
ATOM   1034 N  N   . PHE A 1 140 ? 30.937 9.458   11.632 1.00 121.82 ? 137 PHE A N   1 
ATOM   1035 C  CA  . PHE A 1 140 ? 30.994 8.545   10.495 1.00 122.75 ? 137 PHE A CA  1 
ATOM   1036 C  C   . PHE A 1 140 ? 31.550 9.239   9.258  1.00 129.24 ? 137 PHE A C   1 
ATOM   1037 O  O   . PHE A 1 140 ? 32.441 8.705   8.586  1.00 130.91 ? 137 PHE A O   1 
ATOM   1038 C  CB  . PHE A 1 140 ? 29.623 7.960   10.175 1.00 114.15 ? 137 PHE A CB  1 
ATOM   1039 C  CG  . PHE A 1 140 ? 29.679 6.889   9.122  1.00 115.45 ? 137 PHE A CG  1 
ATOM   1040 C  CD1 . PHE A 1 140 ? 29.991 5.582   9.455  1.00 120.25 ? 137 PHE A CD1 1 
ATOM   1041 C  CD2 . PHE A 1 140 ? 29.526 7.210   7.790  1.00 115.26 ? 137 PHE A CD2 1 
ATOM   1042 C  CE1 . PHE A 1 140 ? 30.073 4.605   8.480  1.00 113.81 ? 137 PHE A CE1 1 
ATOM   1043 C  CE2 . PHE A 1 140 ? 29.610 6.244   6.816  1.00 112.77 ? 137 PHE A CE2 1 
ATOM   1044 C  CZ  . PHE A 1 140 ? 29.884 4.940   7.158  1.00 109.46 ? 137 PHE A CZ  1 
ATOM   1045 N  N   . LYS A 1 141 ? 31.004 10.414  8.913  1.00 129.74 ? 138 LYS A N   1 
ATOM   1046 C  CA  . LYS A 1 141 ? 31.552 11.182  7.800  1.00 128.23 ? 138 LYS A CA  1 
ATOM   1047 C  C   . LYS A 1 141 ? 33.023 11.495  8.028  1.00 136.43 ? 138 LYS A C   1 
ATOM   1048 O  O   . LYS A 1 141 ? 33.794 11.599  7.068  1.00 142.70 ? 138 LYS A O   1 
ATOM   1049 C  CB  . LYS A 1 141 ? 30.746 12.464  7.597  1.00 127.09 ? 138 LYS A CB  1 
ATOM   1050 C  CG  . LYS A 1 141 ? 29.372 12.234  6.982  1.00 124.53 ? 138 LYS A CG  1 
ATOM   1051 C  CD  . LYS A 1 141 ? 28.426 13.378  7.310  1.00 121.68 ? 138 LYS A CD  1 
ATOM   1052 C  CE  . LYS A 1 141 ? 27.195 13.369  6.424  1.00 125.21 ? 138 LYS A CE  1 
ATOM   1053 N  NZ  . LYS A 1 141 ? 27.285 12.336  5.363  1.00 128.69 ? 138 LYS A NZ  1 
ATOM   1054 N  N   . LYS A 1 142 ? 33.433 11.628  9.292  1.00 132.12 ? 139 LYS A N   1 
ATOM   1055 C  CA  . LYS A 1 142 ? 34.856 11.699  9.609  1.00 137.11 ? 139 LYS A CA  1 
ATOM   1056 C  C   . LYS A 1 142 ? 35.547 10.366  9.329  1.00 141.19 ? 139 LYS A C   1 
ATOM   1057 O  O   . LYS A 1 142 ? 36.598 10.334  8.676  1.00 139.83 ? 139 LYS A O   1 
ATOM   1058 C  CB  . LYS A 1 142 ? 35.047 12.113  11.067 1.00 137.96 ? 139 LYS A CB  1 
ATOM   1059 C  CG  . LYS A 1 142 ? 35.264 13.600  11.279 1.00 138.18 ? 139 LYS A CG  1 
ATOM   1060 C  CD  . LYS A 1 142 ? 35.291 13.941  12.757 1.00 135.89 ? 139 LYS A CD  1 
ATOM   1061 C  CE  . LYS A 1 142 ? 36.708 13.911  13.311 1.00 141.75 ? 139 LYS A CE  1 
ATOM   1062 N  NZ  . LYS A 1 142 ? 37.447 12.656  13.001 1.00 140.95 ? 139 LYS A NZ  1 
ATOM   1063 N  N   . TYR A 1 143 ? 34.968 9.253   9.820  1.00 144.34 ? 140 TYR A N   1 
ATOM   1064 C  CA  . TYR A 1 143 ? 35.505 7.921   9.523  1.00 143.72 ? 140 TYR A CA  1 
ATOM   1065 C  C   . TYR A 1 143 ? 35.694 7.735   8.023  1.00 142.70 ? 140 TYR A C   1 
ATOM   1066 O  O   . TYR A 1 143 ? 36.708 7.186   7.576  1.00 143.38 ? 140 TYR A O   1 
ATOM   1067 C  CB  . TYR A 1 143 ? 34.585 6.824   10.096 1.00 143.56 ? 140 TYR A CB  1 
ATOM   1068 C  CG  . TYR A 1 143 ? 34.982 5.374   9.764  1.00 153.74 ? 140 TYR A CG  1 
ATOM   1069 C  CD1 . TYR A 1 143 ? 34.706 4.810   8.514  1.00 151.98 ? 140 TYR A CD1 1 
ATOM   1070 C  CD2 . TYR A 1 143 ? 35.632 4.570   10.707 1.00 155.95 ? 140 TYR A CD2 1 
ATOM   1071 C  CE1 . TYR A 1 143 ? 35.072 3.485   8.211  1.00 155.33 ? 140 TYR A CE1 1 
ATOM   1072 C  CE2 . TYR A 1 143 ? 36.003 3.248   10.411 1.00 155.52 ? 140 TYR A CE2 1 
ATOM   1073 C  CZ  . TYR A 1 143 ? 35.719 2.710   9.163  1.00 154.68 ? 140 TYR A CZ  1 
ATOM   1074 O  OH  . TYR A 1 143 ? 36.077 1.407   8.861  1.00 140.54 ? 140 TYR A OH  1 
ATOM   1075 N  N   . GLU A 1 144 ? 34.730 8.203   7.228  1.00 141.54 ? 141 GLU A N   1 
ATOM   1076 C  CA  . GLU A 1 144 ? 34.825 8.108   5.779  1.00 139.02 ? 141 GLU A CA  1 
ATOM   1077 C  C   . GLU A 1 144 ? 36.024 8.865   5.218  1.00 147.39 ? 141 GLU A C   1 
ATOM   1078 O  O   . GLU A 1 144 ? 36.302 8.748   4.019  1.00 147.70 ? 141 GLU A O   1 
ATOM   1079 C  CB  . GLU A 1 144 ? 33.527 8.619   5.147  1.00 132.01 ? 141 GLU A CB  1 
ATOM   1080 C  CG  . GLU A 1 144 ? 32.454 7.553   5.028  1.00 128.50 ? 141 GLU A CG  1 
ATOM   1081 C  CD  . GLU A 1 144 ? 31.211 8.046   4.317  1.00 129.02 ? 141 GLU A CD  1 
ATOM   1082 O  OE1 . GLU A 1 144 ? 30.620 9.050   4.773  1.00 132.61 ? 141 GLU A OE1 1 
ATOM   1083 O  OE2 . GLU A 1 144 ? 30.813 7.420   3.313  1.00 122.85 ? 141 GLU A OE2 1 
ATOM   1084 N  N   . GLY A 1 145 ? 36.747 9.618   6.046  1.00 146.95 ? 142 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 145 ? 37.889 10.374  5.574  1.00 146.46 ? 142 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 145 ? 37.478 11.586  4.767  1.00 151.41 ? 142 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 145 ? 38.048 11.856  3.704  1.00 154.56 ? 142 GLY A O   1 
ATOM   1088 N  N   . LYS A 1 146 ? 36.482 12.321  5.260  1.00 153.24 ? 143 LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 146 ? 35.971 13.512  4.594  1.00 159.70 ? 143 LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 146 ? 36.524 14.755  5.276  1.00 167.95 ? 143 LYS A C   1 
ATOM   1091 O  O   . LYS A 1 146 ? 36.492 14.859  6.509  1.00 166.17 ? 143 LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 146 ? 34.441 13.537  4.612  1.00 154.88 ? 143 LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 146 ? 33.790 12.430  3.795  1.00 148.34 ? 143 LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 146 ? 32.276 12.512  3.840  1.00 143.09 ? 143 LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 146 ? 31.650 11.524  2.875  1.00 139.78 ? 143 LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 146 ? 30.169 11.595  2.910  1.00 138.90 ? 143 LYS A NZ  1 
ATOM   1097 N  N   . ASP A 1 147 ? 37.023 15.694  4.472  1.00 171.55 ? 144 ASP A N   1 
ATOM   1098 C  CA  . ASP A 1 147 ? 37.562 16.930  5.018  1.00 175.82 ? 144 ASP A CA  1 
ATOM   1099 C  C   . ASP A 1 147 ? 36.489 17.686  5.800  1.00 178.32 ? 144 ASP A C   1 
ATOM   1100 O  O   . ASP A 1 147 ? 35.292 17.408  5.693  1.00 178.39 ? 144 ASP A O   1 
ATOM   1101 C  CB  . ASP A 1 147 ? 38.203 17.764  3.896  1.00 181.39 ? 144 ASP A CB  1 
ATOM   1102 C  CG  . ASP A 1 147 ? 37.195 18.542  3.024  1.00 183.42 ? 144 ASP A CG  1 
ATOM   1103 O  OD1 . ASP A 1 147 ? 37.519 18.770  1.842  1.00 184.48 ? 144 ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A 1 147 ? 36.124 18.985  3.480  1.00 182.63 ? 144 ASP A OD2 1 
ATOM   1105 N  N   . GLN A 1 148 ? 36.943 18.624  6.639  1.00 177.96 ? 145 GLN A N   1 
ATOM   1106 C  CA  . GLN A 1 148 ? 36.031 19.299  7.560  1.00 177.53 ? 145 GLN A CA  1 
ATOM   1107 C  C   . GLN A 1 148 ? 35.049 20.205  6.823  1.00 178.12 ? 145 GLN A C   1 
ATOM   1108 O  O   . GLN A 1 148 ? 33.926 20.417  7.300  1.00 177.32 ? 145 GLN A O   1 
ATOM   1109 C  CB  . GLN A 1 148 ? 36.832 20.086  8.602  1.00 175.95 ? 145 GLN A CB  1 
ATOM   1110 C  CG  . GLN A 1 148 ? 35.998 20.765  9.683  1.00 174.22 ? 145 GLN A CG  1 
ATOM   1111 C  CD  . GLN A 1 148 ? 35.018 19.820  10.355 1.00 171.81 ? 145 GLN A CD  1 
ATOM   1112 O  OE1 . GLN A 1 148 ? 33.814 20.069  10.366 1.00 171.12 ? 145 GLN A OE1 1 
ATOM   1113 N  NE2 . GLN A 1 148 ? 35.528 18.728  10.912 1.00 175.56 ? 145 GLN A NE2 1 
ATOM   1114 N  N   . GLU A 1 149 ? 35.442 20.733  5.660  1.00 180.93 ? 146 GLU A N   1 
ATOM   1115 C  CA  . GLU A 1 149 ? 34.516 21.531  4.862  1.00 180.20 ? 146 GLU A CA  1 
ATOM   1116 C  C   . GLU A 1 149 ? 33.403 20.664  4.281  1.00 177.21 ? 146 GLU A C   1 
ATOM   1117 O  O   . GLU A 1 149 ? 32.255 21.112  4.168  1.00 175.26 ? 146 GLU A O   1 
ATOM   1118 C  CB  . GLU A 1 149 ? 35.272 22.260  3.749  1.00 180.65 ? 146 GLU A CB  1 
ATOM   1119 C  CG  . GLU A 1 149 ? 34.482 22.390  2.459  1.00 180.32 ? 146 GLU A CG  1 
ATOM   1120 C  CD  . GLU A 1 149 ? 35.332 22.846  1.293  1.00 186.32 ? 146 GLU A CD  1 
ATOM   1121 O  OE1 . GLU A 1 149 ? 35.704 24.038  1.253  1.00 188.13 ? 146 GLU A OE1 1 
ATOM   1122 O  OE2 . GLU A 1 149 ? 35.636 22.007  0.419  1.00 187.97 ? 146 GLU A OE2 1 
ATOM   1123 N  N   . THR A 1 150 ? 33.721 19.416  3.921  1.00 177.23 ? 147 THR A N   1 
ATOM   1124 C  CA  . THR A 1 150 ? 32.720 18.523  3.344  1.00 173.14 ? 147 THR A CA  1 
ATOM   1125 C  C   . THR A 1 150 ? 31.682 18.104  4.382  1.00 169.51 ? 147 THR A C   1 
ATOM   1126 O  O   . THR A 1 150 ? 30.475 18.210  4.136  1.00 167.12 ? 147 THR A O   1 
ATOM   1127 C  CB  . THR A 1 150 ? 33.398 17.292  2.737  1.00 172.77 ? 147 THR A CB  1 
ATOM   1128 O  OG1 . THR A 1 150 ? 34.352 17.703  1.749  1.00 175.00 ? 147 THR A OG1 1 
ATOM   1129 C  CG2 . THR A 1 150 ? 32.369 16.385  2.085  1.00 168.73 ? 147 THR A CG2 1 
ATOM   1130 N  N   . ILE A 1 151 ? 32.138 17.642  5.558  1.00 168.64 ? 148 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 151 ? 31.249 17.122  6.605  1.00 163.64 ? 148 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 151 ? 30.066 18.052  6.851  1.00 163.62 ? 148 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 151 ? 28.959 17.596  7.161  1.00 157.63 ? 148 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 151 ? 32.043 16.871  7.911  1.00 156.52 ? 148 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 151 ? 33.288 16.027  7.645  1.00 156.55 ? 148 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 151 ? 31.180 16.154  8.936  1.00 146.92 ? 148 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 151 ? 34.216 15.919  8.829  1.00 152.83 ? 148 ILE A CD1 1 
ATOM   1138 N  N   . ASP A 1 152 ? 30.272 19.364  6.701  1.00 165.58 ? 149 ASP A N   1 
ATOM   1139 C  CA  . ASP A 1 152 ? 29.184 20.324  6.849  1.00 165.09 ? 149 ASP A CA  1 
ATOM   1140 C  C   . ASP A 1 152 ? 28.231 20.328  5.659  1.00 162.59 ? 149 ASP A C   1 
ATOM   1141 O  O   . ASP A 1 152 ? 27.085 20.760  5.808  1.00 162.47 ? 149 ASP A O   1 
ATOM   1142 C  CB  . ASP A 1 152 ? 29.753 21.730  7.050  1.00 171.69 ? 149 ASP A CB  1 
ATOM   1143 C  CG  . ASP A 1 152 ? 30.580 21.850  8.314  1.00 175.82 ? 149 ASP A CG  1 
ATOM   1144 O  OD1 . ASP A 1 152 ? 31.192 20.839  8.719  1.00 172.75 ? 149 ASP A OD1 1 
ATOM   1145 O  OD2 . ASP A 1 152 ? 30.640 22.962  8.887  1.00 181.21 ? 149 ASP A OD2 1 
ATOM   1146 N  N   . ASN A 1 153 ? 28.672 19.862  4.488  1.00 162.70 ? 150 ASN A N   1 
ATOM   1147 C  CA  . ASN A 1 153 ? 27.840 19.954  3.291  1.00 161.06 ? 150 ASN A CA  1 
ATOM   1148 C  C   . ASN A 1 153 ? 26.730 18.907  3.280  1.00 156.81 ? 150 ASN A C   1 
ATOM   1149 O  O   . ASN A 1 153 ? 25.547 19.255  3.223  1.00 159.04 ? 150 ASN A O   1 
ATOM   1150 C  CB  . ASN A 1 153 ? 28.706 19.853  2.036  1.00 165.19 ? 150 ASN A CB  1 
ATOM   1151 C  CG  . ASN A 1 153 ? 29.695 20.999  1.922  1.00 172.94 ? 150 ASN A CG  1 
ATOM   1152 O  OD1 . ASN A 1 153 ? 30.904 20.784  1.847  1.00 177.18 ? 150 ASN A OD1 1 
ATOM   1153 N  ND2 . ASN A 1 153 ? 29.182 22.229  1.915  1.00 166.94 ? 150 ASN A ND2 1 
ATOM   1154 N  N   . GLU A 1 154 ? 27.076 17.617  3.321  1.00 156.10 ? 151 GLU A N   1 
ATOM   1155 C  CA  . GLU A 1 154 ? 26.002 16.631  3.407  1.00 152.18 ? 151 GLU A CA  1 
ATOM   1156 C  C   . GLU A 1 154 ? 25.294 16.660  4.752  1.00 148.34 ? 151 GLU A C   1 
ATOM   1157 O  O   . GLU A 1 154 ? 24.257 16.007  4.895  1.00 147.64 ? 151 GLU A O   1 
ATOM   1158 C  CB  . GLU A 1 154 ? 26.513 15.214  3.134  1.00 146.21 ? 151 GLU A CB  1 
ATOM   1159 C  CG  . GLU A 1 154 ? 27.717 15.140  2.226  1.00 146.69 ? 151 GLU A CG  1 
ATOM   1160 C  CD  . GLU A 1 154 ? 28.999 15.079  3.011  1.00 149.80 ? 151 GLU A CD  1 
ATOM   1161 O  OE1 . GLU A 1 154 ? 29.132 15.864  3.969  1.00 152.86 ? 151 GLU A OE1 1 
ATOM   1162 O  OE2 . GLU A 1 154 ? 29.867 14.246  2.679  1.00 148.56 ? 151 GLU A OE2 1 
ATOM   1163 N  N   . MET A 1 155 ? 25.816 17.401  5.730  1.00 147.82 ? 152 MET A N   1 
ATOM   1164 C  CA  . MET A 1 155 ? 25.126 17.506  7.008  1.00 148.38 ? 152 MET A CA  1 
ATOM   1165 C  C   . MET A 1 155 ? 23.934 18.448  6.912  1.00 152.46 ? 152 MET A C   1 
ATOM   1166 O  O   . MET A 1 155 ? 22.865 18.150  7.456  1.00 152.10 ? 152 MET A O   1 
ATOM   1167 C  CB  . MET A 1 155 ? 26.099 17.956  8.097  1.00 144.77 ? 152 MET A CB  1 
ATOM   1168 C  CG  . MET A 1 155 ? 25.711 17.530  9.506  1.00 143.52 ? 152 MET A CG  1 
ATOM   1169 S  SD  . MET A 1 155 ? 25.524 15.728  9.660  1.00 137.27 ? 152 MET A SD  1 
ATOM   1170 C  CE  . MET A 1 155 ? 27.187 15.254  10.093 1.00 126.76 ? 152 MET A CE  1 
ATOM   1171 N  N   . ASP A 1 156 ? 24.089 19.582  6.217  1.00 153.80 ? 153 ASP A N   1 
ATOM   1172 C  CA  . ASP A 1 156 ? 22.952 20.459  5.940  1.00 157.02 ? 153 ASP A CA  1 
ATOM   1173 C  C   . ASP A 1 156 ? 21.947 19.834  4.976  1.00 159.35 ? 153 ASP A C   1 
ATOM   1174 O  O   . ASP A 1 156 ? 20.898 20.438  4.725  1.00 162.48 ? 153 ASP A O   1 
ATOM   1175 C  CB  . ASP A 1 156 ? 23.421 21.811  5.376  1.00 161.78 ? 153 ASP A CB  1 
ATOM   1176 C  CG  . ASP A 1 156 ? 24.308 22.585  6.343  1.00 160.90 ? 153 ASP A CG  1 
ATOM   1177 O  OD1 . ASP A 1 156 ? 24.563 22.084  7.459  1.00 160.75 ? 153 ASP A OD1 1 
ATOM   1178 O  OD2 . ASP A 1 156 ? 24.744 23.703  5.984  1.00 158.08 ? 153 ASP A OD2 1 
ATOM   1179 N  N   . HIS A 1 157 ? 22.249 18.660  4.419  1.00 166.21 ? 154 HIS A N   1 
ATOM   1180 C  CA  . HIS A 1 157 ? 21.310 17.893  3.608  1.00 163.52 ? 154 HIS A CA  1 
ATOM   1181 C  C   . HIS A 1 157 ? 20.799 16.654  4.342  1.00 160.95 ? 154 HIS A C   1 
ATOM   1182 O  O   . HIS A 1 157 ? 20.181 15.784  3.720  1.00 160.57 ? 154 HIS A O   1 
ATOM   1183 C  CB  . HIS A 1 157 ? 21.957 17.496  2.274  1.00 164.46 ? 154 HIS A CB  1 
ATOM   1184 C  CG  . HIS A 1 157 ? 22.258 18.654  1.365  1.00 170.65 ? 154 HIS A CG  1 
ATOM   1185 N  ND1 . HIS A 1 157 ? 23.457 19.335  1.394  1.00 170.56 ? 154 HIS A ND1 1 
ATOM   1186 C  CD2 . HIS A 1 157 ? 21.525 19.235  0.384  1.00 172.18 ? 154 HIS A CD2 1 
ATOM   1187 C  CE1 . HIS A 1 157 ? 23.444 20.294  0.484  1.00 173.14 ? 154 HIS A CE1 1 
ATOM   1188 N  NE2 . HIS A 1 157 ? 22.284 20.253  -0.145 1.00 172.92 ? 154 HIS A NE2 1 
ATOM   1189 N  N   . PHE A 1 158 ? 21.042 16.561  5.649  1.00 148.57 ? 155 PHE A N   1 
ATOM   1190 C  CA  . PHE A 1 158 ? 20.589 15.449  6.482  1.00 139.31 ? 155 PHE A CA  1 
ATOM   1191 C  C   . PHE A 1 158 ? 19.213 15.786  7.056  1.00 139.61 ? 155 PHE A C   1 
ATOM   1192 O  O   . PHE A 1 158 ? 19.094 16.676  7.906  1.00 132.23 ? 155 PHE A O   1 
ATOM   1193 C  CB  . PHE A 1 158 ? 21.604 15.202  7.595  1.00 131.30 ? 155 PHE A CB  1 
ATOM   1194 C  CG  . PHE A 1 158 ? 21.696 13.775  8.040  1.00 124.24 ? 155 PHE A CG  1 
ATOM   1195 C  CD1 . PHE A 1 158 ? 21.733 12.743  7.117  1.00 122.71 ? 155 PHE A CD1 1 
ATOM   1196 C  CD2 . PHE A 1 158 ? 21.752 13.465  9.393  1.00 122.15 ? 155 PHE A CD2 1 
ATOM   1197 C  CE1 . PHE A 1 158 ? 21.819 11.425  7.534  1.00 117.05 ? 155 PHE A CE1 1 
ATOM   1198 C  CE2 . PHE A 1 158 ? 21.837 12.152  9.821  1.00 113.55 ? 155 PHE A CE2 1 
ATOM   1199 C  CZ  . PHE A 1 158 ? 21.871 11.128  8.890  1.00 116.50 ? 155 PHE A CZ  1 
ATOM   1200 N  N   . LYS A 1 159 ? 18.171 15.082  6.596  1.00 144.60 ? 156 LYS A N   1 
ATOM   1201 C  CA  . LYS A 1 159 ? 16.818 15.306  7.104  1.00 146.49 ? 156 LYS A CA  1 
ATOM   1202 C  C   . LYS A 1 159 ? 16.404 14.147  7.999  1.00 143.40 ? 156 LYS A C   1 
ATOM   1203 O  O   . LYS A 1 159 ? 15.949 13.106  7.501  1.00 142.63 ? 156 LYS A O   1 
ATOM   1204 C  CB  . LYS A 1 159 ? 15.805 15.475  5.966  1.00 152.50 ? 156 LYS A CB  1 
ATOM   1205 C  CG  . LYS A 1 159 ? 14.356 15.416  6.473  1.00 155.46 ? 156 LYS A CG  1 
ATOM   1206 C  CD  . LYS A 1 159 ? 13.348 15.087  5.386  1.00 162.60 ? 156 LYS A CD  1 
ATOM   1207 C  CE  . LYS A 1 159 ? 11.996 14.738  5.996  1.00 156.84 ? 156 LYS A CE  1 
ATOM   1208 N  NZ  . LYS A 1 159 ? 10.933 14.632  4.962  1.00 159.63 ? 156 LYS A NZ  1 
ATOM   1209 N  N   . PRO A 1 160 ? 16.527 14.274  9.321  1.00 137.97 ? 157 PRO A N   1 
ATOM   1210 C  CA  . PRO A 1 160 ? 16.163 13.176  10.224 1.00 134.15 ? 157 PRO A CA  1 
ATOM   1211 C  C   . PRO A 1 160 ? 14.733 13.211  10.741 1.00 130.57 ? 157 PRO A C   1 
ATOM   1212 O  O   . PRO A 1 160 ? 14.356 12.307  11.494 1.00 127.86 ? 157 PRO A O   1 
ATOM   1213 C  CB  . PRO A 1 160 ? 17.145 13.388  11.382 1.00 131.76 ? 157 PRO A CB  1 
ATOM   1214 C  CG  . PRO A 1 160 ? 17.238 14.871  11.459 1.00 132.32 ? 157 PRO A CG  1 
ATOM   1215 C  CD  . PRO A 1 160 ? 17.289 15.322  10.021 1.00 135.53 ? 157 PRO A CD  1 
ATOM   1216 N  N   . THR A 1 161 ? 13.946 14.228  10.377 1.00 139.28 ? 158 THR A N   1 
ATOM   1217 C  CA  . THR A 1 161 ? 12.626 14.404  10.980 1.00 135.91 ? 158 THR A CA  1 
ATOM   1218 C  C   . THR A 1 161 ? 11.707 13.233  10.662 1.00 129.76 ? 158 THR A C   1 
ATOM   1219 O  O   . THR A 1 161 ? 10.909 12.811  11.507 1.00 120.12 ? 158 THR A O   1 
ATOM   1220 C  CB  . THR A 1 161 ? 12.003 15.711  10.493 1.00 131.41 ? 158 THR A CB  1 
ATOM   1221 O  OG1 . THR A 1 161 ? 12.883 16.792  10.808 1.00 133.68 ? 158 THR A OG1 1 
ATOM   1222 C  CG2 . THR A 1 161 ? 10.654 15.950  11.161 1.00 129.68 ? 158 THR A CG2 1 
ATOM   1223 N  N   . GLU A 1 162 ? 11.802 12.710  9.443  1.00 140.12 ? 159 GLU A N   1 
ATOM   1224 C  CA  . GLU A 1 162 ? 11.059 11.539  9.005  1.00 137.12 ? 159 GLU A CA  1 
ATOM   1225 C  C   . GLU A 1 162 ? 11.351 10.365  9.935  1.00 131.34 ? 159 GLU A C   1 
ATOM   1226 O  O   . GLU A 1 162 ? 10.469 9.897   10.669 1.00 126.87 ? 159 GLU A O   1 
ATOM   1227 C  CB  . GLU A 1 162 ? 11.443 11.229  7.552  1.00 141.67 ? 159 GLU A CB  1 
ATOM   1228 C  CG  . GLU A 1 162 ? 11.076 9.862   6.975  1.00 139.23 ? 159 GLU A CG  1 
ATOM   1229 C  CD  . GLU A 1 162 ? 9.822  9.255   7.569  1.00 140.68 ? 159 GLU A CD  1 
ATOM   1230 O  OE1 . GLU A 1 162 ? 8.713  9.713   7.212  1.00 147.21 ? 159 GLU A OE1 1 
ATOM   1231 O  OE2 . GLU A 1 162 ? 9.950  8.298   8.365  1.00 136.03 ? 159 GLU A OE2 1 
ATOM   1232 N  N   . THR A 1 163 ? 12.600 9.900   9.919  1.00 128.83 ? 160 THR A N   1 
ATOM   1233 C  CA  . THR A 1 163 ? 12.944 8.677   10.626 1.00 115.00 ? 160 THR A CA  1 
ATOM   1234 C  C   . THR A 1 163 ? 12.692 8.814   12.124 1.00 117.49 ? 160 THR A C   1 
ATOM   1235 O  O   . THR A 1 163 ? 12.086 7.932   12.744 1.00 111.92 ? 160 THR A O   1 
ATOM   1236 C  CB  . THR A 1 163 ? 14.398 8.315   10.332 1.00 113.22 ? 160 THR A CB  1 
ATOM   1237 O  OG1 . THR A 1 163 ? 14.467 7.663   9.057  1.00 113.02 ? 160 THR A OG1 1 
ATOM   1238 C  CG2 . THR A 1 163 ? 14.957 7.380   11.396 1.00 103.87 ? 160 THR A CG2 1 
ATOM   1239 N  N   . LEU A 1 164 ? 13.118 9.933   12.718 1.00 117.67 ? 161 LEU A N   1 
ATOM   1240 C  CA  . LEU A 1 164 ? 12.960 10.122  14.159 1.00 114.61 ? 161 LEU A CA  1 
ATOM   1241 C  C   . LEU A 1 164 ? 11.499 10.186  14.591 1.00 115.81 ? 161 LEU A C   1 
ATOM   1242 O  O   . LEU A 1 164 ? 11.206 9.987   15.776 1.00 114.69 ? 161 LEU A O   1 
ATOM   1243 C  CB  . LEU A 1 164 ? 13.713 11.382  14.600 1.00 118.24 ? 161 LEU A CB  1 
ATOM   1244 C  CG  . LEU A 1 164 ? 14.975 11.165  15.451 1.00 124.26 ? 161 LEU A CG  1 
ATOM   1245 C  CD1 . LEU A 1 164 ? 16.082 10.514  14.648 1.00 116.79 ? 161 LEU A CD1 1 
ATOM   1246 C  CD2 . LEU A 1 164 ? 15.462 12.496  16.007 1.00 126.17 ? 161 LEU A CD2 1 
ATOM   1247 N  N   . LYS A 1 165 ? 10.578 10.434  13.659 1.00 117.67 ? 162 LYS A N   1 
ATOM   1248 C  CA  . LYS A 1 165 ? 9.154  10.525  13.965 1.00 112.81 ? 162 LYS A CA  1 
ATOM   1249 C  C   . LYS A 1 165 ? 8.447  9.179   13.899 1.00 107.85 ? 162 LYS A C   1 
ATOM   1250 O  O   . LYS A 1 165 ? 7.506  8.957   14.665 1.00 108.41 ? 162 LYS A O   1 
ATOM   1251 C  CB  . LYS A 1 165 ? 8.478  11.517  13.015 1.00 114.01 ? 162 LYS A CB  1 
ATOM   1252 C  CG  . LYS A 1 165 ? 7.090  11.963  13.448 1.00 122.70 ? 162 LYS A CG  1 
ATOM   1253 C  CD  . LYS A 1 165 ? 5.995  11.491  12.487 1.00 117.97 ? 162 LYS A CD  1 
ATOM   1254 C  CE  . LYS A 1 165 ? 4.603  11.732  13.069 1.00 117.25 ? 162 LYS A CE  1 
ATOM   1255 N  NZ  . LYS A 1 165 ? 4.358  10.891  14.299 1.00 118.36 ? 162 LYS A NZ  1 
ATOM   1256 N  N   . GLU A 1 166 ? 8.856  8.287   12.990 1.00 107.64 ? 163 GLU A N   1 
ATOM   1257 C  CA  . GLU A 1 166 ? 8.394  6.902   13.052 1.00 107.36 ? 163 GLU A CA  1 
ATOM   1258 C  C   . GLU A 1 166 ? 8.863  6.235   14.335 1.00 103.64 ? 163 GLU A C   1 
ATOM   1259 O  O   . GLU A 1 166 ? 8.157  5.396   14.912 1.00 93.47  ? 163 GLU A O   1 
ATOM   1260 C  CB  . GLU A 1 166 ? 8.910  6.108   11.852 1.00 110.06 ? 163 GLU A CB  1 
ATOM   1261 C  CG  . GLU A 1 166 ? 8.527  6.626   10.492 1.00 114.42 ? 163 GLU A CG  1 
ATOM   1262 C  CD  . GLU A 1 166 ? 8.620  5.538   9.430  1.00 119.37 ? 163 GLU A CD  1 
ATOM   1263 O  OE1 . GLU A 1 166 ? 7.864  4.548   9.526  1.00 117.83 ? 163 GLU A OE1 1 
ATOM   1264 O  OE2 . GLU A 1 166 ? 9.446  5.665   8.500  1.00 126.71 ? 163 GLU A OE2 1 
ATOM   1265 N  N   . LEU A 1 167 ? 10.078 6.576   14.768 1.00 103.19 ? 164 LEU A N   1 
ATOM   1266 C  CA  . LEU A 1 167 ? 10.613 6.088   16.032 1.00 101.56 ? 164 LEU A CA  1 
ATOM   1267 C  C   . LEU A 1 167 ? 9.753  6.533   17.208 1.00 100.79 ? 164 LEU A C   1 
ATOM   1268 O  O   . LEU A 1 167 ? 9.580  5.789   18.179 1.00 92.62  ? 164 LEU A O   1 
ATOM   1269 C  CB  . LEU A 1 167 ? 12.041 6.600   16.196 1.00 101.69 ? 164 LEU A CB  1 
ATOM   1270 C  CG  . LEU A 1 167 ? 13.003 5.818   17.068 1.00 95.43  ? 164 LEU A CG  1 
ATOM   1271 C  CD1 . LEU A 1 167 ? 12.643 4.358   17.030 1.00 88.40  ? 164 LEU A CD1 1 
ATOM   1272 C  CD2 . LEU A 1 167 ? 14.404 6.043   16.544 1.00 90.65  ? 164 LEU A CD2 1 
ATOM   1273 N  N   . SER A 1 168 ? 9.222  7.756   17.144 1.00 107.79 ? 165 SER A N   1 
ATOM   1274 C  CA  . SER A 1 168 ? 8.411  8.270   18.240 1.00 106.18 ? 165 SER A CA  1 
ATOM   1275 C  C   . SER A 1 168 ? 7.067  7.551   18.323 1.00 98.99  ? 165 SER A C   1 
ATOM   1276 O  O   . SER A 1 168 ? 6.604  7.231   19.423 1.00 95.79  ? 165 SER A O   1 
ATOM   1277 C  CB  . SER A 1 168 ? 8.220  9.777   18.081 1.00 110.39 ? 165 SER A CB  1 
ATOM   1278 O  OG  . SER A 1 168 ? 7.306  10.274  19.038 1.00 110.99 ? 165 SER A OG  1 
ATOM   1279 N  N   . GLU A 1 169 ? 6.423  7.287   17.175 1.00 95.37  ? 166 GLU A N   1 
ATOM   1280 C  CA  . GLU A 1 169 ? 5.182  6.513   17.190 1.00 93.11  ? 166 GLU A CA  1 
ATOM   1281 C  C   . GLU A 1 169 ? 5.424  5.101   17.699 1.00 90.19  ? 166 GLU A C   1 
ATOM   1282 O  O   . GLU A 1 169 ? 4.685  4.602   18.556 1.00 81.85  ? 166 GLU A O   1 
ATOM   1283 C  CB  . GLU A 1 169 ? 4.537  6.449   15.801 1.00 94.85  ? 166 GLU A CB  1 
ATOM   1284 C  CG  . GLU A 1 169 ? 4.652  7.686   14.938 1.00 109.53 ? 166 GLU A CG  1 
ATOM   1285 C  CD  . GLU A 1 169 ? 4.087  7.465   13.536 1.00 112.58 ? 166 GLU A CD  1 
ATOM   1286 O  OE1 . GLU A 1 169 ? 3.740  6.310   13.198 1.00 116.29 ? 166 GLU A OE1 1 
ATOM   1287 O  OE2 . GLU A 1 169 ? 3.983  8.447   12.774 1.00 116.33 ? 166 GLU A OE2 1 
ATOM   1288 N  N   . ALA A 1 170 ? 6.449  4.434   17.162 1.00 91.57  ? 167 ALA A N   1 
ATOM   1289 C  CA  . ALA A 1 170 ? 6.718  3.051   17.535 1.00 84.99  ? 167 ALA A CA  1 
ATOM   1290 C  C   . ALA A 1 170 ? 6.842  2.903   19.045 1.00 85.10  ? 167 ALA A C   1 
ATOM   1291 O  O   . ALA A 1 170 ? 6.248  1.996   19.646 1.00 79.87  ? 167 ALA A O   1 
ATOM   1292 C  CB  . ALA A 1 170 ? 7.986  2.567   16.838 1.00 79.04  ? 167 ALA A CB  1 
ATOM   1293 N  N   . LEU A 1 171 ? 7.599  3.805   19.679 1.00 86.74  ? 168 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 171 ? 7.807  3.727   21.122 1.00 81.60  ? 168 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 171 ? 6.499  3.906   21.883 1.00 84.24  ? 168 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 171 ? 6.235  3.182   22.848 1.00 80.94  ? 168 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 171 ? 8.824  4.779   21.560 1.00 84.50  ? 168 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 171 ? 10.298 4.520   21.260 1.00 83.70  ? 168 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 171 ? 11.109 5.693   21.733 1.00 86.60  ? 168 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 171 ? 10.782 3.244   21.922 1.00 71.57  ? 168 LEU A CD2 1 
ATOM   1301 N  N   . ASP A 1 172 ? 5.660  4.865   21.464 1.00 86.67  ? 169 ASP A N   1 
ATOM   1302 C  CA  . ASP A 1 172 ? 4.386  5.070   22.157 1.00 84.57  ? 169 ASP A CA  1 
ATOM   1303 C  C   . ASP A 1 172 ? 3.497  3.828   22.063 1.00 81.97  ? 169 ASP A C   1 
ATOM   1304 O  O   . ASP A 1 172 ? 2.843  3.450   23.043 1.00 81.27  ? 169 ASP A O   1 
ATOM   1305 C  CB  . ASP A 1 172 ? 3.671  6.301   21.606 1.00 77.89  ? 169 ASP A CB  1 
ATOM   1306 C  CG  . ASP A 1 172 ? 4.426  7.598   21.889 1.00 88.74  ? 169 ASP A CG  1 
ATOM   1307 O  OD1 . ASP A 1 172 ? 5.508  7.511   22.504 1.00 94.48  ? 169 ASP A OD1 1 
ATOM   1308 O  OD2 . ASP A 1 172 ? 3.946  8.694   21.489 1.00 87.22  ? 169 ASP A OD2 1 
ATOM   1309 N  N   . THR A 1 173 ? 3.487  3.164   20.901 1.00 77.81  ? 170 THR A N   1 
ATOM   1310 C  CA  . THR A 1 173 ? 2.745  1.914   20.751 1.00 75.42  ? 170 THR A CA  1 
ATOM   1311 C  C   . THR A 1 173 ? 3.209  0.852   21.746 1.00 78.82  ? 170 THR A C   1 
ATOM   1312 O  O   . THR A 1 173 ? 2.389  0.142   22.345 1.00 78.82  ? 170 THR A O   1 
ATOM   1313 C  CB  . THR A 1 173 ? 2.901  1.390   19.329 1.00 71.31  ? 170 THR A CB  1 
ATOM   1314 O  OG1 . THR A 1 173 ? 2.454  2.388   18.406 1.00 78.03  ? 170 THR A OG1 1 
ATOM   1315 C  CG2 . THR A 1 173 ? 2.084  0.131   19.142 1.00 77.00  ? 170 THR A CG2 1 
ATOM   1316 N  N   . ILE A 1 174 ? 4.524  0.718   21.919 1.00 76.38  ? 171 ILE A N   1 
ATOM   1317 C  CA  . ILE A 1 174 ? 5.057  -0.295  22.817 1.00 73.03  ? 171 ILE A CA  1 
ATOM   1318 C  C   . ILE A 1 174 ? 4.777  0.077   24.267 1.00 74.83  ? 171 ILE A C   1 
ATOM   1319 O  O   . ILE A 1 174 ? 4.542  -0.800  25.109 1.00 74.64  ? 171 ILE A O   1 
ATOM   1320 C  CB  . ILE A 1 174 ? 6.562  -0.483  22.538 1.00 68.68  ? 171 ILE A CB  1 
ATOM   1321 C  CG1 . ILE A 1 174 ? 6.746  -1.207  21.211 1.00 63.98  ? 171 ILE A CG1 1 
ATOM   1322 C  CG2 . ILE A 1 174 ? 7.255  -1.232  23.674 1.00 62.19  ? 171 ILE A CG2 1 
ATOM   1323 C  CD1 . ILE A 1 174 ? 8.145  -1.664  20.960 1.00 62.84  ? 171 ILE A CD1 1 
ATOM   1324 N  N   . LYS A 1 175 ? 4.778  1.371   24.587 1.00 72.99  ? 172 LYS A N   1 
ATOM   1325 C  CA  . LYS A 1 175 ? 4.476  1.779   25.954 1.00 76.53  ? 172 LYS A CA  1 
ATOM   1326 C  C   . LYS A 1 175 ? 3.086  1.308   26.367 1.00 74.60  ? 172 LYS A C   1 
ATOM   1327 O  O   . LYS A 1 175 ? 2.904  0.807   27.480 1.00 71.66  ? 172 LYS A O   1 
ATOM   1328 C  CB  . LYS A 1 175 ? 4.588  3.297   26.088 1.00 76.19  ? 172 LYS A CB  1 
ATOM   1329 C  CG  . LYS A 1 175 ? 4.384  3.812   27.505 1.00 71.55  ? 172 LYS A CG  1 
ATOM   1330 C  CD  . LYS A 1 175 ? 4.586  5.301   27.510 1.00 75.70  ? 172 LYS A CD  1 
ATOM   1331 C  CE  . LYS A 1 175 ? 3.801  5.971   28.616 1.00 85.20  ? 172 LYS A CE  1 
ATOM   1332 N  NZ  . LYS A 1 175 ? 4.620  6.989   29.346 1.00 99.05  ? 172 LYS A NZ  1 
ATOM   1333 N  N   . GLU A 1 176 ? 2.095  1.447   25.477 1.00 79.07  ? 173 GLU A N   1 
ATOM   1334 C  CA  . GLU A 1 176 ? 0.746  0.992   25.783 1.00 80.67  ? 173 GLU A CA  1 
ATOM   1335 C  C   . GLU A 1 176 ? 0.644  -0.520  25.854 1.00 79.38  ? 173 GLU A C   1 
ATOM   1336 O  O   . GLU A 1 176 ? -0.396 -1.030  26.296 1.00 80.87  ? 173 GLU A O   1 
ATOM   1337 C  CB  . GLU A 1 176 ? -0.260 1.491   24.746 1.00 87.89  ? 173 GLU A CB  1 
ATOM   1338 C  CG  . GLU A 1 176 ? 0.053  2.838   24.102 1.00 93.60  ? 173 GLU A CG  1 
ATOM   1339 C  CD  . GLU A 1 176 ? -0.583 4.017   24.829 1.00 105.83 ? 173 GLU A CD  1 
ATOM   1340 O  OE1 . GLU A 1 176 ? -1.050 3.816   25.975 1.00 109.84 ? 173 GLU A OE1 1 
ATOM   1341 O  OE2 . GLU A 1 176 ? -0.662 5.126   24.235 1.00 106.85 ? 173 GLU A OE2 1 
ATOM   1342 N  N   . GLN A 1 177 ? 1.688  -1.236  25.425 1.00 72.00  ? 174 GLN A N   1 
ATOM   1343 C  CA  . GLN A 1 177 ? 1.696  -2.689  25.397 1.00 72.55  ? 174 GLN A CA  1 
ATOM   1344 C  C   . GLN A 1 177 ? 2.428  -3.316  26.577 1.00 68.94  ? 174 GLN A C   1 
ATOM   1345 O  O   . GLN A 1 177 ? 2.364  -4.538  26.744 1.00 62.33  ? 174 GLN A O   1 
ATOM   1346 C  CB  . GLN A 1 177 ? 2.324  -3.186  24.088 1.00 70.45  ? 174 GLN A CB  1 
ATOM   1347 C  CG  . GLN A 1 177 ? 1.368  -3.098  22.896 1.00 72.90  ? 174 GLN A CG  1 
ATOM   1348 C  CD  . GLN A 1 177 ? 1.914  -3.769  21.643 1.00 78.08  ? 174 GLN A CD  1 
ATOM   1349 O  OE1 . GLN A 1 177 ? 3.086  -3.610  21.289 1.00 75.98  ? 174 GLN A OE1 1 
ATOM   1350 N  NE2 . GLN A 1 177 ? 1.061  -4.525  20.967 1.00 81.45  ? 174 GLN A NE2 1 
ATOM   1351 N  N   . VAL A 1 178 ? 3.112  -2.526  27.406 1.00 69.24  ? 175 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 178 ? 3.906  -3.125  28.475 1.00 66.99  ? 175 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 178 ? 3.019  -3.925  29.421 1.00 63.01  ? 175 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 178 ? 3.461  -4.933  29.990 1.00 55.44  ? 175 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 178 ? 4.722  -2.039  29.214 1.00 62.62  ? 175 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 178 ? 5.391  -2.608  30.434 1.00 65.10  ? 175 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 178 ? 5.791  -1.495  28.314 1.00 63.95  ? 175 VAL A CG2 1 
ATOM   1358 N  N   . ASP A 1 179 ? 1.745  -3.532  29.568 1.00 65.25  ? 176 ASP A N   1 
ATOM   1359 C  CA  . ASP A 1 179 ? 0.851  -4.224  30.497 1.00 61.54  ? 176 ASP A CA  1 
ATOM   1360 C  C   . ASP A 1 179 ? 0.420  -5.616  30.013 1.00 63.13  ? 176 ASP A C   1 
ATOM   1361 O  O   . ASP A 1 179 ? -0.282 -6.313  30.750 1.00 63.49  ? 176 ASP A O   1 
ATOM   1362 C  CB  . ASP A 1 179 ? -0.368 -3.337  30.826 1.00 63.15  ? 176 ASP A CB  1 
ATOM   1363 C  CG  . ASP A 1 179 ? -1.191 -2.932  29.600 1.00 83.03  ? 176 ASP A CG  1 
ATOM   1364 O  OD1 . ASP A 1 179 ? -2.041 -3.728  29.124 1.00 88.63  ? 176 ASP A OD1 1 
ATOM   1365 O  OD2 . ASP A 1 179 ? -1.009 -1.786  29.118 1.00 87.79  ? 176 ASP A OD2 1 
ATOM   1366 N  N   . GLU A 1 180 ? 0.863  -6.071  28.837 1.00 65.64  ? 177 GLU A N   1 
ATOM   1367 C  CA  . GLU A 1 180 ? 0.588  -7.425  28.365 1.00 60.91  ? 177 GLU A CA  1 
ATOM   1368 C  C   . GLU A 1 180 ? 1.764  -8.392  28.533 1.00 55.84  ? 177 GLU A C   1 
ATOM   1369 O  O   . GLU A 1 180 ? 1.595  -9.583  28.265 1.00 58.57  ? 177 GLU A O   1 
ATOM   1370 C  CB  . GLU A 1 180 ? 0.154  -7.385  26.887 1.00 59.57  ? 177 GLU A CB  1 
ATOM   1371 C  CG  . GLU A 1 180 ? -0.988 -6.403  26.617 1.00 70.75  ? 177 GLU A CG  1 
ATOM   1372 C  CD  . GLU A 1 180 ? -1.153 -6.046  25.138 1.00 77.86  ? 177 GLU A CD  1 
ATOM   1373 O  OE1 . GLU A 1 180 ? -0.672 -6.818  24.268 1.00 71.34  ? 177 GLU A OE1 1 
ATOM   1374 O  OE2 . GLU A 1 180 ? -1.778 -4.990  24.846 1.00 81.85  ? 177 GLU A OE2 1 
ATOM   1375 N  N   . VAL A 1 181 ? 2.937  -7.920  28.963 1.00 54.68  ? 178 VAL A N   1 
ATOM   1376 C  CA  . VAL A 1 181 ? 4.111  -8.777  29.121 1.00 54.66  ? 178 VAL A CA  1 
ATOM   1377 C  C   . VAL A 1 181 ? 3.917  -9.707  30.315 1.00 55.96  ? 178 VAL A C   1 
ATOM   1378 O  O   . VAL A 1 181 ? 3.511  -9.275  31.401 1.00 50.06  ? 178 VAL A O   1 
ATOM   1379 C  CB  . VAL A 1 181 ? 5.373  -7.913  29.293 1.00 54.75  ? 178 VAL A CB  1 
ATOM   1380 C  CG1 . VAL A 1 181 ? 6.516  -8.735  29.840 1.00 49.45  ? 178 VAL A CG1 1 
ATOM   1381 C  CG2 . VAL A 1 181 ? 5.766  -7.265  27.975 1.00 52.43  ? 178 VAL A CG2 1 
ATOM   1382 N  N   . LEU A 1 182 ? 4.212  -10.996 30.129 1.00 53.45  ? 179 LEU A N   1 
ATOM   1383 C  CA  . LEU A 1 182 ? 3.935  -11.981 31.167 1.00 55.66  ? 179 LEU A CA  1 
ATOM   1384 C  C   . LEU A 1 182 ? 5.148  -12.782 31.630 1.00 49.03  ? 179 LEU A C   1 
ATOM   1385 O  O   . LEU A 1 182 ? 5.087  -13.356 32.713 1.00 49.42  ? 179 LEU A O   1 
ATOM   1386 C  CB  . LEU A 1 182 ? 2.845  -12.976 30.708 1.00 51.59  ? 179 LEU A CB  1 
ATOM   1387 C  CG  . LEU A 1 182 ? 1.414  -12.513 30.364 1.00 55.20  ? 179 LEU A CG  1 
ATOM   1388 C  CD1 . LEU A 1 182 ? 0.626  -13.558 29.553 1.00 48.67  ? 179 LEU A CD1 1 
ATOM   1389 C  CD2 . LEU A 1 182 ? 0.584  -12.160 31.603 1.00 59.82  ? 179 LEU A CD2 1 
ATOM   1390 N  N   . ASP A 1 183 ? 6.233  -12.837 30.859 1.00 50.53  ? 180 ASP A N   1 
ATOM   1391 C  CA  . ASP A 1 183 ? 7.354  -13.738 31.112 1.00 47.71  ? 180 ASP A CA  1 
ATOM   1392 C  C   . ASP A 1 183 ? 8.329  -13.148 32.143 1.00 49.17  ? 180 ASP A C   1 
ATOM   1393 O  O   . ASP A 1 183 ? 8.314  -11.942 32.395 1.00 47.71  ? 180 ASP A O   1 
ATOM   1394 C  CB  . ASP A 1 183 ? 8.063  -14.037 29.791 1.00 45.70  ? 180 ASP A CB  1 
ATOM   1395 C  CG  . ASP A 1 183 ? 7.134  -14.657 28.761 1.00 50.77  ? 180 ASP A CG  1 
ATOM   1396 O  OD1 . ASP A 1 183 ? 6.592  -15.762 29.016 1.00 50.80  ? 180 ASP A OD1 1 
ATOM   1397 O  OD2 . ASP A 1 183 ? 6.923  -14.039 27.690 1.00 52.75  ? 180 ASP A OD2 1 
ATOM   1398 N  N   . PRO A 1 184 ? 9.162  -13.985 32.783 1.00 47.45  ? 181 PRO A N   1 
ATOM   1399 C  CA  . PRO A 1 184 ? 10.112 -13.465 33.781 1.00 47.51  ? 181 PRO A CA  1 
ATOM   1400 C  C   . PRO A 1 184 ? 10.987 -12.368 33.203 1.00 44.93  ? 181 PRO A C   1 
ATOM   1401 O  O   . PRO A 1 184 ? 11.407 -12.439 32.048 1.00 43.90  ? 181 PRO A O   1 
ATOM   1402 C  CB  . PRO A 1 184 ? 10.937 -14.699 34.160 1.00 43.10  ? 181 PRO A CB  1 
ATOM   1403 C  CG  . PRO A 1 184 ? 9.999  -15.847 33.953 1.00 45.38  ? 181 PRO A CG  1 
ATOM   1404 C  CD  . PRO A 1 184 ? 9.136  -15.462 32.772 1.00 44.80  ? 181 PRO A CD  1 
ATOM   1405 N  N   . ILE A 1 185 ? 11.265 -11.337 34.009 1.00 43.19  ? 182 ILE A N   1 
ATOM   1406 C  CA  . ILE A 1 185 ? 11.954 -10.161 33.487 1.00 45.29  ? 182 ILE A CA  1 
ATOM   1407 C  C   . ILE A 1 185 ? 12.998 -9.641  34.475 1.00 45.27  ? 182 ILE A C   1 
ATOM   1408 O  O   . ILE A 1 185 ? 12.840 -9.710  35.694 1.00 42.03  ? 182 ILE A O   1 
ATOM   1409 C  CB  . ILE A 1 185 ? 10.941 -9.061  33.101 1.00 43.24  ? 182 ILE A CB  1 
ATOM   1410 C  CG1 . ILE A 1 185 ? 11.637 -7.804  32.586 1.00 44.73  ? 182 ILE A CG1 1 
ATOM   1411 C  CG2 . ILE A 1 185 ? 10.072 -8.698  34.271 1.00 45.53  ? 182 ILE A CG2 1 
ATOM   1412 C  CD1 . ILE A 1 185 ? 10.740 -6.930  31.724 1.00 46.10  ? 182 ILE A CD1 1 
ATOM   1413 N  N   . LEU A 1 186 ? 14.080 -9.120  33.923 1.00 48.69  ? 183 LEU A N   1 
ATOM   1414 C  CA  . LEU A 1 186 ? 15.100 -8.395  34.656 1.00 48.25  ? 183 LEU A CA  1 
ATOM   1415 C  C   . LEU A 1 186 ? 15.233 -7.024  33.999 1.00 46.51  ? 183 LEU A C   1 
ATOM   1416 O  O   . LEU A 1 186 ? 15.535 -6.931  32.802 1.00 45.17  ? 183 LEU A O   1 
ATOM   1417 C  CB  . LEU A 1 186 ? 16.421 -9.176  34.643 1.00 44.74  ? 183 LEU A CB  1 
ATOM   1418 C  CG  . LEU A 1 186 ? 17.723 -8.437  34.986 1.00 48.68  ? 183 LEU A CG  1 
ATOM   1419 C  CD1 . LEU A 1 186 ? 17.664 -7.845  36.391 1.00 51.66  ? 183 LEU A CD1 1 
ATOM   1420 C  CD2 . LEU A 1 186 ? 18.920 -9.354  34.856 1.00 46.73  ? 183 LEU A CD2 1 
ATOM   1421 N  N   . VAL A 1 187 ? 14.980 -5.970  34.769 1.00 49.56  ? 184 VAL A N   1 
ATOM   1422 C  CA  . VAL A 1 187 ? 15.066 -4.591  34.298 1.00 46.62  ? 184 VAL A CA  1 
ATOM   1423 C  C   . VAL A 1 187 ? 16.398 -4.006  34.771 1.00 49.21  ? 184 VAL A C   1 
ATOM   1424 O  O   . VAL A 1 187 ? 16.672 -3.965  35.979 1.00 49.96  ? 184 VAL A O   1 
ATOM   1425 C  CB  . VAL A 1 187 ? 13.870 -3.773  34.817 1.00 50.49  ? 184 VAL A CB  1 
ATOM   1426 C  CG1 . VAL A 1 187 ? 13.875 -2.341  34.272 1.00 52.83  ? 184 VAL A CG1 1 
ATOM   1427 C  CG2 . VAL A 1 187 ? 12.561 -4.464  34.434 1.00 48.93  ? 184 VAL A CG2 1 
ATOM   1428 N  N   . ILE A 1 188 ? 17.230 -3.546  33.833 1.00 49.82  ? 185 ILE A N   1 
ATOM   1429 C  CA  . ILE A 1 188 ? 18.538 -2.959  34.142 1.00 56.35  ? 185 ILE A CA  1 
ATOM   1430 C  C   . ILE A 1 188 ? 18.547 -1.487  33.728 1.00 53.94  ? 185 ILE A C   1 
ATOM   1431 O  O   . ILE A 1 188 ? 18.139 -1.153  32.614 1.00 54.92  ? 185 ILE A O   1 
ATOM   1432 C  CB  . ILE A 1 188 ? 19.681 -3.730  33.452 1.00 50.88  ? 185 ILE A CB  1 
ATOM   1433 C  CG1 . ILE A 1 188 ? 20.017 -4.997  34.251 1.00 51.36  ? 185 ILE A CG1 1 
ATOM   1434 C  CG2 . ILE A 1 188 ? 20.903 -2.843  33.288 1.00 52.55  ? 185 ILE A CG2 1 
ATOM   1435 C  CD1 . ILE A 1 188 ? 20.783 -6.059  33.468 1.00 48.97  ? 185 ILE A CD1 1 
ATOM   1436 N  N   . GLN A 1 189 ? 19.003 -0.604  34.618 1.00 57.01  ? 186 GLN A N   1 
ATOM   1437 C  CA  . GLN A 1 189 ? 18.997 0.814   34.279 1.00 60.28  ? 186 GLN A CA  1 
ATOM   1438 C  C   . GLN A 1 189 ? 20.186 1.522   34.899 1.00 63.33  ? 186 GLN A C   1 
ATOM   1439 O  O   . GLN A 1 189 ? 20.504 1.311   36.072 1.00 59.49  ? 186 GLN A O   1 
ATOM   1440 C  CB  . GLN A 1 189 ? 17.705 1.498   34.722 1.00 61.85  ? 186 GLN A CB  1 
ATOM   1441 C  CG  . GLN A 1 189 ? 17.696 3.012   34.492 1.00 65.75  ? 186 GLN A CG  1 
ATOM   1442 C  CD  . GLN A 1 189 ? 17.760 3.414   33.023 1.00 67.66  ? 186 GLN A CD  1 
ATOM   1443 O  OE1 . GLN A 1 189 ? 17.042 2.866   32.182 1.00 62.35  ? 186 GLN A OE1 1 
ATOM   1444 N  NE2 . GLN A 1 189 ? 18.602 4.403   32.716 1.00 68.74  ? 186 GLN A NE2 1 
ATOM   1445 N  N   . ALA A 1 190 ? 20.834 2.361   34.093 1.00 68.07  ? 187 ALA A N   1 
ATOM   1446 C  CA  . ALA A 1 190 ? 21.909 3.211   34.574 1.00 74.53  ? 187 ALA A CA  1 
ATOM   1447 C  C   . ALA A 1 190 ? 21.318 4.441   35.253 1.00 78.46  ? 187 ALA A C   1 
ATOM   1448 O  O   . ALA A 1 190 ? 20.397 5.072   34.728 1.00 77.44  ? 187 ALA A O   1 
ATOM   1449 C  CB  . ALA A 1 190 ? 22.827 3.613   33.424 1.00 74.85  ? 187 ALA A CB  1 
ATOM   1450 N  N   . GLU A 1 191 ? 21.839 4.765   36.436 1.00 92.41  ? 188 GLU A N   1 
ATOM   1451 C  CA  . GLU A 1 191 ? 21.270 5.847   37.235 1.00 96.38  ? 188 GLU A CA  1 
ATOM   1452 C  C   . GLU A 1 191 ? 21.451 7.194   36.542 1.00 99.80  ? 188 GLU A C   1 
ATOM   1453 O  O   . GLU A 1 191 ? 20.478 7.916   36.295 1.00 102.23 ? 188 GLU A O   1 
ATOM   1454 C  CB  . GLU A 1 191 ? 21.903 5.848   38.633 1.00 98.94  ? 188 GLU A CB  1 
ATOM   1455 C  CG  . GLU A 1 191 ? 20.907 5.672   39.787 1.00 99.43  ? 188 GLU A CG  1 
ATOM   1456 C  CD  . GLU A 1 191 ? 21.586 5.599   41.152 1.00 105.46 ? 188 GLU A CD  1 
ATOM   1457 O  OE1 . GLU A 1 191 ? 22.475 4.739   41.326 1.00 101.68 ? 188 GLU A OE1 1 
ATOM   1458 O  OE2 . GLU A 1 191 ? 21.262 6.431   42.035 1.00 115.25 ? 188 GLU A OE2 1 
ATOM   1459 N  N   . ASN A 1 192 ? 22.692 7.543   36.201 1.00 94.09  ? 189 ASN A N   1 
ATOM   1460 C  CA  . ASN A 1 192 ? 22.975 8.830   35.564 1.00 99.30  ? 189 ASN A CA  1 
ATOM   1461 C  C   . ASN A 1 192 ? 22.966 8.671   34.041 1.00 98.64  ? 189 ASN A C   1 
ATOM   1462 O  O   . ASN A 1 192 ? 23.998 8.671   33.368 1.00 100.70 ? 189 ASN A O   1 
ATOM   1463 C  CB  . ASN A 1 192 ? 24.300 9.391   36.064 1.00 107.17 ? 189 ASN A CB  1 
ATOM   1464 C  CG  . ASN A 1 192 ? 24.425 9.329   37.579 1.00 108.40 ? 189 ASN A CG  1 
ATOM   1465 O  OD1 . ASN A 1 192 ? 23.649 9.959   38.300 1.00 111.36 ? 189 ASN A OD1 1 
ATOM   1466 N  ND2 . ASN A 1 192 ? 25.406 8.567   38.069 1.00 105.77 ? 189 ASN A ND2 1 
ATOM   1467 N  N   . ASP A 1 193 ? 21.757 8.545   33.501 1.00 98.01  ? 190 ASP A N   1 
ATOM   1468 C  CA  . ASP A 1 193 ? 21.558 8.420   32.064 1.00 94.13  ? 190 ASP A CA  1 
ATOM   1469 C  C   . ASP A 1 193 ? 21.252 9.781   31.449 1.00 96.88  ? 190 ASP A C   1 
ATOM   1470 O  O   . ASP A 1 193 ? 20.328 10.477  31.881 1.00 96.80  ? 190 ASP A O   1 
ATOM   1471 C  CB  . ASP A 1 193 ? 20.424 7.444   31.764 1.00 85.60  ? 190 ASP A CB  1 
ATOM   1472 C  CG  . ASP A 1 193 ? 20.476 6.923   30.348 1.00 84.91  ? 190 ASP A CG  1 
ATOM   1473 O  OD1 . ASP A 1 193 ? 20.671 7.746   29.425 1.00 90.11  ? 190 ASP A OD1 1 
ATOM   1474 O  OD2 . ASP A 1 193 ? 20.327 5.698   30.155 1.00 77.52  ? 190 ASP A OD2 1 
ATOM   1475 N  N   . ASN A 1 194 ? 22.026 10.153  30.433 1.00 102.14 ? 191 ASN A N   1 
ATOM   1476 C  CA  . ASN A 1 194 ? 21.789 11.392  29.707 1.00 103.47 ? 191 ASN A CA  1 
ATOM   1477 C  C   . ASN A 1 194 ? 20.958 11.197  28.452 1.00 103.02 ? 191 ASN A C   1 
ATOM   1478 O  O   . ASN A 1 194 ? 20.630 12.186  27.787 1.00 103.47 ? 191 ASN A O   1 
ATOM   1479 C  CB  . ASN A 1 194 ? 23.113 12.056  29.308 1.00 108.99 ? 191 ASN A CB  1 
ATOM   1480 C  CG  . ASN A 1 194 ? 24.080 12.178  30.461 1.00 113.25 ? 191 ASN A CG  1 
ATOM   1481 O  OD1 . ASN A 1 194 ? 25.279 11.953  30.297 1.00 120.97 ? 191 ASN A OD1 1 
ATOM   1482 N  ND2 . ASN A 1 194 ? 23.567 12.536  31.637 1.00 109.69 ? 191 ASN A ND2 1 
ATOM   1483 N  N   . MET A 1 195 ? 20.613 9.961   28.103 1.00 95.49  ? 192 MET A N   1 
ATOM   1484 C  CA  . MET A 1 195 ? 19.987 9.731   26.812 1.00 91.87  ? 192 MET A CA  1 
ATOM   1485 C  C   . MET A 1 195 ? 18.490 9.476   26.916 1.00 90.85  ? 192 MET A C   1 
ATOM   1486 O  O   . MET A 1 195 ? 17.702 10.091  26.188 1.00 95.16  ? 192 MET A O   1 
ATOM   1487 C  CB  . MET A 1 195 ? 20.692 8.578   26.093 1.00 81.86  ? 192 MET A CB  1 
ATOM   1488 C  CG  . MET A 1 195 ? 20.239 8.456   24.660 1.00 87.06  ? 192 MET A CG  1 
ATOM   1489 S  SD  . MET A 1 195 ? 21.124 9.603   23.569 1.00 104.59 ? 192 MET A SD  1 
ATOM   1490 C  CE  . MET A 1 195 ? 22.582 10.025  24.533 1.00 96.87  ? 192 MET A CE  1 
ATOM   1491 N  N   . ILE A 1 196 ? 18.076 8.584   27.806 1.00 84.43  ? 193 ILE A N   1 
ATOM   1492 C  CA  . ILE A 1 196 ? 16.667 8.364   28.082 1.00 82.31  ? 193 ILE A CA  1 
ATOM   1493 C  C   . ILE A 1 196 ? 16.333 8.938   29.460 1.00 85.22  ? 193 ILE A C   1 
ATOM   1494 O  O   . ILE A 1 196 ? 17.195 9.445   30.178 1.00 88.30  ? 193 ILE A O   1 
ATOM   1495 C  CB  . ILE A 1 196 ? 16.282 6.872   27.970 1.00 81.87  ? 193 ILE A CB  1 
ATOM   1496 C  CG1 . ILE A 1 196 ? 17.053 6.001   28.971 1.00 77.52  ? 193 ILE A CG1 1 
ATOM   1497 C  CG2 . ILE A 1 196 ? 16.570 6.372   26.579 1.00 81.34  ? 193 ILE A CG2 1 
ATOM   1498 C  CD1 . ILE A 1 196 ? 16.187 4.992   29.680 1.00 68.58  ? 193 ILE A CD1 1 
ATOM   1499 N  N   . ASP A 1 197 ? 15.055 8.897   29.804 1.00 85.44  ? 194 ASP A N   1 
ATOM   1500 C  CA  . ASP A 1 197 ? 14.639 9.209   31.162 1.00 81.40  ? 194 ASP A CA  1 
ATOM   1501 C  C   . ASP A 1 197 ? 14.763 7.954   32.005 1.00 78.96  ? 194 ASP A C   1 
ATOM   1502 O  O   . ASP A 1 197 ? 14.019 6.999   31.759 1.00 80.25  ? 194 ASP A O   1 
ATOM   1503 C  CB  . ASP A 1 197 ? 13.197 9.695   31.201 1.00 87.94  ? 194 ASP A CB  1 
ATOM   1504 C  CG  . ASP A 1 197 ? 12.708 9.948   32.625 1.00 91.67  ? 194 ASP A CG  1 
ATOM   1505 O  OD1 . ASP A 1 197 ? 13.545 10.159  33.540 1.00 88.30  ? 194 ASP A OD1 1 
ATOM   1506 O  OD2 . ASP A 1 197 ? 11.475 9.862   32.838 1.00 96.50  ? 194 ASP A OD2 1 
ATOM   1507 N  N   . PRO A 1 198 ? 15.644 7.919   33.014 1.00 81.12  ? 195 PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 198 ? 15.888 6.649   33.728 1.00 80.41  ? 195 PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 198 ? 14.676 6.154   34.495 1.00 76.63  ? 195 PRO A C   1 
ATOM   1510 O  O   . PRO A 1 198 ? 14.597 4.957   34.796 1.00 70.41  ? 195 PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 198 ? 17.065 6.970   34.665 1.00 81.44  ? 195 PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 198 ? 17.439 8.412   34.422 1.00 83.24  ? 195 PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 198 ? 16.382 9.055   33.593 1.00 81.29  ? 195 PRO A CD  1 
ATOM   1514 N  N   . GLN A 1 199 ? 13.711 7.034   34.777 1.00 78.53  ? 196 GLN A N   1 
ATOM   1515 C  CA  . GLN A 1 199 ? 12.418 6.649   35.337 1.00 78.35  ? 196 GLN A CA  1 
ATOM   1516 C  C   . GLN A 1 199 ? 11.658 5.650   34.463 1.00 72.56  ? 196 GLN A C   1 
ATOM   1517 O  O   . GLN A 1 199 ? 10.671 5.073   34.928 1.00 69.43  ? 196 GLN A O   1 
ATOM   1518 C  CB  . GLN A 1 199 ? 11.566 7.905   35.538 1.00 80.05  ? 196 GLN A CB  1 
ATOM   1519 C  CG  . GLN A 1 199 ? 10.597 7.819   36.695 1.00 89.52  ? 196 GLN A CG  1 
ATOM   1520 C  CD  . GLN A 1 199 ? 11.282 7.602   38.036 1.00 96.80  ? 196 GLN A CD  1 
ATOM   1521 O  OE1 . GLN A 1 199 ? 12.401 8.080   38.265 1.00 96.32  ? 196 GLN A OE1 1 
ATOM   1522 N  NE2 . GLN A 1 199 ? 10.618 6.868   38.925 1.00 94.23  ? 196 GLN A NE2 1 
ATOM   1523 N  N   . SER A 1 200 ? 12.065 5.459   33.207 1.00 73.37  ? 197 SER A N   1 
ATOM   1524 C  CA  . SER A 1 200 ? 11.407 4.479   32.352 1.00 67.70  ? 197 SER A CA  1 
ATOM   1525 C  C   . SER A 1 200 ? 11.492 3.089   32.958 1.00 66.98  ? 197 SER A C   1 
ATOM   1526 O  O   . SER A 1 200 ? 10.560 2.283   32.819 1.00 61.90  ? 197 SER A O   1 
ATOM   1527 C  CB  . SER A 1 200 ? 12.048 4.487   30.966 1.00 69.40  ? 197 SER A CB  1 
ATOM   1528 O  OG  . SER A 1 200 ? 12.125 5.800   30.445 1.00 71.03  ? 197 SER A OG  1 
ATOM   1529 N  N   . ALA A 1 201 ? 12.618 2.787   33.620 1.00 66.49  ? 198 ALA A N   1 
ATOM   1530 C  CA  . ALA A 1 201 ? 12.809 1.476   34.230 1.00 64.01  ? 198 ALA A CA  1 
ATOM   1531 C  C   . ALA A 1 201 ? 11.751 1.208   35.296 1.00 62.51  ? 198 ALA A C   1 
ATOM   1532 O  O   . ALA A 1 201 ? 11.221 0.099   35.382 1.00 59.12  ? 198 ALA A O   1 
ATOM   1533 C  CB  . ALA A 1 201 ? 14.216 1.361   34.819 1.00 56.70  ? 198 ALA A CB  1 
ATOM   1534 N  N   . ASN A 1 202 ? 11.411 2.218   36.099 1.00 64.32  ? 199 ASN A N   1 
ATOM   1535 C  CA  . ASN A 1 202 ? 10.306 2.072   37.044 1.00 66.90  ? 199 ASN A CA  1 
ATOM   1536 C  C   . ASN A 1 202 ? 8.974  1.848   36.323 1.00 65.85  ? 199 ASN A C   1 
ATOM   1537 O  O   . ASN A 1 202 ? 8.150  1.035   36.768 1.00 61.51  ? 199 ASN A O   1 
ATOM   1538 C  CB  . ASN A 1 202 ? 10.225 3.300   37.957 1.00 67.02  ? 199 ASN A CB  1 
ATOM   1539 C  CG  . ASN A 1 202 ? 11.168 3.206   39.152 1.00 75.04  ? 199 ASN A CG  1 
ATOM   1540 O  OD1 . ASN A 1 202 ? 11.671 2.128   39.486 1.00 74.97  ? 199 ASN A OD1 1 
ATOM   1541 N  ND2 . ASN A 1 202 ? 11.396 4.339   39.816 1.00 79.54  ? 199 ASN A ND2 1 
ATOM   1542 N  N   . TYR A 1 203 ? 8.733  2.568   35.220 1.00 61.73  ? 200 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 203 ? 7.515  2.328   34.460 1.00 61.71  ? 200 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 203 ? 7.414  0.873   34.018 1.00 60.16  ? 200 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 203 ? 6.337  0.269   34.080 1.00 61.67  ? 200 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 203 ? 7.429  3.253   33.244 1.00 63.26  ? 200 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 203 ? 6.061  3.163   32.613 1.00 63.53  ? 200 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 203 ? 5.013  3.945   33.083 1.00 70.38  ? 200 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 203 ? 5.796  2.249   31.599 1.00 64.17  ? 200 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 203 ? 3.742  3.850   32.539 1.00 71.78  ? 200 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 203 ? 4.530  2.137   31.057 1.00 68.08  ? 200 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 203 ? 3.505  2.940   31.530 1.00 73.96  ? 200 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 203 ? 2.238  2.845   30.987 1.00 78.64  ? 200 TYR A OH  1 
ATOM   1554 N  N   . ILE A 1 204 ? 8.517  0.297   33.549 1.00 59.71  ? 201 ILE A N   1 
ATOM   1555 C  CA  . ILE A 1 204 ? 8.473  -1.079  33.076 1.00 57.12  ? 201 ILE A CA  1 
ATOM   1556 C  C   . ILE A 1 204 ? 8.243  -2.037  34.243 1.00 59.80  ? 201 ILE A C   1 
ATOM   1557 O  O   . ILE A 1 204 ? 7.324  -2.869  34.216 1.00 55.88  ? 201 ILE A O   1 
ATOM   1558 C  CB  . ILE A 1 204 ? 9.760  -1.415  32.304 1.00 54.63  ? 201 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A 1 204 ? 9.908  -0.490  31.097 1.00 57.33  ? 201 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A 1 204 ? 9.756  -2.872  31.868 1.00 52.65  ? 201 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A 1 204 ? 11.149 -0.745  30.283 1.00 56.17  ? 201 ILE A CD1 1 
ATOM   1562 N  N   . TYR A 1 205 ? 9.078  -1.931  35.287 1.00 56.83  ? 202 TYR A N   1 
ATOM   1563 C  CA  . TYR A 1 205 ? 9.027  -2.878  36.395 1.00 53.92  ? 202 TYR A CA  1 
ATOM   1564 C  C   . TYR A 1 205 ? 7.654  -2.888  37.048 1.00 55.88  ? 202 TYR A C   1 
ATOM   1565 O  O   . TYR A 1 205 ? 7.184  -3.943  37.485 1.00 53.84  ? 202 TYR A O   1 
ATOM   1566 C  CB  . TYR A 1 205 ? 10.120 -2.541  37.423 1.00 53.67  ? 202 TYR A CB  1 
ATOM   1567 C  CG  . TYR A 1 205 ? 10.143 -3.418  38.677 1.00 53.12  ? 202 TYR A CG  1 
ATOM   1568 C  CD1 . TYR A 1 205 ? 10.776 -4.656  38.673 1.00 49.50  ? 202 TYR A CD1 1 
ATOM   1569 C  CD2 . TYR A 1 205 ? 9.544  -2.989  39.872 1.00 53.68  ? 202 TYR A CD2 1 
ATOM   1570 C  CE1 . TYR A 1 205 ? 10.816 -5.460  39.816 1.00 47.66  ? 202 TYR A CE1 1 
ATOM   1571 C  CE2 . TYR A 1 205 ? 9.564  -3.786  41.022 1.00 52.36  ? 202 TYR A CE2 1 
ATOM   1572 C  CZ  . TYR A 1 205 ? 10.200 -5.033  40.981 1.00 53.57  ? 202 TYR A CZ  1 
ATOM   1573 O  OH  . TYR A 1 205 ? 10.219 -5.853  42.105 1.00 48.29  ? 202 TYR A OH  1 
ATOM   1574 N  N   . ASP A 1 206 ? 6.988  -1.735  37.094 1.00 56.53  ? 203 ASP A N   1 
ATOM   1575 C  CA  . ASP A 1 206 ? 5.711  -1.610  37.778 1.00 59.34  ? 203 ASP A CA  1 
ATOM   1576 C  C   . ASP A 1 206 ? 4.517  -2.043  36.930 1.00 59.63  ? 203 ASP A C   1 
ATOM   1577 O  O   . ASP A 1 206 ? 3.459  -2.344  37.495 1.00 61.61  ? 203 ASP A O   1 
ATOM   1578 C  CB  . ASP A 1 206 ? 5.494  -0.159  38.221 1.00 60.36  ? 203 ASP A CB  1 
ATOM   1579 C  CG  . ASP A 1 206 ? 6.192  0.168   39.526 1.00 66.21  ? 203 ASP A CG  1 
ATOM   1580 O  OD1 . ASP A 1 206 ? 6.511  -0.772  40.286 1.00 66.02  ? 203 ASP A OD1 1 
ATOM   1581 O  OD2 . ASP A 1 206 ? 6.402  1.377   39.805 1.00 74.23  ? 203 ASP A OD2 1 
ATOM   1582 N  N   . HIS A 1 207 ? 4.644  -2.069  35.598 1.00 60.45  ? 204 HIS A N   1 
ATOM   1583 C  CA  . HIS A 1 207 ? 3.481  -2.227  34.731 1.00 58.70  ? 204 HIS A CA  1 
ATOM   1584 C  C   . HIS A 1 207 ? 3.411  -3.546  33.966 1.00 57.30  ? 204 HIS A C   1 
ATOM   1585 O  O   . HIS A 1 207 ? 2.328  -3.887  33.484 1.00 58.72  ? 204 HIS A O   1 
ATOM   1586 C  CB  . HIS A 1 207 ? 3.412  -1.072  33.727 1.00 57.86  ? 204 HIS A CB  1 
ATOM   1587 C  CG  . HIS A 1 207 ? 3.011  0.223   34.346 1.00 64.18  ? 204 HIS A CG  1 
ATOM   1588 N  ND1 . HIS A 1 207 ? 3.921  1.079   34.926 1.00 64.47  ? 204 HIS A ND1 1 
ATOM   1589 C  CD2 . HIS A 1 207 ? 1.792  0.795   34.510 1.00 66.73  ? 204 HIS A CD2 1 
ATOM   1590 C  CE1 . HIS A 1 207 ? 3.281  2.132   35.408 1.00 68.48  ? 204 HIS A CE1 1 
ATOM   1591 N  NE2 . HIS A 1 207 ? 1.989  1.985   35.166 1.00 67.73  ? 204 HIS A NE2 1 
ATOM   1592 N  N   . VAL A 1 208 ? 4.517  -4.280  33.813 1.00 52.68  ? 205 VAL A N   1 
ATOM   1593 C  CA  . VAL A 1 208 ? 4.410  -5.626  33.264 1.00 56.96  ? 205 VAL A CA  1 
ATOM   1594 C  C   . VAL A 1 208 ? 3.514  -6.474  34.184 1.00 54.71  ? 205 VAL A C   1 
ATOM   1595 O  O   . VAL A 1 208 ? 3.373  -6.201  35.382 1.00 56.46  ? 205 VAL A O   1 
ATOM   1596 C  CB  . VAL A 1 208 ? 5.794  -6.281  33.079 1.00 54.92  ? 205 VAL A CB  1 
ATOM   1597 C  CG1 . VAL A 1 208 ? 6.618  -5.549  32.046 1.00 48.58  ? 205 VAL A CG1 1 
ATOM   1598 C  CG2 . VAL A 1 208 ? 6.549  -6.366  34.408 1.00 52.58  ? 205 VAL A CG2 1 
ATOM   1599 N  N   . ASP A 1 209 ? 2.885  -7.499  33.616 1.00 54.29  ? 206 ASP A N   1 
ATOM   1600 C  CA  . ASP A 1 209 ? 2.094  -8.450  34.389 1.00 56.37  ? 206 ASP A CA  1 
ATOM   1601 C  C   . ASP A 1 209 ? 2.902  -9.692  34.788 1.00 52.78  ? 206 ASP A C   1 
ATOM   1602 O  O   . ASP A 1 209 ? 2.317  -10.727 35.105 1.00 56.38  ? 206 ASP A O   1 
ATOM   1603 C  CB  . ASP A 1 209 ? 0.838  -8.859  33.608 1.00 54.77  ? 206 ASP A CB  1 
ATOM   1604 C  CG  . ASP A 1 209 ? -0.337 -9.206  34.517 1.00 68.41  ? 206 ASP A CG  1 
ATOM   1605 O  OD1 . ASP A 1 209 ? -0.146 -9.209  35.757 1.00 74.43  ? 206 ASP A OD1 1 
ATOM   1606 O  OD2 . ASP A 1 209 ? -1.457 -9.459  34.000 1.00 72.27  ? 206 ASP A OD2 1 
ATOM   1607 N  N   . SER A 1 210 ? 4.228  -9.610  34.792 1.00 50.47  ? 207 SER A N   1 
ATOM   1608 C  CA  . SER A 1 210 ? 5.025  -10.778 35.132 1.00 53.74  ? 207 SER A CA  1 
ATOM   1609 C  C   . SER A 1 210 ? 4.856  -11.170 36.595 1.00 49.90  ? 207 SER A C   1 
ATOM   1610 O  O   . SER A 1 210 ? 4.701  -10.325 37.480 1.00 47.56  ? 207 SER A O   1 
ATOM   1611 C  CB  . SER A 1 210 ? 6.499  -10.529 34.837 1.00 48.46  ? 207 SER A CB  1 
ATOM   1612 O  OG  . SER A 1 210 ? 6.628  -9.991  33.538 1.00 54.30  ? 207 SER A OG  1 
ATOM   1613 N  N   . ASP A 1 211 ? 4.897  -12.479 36.828 1.00 50.08  ? 208 ASP A N   1 
ATOM   1614 C  CA  . ASP A 1 211 ? 4.886  -13.088 38.146 1.00 51.07  ? 208 ASP A CA  1 
ATOM   1615 C  C   . ASP A 1 211 ? 6.274  -13.210 38.753 1.00 50.32  ? 208 ASP A C   1 
ATOM   1616 O  O   . ASP A 1 211 ? 6.410  -13.669 39.894 1.00 53.55  ? 208 ASP A O   1 
ATOM   1617 C  CB  . ASP A 1 211 ? 4.243  -14.469 38.062 1.00 50.87  ? 208 ASP A CB  1 
ATOM   1618 C  CG  . ASP A 1 211 ? 2.741  -14.397 38.041 1.00 57.73  ? 208 ASP A CG  1 
ATOM   1619 O  OD1 . ASP A 1 211 ? 2.188  -13.267 38.095 1.00 59.96  ? 208 ASP A OD1 1 
ATOM   1620 O  OD2 . ASP A 1 211 ? 2.108  -15.476 38.023 1.00 64.15  ? 208 ASP A OD2 1 
ATOM   1621 N  N   . ASP A 1 212 ? 7.298  -12.782 38.031 1.00 46.65  ? 209 ASP A N   1 
ATOM   1622 C  CA  . ASP A 1 212 ? 8.681  -13.019 38.423 1.00 50.84  ? 209 ASP A CA  1 
ATOM   1623 C  C   . ASP A 1 212 ? 9.478  -11.838 37.875 1.00 49.27  ? 209 ASP A C   1 
ATOM   1624 O  O   . ASP A 1 212 ? 9.767  -11.798 36.676 1.00 45.62  ? 209 ASP A O   1 
ATOM   1625 C  CB  . ASP A 1 212 ? 9.158  -14.356 37.863 1.00 47.61  ? 209 ASP A CB  1 
ATOM   1626 C  CG  . ASP A 1 212 ? 10.582 -14.698 38.254 1.00 51.84  ? 209 ASP A CG  1 
ATOM   1627 O  OD1 . ASP A 1 212 ? 11.275 -13.856 38.870 1.00 53.36  ? 209 ASP A OD1 1 
ATOM   1628 O  OD2 . ASP A 1 212 ? 11.021 -15.820 37.906 1.00 53.78  ? 209 ASP A OD2 1 
ATOM   1629 N  N   . LYS A 1 213 ? 9.814  -10.875 38.735 1.00 49.81  ? 210 LYS A N   1 
ATOM   1630 C  CA  . LYS A 1 213 ? 10.482 -9.691  38.207 1.00 48.37  ? 210 LYS A CA  1 
ATOM   1631 C  C   . LYS A 1 213 ? 11.504 -9.134  39.186 1.00 46.34  ? 210 LYS A C   1 
ATOM   1632 O  O   . LYS A 1 213 ? 11.477 -9.406  40.382 1.00 48.52  ? 210 LYS A O   1 
ATOM   1633 C  CB  . LYS A 1 213 ? 9.474  -8.608  37.812 1.00 44.72  ? 210 LYS A CB  1 
ATOM   1634 C  CG  . LYS A 1 213 ? 8.533  -8.168  38.899 1.00 49.78  ? 210 LYS A CG  1 
ATOM   1635 C  CD  . LYS A 1 213 ? 7.353  -7.453  38.269 1.00 50.56  ? 210 LYS A CD  1 
ATOM   1636 C  CE  . LYS A 1 213 ? 6.635  -6.568  39.249 1.00 51.77  ? 210 LYS A CE  1 
ATOM   1637 N  NZ  . LYS A 1 213 ? 5.433  -5.987  38.606 1.00 52.81  ? 210 LYS A NZ  1 
ATOM   1638 N  N   . ASN A 1 214 ? 12.361 -8.278  38.655 1.00 60.82  ? 211 ASN A N   1 
ATOM   1639 C  CA  . ASN A 1 214 ? 13.634 -7.919  39.250 1.00 61.43  ? 211 ASN A CA  1 
ATOM   1640 C  C   . ASN A 1 214 ? 14.090 -6.622  38.601 1.00 61.69  ? 211 ASN A C   1 
ATOM   1641 O  O   . ASN A 1 214 ? 14.025 -6.503  37.376 1.00 61.40  ? 211 ASN A O   1 
ATOM   1642 C  CB  . ASN A 1 214 ? 14.668 -9.018  38.975 1.00 61.99  ? 211 ASN A CB  1 
ATOM   1643 C  CG  . ASN A 1 214 ? 15.677 -9.166  40.078 1.00 69.39  ? 211 ASN A CG  1 
ATOM   1644 O  OD1 . ASN A 1 214 ? 16.313 -10.215 40.194 1.00 74.97  ? 211 ASN A OD1 1 
ATOM   1645 N  ND2 . ASN A 1 214 ? 15.819 -8.126  40.929 1.00 69.76  ? 211 ASN A ND2 1 
ATOM   1646 N  N   . ILE A 1 215 ? 14.578 -5.669  39.397 1.00 52.74  ? 212 ILE A N   1 
ATOM   1647 C  CA  . ILE A 1 215 ? 15.138 -4.446  38.832 1.00 50.86  ? 212 ILE A CA  1 
ATOM   1648 C  C   . ILE A 1 215 ? 16.469 -4.133  39.518 1.00 54.62  ? 212 ILE A C   1 
ATOM   1649 O  O   . ILE A 1 215 ? 16.569 -4.189  40.751 1.00 53.55  ? 212 ILE A O   1 
ATOM   1650 C  CB  . ILE A 1 215 ? 14.144 -3.266  38.929 1.00 55.93  ? 212 ILE A CB  1 
ATOM   1651 C  CG1 . ILE A 1 215 ? 14.760 -1.989  38.348 1.00 56.42  ? 212 ILE A CG1 1 
ATOM   1652 C  CG2 . ILE A 1 215 ? 13.657 -3.040  40.370 1.00 52.61  ? 212 ILE A CG2 1 
ATOM   1653 C  CD1 . ILE A 1 215 ? 13.767 -0.847  38.153 1.00 57.86  ? 212 ILE A CD1 1 
ATOM   1654 N  N   . LYS A 1 216 ? 17.493 -3.805  38.717 1.00 51.66  ? 213 LYS A N   1 
ATOM   1655 C  CA  . LYS A 1 216 ? 18.828 -3.470  39.217 1.00 57.72  ? 213 LYS A CA  1 
ATOM   1656 C  C   . LYS A 1 216 ? 19.276 -2.114  38.669 1.00 55.15  ? 213 LYS A C   1 
ATOM   1657 O  O   . LYS A 1 216 ? 19.118 -1.832  37.478 1.00 55.68  ? 213 LYS A O   1 
ATOM   1658 C  CB  . LYS A 1 216 ? 19.897 -4.540  38.832 1.00 57.30  ? 213 LYS A CB  1 
ATOM   1659 C  CG  . LYS A 1 216 ? 19.818 -5.895  39.526 1.00 52.61  ? 213 LYS A CG  1 
ATOM   1660 C  CD  . LYS A 1 216 ? 20.147 -5.794  40.988 1.00 69.05  ? 213 LYS A CD  1 
ATOM   1661 C  CE  . LYS A 1 216 ? 20.930 -7.016  41.508 1.00 78.75  ? 213 LYS A CE  1 
ATOM   1662 N  NZ  . LYS A 1 216 ? 20.309 -8.297  41.061 1.00 79.43  ? 213 LYS A NZ  1 
ATOM   1663 N  N   . TRP A 1 217 ? 19.894 -1.312  39.530 1.00 53.89  ? 214 TRP A N   1 
ATOM   1664 C  CA  . TRP A 1 217 ? 20.340 0.045   39.247 1.00 54.72  ? 214 TRP A CA  1 
ATOM   1665 C  C   . TRP A 1 217 ? 21.862 0.153   39.354 1.00 65.57  ? 214 TRP A C   1 
ATOM   1666 O  O   . TRP A 1 217 ? 22.460 -0.325  40.328 1.00 65.02  ? 214 TRP A O   1 
ATOM   1667 C  CB  . TRP A 1 217 ? 19.725 1.030   40.251 1.00 59.43  ? 214 TRP A CB  1 
ATOM   1668 C  CG  . TRP A 1 217 ? 18.243 1.155   40.195 1.00 64.68  ? 214 TRP A CG  1 
ATOM   1669 C  CD1 . TRP A 1 217 ? 17.326 0.494   40.970 1.00 63.63  ? 214 TRP A CD1 1 
ATOM   1670 C  CD2 . TRP A 1 217 ? 17.492 2.014   39.329 1.00 65.23  ? 214 TRP A CD2 1 
ATOM   1671 N  NE1 . TRP A 1 217 ? 16.049 0.892   40.638 1.00 64.01  ? 214 TRP A NE1 1 
ATOM   1672 C  CE2 . TRP A 1 217 ? 16.123 1.821   39.631 1.00 63.90  ? 214 TRP A CE2 1 
ATOM   1673 C  CE3 . TRP A 1 217 ? 17.846 2.934   38.331 1.00 65.27  ? 214 TRP A CE3 1 
ATOM   1674 C  CZ2 . TRP A 1 217 ? 15.109 2.510   38.967 1.00 63.56  ? 214 TRP A CZ2 1 
ATOM   1675 C  CZ3 . TRP A 1 217 ? 16.840 3.618   37.679 1.00 67.73  ? 214 TRP A CZ3 1 
ATOM   1676 C  CH2 . TRP A 1 217 ? 15.486 3.398   37.993 1.00 66.64  ? 214 TRP A CH2 1 
ATOM   1677 N  N   . TYR A 1 218 ? 22.487 0.847   38.397 1.00 69.80  ? 215 TYR A N   1 
ATOM   1678 C  CA  . TYR A 1 218 ? 23.941 0.993   38.352 1.00 69.44  ? 215 TYR A CA  1 
ATOM   1679 C  C   . TYR A 1 218 ? 24.303 2.467   38.393 1.00 76.22  ? 215 TYR A C   1 
ATOM   1680 O  O   . TYR A 1 218 ? 23.881 3.239   37.526 1.00 76.28  ? 215 TYR A O   1 
ATOM   1681 C  CB  . TYR A 1 218 ? 24.510 0.320   37.105 1.00 72.79  ? 215 TYR A CB  1 
ATOM   1682 C  CG  . TYR A 1 218 ? 24.138 -1.128  37.093 1.00 68.23  ? 215 TYR A CG  1 
ATOM   1683 C  CD1 . TYR A 1 218 ? 22.910 -1.543  36.588 1.00 59.56  ? 215 TYR A CD1 1 
ATOM   1684 C  CD2 . TYR A 1 218 ? 24.987 -2.084  37.645 1.00 69.53  ? 215 TYR A CD2 1 
ATOM   1685 C  CE1 . TYR A 1 218 ? 22.546 -2.885  36.605 1.00 60.49  ? 215 TYR A CE1 1 
ATOM   1686 C  CE2 . TYR A 1 218 ? 24.637 -3.427  37.666 1.00 64.63  ? 215 TYR A CE2 1 
ATOM   1687 C  CZ  . TYR A 1 218 ? 23.414 -3.818  37.147 1.00 61.13  ? 215 TYR A CZ  1 
ATOM   1688 O  OH  . TYR A 1 218 ? 23.071 -5.145  37.162 1.00 58.83  ? 215 TYR A OH  1 
ATOM   1689 N  N   . SER A 1 219 ? 25.112 2.838   39.380 1.00 81.32  ? 216 SER A N   1 
ATOM   1690 C  CA  . SER A 1 219 ? 25.312 4.217   39.792 1.00 84.64  ? 216 SER A CA  1 
ATOM   1691 C  C   . SER A 1 219 ? 26.468 4.914   39.089 1.00 90.69  ? 216 SER A C   1 
ATOM   1692 O  O   . SER A 1 219 ? 26.630 6.130   39.263 1.00 89.92  ? 216 SER A O   1 
ATOM   1693 C  CB  . SER A 1 219 ? 25.573 4.260   41.294 1.00 92.51  ? 216 SER A CB  1 
ATOM   1694 O  OG  . SER A 1 219 ? 26.809 3.630   41.579 1.00 91.71  ? 216 SER A OG  1 
ATOM   1695 N  N   . GLU A 1 220 ? 27.291 4.188   38.333 1.00 88.15  ? 217 GLU A N   1 
ATOM   1696 C  CA  . GLU A 1 220 ? 28.477 4.777   37.735 1.00 89.10  ? 217 GLU A CA  1 
ATOM   1697 C  C   . GLU A 1 220 ? 28.540 4.617   36.223 1.00 88.22  ? 217 GLU A C   1 
ATOM   1698 O  O   . GLU A 1 220 ? 29.533 5.037   35.615 1.00 89.49  ? 217 GLU A O   1 
ATOM   1699 C  CB  . GLU A 1 220 ? 29.750 4.178   38.358 1.00 90.15  ? 217 GLU A CB  1 
ATOM   1700 C  CG  . GLU A 1 220 ? 29.703 3.972   39.875 1.00 96.59  ? 217 GLU A CG  1 
ATOM   1701 C  CD  . GLU A 1 220 ? 30.110 5.219   40.658 1.00 104.50 ? 217 GLU A CD  1 
ATOM   1702 O  OE1 . GLU A 1 220 ? 31.029 5.937   40.202 1.00 108.37 ? 217 GLU A OE1 1 
ATOM   1703 O  OE2 . GLU A 1 220 ? 29.520 5.474   41.738 1.00 104.72 ? 217 GLU A OE2 1 
ATOM   1704 N  N   . SER A 1 221 ? 27.528 4.038   35.597 1.00 77.76  ? 218 SER A N   1 
ATOM   1705 C  CA  . SER A 1 221 ? 27.576 3.755   34.173 1.00 78.73  ? 218 SER A CA  1 
ATOM   1706 C  C   . SER A 1 221 ? 26.827 4.818   33.383 1.00 78.83  ? 218 SER A C   1 
ATOM   1707 O  O   . SER A 1 221 ? 26.018 5.575   33.925 1.00 82.41  ? 218 SER A O   1 
ATOM   1708 C  CB  . SER A 1 221 ? 26.981 2.375   33.879 1.00 77.01  ? 218 SER A CB  1 
ATOM   1709 O  OG  . SER A 1 221 ? 27.457 1.430   34.814 1.00 78.38  ? 218 SER A OG  1 
ATOM   1710 N  N   . GLY A 1 222 ? 27.106 4.853   32.078 1.00 76.93  ? 219 GLY A N   1 
ATOM   1711 C  CA  . GLY A 1 222 ? 26.346 5.643   31.128 1.00 74.91  ? 219 GLY A CA  1 
ATOM   1712 C  C   . GLY A 1 222 ? 25.245 4.832   30.470 1.00 70.27  ? 219 GLY A C   1 
ATOM   1713 O  O   . GLY A 1 222 ? 24.876 3.747   30.928 1.00 71.06  ? 219 GLY A O   1 
ATOM   1714 N  N   . HIS A 1 223 ? 24.723 5.370   29.361 1.00 73.90  ? 220 HIS A N   1 
ATOM   1715 C  CA  . HIS A 1 223 ? 23.570 4.755   28.707 1.00 67.99  ? 220 HIS A CA  1 
ATOM   1716 C  C   . HIS A 1 223 ? 23.940 3.452   27.997 1.00 67.91  ? 220 HIS A C   1 
ATOM   1717 O  O   . HIS A 1 223 ? 23.176 2.480   28.047 1.00 64.63  ? 220 HIS A O   1 
ATOM   1718 C  CB  . HIS A 1 223 ? 22.935 5.737   27.722 1.00 72.66  ? 220 HIS A CB  1 
ATOM   1719 C  CG  . HIS A 1 223 ? 21.745 5.173   27.003 1.00 73.41  ? 220 HIS A CG  1 
ATOM   1720 N  ND1 . HIS A 1 223 ? 20.579 4.821   27.651 1.00 72.82  ? 220 HIS A ND1 1 
ATOM   1721 C  CD2 . HIS A 1 223 ? 21.549 4.883   25.695 1.00 66.84  ? 220 HIS A CD2 1 
ATOM   1722 C  CE1 . HIS A 1 223 ? 19.715 4.344   26.772 1.00 70.56  ? 220 HIS A CE1 1 
ATOM   1723 N  NE2 . HIS A 1 223 ? 20.279 4.371   25.578 1.00 63.32  ? 220 HIS A NE2 1 
ATOM   1724 N  N   . VAL A 1 224 ? 25.089 3.407   27.316 1.00 68.07  ? 221 VAL A N   1 
ATOM   1725 C  CA  . VAL A 1 224 ? 25.537 2.177   26.660 1.00 64.87  ? 221 VAL A CA  1 
ATOM   1726 C  C   . VAL A 1 224 ? 26.181 1.286   27.713 1.00 65.70  ? 221 VAL A C   1 
ATOM   1727 O  O   . VAL A 1 224 ? 27.411 1.151   27.758 1.00 64.47  ? 221 VAL A O   1 
ATOM   1728 C  CB  . VAL A 1 224 ? 26.508 2.482   25.510 1.00 69.09  ? 221 VAL A CB  1 
ATOM   1729 C  CG1 . VAL A 1 224 ? 26.873 1.205   24.758 1.00 71.87  ? 221 VAL A CG1 1 
ATOM   1730 C  CG2 . VAL A 1 224 ? 25.875 3.466   24.583 1.00 71.00  ? 221 VAL A CG2 1 
ATOM   1731 N  N   . ILE A 1 225 ? 25.345 0.667   28.559 1.00 64.11  ? 222 ILE A N   1 
ATOM   1732 C  CA  . ILE A 1 225 ? 25.818 0.118   29.828 1.00 64.74  ? 222 ILE A CA  1 
ATOM   1733 C  C   . ILE A 1 225 ? 26.687 -1.120  29.617 1.00 64.48  ? 222 ILE A C   1 
ATOM   1734 O  O   . ILE A 1 225 ? 27.612 -1.375  30.402 1.00 65.86  ? 222 ILE A O   1 
ATOM   1735 C  CB  . ILE A 1 225 ? 24.623 -0.160  30.773 1.00 64.82  ? 222 ILE A CB  1 
ATOM   1736 C  CG1 . ILE A 1 225 ? 25.117 -0.446  32.202 1.00 60.86  ? 222 ILE A CG1 1 
ATOM   1737 C  CG2 . ILE A 1 225 ? 23.738 -1.308  30.255 1.00 59.64  ? 222 ILE A CG2 1 
ATOM   1738 C  CD1 . ILE A 1 225 ? 24.056 -0.336  33.259 1.00 62.52  ? 222 ILE A CD1 1 
ATOM   1739 N  N   . THR A 1 226 ? 26.427 -1.894  28.559 1.00 64.79  ? 223 THR A N   1 
ATOM   1740 C  CA  . THR A 1 226 ? 27.164 -3.117  28.243 1.00 61.06  ? 223 THR A CA  1 
ATOM   1741 C  C   . THR A 1 226 ? 28.614 -2.866  27.843 1.00 62.54  ? 223 THR A C   1 
ATOM   1742 O  O   . THR A 1 226 ? 29.327 -3.839  27.587 1.00 66.44  ? 223 THR A O   1 
ATOM   1743 C  CB  . THR A 1 226 ? 26.458 -3.868  27.111 1.00 60.07  ? 223 THR A CB  1 
ATOM   1744 O  OG1 . THR A 1 226 ? 26.282 -2.966  26.013 1.00 67.06  ? 223 THR A OG1 1 
ATOM   1745 C  CG2 . THR A 1 226 ? 25.086 -4.355  27.542 1.00 49.98  ? 223 THR A CG2 1 
ATOM   1746 N  N   . ILE A 1 227 ? 29.081 -1.618  27.754 1.00 60.89  ? 224 ILE A N   1 
ATOM   1747 C  CA  . ILE A 1 227 ? 30.489 -1.382  27.441 1.00 69.36  ? 224 ILE A CA  1 
ATOM   1748 C  C   . ILE A 1 227 ? 31.129 -0.396  28.413 1.00 71.57  ? 224 ILE A C   1 
ATOM   1749 O  O   . ILE A 1 227 ? 32.288 -0.011  28.228 1.00 62.92  ? 224 ILE A O   1 
ATOM   1750 C  CB  . ILE A 1 227 ? 30.682 -0.881  25.991 1.00 68.47  ? 224 ILE A CB  1 
ATOM   1751 C  CG1 . ILE A 1 227 ? 30.277 0.594   25.883 1.00 68.49  ? 224 ILE A CG1 1 
ATOM   1752 C  CG2 . ILE A 1 227 ? 29.934 -1.759  24.982 1.00 65.29  ? 224 ILE A CG2 1 
ATOM   1753 C  CD1 . ILE A 1 227 ? 30.542 1.205   24.535 1.00 61.88  ? 224 ILE A CD1 1 
ATOM   1754 N  N   . ASP A 1 228 ? 30.399 0.012   29.455 1.00 68.90  ? 225 ASP A N   1 
ATOM   1755 C  CA  . ASP A 1 228 ? 30.909 1.002   30.398 1.00 69.60  ? 225 ASP A CA  1 
ATOM   1756 C  C   . ASP A 1 228 ? 31.677 0.303   31.523 1.00 74.86  ? 225 ASP A C   1 
ATOM   1757 O  O   . ASP A 1 228 ? 31.908 -0.911  31.484 1.00 73.60  ? 225 ASP A O   1 
ATOM   1758 C  CB  . ASP A 1 228 ? 29.772 1.859   30.951 1.00 73.85  ? 225 ASP A CB  1 
ATOM   1759 C  CG  . ASP A 1 228 ? 30.115 3.335   31.007 1.00 79.29  ? 225 ASP A CG  1 
ATOM   1760 O  OD1 . ASP A 1 228 ? 31.278 3.698   31.323 1.00 85.58  ? 225 ASP A OD1 1 
ATOM   1761 O  OD2 . ASP A 1 228 ? 29.199 4.145   30.743 1.00 78.50  ? 225 ASP A OD2 1 
ATOM   1762 N  N   . LYS A 1 229 ? 32.054 1.071   32.559 1.00 77.84  ? 226 LYS A N   1 
ATOM   1763 C  CA  . LYS A 1 229 ? 32.990 0.594   33.580 1.00 78.44  ? 226 LYS A CA  1 
ATOM   1764 C  C   . LYS A 1 229 ? 32.408 -0.481  34.492 1.00 77.15  ? 226 LYS A C   1 
ATOM   1765 O  O   . LYS A 1 229 ? 33.179 -1.227  35.111 1.00 76.93  ? 226 LYS A O   1 
ATOM   1766 C  CB  . LYS A 1 229 ? 33.493 1.769   34.427 1.00 86.22  ? 226 LYS A CB  1 
ATOM   1767 C  CG  . LYS A 1 229 ? 32.446 2.839   34.766 1.00 86.42  ? 226 LYS A CG  1 
ATOM   1768 C  CD  . LYS A 1 229 ? 33.118 4.174   35.165 1.00 87.06  ? 226 LYS A CD  1 
ATOM   1769 C  CE  . LYS A 1 229 ? 33.981 4.029   36.416 1.00 86.67  ? 226 LYS A CE  1 
ATOM   1770 N  NZ  . LYS A 1 229 ? 35.098 5.033   36.508 1.00 108.75 ? 226 LYS A NZ  1 
ATOM   1771 N  N   . GLU A 1 230 ? 31.083 -0.597  34.581 1.00 77.86  ? 227 GLU A N   1 
ATOM   1772 C  CA  . GLU A 1 230 ? 30.463 -1.551  35.488 1.00 76.32  ? 227 GLU A CA  1 
ATOM   1773 C  C   . GLU A 1 230 ? 29.977 -2.802  34.774 1.00 71.38  ? 227 GLU A C   1 
ATOM   1774 O  O   . GLU A 1 230 ? 29.155 -3.539  35.331 1.00 68.83  ? 227 GLU A O   1 
ATOM   1775 C  CB  . GLU A 1 230 ? 29.303 -0.890  36.244 1.00 75.32  ? 227 GLU A CB  1 
ATOM   1776 C  CG  . GLU A 1 230 ? 29.719 0.208   37.246 1.00 73.83  ? 227 GLU A CG  1 
ATOM   1777 C  CD  . GLU A 1 230 ? 28.534 0.748   38.032 1.00 80.14  ? 227 GLU A CD  1 
ATOM   1778 O  OE1 . GLU A 1 230 ? 27.700 1.478   37.448 1.00 80.17  ? 227 GLU A OE1 1 
ATOM   1779 O  OE2 . GLU A 1 230 ? 28.426 0.437   39.236 1.00 82.86  ? 227 GLU A OE2 1 
ATOM   1780 N  N   . LYS A 1 231 ? 30.497 -3.075  33.570 1.00 67.04  ? 228 LYS A N   1 
ATOM   1781 C  CA  . LYS A 1 231 ? 29.860 -4.055  32.690 1.00 71.32  ? 228 LYS A CA  1 
ATOM   1782 C  C   . LYS A 1 231 ? 29.980 -5.484  33.221 1.00 66.17  ? 228 LYS A C   1 
ATOM   1783 O  O   . LYS A 1 231 ? 29.029 -6.265  33.091 1.00 61.85  ? 228 LYS A O   1 
ATOM   1784 C  CB  . LYS A 1 231 ? 30.425 -3.936  31.264 1.00 69.15  ? 228 LYS A CB  1 
ATOM   1785 C  CG  . LYS A 1 231 ? 31.853 -4.415  31.050 1.00 71.46  ? 228 LYS A CG  1 
ATOM   1786 C  CD  . LYS A 1 231 ? 32.368 -4.019  29.676 1.00 66.06  ? 228 LYS A CD  1 
ATOM   1787 C  CE  . LYS A 1 231 ? 33.593 -3.132  29.795 1.00 74.84  ? 228 LYS A CE  1 
ATOM   1788 N  NZ  . LYS A 1 231 ? 34.812 -3.902  30.134 1.00 80.41  ? 228 LYS A NZ  1 
ATOM   1789 N  N   . GLU A 1 232 ? 31.105 -5.829  33.852 1.00 65.72  ? 229 GLU A N   1 
ATOM   1790 C  CA  . GLU A 1 232 ? 31.262 -7.161  34.429 1.00 66.30  ? 229 GLU A CA  1 
ATOM   1791 C  C   . GLU A 1 232 ? 30.219 -7.433  35.512 1.00 69.32  ? 229 GLU A C   1 
ATOM   1792 O  O   . GLU A 1 232 ? 29.694 -8.551  35.608 1.00 66.52  ? 229 GLU A O   1 
ATOM   1793 C  CB  . GLU A 1 232 ? 32.664 -7.313  35.007 1.00 70.14  ? 229 GLU A CB  1 
ATOM   1794 C  CG  . GLU A 1 232 ? 33.791 -7.183  33.998 1.00 81.69  ? 229 GLU A CG  1 
ATOM   1795 C  CD  . GLU A 1 232 ? 34.428 -5.800  34.033 1.00 89.66  ? 229 GLU A CD  1 
ATOM   1796 O  OE1 . GLU A 1 232 ? 35.528 -5.637  33.459 1.00 100.22 ? 229 GLU A OE1 1 
ATOM   1797 O  OE2 . GLU A 1 232 ? 33.820 -4.863  34.605 1.00 90.39  ? 229 GLU A OE2 1 
ATOM   1798 N  N   . GLN A 1 233 ? 29.927 -6.436  36.355 1.00 64.81  ? 230 GLN A N   1 
ATOM   1799 C  CA  . GLN A 1 233 ? 28.822 -6.576  37.299 1.00 67.91  ? 230 GLN A CA  1 
ATOM   1800 C  C   . GLN A 1 233 ? 27.499 -6.829  36.580 1.00 65.77  ? 230 GLN A C   1 
ATOM   1801 O  O   . GLN A 1 233 ? 26.696 -7.662  37.020 1.00 60.26  ? 230 GLN A O   1 
ATOM   1802 C  CB  . GLN A 1 233 ? 28.700 -5.331  38.173 1.00 71.85  ? 230 GLN A CB  1 
ATOM   1803 C  CG  . GLN A 1 233 ? 27.876 -5.533  39.454 1.00 81.23  ? 230 GLN A CG  1 
ATOM   1804 C  CD  . GLN A 1 233 ? 28.219 -6.810  40.224 1.00 86.60  ? 230 GLN A CD  1 
ATOM   1805 O  OE1 . GLN A 1 233 ? 27.317 -7.549  40.658 1.00 87.10  ? 230 GLN A OE1 1 
ATOM   1806 N  NE2 . GLN A 1 233 ? 29.519 -7.032  40.466 1.00 83.62  ? 230 GLN A NE2 1 
ATOM   1807 N  N   . VAL A 1 234 ? 27.246 -6.103  35.486 1.00 62.68  ? 231 VAL A N   1 
ATOM   1808 C  CA  . VAL A 1 234 ? 25.990 -6.262  34.762 1.00 60.07  ? 231 VAL A CA  1 
ATOM   1809 C  C   . VAL A 1 234 ? 25.913 -7.648  34.134 1.00 60.25  ? 231 VAL A C   1 
ATOM   1810 O  O   . VAL A 1 234 ? 24.852 -8.291  34.152 1.00 53.92  ? 231 VAL A O   1 
ATOM   1811 C  CB  . VAL A 1 234 ? 25.827 -5.152  33.705 1.00 61.90  ? 231 VAL A CB  1 
ATOM   1812 C  CG1 . VAL A 1 234 ? 24.550 -5.344  32.930 1.00 55.14  ? 231 VAL A CG1 1 
ATOM   1813 C  CG2 . VAL A 1 234 ? 25.841 -3.778  34.348 1.00 60.47  ? 231 VAL A CG2 1 
ATOM   1814 N  N   . PHE A 1 235 ? 27.031 -8.133  33.573 1.00 59.28  ? 232 PHE A N   1 
ATOM   1815 C  CA  . PHE A 1 235 ? 27.054 -9.486  33.007 1.00 61.03  ? 232 PHE A CA  1 
ATOM   1816 C  C   . PHE A 1 235 ? 26.689 -10.520 34.070 1.00 60.73  ? 232 PHE A C   1 
ATOM   1817 O  O   . PHE A 1 235 ? 25.859 -11.410 33.843 1.00 54.17  ? 232 PHE A O   1 
ATOM   1818 C  CB  . PHE A 1 235 ? 28.433 -9.824  32.417 1.00 54.53  ? 232 PHE A CB  1 
ATOM   1819 C  CG  . PHE A 1 235 ? 28.879 -8.920  31.285 1.00 58.42  ? 232 PHE A CG  1 
ATOM   1820 C  CD1 . PHE A 1 235 ? 27.998 -8.022  30.677 1.00 58.51  ? 232 PHE A CD1 1 
ATOM   1821 C  CD2 . PHE A 1 235 ? 30.199 -8.969  30.831 1.00 56.87  ? 232 PHE A CD2 1 
ATOM   1822 C  CE1 . PHE A 1 235 ? 28.427 -7.194  29.640 1.00 53.00  ? 232 PHE A CE1 1 
ATOM   1823 C  CE2 . PHE A 1 235 ? 30.630 -8.141  29.802 1.00 57.69  ? 232 PHE A CE2 1 
ATOM   1824 C  CZ  . PHE A 1 235 ? 29.734 -7.252  29.207 1.00 55.66  ? 232 PHE A CZ  1 
ATOM   1825 N  N   . GLU A 1 236 ? 27.294 -10.406 35.246 1.00 59.91  ? 233 GLU A N   1 
ATOM   1826 C  CA  . GLU A 1 236 ? 27.058 -11.392 36.288 1.00 63.45  ? 233 GLU A CA  1 
ATOM   1827 C  C   . GLU A 1 236 ? 25.599 -11.409 36.749 1.00 58.59  ? 233 GLU A C   1 
ATOM   1828 O  O   . GLU A 1 236 ? 25.044 -12.480 37.031 1.00 58.65  ? 233 GLU A O   1 
ATOM   1829 C  CB  . GLU A 1 236 ? 27.994 -11.118 37.454 1.00 64.84  ? 233 GLU A CB  1 
ATOM   1830 C  CG  . GLU A 1 236 ? 27.871 -12.134 38.515 1.00 69.20  ? 233 GLU A CG  1 
ATOM   1831 C  CD  . GLU A 1 236 ? 28.729 -13.332 38.194 1.00 84.45  ? 233 GLU A CD  1 
ATOM   1832 O  OE1 . GLU A 1 236 ? 29.723 -13.167 37.419 1.00 82.37  ? 233 GLU A OE1 1 
ATOM   1833 O  OE2 . GLU A 1 236 ? 28.411 -14.429 38.726 1.00 87.67  ? 233 GLU A OE2 1 
ATOM   1834 N  N   . ASP A 1 237 ? 24.963 -10.239 36.845 1.00 52.81  ? 234 ASP A N   1 
ATOM   1835 C  CA  . ASP A 1 237 ? 23.571 -10.211 37.282 1.00 57.78  ? 234 ASP A CA  1 
ATOM   1836 C  C   . ASP A 1 237 ? 22.654 -10.829 36.236 1.00 54.03  ? 234 ASP A C   1 
ATOM   1837 O  O   . ASP A 1 237 ? 21.617 -11.398 36.583 1.00 54.68  ? 234 ASP A O   1 
ATOM   1838 C  CB  . ASP A 1 237 ? 23.123 -8.784  37.568 1.00 58.90  ? 234 ASP A CB  1 
ATOM   1839 C  CG  . ASP A 1 237 ? 23.747 -8.210  38.803 1.00 60.83  ? 234 ASP A CG  1 
ATOM   1840 O  OD1 . ASP A 1 237 ? 24.155 -8.977  39.712 1.00 67.61  ? 234 ASP A OD1 1 
ATOM   1841 O  OD2 . ASP A 1 237 ? 23.831 -6.967  38.862 1.00 62.40  ? 234 ASP A OD2 1 
ATOM   1842 N  N   . ILE A 1 238 ? 23.013 -10.703 34.961 1.00 53.43  ? 235 ILE A N   1 
ATOM   1843 C  CA  . ILE A 1 238 ? 22.287 -11.357 33.882 1.00 52.39  ? 235 ILE A CA  1 
ATOM   1844 C  C   . ILE A 1 238 ? 22.396 -12.874 34.002 1.00 51.29  ? 235 ILE A C   1 
ATOM   1845 O  O   . ILE A 1 238 ? 21.401 -13.606 33.841 1.00 46.55  ? 235 ILE A O   1 
ATOM   1846 C  CB  . ILE A 1 238 ? 22.815 -10.844 32.527 1.00 46.00  ? 235 ILE A CB  1 
ATOM   1847 C  CG1 . ILE A 1 238 ? 22.436 -9.377  32.347 1.00 47.20  ? 235 ILE A CG1 1 
ATOM   1848 C  CG2 . ILE A 1 238 ? 22.306 -11.696 31.366 1.00 42.17  ? 235 ILE A CG2 1 
ATOM   1849 C  CD1 . ILE A 1 238 ? 22.927 -8.757  31.063 1.00 45.16  ? 235 ILE A CD1 1 
ATOM   1850 N  N   . TYR A 1 239 ? 23.603 -13.365 34.275 1.00 50.30  ? 236 TYR A N   1 
ATOM   1851 C  CA  . TYR A 1 239 ? 23.825 -14.791 34.495 1.00 52.23  ? 236 TYR A CA  1 
ATOM   1852 C  C   . TYR A 1 239 ? 22.991 -15.313 35.660 1.00 50.79  ? 236 TYR A C   1 
ATOM   1853 O  O   . TYR A 1 239 ? 22.350 -16.362 35.544 1.00 47.42  ? 236 TYR A O   1 
ATOM   1854 C  CB  . TYR A 1 239 ? 25.318 -15.035 34.750 1.00 55.20  ? 236 TYR A CB  1 
ATOM   1855 C  CG  . TYR A 1 239 ? 25.685 -16.457 35.086 1.00 47.84  ? 236 TYR A CG  1 
ATOM   1856 C  CD1 . TYR A 1 239 ? 25.577 -17.466 34.141 1.00 47.36  ? 236 TYR A CD1 1 
ATOM   1857 C  CD2 . TYR A 1 239 ? 26.149 -16.787 36.337 1.00 53.01  ? 236 TYR A CD2 1 
ATOM   1858 C  CE1 . TYR A 1 239 ? 25.923 -18.768 34.439 1.00 51.04  ? 236 TYR A CE1 1 
ATOM   1859 C  CE2 . TYR A 1 239 ? 26.498 -18.092 36.655 1.00 53.11  ? 236 TYR A CE2 1 
ATOM   1860 C  CZ  . TYR A 1 239 ? 26.377 -19.074 35.703 1.00 54.86  ? 236 TYR A CZ  1 
ATOM   1861 O  OH  . TYR A 1 239 ? 26.738 -20.361 36.020 1.00 62.28  ? 236 TYR A OH  1 
ATOM   1862 N  N   . GLN A 1 240 ? 23.038 -14.622 36.815 1.00 55.48  ? 237 GLN A N   1 
ATOM   1863 C  CA  . GLN A 1 240 ? 22.195 -14.964 37.971 1.00 56.14  ? 237 GLN A CA  1 
ATOM   1864 C  C   . GLN A 1 240 ? 20.735 -15.168 37.555 1.00 51.75  ? 237 GLN A C   1 
ATOM   1865 O  O   . GLN A 1 240 ? 20.085 -16.137 37.959 1.00 51.94  ? 237 GLN A O   1 
ATOM   1866 C  CB  . GLN A 1 240 ? 22.258 -13.850 39.024 1.00 63.65  ? 237 GLN A CB  1 
ATOM   1867 C  CG  . GLN A 1 240 ? 23.457 -13.760 39.998 1.00 71.05  ? 237 GLN A CG  1 
ATOM   1868 C  CD  . GLN A 1 240 ? 24.203 -15.066 40.256 1.00 83.05  ? 237 GLN A CD  1 
ATOM   1869 O  OE1 . GLN A 1 240 ? 23.657 -15.993 40.866 1.00 89.75  ? 237 GLN A OE1 1 
ATOM   1870 N  NE2 . GLN A 1 240 ? 25.476 -15.121 39.850 1.00 75.05  ? 237 GLN A NE2 1 
ATOM   1871 N  N   . PHE A 1 241 ? 20.208 -14.240 36.753 1.00 44.58  ? 238 PHE A N   1 
ATOM   1872 C  CA  . PHE A 1 241 ? 18.829 -14.310 36.263 1.00 49.91  ? 238 PHE A CA  1 
ATOM   1873 C  C   . PHE A 1 241 ? 18.599 -15.550 35.397 1.00 51.62  ? 238 PHE A C   1 
ATOM   1874 O  O   . PHE A 1 241 ? 17.621 -16.286 35.592 1.00 48.41  ? 238 PHE A O   1 
ATOM   1875 C  CB  . PHE A 1 241 ? 18.509 -13.030 35.470 1.00 46.51  ? 238 PHE A CB  1 
ATOM   1876 C  CG  . PHE A 1 241 ? 17.170 -13.045 34.802 1.00 46.54  ? 238 PHE A CG  1 
ATOM   1877 C  CD1 . PHE A 1 241 ? 15.997 -12.997 35.559 1.00 48.32  ? 238 PHE A CD1 1 
ATOM   1878 C  CD2 . PHE A 1 241 ? 17.071 -13.105 33.412 1.00 42.52  ? 238 PHE A CD2 1 
ATOM   1879 C  CE1 . PHE A 1 241 ? 14.740 -13.004 34.933 1.00 44.08  ? 238 PHE A CE1 1 
ATOM   1880 C  CE2 . PHE A 1 241 ? 15.830 -13.124 32.778 1.00 43.29  ? 238 PHE A CE2 1 
ATOM   1881 C  CZ  . PHE A 1 241 ? 14.662 -13.071 33.546 1.00 44.51  ? 238 PHE A CZ  1 
ATOM   1882 N  N   . LEU A 1 242 ? 19.490 -15.782 34.422 1.00 46.03  ? 239 LEU A N   1 
ATOM   1883 C  CA  . LEU A 1 242 ? 19.354 -16.911 33.510 1.00 47.22  ? 239 LEU A CA  1 
ATOM   1884 C  C   . LEU A 1 242 ? 19.320 -18.231 34.260 1.00 51.19  ? 239 LEU A C   1 
ATOM   1885 O  O   . LEU A 1 242 ? 18.546 -19.127 33.910 1.00 51.30  ? 239 LEU A O   1 
ATOM   1886 C  CB  . LEU A 1 242 ? 20.511 -16.918 32.500 1.00 48.73  ? 239 LEU A CB  1 
ATOM   1887 C  CG  . LEU A 1 242 ? 20.534 -15.692 31.586 1.00 56.00  ? 239 LEU A CG  1 
ATOM   1888 C  CD1 . LEU A 1 242 ? 21.747 -15.694 30.645 1.00 46.40  ? 239 LEU A CD1 1 
ATOM   1889 C  CD2 . LEU A 1 242 ? 19.191 -15.554 30.817 1.00 48.24  ? 239 LEU A CD2 1 
ATOM   1890 N  N   . GLU A 1 243 ? 20.170 -18.383 35.279 1.00 53.21  ? 240 GLU A N   1 
ATOM   1891 C  CA  . GLU A 1 243 ? 20.248 -19.652 35.996 1.00 54.31  ? 240 GLU A CA  1 
ATOM   1892 C  C   . GLU A 1 243 ? 19.005 -19.915 36.839 1.00 57.06  ? 240 GLU A C   1 
ATOM   1893 O  O   . GLU A 1 243 ? 18.794 -21.058 37.272 1.00 58.65  ? 240 GLU A O   1 
ATOM   1894 C  CB  . GLU A 1 243 ? 21.492 -19.681 36.898 1.00 52.77  ? 240 GLU A CB  1 
ATOM   1895 C  CG  . GLU A 1 243 ? 22.804 -19.869 36.180 1.00 52.62  ? 240 GLU A CG  1 
ATOM   1896 C  CD  . GLU A 1 243 ? 22.967 -21.274 35.658 1.00 55.84  ? 240 GLU A CD  1 
ATOM   1897 O  OE1 . GLU A 1 243 ? 22.829 -22.223 36.464 1.00 59.54  ? 240 GLU A OE1 1 
ATOM   1898 O  OE2 . GLU A 1 243 ? 23.227 -21.427 34.444 1.00 55.55  ? 240 GLU A OE2 1 
ATOM   1899 N  N   . SER A 1 244 ? 18.189 -18.884 37.086 1.00 56.38  ? 241 SER A N   1 
ATOM   1900 C  CA  . SER A 1 244 ? 17.004 -19.006 37.925 1.00 54.21  ? 241 SER A CA  1 
ATOM   1901 C  C   . SER A 1 244 ? 15.749 -19.368 37.142 1.00 56.01  ? 241 SER A C   1 
ATOM   1902 O  O   . SER A 1 244 ? 14.702 -19.571 37.755 1.00 61.09  ? 241 SER A O   1 
ATOM   1903 C  CB  . SER A 1 244 ? 16.760 -17.698 38.681 1.00 48.35  ? 241 SER A CB  1 
ATOM   1904 O  OG  . SER A 1 244 ? 16.230 -16.714 37.790 1.00 52.17  ? 241 SER A OG  1 
ATOM   1905 N  N   . LEU A 1 245 ? 15.821 -19.430 35.817 1.00 55.09  ? 242 LEU A N   1 
ATOM   1906 C  CA  . LEU A 1 245 ? 14.682 -19.791 34.989 1.00 57.55  ? 242 LEU A CA  1 
ATOM   1907 C  C   . LEU A 1 245 ? 14.520 -21.313 34.970 1.00 66.35  ? 242 LEU A C   1 
ATOM   1908 O  O   . LEU A 1 245 ? 15.301 -22.057 35.563 1.00 62.82  ? 242 LEU A O   1 
ATOM   1909 C  CB  . LEU A 1 245 ? 14.854 -19.210 33.586 1.00 51.77  ? 242 LEU A CB  1 
ATOM   1910 C  CG  . LEU A 1 245 ? 15.124 -17.701 33.591 1.00 54.78  ? 242 LEU A CG  1 
ATOM   1911 C  CD1 . LEU A 1 245 ? 15.504 -17.167 32.203 1.00 47.00  ? 242 LEU A CD1 1 
ATOM   1912 C  CD2 . LEU A 1 245 ? 13.945 -16.923 34.196 1.00 47.13  ? 242 LEU A CD2 1 
ATOM   1913 N  N   . ASP A 1 246 ? 13.490 -21.799 34.288 1.00 73.30  ? 243 ASP A N   1 
ATOM   1914 C  CA  . ASP A 1 246 ? 13.198 -23.226 34.270 1.00 75.42  ? 243 ASP A CA  1 
ATOM   1915 C  C   . ASP A 1 246 ? 13.517 -23.816 32.895 1.00 75.74  ? 243 ASP A C   1 
ATOM   1916 O  O   . ASP A 1 246 ? 12.673 -24.267 32.122 1.00 77.45  ? 243 ASP A O   1 
ATOM   1917 C  CB  . ASP A 1 246 ? 11.741 -23.498 34.830 1.00 80.35  ? 243 ASP A CB  1 
ATOM   1918 C  CG  . ASP A 1 246 ? 10.614 -23.311 33.806 1.00 90.62  ? 243 ASP A CG  1 
ATOM   1919 O  OD1 . ASP A 1 246 ? 9.446  -23.585 34.166 1.00 92.81  ? 243 ASP A OD1 1 
ATOM   1920 O  OD2 . ASP A 1 246 ? 10.844 -22.778 32.693 1.00 88.61  ? 243 ASP A OD2 1 
ATOM   1921 N  N   . TRP A 1 247 ? 14.816 -23.836 32.615 1.00 71.69  ? 244 TRP A N   1 
ATOM   1922 C  CA  . TRP A 1 247 ? 15.322 -24.563 31.461 1.00 71.30  ? 244 TRP A CA  1 
ATOM   1923 C  C   . TRP A 1 247 ? 14.964 -26.043 31.563 1.00 77.43  ? 244 TRP A C   1 
ATOM   1924 O  O   . TRP A 1 247 ? 15.018 -26.648 32.637 1.00 76.58  ? 244 TRP A O   1 
ATOM   1925 C  CB  . TRP A 1 247 ? 16.840 -24.387 31.336 1.00 69.11  ? 244 TRP A CB  1 
ATOM   1926 C  CG  . TRP A 1 247 ? 17.242 -22.942 31.327 1.00 63.20  ? 244 TRP A CG  1 
ATOM   1927 C  CD1 . TRP A 1 247 ? 17.654 -22.199 32.403 1.00 58.03  ? 244 TRP A CD1 1 
ATOM   1928 C  CD2 . TRP A 1 247 ? 17.239 -22.052 30.197 1.00 58.60  ? 244 TRP A CD2 1 
ATOM   1929 N  NE1 . TRP A 1 247 ? 17.924 -20.904 32.004 1.00 60.49  ? 244 TRP A NE1 1 
ATOM   1930 C  CE2 . TRP A 1 247 ? 17.669 -20.783 30.662 1.00 56.97  ? 244 TRP A CE2 1 
ATOM   1931 C  CE3 . TRP A 1 247 ? 16.904 -22.198 28.845 1.00 56.33  ? 244 TRP A CE3 1 
ATOM   1932 C  CZ2 . TRP A 1 247 ? 17.789 -19.668 29.818 1.00 54.84  ? 244 TRP A CZ2 1 
ATOM   1933 C  CZ3 . TRP A 1 247 ? 17.025 -21.077 27.995 1.00 54.21  ? 244 TRP A CZ3 1 
ATOM   1934 C  CH2 . TRP A 1 247 ? 17.475 -19.836 28.489 1.00 52.53  ? 244 TRP A CH2 1 
ATOM   1935 N  N   . SER A 1 248 ? 14.595 -26.626 30.427 1.00 80.07  ? 245 SER A N   1 
ATOM   1936 C  CA  . SER A 1 248 ? 14.355 -28.059 30.386 1.00 82.71  ? 245 SER A CA  1 
ATOM   1937 C  C   . SER A 1 248 ? 15.644 -28.859 30.553 1.00 89.55  ? 245 SER A C   1 
ATOM   1938 O  O   . SER A 1 248 ? 15.605 -30.027 30.963 1.00 88.64  ? 245 SER A O   1 
ATOM   1939 C  CB  . SER A 1 248 ? 13.643 -28.403 29.078 1.00 81.67  ? 245 SER A CB  1 
ATOM   1940 O  OG  . SER A 1 248 ? 14.483 -29.153 28.220 1.00 89.27  ? 245 SER A OG  1 
ATOM   1941 N  N   . GLU A 1 249 ? 16.784 -28.240 30.281 1.00 106.14 ? 246 GLU A N   1 
ATOM   1942 C  CA  . GLU A 1 249 ? 18.071 -28.913 30.360 1.00 108.54 ? 246 GLU A CA  1 
ATOM   1943 C  C   . GLU A 1 249 ? 19.191 -27.883 30.495 1.00 106.09 ? 246 GLU A C   1 
ATOM   1944 O  O   . GLU A 1 249 ? 19.057 -26.742 30.041 1.00 104.11 ? 246 GLU A O   1 
ATOM   1945 C  CB  . GLU A 1 249 ? 18.294 -29.774 29.122 1.00 110.69 ? 246 GLU A CB  1 
ATOM   1946 C  CG  . GLU A 1 249 ? 18.332 -31.265 29.386 1.00 118.65 ? 246 GLU A CG  1 
ATOM   1947 C  CD  . GLU A 1 249 ? 19.001 -32.016 28.250 1.00 131.28 ? 246 GLU A CD  1 
ATOM   1948 O  OE1 . GLU A 1 249 ? 19.828 -32.915 28.529 1.00 137.92 ? 246 GLU A OE1 1 
ATOM   1949 O  OE2 . GLU A 1 249 ? 18.720 -31.678 27.075 1.00 131.48 ? 246 GLU A OE2 1 
ATOM   1950 O  OXT . GLU A 1 249 ? 20.244 -28.175 31.067 1.00 108.81 ? 246 GLU A OXT 1 
HETATM 1951 CA CA  . CA  B 2 .   ? 13.549 -13.361 39.608 0.36 59.50  ? 301 CA  A CA  1 
HETATM 1952 CA CA  . CA  C 2 .   ? -1.151 -9.575  37.906 0.59 76.91  ? 302 CA  A CA  1 
HETATM 1953 CA CA  . CA  D 2 .   ? 24.662 -24.441 12.559 0.44 82.16  ? 303 CA  A CA  1 
HETATM 1954 CA CA  . CA  E 2 .   ? -2.520 -2.027  27.131 0.99 95.08  ? 304 CA  A CA  1 
HETATM 1955 O  O   . HOH F 3 .   ? 23.977 -0.500  20.233 1.00 63.75  ? 401 HOH A O   1 
HETATM 1956 O  O   . HOH F 3 .   ? 26.718 1.009   40.815 1.00 78.36  ? 402 HOH A O   1 
HETATM 1957 O  O   . HOH F 3 .   ? 24.039 -25.564 14.684 1.00 84.57  ? 403 HOH A O   1 
HETATM 1958 O  O   . HOH F 3 .   ? 31.581 -10.198 35.531 1.00 68.37  ? 404 HOH A O   1 
HETATM 1959 O  O   . HOH F 3 .   ? 5.719  -11.836 27.686 1.00 56.34  ? 405 HOH A O   1 
HETATM 1960 O  O   . HOH F 3 .   ? 7.722  -17.726 30.116 1.00 56.84  ? 406 HOH A O   1 
HETATM 1961 O  O   . HOH F 3 .   ? 30.788 -5.238  23.490 1.00 60.55  ? 407 HOH A O   1 
HETATM 1962 O  O   . HOH F 3 .   ? 30.159 -25.181 19.470 1.00 60.08  ? 408 HOH A O   1 
HETATM 1963 O  O   . HOH F 3 .   ? 17.624 -3.408  42.975 1.00 61.69  ? 409 HOH A O   1 
HETATM 1964 O  O   . HOH F 3 .   ? 26.778 -21.769 33.839 1.00 64.14  ? 410 HOH A O   1 
HETATM 1965 O  O   . HOH F 3 .   ? 3.846  -7.829  37.693 1.00 54.32  ? 411 HOH A O   1 
HETATM 1966 O  O   . HOH F 3 .   ? 27.497 -16.812 23.714 1.00 52.07  ? 412 HOH A O   1 
HETATM 1967 O  O   . HOH F 3 .   ? 3.800  -20.458 20.104 1.00 52.66  ? 413 HOH A O   1 
HETATM 1968 O  O   . HOH F 3 .   ? 24.418 -6.113  9.253  1.00 74.46  ? 414 HOH A O   1 
HETATM 1969 O  O   . HOH F 3 .   ? 15.916 -10.339 8.933  1.00 72.21  ? 415 HOH A O   1 
HETATM 1970 O  O   . HOH F 3 .   ? 18.586 3.182   21.146 1.00 59.26  ? 416 HOH A O   1 
HETATM 1971 O  O   . HOH F 3 .   ? 0.748  -10.970 37.578 1.00 62.36  ? 417 HOH A O   1 
HETATM 1972 O  O   . HOH F 3 .   ? 28.620 -0.388  32.689 1.00 63.92  ? 418 HOH A O   1 
HETATM 1973 O  O   . HOH F 3 .   ? 11.910 -20.344 24.288 1.00 47.01  ? 419 HOH A O   1 
HETATM 1974 O  O   . HOH F 3 .   ? 6.336  -14.197 35.276 1.00 46.45  ? 420 HOH A O   1 
HETATM 1975 O  O   . HOH F 3 .   ? 13.663 -15.189 38.151 1.00 66.24  ? 421 HOH A O   1 
HETATM 1976 O  O   . HOH F 3 .   ? 10.626 -22.177 20.674 1.00 65.08  ? 422 HOH A O   1 
HETATM 1977 O  O   . HOH F 3 .   ? 27.357 -23.879 12.671 1.00 88.62  ? 423 HOH A O   1 
HETATM 1978 O  O   . HOH F 3 .   ? 28.257 4.426   28.149 1.00 74.35  ? 424 HOH A O   1 
HETATM 1979 O  O   . HOH F 3 .   ? 33.559 -23.510 24.896 1.00 69.20  ? 425 HOH A O   1 
HETATM 1980 O  O   . HOH F 3 .   ? 25.135 1.452   13.561 1.00 74.99  ? 426 HOH A O   1 
HETATM 1981 O  O   . HOH F 3 .   ? 1.363  0.469   29.793 1.00 72.84  ? 427 HOH A O   1 
HETATM 1982 O  O   . HOH F 3 .   ? 31.870 -22.715 27.441 1.00 63.65  ? 428 HOH A O   1 
HETATM 1983 O  O   . HOH F 3 .   ? -0.273 -13.625 39.416 1.00 68.75  ? 429 HOH A O   1 
HETATM 1984 O  O   . HOH F 3 .   ? 9.650  -18.028 36.821 1.00 58.94  ? 430 HOH A O   1 
HETATM 1985 O  O   . HOH F 3 .   ? 0.647  -11.875 22.968 1.00 61.77  ? 431 HOH A O   1 
HETATM 1986 O  O   . HOH F 3 .   ? 6.690  -15.719 25.437 1.00 43.22  ? 432 HOH A O   1 
HETATM 1987 O  O   . HOH F 3 .   ? 20.094 -10.726 38.869 1.00 60.29  ? 433 HOH A O   1 
HETATM 1988 O  O   . HOH F 3 .   ? 3.503  -14.430 23.784 1.00 48.81  ? 434 HOH A O   1 
HETATM 1989 O  O   . HOH F 3 .   ? 12.276 -12.255 40.977 0.50 53.31  ? 435 HOH A O   1 
HETATM 1990 O  O   . HOH F 3 .   ? 13.005 -14.882 40.869 1.00 57.59  ? 436 HOH A O   1 
HETATM 1991 O  O   . HOH F 3 .   ? 14.652 1.412   31.633 1.00 54.99  ? 437 HOH A O   1 
HETATM 1992 O  O   . HOH F 3 .   ? 7.947  1.536   42.220 1.00 84.57  ? 438 HOH A O   1 
HETATM 1993 O  O   . HOH F 3 .   ? 15.657 -1.274  31.129 1.00 49.76  ? 439 HOH A O   1 
HETATM 1994 O  O   . HOH F 3 .   ? 6.979  -19.000 19.520 1.00 57.06  ? 440 HOH A O   1 
HETATM 1995 O  O   . HOH F 3 .   ? -4.176 -3.624  25.803 1.00 89.14  ? 441 HOH A O   1 
HETATM 1996 O  O   . HOH F 3 .   ? 3.583  -5.420  40.802 1.00 63.37  ? 442 HOH A O   1 
HETATM 1997 O  O   . HOH F 3 .   ? 28.904 -5.928  25.565 1.00 55.43  ? 443 HOH A O   1 
HETATM 1998 O  O   . HOH F 3 .   ? 31.633 -8.306  13.573 1.00 73.56  ? 444 HOH A O   1 
HETATM 1999 O  O   . HOH F 3 .   ? 10.952 -19.701 32.158 1.00 62.09  ? 445 HOH A O   1 
HETATM 2000 O  O   . HOH F 3 .   ? 30.910 -7.260  16.697 1.00 60.31  ? 446 HOH A O   1 
HETATM 2001 O  O   . HOH F 3 .   ? 23.381 -24.217 27.878 1.00 64.41  ? 447 HOH A O   1 
HETATM 2002 O  O   . HOH F 3 .   ? 34.313 -16.676 25.389 1.00 50.53  ? 448 HOH A O   1 
HETATM 2003 O  O   . HOH F 3 .   ? 13.181 -11.759 37.849 1.00 58.87  ? 449 HOH A O   1 
HETATM 2004 O  O   . HOH F 3 .   ? 13.919 -26.604 17.478 1.00 71.04  ? 450 HOH A O   1 
HETATM 2005 O  O   . HOH F 3 .   ? 24.393 -5.644  41.520 1.00 73.18  ? 451 HOH A O   1 
HETATM 2006 O  O   . HOH F 3 .   ? 3.706  -12.506 15.184 1.00 59.30  ? 452 HOH A O   1 
HETATM 2007 O  O   . HOH F 3 .   ? 15.548 -13.962 38.888 1.00 64.66  ? 453 HOH A O   1 
HETATM 2008 O  O   . HOH F 3 .   ? 31.203 -11.164 13.928 1.00 59.32  ? 454 HOH A O   1 
HETATM 2009 O  O   . HOH F 3 .   ? 11.166 -19.923 34.964 1.00 57.30  ? 455 HOH A O   1 
HETATM 2010 O  O   . HOH F 3 .   ? 30.156 -16.139 14.797 1.00 60.96  ? 456 HOH A O   1 
HETATM 2011 O  O   . HOH F 3 .   ? 2.979  -14.322 34.755 1.00 62.86  ? 457 HOH A O   1 
HETATM 2012 O  O   . HOH F 3 .   ? 23.505 -26.658 13.263 1.00 90.60  ? 458 HOH A O   1 
HETATM 2013 O  O   . HOH F 3 .   ? 30.106 -21.024 17.101 1.00 61.17  ? 459 HOH A O   1 
HETATM 2014 O  O   . HOH F 3 .   ? 33.816 -10.707 27.902 1.00 64.11  ? 460 HOH A O   1 
HETATM 2015 O  O   . HOH F 3 .   ? 4.382  -17.501 25.785 1.00 61.74  ? 461 HOH A O   1 
HETATM 2016 O  O   . HOH F 3 .   ? -4.634 -4.881  27.686 1.00 82.84  ? 462 HOH A O   1 
HETATM 2017 O  O   . HOH F 3 .   ? 0.807  -8.166  38.619 1.00 71.06  ? 463 HOH A O   1 
HETATM 2018 O  O   . HOH F 3 .   ? -3.402 -0.571  25.208 1.00 98.58  ? 464 HOH A O   1 
HETATM 2019 O  O   . HOH F 3 .   ? 20.655 -9.840  11.092 1.00 63.15  ? 465 HOH A O   1 
HETATM 2020 O  O   . HOH F 3 .   ? -1.774 -11.867 36.819 1.00 76.46  ? 466 HOH A O   1 
HETATM 2021 O  O   . HOH F 3 .   ? -2.352 -7.518  37.634 1.00 84.09  ? 467 HOH A O   1 
HETATM 2022 O  O   . HOH F 3 .   ? 10.763 0.323   42.204 1.00 78.98  ? 468 HOH A O   1 
HETATM 2023 O  O   . HOH F 3 .   ? 24.374 -25.611 10.462 1.00 87.55  ? 469 HOH A O   1 
HETATM 2024 O  O   . HOH F 3 .   ? 32.015 -17.185 16.103 1.00 66.12  ? 470 HOH A O   1 
HETATM 2025 O  O   . HOH F 3 .   ? 23.162 1.331   21.552 1.00 65.30  ? 471 HOH A O   1 
HETATM 2026 O  O   . HOH F 3 .   ? 32.276 -14.455 15.000 1.00 66.27  ? 472 HOH A O   1 
HETATM 2027 O  O   . HOH F 3 .   ? 18.203 -11.908 11.472 1.00 60.37  ? 473 HOH A O   1 
HETATM 2028 O  O   . HOH F 3 .   ? -4.293 -6.423  30.275 1.00 86.44  ? 474 HOH A O   1 
HETATM 2029 O  O   . HOH F 3 .   ? 34.767 -9.105  22.976 1.00 63.92  ? 475 HOH A O   1 
HETATM 2030 O  O   . HOH F 3 .   ? 5.590  -18.764 15.854 1.00 71.25  ? 476 HOH A O   1 
HETATM 2031 O  O   . HOH F 3 .   ? 4.248  -6.009  14.381 1.00 70.36  ? 477 HOH A O   1 
HETATM 2032 O  O   . HOH F 3 .   ? 6.760  -16.998 35.748 1.00 59.68  ? 478 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   . LEU A 8   ? 0.8760 1.2930 0.8878 -0.1835 0.2755  0.3745  5   LEU A N   
2    C CA  . LEU A 8   ? 0.9038 1.2821 0.8777 -0.1721 0.2417  0.3738  5   LEU A CA  
3    C C   . LEU A 8   ? 0.8993 1.3040 0.8688 -0.1499 0.2263  0.3392  5   LEU A C   
4    O O   . LEU A 8   ? 0.9191 1.3547 0.8655 -0.1325 0.2431  0.3190  5   LEU A O   
5    C CB  . LEU A 8   ? 1.0299 1.3713 0.9223 -0.1607 0.2421  0.3963  5   LEU A CB  
6    C CG  . LEU A 8   ? 1.0814 1.3700 0.9721 -0.1792 0.2411  0.4341  5   LEU A CG  
7    C CD1 . LEU A 8   ? 1.0562 1.3052 0.8696 -0.1612 0.2284  0.4548  5   LEU A CD1 
8    C CD2 . LEU A 8   ? 1.0765 1.3360 1.0253 -0.1966 0.2180  0.4338  5   LEU A CD2 
9    N N   . PRO A 9   ? 0.8946 1.2813 0.8827 -0.1508 0.1962  0.3319  6   PRO A N   
10   C CA  . PRO A 9   ? 0.8011 1.2074 0.7994 -0.1326 0.1802  0.2946  6   PRO A CA  
11   C C   . PRO A 9   ? 0.7981 1.2038 0.7298 -0.1058 0.1753  0.2768  6   PRO A C   
12   O O   . PRO A 9   ? 0.8494 1.2375 0.7215 -0.1008 0.1749  0.2966  6   PRO A O   
13   C CB  . PRO A 9   ? 0.7752 1.1354 0.7982 -0.1380 0.1454  0.2856  6   PRO A CB  
14   C CG  . PRO A 9   ? 0.8069 1.1431 0.8583 -0.1677 0.1502  0.3165  6   PRO A CG  
15   C CD  . PRO A 9   ? 0.8921 1.2312 0.9023 -0.1706 0.1770  0.3520  6   PRO A CD  
16   N N   . LYS A 10  ? 0.7555 1.1799 0.6988 -0.0897 0.1693  0.2398  7   LYS A N   
17   C CA  . LYS A 10  ? 0.7485 1.1748 0.6398 -0.0680 0.1638  0.2139  7   LYS A CA  
18   C C   . LYS A 10  ? 0.7105 1.1264 0.6297 -0.0566 0.1389  0.1799  7   LYS A C   
19   O O   . LYS A 10  ? 0.6883 1.1067 0.6642 -0.0627 0.1331  0.1743  7   LYS A O   
20   C CB  . LYS A 10  ? 0.7977 1.2628 0.6663 -0.0600 0.1999  0.2033  7   LYS A CB  
21   C CG  . LYS A 10  ? 0.9928 1.4683 0.8658 -0.0731 0.2314  0.2310  7   LYS A CG  
22   C CD  . LYS A 10  ? 1.1615 1.6515 0.9973 -0.0608 0.2645  0.2142  7   LYS A CD  
23   C CE  . LYS A 10  ? 1.2539 1.7778 1.1517 -0.0523 0.2864  0.1899  7   LYS A CE  
24   N NZ  . LYS A 10  ? 1.2260 1.7739 1.2049 -0.0690 0.2994  0.2101  7   LYS A NZ  
25   N N   . PRO A 11  ? 0.7432 1.1481 0.6231 -0.0419 0.1228  0.1582  8   PRO A N   
26   C CA  . PRO A 11  ? 0.6686 1.0615 0.5755 -0.0329 0.1019  0.1292  8   PRO A CA  
27   C C   . PRO A 11  ? 0.6239 1.0396 0.5682 -0.0267 0.1186  0.1066  8   PRO A C   
28   O O   . PRO A 11  ? 0.5804 1.0241 0.5234 -0.0243 0.1475  0.1060  8   PRO A O   
29   C CB  . PRO A 11  ? 0.6166 1.0008 0.4735 -0.0224 0.0855  0.1129  8   PRO A CB  
30   C CG  . PRO A 11  ? 0.6938 1.0764 0.5010 -0.0260 0.0851  0.1409  8   PRO A CG  
31   C CD  . PRO A 11  ? 0.7066 1.1076 0.5159 -0.0355 0.1181  0.1624  8   PRO A CD  
32   N N   . PHE A 12  ? 0.5780 0.9815 0.5570 -0.0219 0.1022  0.0898  9   PHE A N   
33   C CA  . PHE A 12  ? 0.5679 0.9893 0.5837 -0.0123 0.1148  0.0715  9   PHE A CA  
34   C C   . PHE A 12  ? 0.4974 0.8962 0.5114 -0.0008 0.0994  0.0449  9   PHE A C   
35   O O   . PHE A 12  ? 0.5325 0.9068 0.5330 -0.0031 0.0772  0.0431  9   PHE A O   
36   C CB  . PHE A 12  ? 0.5046 0.9428 0.5803 -0.0213 0.1143  0.0869  9   PHE A CB  
37   C CG  . PHE A 12  ? 0.5755 0.9847 0.6649 -0.0303 0.0856  0.0918  9   PHE A CG  
38   C CD1 . PHE A 12  ? 0.5055 0.8956 0.6027 -0.0205 0.0698  0.0743  9   PHE A CD1 
39   C CD2 . PHE A 12  ? 0.5528 0.9490 0.6439 -0.0485 0.0773  0.1136  9   PHE A CD2 
40   C CE1 . PHE A 12  ? 0.4864 0.8487 0.5881 -0.0275 0.0481  0.0775  9   PHE A CE1 
41   C CE2 . PHE A 12  ? 0.5598 0.9232 0.6566 -0.0552 0.0541  0.1135  9   PHE A CE2 
42   C CZ  . PHE A 12  ? 0.4544 0.8027 0.5542 -0.0441 0.0405  0.0950  9   PHE A CZ  
43   N N   . PHE A 13  ? 0.5340 0.9418 0.5673 0.0123  0.1140  0.0259  10  PHE A N   
44   C CA  . PHE A 13  ? 0.5649 0.9487 0.5981 0.0226  0.1056  0.0004  10  PHE A CA  
45   C C   . PHE A 13  ? 0.5253 0.9193 0.6080 0.0356  0.1173  -0.0033 10  PHE A C   
46   O O   . PHE A 13  ? 0.5780 0.9929 0.6709 0.0467  0.1435  -0.0092 10  PHE A O   
47   C CB  . PHE A 13  ? 0.5355 0.9103 0.5190 0.0271  0.1139  -0.0245 10  PHE A CB  
48   C CG  . PHE A 13  ? 0.5957 0.9409 0.5771 0.0313  0.1024  -0.0513 10  PHE A CG  
49   C CD1 . PHE A 13  ? 0.5976 0.9250 0.6075 0.0285  0.0825  -0.0466 10  PHE A CD1 
50   C CD2 . PHE A 13  ? 0.7093 1.0418 0.6578 0.0366  0.1138  -0.0823 10  PHE A CD2 
51   C CE1 . PHE A 13  ? 0.6914 0.9920 0.7038 0.0297  0.0751  -0.0685 10  PHE A CE1 
52   C CE2 . PHE A 13  ? 0.7318 1.0334 0.6828 0.0363  0.1035  -0.1076 10  PHE A CE2 
53   C CZ  . PHE A 13  ? 0.6952 0.9825 0.6816 0.0323  0.0846  -0.0985 10  PHE A CZ  
54   N N   . PHE A 14  ? 0.5382 0.9189 0.6510 0.0360  0.0992  0.0021  11  PHE A N   
55   C CA  . PHE A 14  ? 0.5163 0.9054 0.6757 0.0501  0.1040  0.0033  11  PHE A CA  
56   C C   . PHE A 14  ? 0.4992 0.8509 0.6538 0.0605  0.0994  -0.0151 11  PHE A C   
57   O O   . PHE A 14  ? 0.4803 0.8074 0.6272 0.0532  0.0800  -0.0123 11  PHE A O   
58   C CB  . PHE A 14  ? 0.4790 0.8819 0.6720 0.0413  0.0850  0.0267  11  PHE A CB  
59   C CG  . PHE A 14  ? 0.4803 0.9137 0.6825 0.0248  0.0864  0.0457  11  PHE A CG  
60   C CD1 . PHE A 14  ? 0.4325 0.8968 0.6375 0.0262  0.1126  0.0480  11  PHE A CD1 
61   C CD2 . PHE A 14  ? 0.4448 0.8718 0.6506 0.0068  0.0638  0.0609  11  PHE A CD2 
62   C CE1 . PHE A 14  ? 0.4315 0.9227 0.6488 0.0083  0.1164  0.0691  11  PHE A CE1 
63   C CE2 . PHE A 14  ? 0.4616 0.9100 0.6787 -0.0119 0.0651  0.0784  11  PHE A CE2 
64   C CZ  . PHE A 14  ? 0.4633 0.9452 0.6890 -0.0119 0.0916  0.0846  11  PHE A CZ  
65   N N   . GLU A 15  ? 0.5110 0.8556 0.6712 0.0773  0.1201  -0.0336 12  GLU A N   
66   C CA  . GLU A 15  ? 0.5844 0.8871 0.7408 0.0851  0.1194  -0.0526 12  GLU A CA  
67   C C   . GLU A 15  ? 0.5587 0.8567 0.7612 0.1019  0.1183  -0.0389 12  GLU A C   
68   O O   . GLU A 15  ? 0.5944 0.9134 0.8317 0.1207  0.1353  -0.0348 12  GLU A O   
69   C CB  . GLU A 15  ? 0.6132 0.8995 0.7444 0.0935  0.1423  -0.0840 12  GLU A CB  
70   C CG  . GLU A 15  ? 0.7560 1.0434 0.8317 0.0766  0.1380  -0.0984 12  GLU A CG  
71   C CD  . GLU A 15  ? 0.8756 1.1323 0.9143 0.0790  0.1508  -0.1363 12  GLU A CD  
72   O OE1 . GLU A 15  ? 0.9326 1.1549 0.9640 0.0698  0.1361  -0.1526 12  GLU A OE1 
73   O OE2 . GLU A 15  ? 0.8527 1.1192 0.8694 0.0886  0.1765  -0.1506 12  GLU A OE2 
74   N N   . GLU A 16  ? 0.5704 0.8416 0.7733 0.0968  0.0998  -0.0304 13  GLU A N   
75   C CA  . GLU A 16  ? 0.5326 0.7914 0.7689 0.1131  0.0968  -0.0156 13  GLU A CA  
76   C C   . GLU A 16  ? 0.6434 0.8493 0.8678 0.1125  0.0966  -0.0258 13  GLU A C   
77   O O   . GLU A 16  ? 0.6966 0.8734 0.9173 0.1186  0.1134  -0.0495 13  GLU A O   
78   C CB  . GLU A 16  ? 0.5440 0.8264 0.7917 0.1063  0.0736  0.0130  13  GLU A CB  
79   C CG  . GLU A 16  ? 0.5501 0.8860 0.8212 0.1035  0.0728  0.0253  13  GLU A CG  
80   C CD  . GLU A 16  ? 0.5662 0.9325 0.8900 0.1276  0.0862  0.0337  13  GLU A CD  
81   O OE1 . GLU A 16  ? 0.5887 0.9910 0.9307 0.1313  0.1056  0.0296  13  GLU A OE1 
82   O OE2 . GLU A 16  ? 0.6214 0.9763 0.9696 0.1447  0.0793  0.0465  13  GLU A OE2 
83   N N   . GLY A 17  ? 0.5807 0.7715 0.7972 0.1034  0.0798  -0.0095 14  GLY A N   
84   C CA  . GLY A 17  ? 0.6577 0.8019 0.8667 0.0993  0.0821  -0.0151 14  GLY A CA  
85   C C   . GLY A 17  ? 0.6907 0.8251 0.8746 0.0778  0.0803  -0.0362 14  GLY A C   
86   O O   . GLY A 17  ? 0.6451 0.8047 0.8124 0.0687  0.0776  -0.0481 14  GLY A O   
87   N N   . LYS A 18  ? 0.7100 0.8097 0.8942 0.0693  0.0811  -0.0373 15  LYS A N   
88   C CA  . LYS A 18  ? 0.7104 0.8022 0.8846 0.0489  0.0785  -0.0568 15  LYS A CA  
89   C C   . LYS A 18  ? 0.7010 0.8136 0.8643 0.0357  0.0658  -0.0443 15  LYS A C   
90   O O   . LYS A 18  ? 0.7201 0.8402 0.8807 0.0204  0.0603  -0.0573 15  LYS A O   
91   C CB  . LYS A 18  ? 0.7876 0.8330 0.9777 0.0435  0.0883  -0.0636 15  LYS A CB  
92   C CG  . LYS A 18  ? 0.9214 0.9349 1.1180 0.0501  0.1021  -0.0902 15  LYS A CG  
93   C CD  . LYS A 18  ? 1.0154 1.0332 1.1952 0.0309  0.0972  -0.1259 15  LYS A CD  
94   C CE  . LYS A 18  ? 1.0952 1.0840 1.2670 0.0402  0.1125  -0.1578 15  LYS A CE  
95   N NZ  . LYS A 18  ? 1.0828 1.1063 1.2218 0.0428  0.1115  -0.1762 15  LYS A NZ  
96   N N   . ARG A 19  ? 0.6481 0.7694 0.8057 0.0415  0.0604  -0.0202 16  ARG A N   
97   C CA  . ARG A 19  ? 0.6629 0.7991 0.8066 0.0322  0.0517  -0.0112 16  ARG A CA  
98   C C   . ARG A 19  ? 0.6134 0.7814 0.7452 0.0311  0.0427  -0.0139 16  ARG A C   
99   O O   . ARG A 19  ? 0.5511 0.7329 0.6840 0.0392  0.0413  -0.0077 16  ARG A O   
100  C CB  . ARG A 19  ? 0.6508 0.7745 0.7833 0.0371  0.0503  0.0120  16  ARG A CB  
101  C CG  . ARG A 19  ? 0.6674 0.7581 0.8071 0.0431  0.0603  0.0234  16  ARG A CG  
102  C CD  . ARG A 19  ? 0.6779 0.7603 0.7928 0.0486  0.0552  0.0480  16  ARG A CD  
103  N NE  . ARG A 19  ? 0.8056 0.8543 0.9195 0.0546  0.0651  0.0654  16  ARG A NE  
104  C CZ  . ARG A 19  ? 0.8550 0.8907 0.9399 0.0601  0.0615  0.0889  16  ARG A CZ  
105  N NH1 . ARG A 19  ? 0.6991 0.7510 0.7531 0.0590  0.0464  0.0942  16  ARG A NH1 
106  N NH2 . ARG A 19  ? 0.8221 0.8240 0.9049 0.0655  0.0728  0.1077  16  ARG A NH2 
107  N N   . ALA A 20  ? 0.5798 0.7614 0.7045 0.0215  0.0368  -0.0202 17  ALA A N   
108  C CA  . ALA A 20  ? 0.5919 0.7988 0.7033 0.0199  0.0301  -0.0208 17  ALA A CA  
109  C C   . ALA A 20  ? 0.5509 0.7624 0.6527 0.0158  0.0222  -0.0081 17  ALA A C   
110  O O   . ALA A 20  ? 0.4657 0.6673 0.5725 0.0137  0.0229  -0.0057 17  ALA A O   
111  C CB  . ALA A 20  ? 0.4967 0.7153 0.6016 0.0147  0.0287  -0.0400 17  ALA A CB  
112  N N   . VAL A 21  ? 0.4448 0.6697 0.5354 0.0150  0.0177  0.0001  18  VAL A N   
113  C CA  . VAL A 21  ? 0.5424 0.7646 0.6223 0.0115  0.0113  0.0112  18  VAL A CA  
114  C C   . VAL A 21  ? 0.5470 0.7876 0.6170 0.0084  0.0072  0.0138  18  VAL A C   
115  O O   . VAL A 21  ? 0.4903 0.7467 0.5564 0.0073  0.0109  0.0139  18  VAL A O   
116  C CB  . VAL A 21  ? 0.5222 0.7338 0.5951 0.0095  0.0080  0.0221  18  VAL A CB  
117  C CG1 . VAL A 21  ? 0.4656 0.6602 0.5249 0.0062  0.0043  0.0287  18  VAL A CG1 
118  C CG2 . VAL A 21  ? 0.5207 0.7175 0.5956 0.0138  0.0101  0.0228  18  VAL A CG2 
119  N N   . LEU A 22  ? 0.4802 0.7197 0.5471 0.0086  0.0011  0.0189  19  LEU A N   
120  C CA  . LEU A 22  ? 0.4856 0.7380 0.5389 0.0072  -0.0050 0.0282  19  LEU A CA  
121  C C   . LEU A 22  ? 0.5140 0.7477 0.5615 0.0058  -0.0059 0.0449  19  LEU A C   
122  O O   . LEU A 22  ? 0.5094 0.7217 0.5625 0.0099  -0.0055 0.0470  19  LEU A O   
123  C CB  . LEU A 22  ? 0.4595 0.7252 0.5181 0.0101  -0.0149 0.0252  19  LEU A CB  
124  C CG  . LEU A 22  ? 0.5405 0.8207 0.5818 0.0114  -0.0258 0.0391  19  LEU A CG  
125  C CD1 . LEU A 22  ? 0.4660 0.7622 0.4779 0.0062  -0.0233 0.0349  19  LEU A CD1 
126  C CD2 . LEU A 22  ? 0.4229 0.7206 0.4804 0.0157  -0.0406 0.0393  19  LEU A CD2 
127  N N   . LEU A 23  ? 0.4972 0.7363 0.5335 -0.0007 -0.0043 0.0559  20  LEU A N   
128  C CA  . LEU A 23  ? 0.5158 0.7327 0.5483 -0.0073 -0.0048 0.0706  20  LEU A CA  
129  C C   . LEU A 23  ? 0.5318 0.7463 0.5513 -0.0065 -0.0076 0.0895  20  LEU A C   
130  O O   . LEU A 23  ? 0.5943 0.8321 0.6006 -0.0088 -0.0055 0.0965  20  LEU A O   
131  C CB  . LEU A 23  ? 0.5536 0.7798 0.5927 -0.0193 -0.0006 0.0727  20  LEU A CB  
132  C CG  . LEU A 23  ? 0.5279 0.7603 0.5810 -0.0187 -0.0006 0.0602  20  LEU A CG  
133  C CD1 . LEU A 23  ? 0.5477 0.8060 0.6185 -0.0277 0.0027  0.0658  20  LEU A CD1 
134  C CD2 . LEU A 23  ? 0.5320 0.7316 0.5794 -0.0194 -0.0069 0.0561  20  LEU A CD2 
135  N N   . LEU A 24  ? 0.4746 0.6577 0.4948 -0.0020 -0.0104 0.0991  21  LEU A N   
136  C CA  . LEU A 24  ? 0.5760 0.7491 0.5874 0.0031  -0.0141 0.1214  21  LEU A CA  
137  C C   . LEU A 24  ? 0.6256 0.7576 0.6336 -0.0072 -0.0096 0.1349  21  LEU A C   
138  O O   . LEU A 24  ? 0.6115 0.7092 0.6240 -0.0086 -0.0077 0.1245  21  LEU A O   
139  C CB  . LEU A 24  ? 0.5413 0.7125 0.5654 0.0217  -0.0207 0.1222  21  LEU A CB  
140  C CG  . LEU A 24  ? 0.5226 0.7313 0.5577 0.0267  -0.0266 0.1056  21  LEU A CG  
141  C CD1 . LEU A 24  ? 0.4860 0.6976 0.5474 0.0428  -0.0313 0.1069  21  LEU A CD1 
142  C CD2 . LEU A 24  ? 0.5153 0.7585 0.5304 0.0229  -0.0349 0.1094  21  LEU A CD2 
143  N N   . HIS A 25  ? 0.6269 0.7591 0.6233 -0.0157 -0.0072 0.1578  22  HIS A N   
144  C CA  . HIS A 25  ? 0.6501 0.7421 0.6467 -0.0308 -0.0024 0.1724  22  HIS A CA  
145  C C   . HIS A 25  ? 0.6902 0.7367 0.6832 -0.0174 -0.0040 0.1913  22  HIS A C   
146  O O   . HIS A 25  ? 0.6334 0.6870 0.6287 0.0052  -0.0100 0.1949  22  HIS A O   
147  C CB  . HIS A 25  ? 0.6353 0.7500 0.6269 -0.0494 0.0061  0.1903  22  HIS A CB  
148  C CG  . HIS A 25  ? 0.7040 0.8393 0.6722 -0.0407 0.0078  0.2144  22  HIS A CG  
149  N ND1 . HIS A 25  ? 0.7568 0.8603 0.7119 -0.0356 0.0068  0.2451  22  HIS A ND1 
150  C CD2 . HIS A 25  ? 0.7581 0.9396 0.7079 -0.0363 0.0104  0.2126  22  HIS A CD2 
151  C CE1 . HIS A 25  ? 0.7371 0.8703 0.6642 -0.0283 0.0060  0.2634  22  HIS A CE1 
152  N NE2 . HIS A 25  ? 0.7778 0.9577 0.6985 -0.0295 0.0084  0.2416  22  HIS A NE2 
153  N N   . GLY A 26  ? 0.6971 0.6959 0.6893 -0.0317 0.0012  0.2045  23  GLY A N   
154  C CA  . GLY A 26  ? 0.7483 0.6912 0.7395 -0.0185 0.0026  0.2219  23  GLY A CA  
155  C C   . GLY A 26  ? 0.8723 0.8098 0.8521 -0.0172 0.0042  0.2626  23  GLY A C   
156  O O   . GLY A 26  ? 0.8124 0.7884 0.7802 -0.0297 0.0069  0.2774  23  GLY A O   
157  N N   . PHE A 27  ? 0.8744 0.7602 0.8568 0.0005  0.0048  0.2822  24  PHE A N   
158  C CA  . PHE A 27  ? 0.8820 0.7517 0.8519 0.0061  0.0054  0.3269  24  PHE A CA  
159  C C   . PHE A 27  ? 1.0252 0.8750 0.9871 -0.0283 0.0173  0.3439  24  PHE A C   
160  O O   . PHE A 27  ? 1.0553 0.8598 1.0293 -0.0508 0.0239  0.3289  24  PHE A O   
161  C CB  . PHE A 27  ? 1.0027 0.8096 0.9850 0.0329  0.0061  0.3426  24  PHE A CB  
162  C CG  . PHE A 27  ? 1.0372 0.8155 1.0078 0.0419  0.0061  0.3939  24  PHE A CG  
163  C CD1 . PHE A 27  ? 1.0891 0.9212 1.0374 0.0505  -0.0049 0.4246  24  PHE A CD1 
164  C CD2 . PHE A 27  ? 1.1386 0.8307 1.1163 0.0431  0.0168  0.4116  24  PHE A CD2 
165  C CE1 . PHE A 27  ? 1.1832 0.9871 1.1143 0.0602  -0.0058 0.4769  24  PHE A CE1 
166  C CE2 . PHE A 27  ? 1.2121 0.8716 1.1793 0.0530  0.0177  0.4639  24  PHE A CE2 
167  C CZ  . PHE A 27  ? 1.1995 0.9171 1.1425 0.0621  0.0059  0.4987  24  PHE A CZ  
168  N N   . THR A 28  ? 0.9950 0.8808 0.9353 -0.0338 0.0202  0.3748  25  THR A N   
169  C CA  . THR A 28  ? 1.0229 0.9114 0.9580 -0.0668 0.0359  0.3944  25  THR A CA  
170  C C   . THR A 28  ? 0.9429 0.8674 0.8989 -0.0944 0.0414  0.3606  25  THR A C   
171  O O   . THR A 28  ? 0.9330 0.8585 0.9012 -0.1253 0.0548  0.3723  25  THR A O   
172  C CB  . THR A 28  ? 1.0966 0.9058 1.0384 -0.0809 0.0460  0.4248  25  THR A CB  
173  O OG1 . THR A 28  ? 1.0064 0.7720 0.9757 -0.1047 0.0478  0.3947  25  THR A OG1 
174  C CG2 . THR A 28  ? 1.1546 0.9147 1.0876 -0.0464 0.0383  0.4522  25  THR A CG2 
175  N N   . GLY A 29  ? 0.8882 0.8462 0.8527 -0.0840 0.0314  0.3220  26  GLY A N   
176  C CA  . GLY A 29  ? 0.8253 0.8270 0.8084 -0.1034 0.0342  0.2948  26  GLY A CA  
177  C C   . GLY A 29  ? 0.8043 0.8766 0.7733 -0.0971 0.0402  0.2943  26  GLY A C   
178  O O   . GLY A 29  ? 0.8114 0.8994 0.7493 -0.0828 0.0418  0.3156  26  GLY A O   
179  N N   . ASN A 30  ? 0.7463 0.8599 0.7365 -0.1074 0.0429  0.2691  27  ASN A N   
180  C CA  . ASN A 30  ? 0.7362 0.9104 0.7148 -0.0996 0.0515  0.2620  27  ASN A CA  
181  C C   . ASN A 30  ? 0.7301 0.9333 0.7358 -0.0991 0.0466  0.2271  27  ASN A C   
182  O O   . ASN A 30  ? 0.7428 0.9208 0.7680 -0.1032 0.0341  0.2101  27  ASN A O   
183  C CB  . ASN A 30  ? 0.7584 0.9592 0.7332 -0.1166 0.0750  0.2889  27  ASN A CB  
184  C CG  . ASN A 30  ? 0.7505 0.9394 0.7672 -0.1476 0.0828  0.2990  27  ASN A CG  
185  O OD1 . ASN A 30  ? 0.7578 0.9638 0.8131 -0.1586 0.0771  0.2766  27  ASN A OD1 
186  N ND2 . ASN A 30  ? 0.8533 1.0116 0.8637 -0.1632 0.0938  0.3344  27  ASN A ND2 
187  N N   . SER A 31  ? 0.6825 0.9353 0.6844 -0.0922 0.0572  0.2166  28  SER A N   
188  C CA  . SER A 31  ? 0.6203 0.8972 0.6447 -0.0853 0.0521  0.1859  28  SER A CA  
189  C C   . SER A 31  ? 0.6072 0.8925 0.6769 -0.1047 0.0511  0.1826  28  SER A C   
190  O O   . SER A 31  ? 0.5787 0.8646 0.6655 -0.1008 0.0384  0.1616  28  SER A O   
191  C CB  . SER A 31  ? 0.6204 0.9412 0.6310 -0.0729 0.0668  0.1752  28  SER A CB  
192  O OG  . SER A 31  ? 0.6878 1.0424 0.7120 -0.0848 0.0910  0.1900  28  SER A OG  
193  N N   . SER A 32  ? 0.6102 0.9029 0.7002 -0.1274 0.0626  0.2050  29  SER A N   
194  C CA  . SER A 32  ? 0.6339 0.9427 0.7736 -0.1496 0.0573  0.2024  29  SER A CA  
195  C C   . SER A 32  ? 0.6558 0.9150 0.7961 -0.1587 0.0318  0.1891  29  SER A C   
196  O O   . SER A 32  ? 0.5347 0.8070 0.7075 -0.1730 0.0181  0.1785  29  SER A O   
197  C CB  . SER A 32  ? 0.6268 0.9541 0.7935 -0.1762 0.0759  0.2310  29  SER A CB  
198  O OG  . SER A 32  ? 0.7405 1.0112 0.8974 -0.1953 0.0690  0.2471  29  SER A OG  
199  N N   . ASP A 33  ? 0.6775 0.8819 0.7812 -0.1487 0.0249  0.1887  30  ASP A N   
200  C CA  . ASP A 33  ? 0.6608 0.8139 0.7565 -0.1520 0.0060  0.1715  30  ASP A CA  
201  C C   . ASP A 33  ? 0.6298 0.7958 0.7218 -0.1352 -0.0057 0.1448  30  ASP A C   
202  O O   . ASP A 33  ? 0.6204 0.7564 0.7079 -0.1425 -0.0208 0.1288  30  ASP A O   
203  C CB  . ASP A 33  ? 0.6766 0.7707 0.7398 -0.1396 0.0067  0.1794  30  ASP A CB  
204  C CG  . ASP A 33  ? 0.7635 0.8243 0.8295 -0.1596 0.0149  0.2067  30  ASP A CG  
205  O OD1 . ASP A 33  ? 0.7960 0.8592 0.8899 -0.1906 0.0139  0.2107  30  ASP A OD1 
206  O OD2 . ASP A 33  ? 0.8613 0.8949 0.9046 -0.1453 0.0214  0.2263  30  ASP A OD2 
207  N N   . VAL A 34  ? 0.6233 0.8286 0.7131 -0.1141 0.0017  0.1393  31  VAL A N   
208  C CA  . VAL A 34  ? 0.6066 0.8203 0.6936 -0.0979 -0.0065 0.1176  31  VAL A CA  
209  C C   . VAL A 34  ? 0.5589 0.8276 0.6755 -0.0948 -0.0021 0.1142  31  VAL A C   
210  O O   . VAL A 34  ? 0.5349 0.8127 0.6500 -0.0783 -0.0046 0.1000  31  VAL A O   
211  C CB  . VAL A 34  ? 0.5919 0.7916 0.6522 -0.0736 -0.0034 0.1105  31  VAL A CB  
212  C CG1 . VAL A 34  ? 0.5929 0.7393 0.6332 -0.0711 -0.0082 0.1118  31  VAL A CG1 
213  C CG2 . VAL A 34  ? 0.5412 0.7694 0.5930 -0.0647 0.0092  0.1210  31  VAL A CG2 
214  N N   . ARG A 35  ? 0.5082 0.8130 0.6558 -0.1097 0.0067  0.1284  32  ARG A N   
215  C CA  . ARG A 35  ? 0.5043 0.8644 0.6846 -0.1010 0.0174  0.1269  32  ARG A CA  
216  C C   . ARG A 35  ? 0.4840 0.8597 0.6939 -0.1025 -0.0014 0.1185  32  ARG A C   
217  O O   . ARG A 35  ? 0.4814 0.8755 0.6993 -0.0824 0.0002  0.1090  32  ARG A O   
218  C CB  . ARG A 35  ? 0.4524 0.8519 0.6619 -0.1151 0.0374  0.1469  32  ARG A CB  
219  C CG  . ARG A 35  ? 0.4847 0.9357 0.7158 -0.0974 0.0595  0.1439  32  ARG A CG  
220  C CD  . ARG A 35  ? 0.4369 0.9321 0.7011 -0.1108 0.0844  0.1644  32  ARG A CD  
221  N NE  . ARG A 35  ? 0.4903 1.0336 0.7759 -0.0902 0.1104  0.1590  32  ARG A NE  
222  C CZ  . ARG A 35  ? 0.5099 1.0540 0.7553 -0.0736 0.1361  0.1534  32  ARG A CZ  
223  N NH1 . ARG A 35  ? 0.4991 1.0043 0.6823 -0.0742 0.1349  0.1548  32  ARG A NH1 
224  N NH2 . ARG A 35  ? 0.4250 1.0098 0.6923 -0.0552 0.1632  0.1460  32  ARG A NH2 
225  N N   . GLN A 36  ? 0.4657 0.8322 0.6904 -0.1269 -0.0207 0.1226  33  GLN A N   
226  C CA  . GLN A 36  ? 0.4821 0.8608 0.7250 -0.1300 -0.0453 0.1156  33  GLN A CA  
227  C C   . GLN A 36  ? 0.4267 0.7721 0.6297 -0.1084 -0.0535 0.0996  33  GLN A C   
228  O O   . GLN A 36  ? 0.4075 0.7758 0.6255 -0.0949 -0.0614 0.0975  33  GLN A O   
229  C CB  . GLN A 36  ? 0.5325 0.8916 0.7802 -0.1630 -0.0687 0.1169  33  GLN A CB  
230  C CG  . GLN A 36  ? 0.5071 0.9172 0.8156 -0.1879 -0.0670 0.1341  33  GLN A CG  
231  C CD  . GLN A 36  ? 0.7174 1.0930 1.0244 -0.2259 -0.0841 0.1350  33  GLN A CD  
232  O OE1 . GLN A 36  ? 0.7516 1.0749 1.0263 -0.2334 -0.0729 0.1368  33  GLN A OE1 
233  N NE2 . GLN A 36  ? 0.7536 1.1564 1.0964 -0.2504 -0.1135 0.1338  33  GLN A NE2 
234  N N   . LEU A 37  ? 0.5251 0.8179 0.6813 -0.1036 -0.0498 0.0910  34  LEU A N   
235  C CA  . LEU A 37  ? 0.5162 0.7829 0.6407 -0.0832 -0.0514 0.0780  34  LEU A CA  
236  C C   . LEU A 37  ? 0.4727 0.7680 0.6111 -0.0599 -0.0359 0.0765  34  LEU A C   
237  O O   . LEU A 37  ? 0.4295 0.7236 0.5653 -0.0459 -0.0399 0.0712  34  LEU A O   
238  C CB  . LEU A 37  ? 0.5010 0.7149 0.5847 -0.0803 -0.0461 0.0710  34  LEU A CB  
239  C CG  . LEU A 37  ? 0.5210 0.7125 0.5788 -0.0593 -0.0402 0.0601  34  LEU A CG  
240  C CD1 . LEU A 37  ? 0.5006 0.6774 0.5403 -0.0582 -0.0530 0.0528  34  LEU A CD1 
241  C CD2 . LEU A 37  ? 0.5380 0.6898 0.5714 -0.0552 -0.0322 0.0576  34  LEU A CD2 
242  N N   . GLY A 38  ? 0.4286 0.7461 0.5782 -0.0562 -0.0173 0.0812  35  GLY A N   
243  C CA  . GLY A 38  ? 0.4358 0.7770 0.5962 -0.0361 -0.0018 0.0753  35  GLY A CA  
244  C C   . GLY A 38  ? 0.4514 0.8299 0.6534 -0.0288 -0.0037 0.0792  35  GLY A C   
245  O O   . GLY A 38  ? 0.4036 0.7816 0.6101 -0.0100 0.0004  0.0722  35  GLY A O   
246  N N   . ARG A 39  ? 0.4156 0.8276 0.6538 -0.0438 -0.0103 0.0922  36  ARG A N   
247  C CA  . ARG A 39  ? 0.4514 0.9075 0.7395 -0.0348 -0.0147 0.0995  36  ARG A CA  
248  C C   . ARG A 39  ? 0.4444 0.8826 0.7228 -0.0296 -0.0405 0.0986  36  ARG A C   
249  O O   . ARG A 39  ? 0.3377 0.7952 0.6422 -0.0097 -0.0412 0.1024  36  ARG A O   
250  C CB  . ARG A 39  ? 0.4163 0.9202 0.7543 -0.0554 -0.0178 0.1154  36  ARG A CB  
251  C CG  . ARG A 39  ? 0.4036 0.9379 0.7598 -0.0544 0.0149  0.1210  36  ARG A CG  
252  C CD  . ARG A 39  ? 0.3661 0.9314 0.7491 -0.0250 0.0390  0.1167  36  ARG A CD  
253  N NE  . ARG A 39  ? 0.4151 1.0185 0.8198 -0.0253 0.0723  0.1235  36  ARG A NE  
254  C CZ  . ARG A 39  ? 0.3401 0.9485 0.7341 -0.0022 0.1039  0.1123  36  ARG A CZ  
255  N NH1 . ARG A 39  ? 0.2945 0.8713 0.6631 0.0213  0.1048  0.0934  36  ARG A NH1 
256  N NH2 . ARG A 39  ? 0.2921 0.9342 0.6975 -0.0043 0.1367  0.1194  36  ARG A NH2 
257  N N   . PHE A 40  ? 0.4697 0.8678 0.7075 -0.0456 -0.0598 0.0942  37  PHE A N   
258  C CA  . PHE A 40  ? 0.4715 0.8491 0.6868 -0.0416 -0.0824 0.0936  37  PHE A CA  
259  C C   . PHE A 40  ? 0.4855 0.8348 0.6766 -0.0170 -0.0687 0.0870  37  PHE A C   
260  O O   . PHE A 40  ? 0.4773 0.8314 0.6762 -0.0019 -0.0765 0.0941  37  PHE A O   
261  C CB  . PHE A 40  ? 0.4650 0.8004 0.6345 -0.0639 -0.1006 0.0864  37  PHE A CB  
262  C CG  . PHE A 40  ? 0.5014 0.8078 0.6298 -0.0597 -0.1198 0.0837  37  PHE A CG  
263  C CD1 . PHE A 40  ? 0.6105 0.9378 0.7458 -0.0707 -0.1516 0.0915  37  PHE A CD1 
264  C CD2 . PHE A 40  ? 0.5436 0.8053 0.6266 -0.0456 -0.1064 0.0751  37  PHE A CD2 
265  C CE1 . PHE A 40  ? 0.6736 0.9730 0.7600 -0.0665 -0.1696 0.0910  37  PHE A CE1 
266  C CE2 . PHE A 40  ? 0.6438 0.8779 0.6832 -0.0415 -0.1195 0.0753  37  PHE A CE2 
267  C CZ  . PHE A 40  ? 0.6543 0.9048 0.6897 -0.0513 -0.1509 0.0833  37  PHE A CZ  
268  N N   . LEU A 41  ? 0.4708 0.7914 0.6357 -0.0136 -0.0494 0.0753  38  LEU A N   
269  C CA  . LEU A 41  ? 0.4724 0.7681 0.6214 0.0047  -0.0362 0.0679  38  LEU A CA  
270  C C   . LEU A 41  ? 0.4986 0.8194 0.6847 0.0242  -0.0232 0.0697  38  LEU A C   
271  O O   . LEU A 41  ? 0.4660 0.7686 0.6500 0.0394  -0.0199 0.0700  38  LEU A O   
272  C CB  . LEU A 41  ? 0.4422 0.7135 0.5661 0.0024  -0.0217 0.0558  38  LEU A CB  
273  C CG  . LEU A 41  ? 0.5148 0.7518 0.6028 -0.0092 -0.0284 0.0527  38  LEU A CG  
274  C CD1 . LEU A 41  ? 0.4854 0.7113 0.5631 -0.0082 -0.0159 0.0457  38  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.4667 0.6731 0.5271 -0.0045 -0.0334 0.0518  38  LEU A CD2 
276  N N   . GLN A 42  ? 0.4441 0.8032 0.6641 0.0248  -0.0123 0.0712  39  GLN A N   
277  C CA  . GLN A 42  ? 0.3868 0.7655 0.6405 0.0464  0.0057  0.0693  39  GLN A CA  
278  C C   . GLN A 42  ? 0.4931 0.8875 0.7794 0.0603  -0.0082 0.0851  39  GLN A C   
279  O O   . GLN A 42  ? 0.4709 0.8507 0.7677 0.0820  0.0009  0.0846  39  GLN A O   
280  C CB  . GLN A 42  ? 0.3925 0.8123 0.6738 0.0444  0.0240  0.0692  39  GLN A CB  
281  C CG  . GLN A 42  ? 0.3597 0.8105 0.6876 0.0683  0.0438  0.0700  39  GLN A CG  
282  C CD  . GLN A 42  ? 0.4355 0.9274 0.7850 0.0661  0.0686  0.0697  39  GLN A CD  
283  O OE1 . GLN A 42  ? 0.4677 0.9938 0.8380 0.0477  0.0623  0.0841  39  GLN A OE1 
284  N NE2 . GLN A 42  ? 0.3461 0.8318 0.6879 0.0833  0.0984  0.0526  39  GLN A NE2 
285  N N   . LYS A 43  ? 0.4696 0.8912 0.7714 0.0471  -0.0328 0.1002  40  LYS A N   
286  C CA  . LYS A 43  ? 0.4387 0.8828 0.7712 0.0589  -0.0536 0.1190  40  LYS A CA  
287  C C   . LYS A 43  ? 0.4762 0.8727 0.7663 0.0677  -0.0643 0.1224  40  LYS A C   
288  O O   . LYS A 43  ? 0.4562 0.8593 0.7679 0.0878  -0.0725 0.1388  40  LYS A O   
289  C CB  . LYS A 43  ? 0.3994 0.8838 0.7532 0.0358  -0.0817 0.1311  40  LYS A CB  
290  C CG  . LYS A 43  ? 0.5520 1.0536 0.9168 0.0386  -0.1162 0.1497  40  LYS A CG  
291  C CD  . LYS A 43  ? 0.7602 1.2464 1.0820 0.0064  -0.1472 0.1464  40  LYS A CD  
292  C CE  . LYS A 43  ? 0.7569 1.2941 1.1261 -0.0199 -0.1592 0.1501  40  LYS A CE  
293  N NZ  . LYS A 43  ? 0.8590 1.3907 1.2001 -0.0491 -0.2005 0.1505  40  LYS A NZ  
294  N N   . LYS A 44  ? 0.4535 0.8028 0.6871 0.0554  -0.0611 0.1095  41  LYS A N   
295  C CA  . LYS A 44  ? 0.5085 0.8115 0.7027 0.0637  -0.0614 0.1123  41  LYS A CA  
296  C C   . LYS A 44  ? 0.5314 0.8065 0.7309 0.0800  -0.0334 0.1023  41  LYS A C   
297  O O   . LYS A 44  ? 0.5594 0.7961 0.7343 0.0860  -0.0294 0.1066  41  LYS A O   
298  C CB  . LYS A 44  ? 0.5183 0.7851 0.6539 0.0444  -0.0673 0.1033  41  LYS A CB  
299  C CG  . LYS A 44  ? 0.5935 0.8699 0.7076 0.0253  -0.0965 0.1083  41  LYS A CG  
300  C CD  . LYS A 44  ? 0.4896 0.7853 0.6101 0.0329  -0.1239 0.1298  41  LYS A CD  
301  C CE  . LYS A 44  ? 0.5726 0.8657 0.6536 0.0099  -0.1558 0.1293  41  LYS A CE  
302  N NZ  . LYS A 44  ? 0.6207 0.9451 0.7119 0.0141  -0.1915 0.1517  41  LYS A NZ  
303  N N   . GLY A 45  ? 0.5417 0.8328 0.7693 0.0850  -0.0134 0.0885  42  GLY A N   
304  C CA  . GLY A 45  ? 0.4881 0.7507 0.7191 0.0977  0.0105  0.0745  42  GLY A CA  
305  C C   . GLY A 45  ? 0.5393 0.7763 0.7383 0.0831  0.0215  0.0535  42  GLY A C   
306  O O   . GLY A 45  ? 0.5836 0.7925 0.7817 0.0883  0.0371  0.0401  42  GLY A O   
307  N N   . TYR A 46  ? 0.5502 0.7951 0.7259 0.0648  0.0127  0.0507  43  TYR A N   
308  C CA  . TYR A 46  ? 0.5212 0.7514 0.6742 0.0534  0.0205  0.0342  43  TYR A CA  
309  C C   . TYR A 46  ? 0.5296 0.7849 0.6900 0.0513  0.0303  0.0222  43  TYR A C   
310  O O   . TYR A 46  ? 0.4399 0.7269 0.6150 0.0497  0.0285  0.0298  43  TYR A O   
311  C CB  . TYR A 46  ? 0.4624 0.6831 0.5867 0.0389  0.0085  0.0390  43  TYR A CB  
312  C CG  . TYR A 46  ? 0.6081 0.7965 0.7113 0.0399  0.0069  0.0454  43  TYR A CG  
313  C CD1 . TYR A 46  ? 0.5580 0.7415 0.6533 0.0446  -0.0047 0.0616  43  TYR A CD1 
314  C CD2 . TYR A 46  ? 0.5772 0.7437 0.6690 0.0359  0.0173  0.0373  43  TYR A CD2 
315  C CE1 . TYR A 46  ? 0.5873 0.7400 0.6547 0.0457  -0.0031 0.0695  43  TYR A CE1 
316  C CE2 . TYR A 46  ? 0.6332 0.7724 0.7067 0.0366  0.0216  0.0452  43  TYR A CE2 
317  C CZ  . TYR A 46  ? 0.6060 0.7358 0.6626 0.0417  0.0128  0.0614  43  TYR A CZ  
318  O OH  . TYR A 46  ? 0.5949 0.6962 0.6238 0.0426  0.0193  0.0714  43  TYR A OH  
319  N N   . THR A 47  ? 0.5170 0.7591 0.6667 0.0502  0.0408  0.0039  44  THR A N   
320  C CA  . THR A 47  ? 0.4933 0.7540 0.6330 0.0462  0.0487  -0.0084 44  THR A CA  
321  C C   . THR A 47  ? 0.5173 0.7843 0.6357 0.0318  0.0377  -0.0017 44  THR A C   
322  O O   . THR A 47  ? 0.5009 0.7496 0.6097 0.0261  0.0288  0.0011  44  THR A O   
323  C CB  . THR A 47  ? 0.5207 0.7616 0.6506 0.0479  0.0585  -0.0324 44  THR A CB  
324  O OG1 . THR A 47  ? 0.5734 0.8055 0.7226 0.0637  0.0738  -0.0410 44  THR A OG1 
325  C CG2 . THR A 47  ? 0.5279 0.7833 0.6304 0.0398  0.0600  -0.0453 44  THR A CG2 
326  N N   . SER A 48  ? 0.5100 0.8012 0.6223 0.0271  0.0410  0.0029  45  SER A N   
327  C CA  . SER A 48  ? 0.5286 0.8192 0.6213 0.0153  0.0315  0.0119  45  SER A CA  
328  C C   . SER A 48  ? 0.5165 0.8250 0.5889 0.0122  0.0391  0.0102  45  SER A C   
329  O O   . SER A 48  ? 0.5342 0.8616 0.6093 0.0173  0.0545  0.0053  45  SER A O   
330  C CB  . SER A 48  ? 0.5002 0.7925 0.6021 0.0070  0.0221  0.0297  45  SER A CB  
331  O OG  . SER A 48  ? 0.5447 0.8666 0.6646 0.0039  0.0288  0.0390  45  SER A OG  
332  N N   . TYR A 49  ? 0.5302 0.8322 0.5808 0.0059  0.0294  0.0154  46  TYR A N   
333  C CA  . TYR A 49  ? 0.5307 0.8466 0.5521 0.0031  0.0324  0.0181  46  TYR A CA  
334  C C   . TYR A 49  ? 0.5431 0.8524 0.5547 -0.0038 0.0224  0.0402  46  TYR A C   
335  O O   . TYR A 49  ? 0.5144 0.8051 0.5326 -0.0031 0.0104  0.0433  46  TYR A O   
336  C CB  . TYR A 49  ? 0.4882 0.8019 0.4885 0.0055  0.0271  -0.0022 46  TYR A CB  
337  C CG  . TYR A 49  ? 0.5789 0.9071 0.5386 0.0026  0.0256  0.0016  46  TYR A CG  
338  C CD1 . TYR A 49  ? 0.6059 0.9502 0.5442 0.0032  0.0448  0.0037  46  TYR A CD1 
339  C CD2 . TYR A 49  ? 0.6055 0.9343 0.5484 0.0001  0.0055  0.0061  46  TYR A CD2 
340  C CE1 . TYR A 49  ? 0.5750 0.9307 0.4657 0.0004  0.0448  0.0098  46  TYR A CE1 
341  C CE2 . TYR A 49  ? 0.6342 0.9768 0.5336 -0.0018 0.0004  0.0132  46  TYR A CE2 
342  C CZ  . TYR A 49  ? 0.6284 0.9819 0.4964 -0.0022 0.0204  0.0151  46  TYR A CZ  
343  O OH  . TYR A 49  ? 0.6734 1.0388 0.4881 -0.0042 0.0165  0.0246  46  TYR A OH  
344  N N   . ALA A 50  ? 0.5226 0.8447 0.5190 -0.0093 0.0305  0.0563  47  ALA A N   
345  C CA  . ALA A 50  ? 0.5256 0.8348 0.5158 -0.0165 0.0244  0.0811  47  ALA A CA  
346  C C   . ALA A 50  ? 0.6296 0.9498 0.5820 -0.0171 0.0274  0.0952  47  ALA A C   
347  O O   . ALA A 50  ? 0.6192 0.9568 0.5611 -0.0226 0.0449  0.1051  47  ALA A O   
348  C CB  . ALA A 50  ? 0.4776 0.7866 0.4928 -0.0282 0.0315  0.0943  47  ALA A CB  
349  N N   . PRO A 51  ? 0.6238 0.9374 0.5558 -0.0111 0.0111  0.0989  48  PRO A N   
350  C CA  . PRO A 51  ? 0.6725 0.9955 0.5620 -0.0109 0.0090  0.1176  48  PRO A CA  
351  C C   . PRO A 51  ? 0.6557 0.9584 0.5451 -0.0157 0.0100  0.1526  48  PRO A C   
352  O O   . PRO A 51  ? 0.7086 0.9868 0.6296 -0.0197 0.0097  0.1579  48  PRO A O   
353  C CB  . PRO A 51  ? 0.6192 0.9473 0.4982 -0.0022 -0.0148 0.1076  48  PRO A CB  
354  C CG  . PRO A 51  ? 0.6177 0.9288 0.5422 0.0018  -0.0227 0.0987  48  PRO A CG  
355  C CD  . PRO A 51  ? 0.5372 0.8409 0.4863 -0.0036 -0.0060 0.0859  48  PRO A CD  
356  N N   . GLN A 52  ? 0.7079 1.0166 0.5562 -0.0160 0.0114  0.1767  49  GLN A N   
357  C CA  . GLN A 52  ? 0.7435 1.0273 0.5878 -0.0202 0.0133  0.2145  49  GLN A CA  
358  C C   . GLN A 52  ? 0.7637 1.0436 0.5772 -0.0073 -0.0079 0.2366  49  GLN A C   
359  O O   . GLN A 52  ? 0.8224 1.1291 0.5972 -0.0017 -0.0182 0.2296  49  GLN A O   
360  C CB  . GLN A 52  ? 0.7497 1.0436 0.5763 -0.0344 0.0398  0.2342  49  GLN A CB  
361  C CG  . GLN A 52  ? 0.7558 1.0592 0.6263 -0.0474 0.0583  0.2188  49  GLN A CG  
362  C CD  . GLN A 52  ? 0.8118 1.1243 0.6856 -0.0649 0.0848  0.2448  49  GLN A CD  
363  O OE1 . GLN A 52  ? 0.7725 1.0796 0.6922 -0.0805 0.0912  0.2476  49  GLN A OE1 
364  N NE2 . GLN A 52  ? 0.8001 1.1284 0.6246 -0.0642 0.1001  0.2641  49  GLN A NE2 
365  N N   . TYR A 53  ? 0.8086 1.0541 0.6387 -0.0021 -0.0155 0.2630  50  TYR A N   
366  C CA  . TYR A 53  ? 0.8426 1.0876 0.6518 0.0144  -0.0378 0.2884  50  TYR A CA  
367  C C   . TYR A 53  ? 0.9107 1.1607 0.6637 0.0108  -0.0320 0.3241  50  TYR A C   
368  O O   . TYR A 53  ? 0.9207 1.1646 0.6605 -0.0052 -0.0062 0.3358  50  TYR A O   
369  C CB  . TYR A 53  ? 0.8949 1.0978 0.7407 0.0265  -0.0453 0.3073  50  TYR A CB  
370  C CG  . TYR A 53  ? 0.8203 1.0094 0.7154 0.0300  -0.0452 0.2765  50  TYR A CG  
371  C CD1 . TYR A 53  ? 0.8095 1.0304 0.7218 0.0372  -0.0572 0.2461  50  TYR A CD1 
372  C CD2 . TYR A 53  ? 0.8433 0.9841 0.7644 0.0247  -0.0326 0.2782  50  TYR A CD2 
373  C CE1 . TYR A 53  ? 0.7514 0.9577 0.7045 0.0404  -0.0532 0.2213  50  TYR A CE1 
374  C CE2 . TYR A 53  ? 0.7986 0.9238 0.7533 0.0278  -0.0307 0.2501  50  TYR A CE2 
375  C CZ  . TYR A 53  ? 0.7540 0.9125 0.7238 0.0367  -0.0396 0.2237  50  TYR A CZ  
376  O OH  . TYR A 53  ? 0.7032 0.8432 0.7011 0.0398  -0.0341 0.1999  50  TYR A OH  
377  N N   . GLU A 54  ? 0.9839 1.2476 0.7055 0.0257  -0.0569 0.3441  51  GLU A N   
378  C CA  . GLU A 54  ? 1.0089 1.2702 0.6722 0.0248  -0.0546 0.3754  51  GLU A CA  
379  C C   . GLU A 54  ? 1.0654 1.2759 0.7409 0.0223  -0.0393 0.4160  51  GLU A C   
380  O O   . GLU A 54  ? 1.0482 1.2265 0.7683 0.0313  -0.0454 0.4296  51  GLU A O   
381  C CB  . GLU A 54  ? 1.0581 1.3373 0.6984 0.0413  -0.0901 0.3761  51  GLU A CB  
382  C CG  . GLU A 54  ? 1.0860 1.3592 0.6591 0.0412  -0.0926 0.3970  51  GLU A CG  
383  C CD  . GLU A 54  ? 1.2621 1.5509 0.8221 0.0579  -0.1339 0.4022  51  GLU A CD  
384  O OE1 . GLU A 54  ? 1.1900 1.4580 0.7773 0.0749  -0.1497 0.4335  51  GLU A OE1 
385  O OE2 . GLU A 54  ? 1.3587 1.6796 0.8835 0.0540  -0.1509 0.3735  51  GLU A OE2 
386  N N   . GLY A 55  ? 1.1236 1.3229 0.7604 0.0090  -0.0163 0.4335  52  GLY A N   
387  C CA  . GLY A 55  ? 1.1611 1.3106 0.8094 -0.0001 0.0028  0.4692  52  GLY A CA  
388  C C   . GLY A 55  ? 1.1147 1.2493 0.8092 -0.0226 0.0294  0.4635  52  GLY A C   
389  O O   . GLY A 55  ? 1.1218 1.2170 0.8251 -0.0374 0.0484  0.4891  52  GLY A O   
390  N N   . HIS A 56  ? 1.0411 1.2047 0.7664 -0.0276 0.0299  0.4311  53  HIS A N   
391  C CA  . HIS A 56  ? 1.0398 1.1886 0.8161 -0.0490 0.0484  0.4152  53  HIS A CA  
392  C C   . HIS A 56  ? 1.0071 1.1973 0.7768 -0.0687 0.0771  0.4061  53  HIS A C   
393  O O   . HIS A 56  ? 1.0075 1.2356 0.7336 -0.0625 0.0830  0.3976  53  HIS A O   
394  C CB  . HIS A 56  ? 0.9247 1.0716 0.7455 -0.0408 0.0321  0.3718  53  HIS A CB  
395  C CG  . HIS A 56  ? 0.9596 1.0597 0.8015 -0.0240 0.0139  0.3801  53  HIS A CG  
396  N ND1 . HIS A 56  ? 1.0266 1.1263 0.8483 0.0011  -0.0064 0.4009  53  HIS A ND1 
397  C CD2 . HIS A 56  ? 0.8662 0.9186 0.7475 -0.0273 0.0141  0.3700  53  HIS A CD2 
398  C CE1 . HIS A 56  ? 0.9998 1.0550 0.8542 0.0152  -0.0148 0.4045  53  HIS A CE1 
399  N NE2 . HIS A 56  ? 0.9118 0.9339 0.7977 -0.0020 -0.0011 0.3842  53  HIS A NE2 
400  N N   . ALA A 57  ? 0.9583 1.1385 0.7757 -0.0922 0.0942  0.4030  54  ALA A N   
401  C CA  . ALA A 57  ? 0.9646 1.1839 0.7912 -0.1124 0.1255  0.4043  54  ALA A CA  
402  C C   . ALA A 57  ? 1.1297 1.3460 0.9057 -0.1105 0.1429  0.4268  54  ALA A C   
403  O O   . ALA A 57  ? 1.0879 1.3422 0.8396 -0.1089 0.1629  0.4142  54  ALA A O   
404  C CB  . ALA A 57  ? 0.9027 1.1732 0.7397 -0.1046 0.1282  0.3605  54  ALA A CB  
405  N N   . ALA A 58  ? 1.1769 1.3425 0.9355 -0.1098 0.1366  0.4605  55  ALA A N   
406  C CA  . ALA A 58  ? 1.1687 1.3220 0.8680 -0.1041 0.1460  0.4868  55  ALA A CA  
407  C C   . ALA A 58  ? 1.2701 1.3604 0.9794 -0.1141 0.1478  0.5249  55  ALA A C   
408  O O   . ALA A 58  ? 1.2824 1.3364 1.0400 -0.1222 0.1386  0.5260  55  ALA A O   
409  C CB  . ALA A 58  ? 1.1698 1.3339 0.8103 -0.0760 0.1193  0.4811  55  ALA A CB  
410  N N   . PRO A 59  ? 1.3670 1.4378 1.0289 -0.1150 0.1611  0.5555  56  PRO A N   
411  C CA  . PRO A 59  ? 1.4251 1.4282 1.0890 -0.1207 0.1607  0.5939  56  PRO A CA  
412  C C   . PRO A 59  ? 1.4684 1.4330 1.1382 -0.0962 0.1262  0.5989  56  PRO A C   
413  O O   . PRO A 59  ? 1.4492 1.4403 1.0916 -0.0700 0.1011  0.5874  56  PRO A O   
414  C CB  . PRO A 59  ? 1.3621 1.3607 0.9554 -0.1175 0.1749  0.6237  56  PRO A CB  
415  C CG  . PRO A 59  ? 1.4020 1.4621 0.9704 -0.1213 0.1958  0.5999  56  PRO A CG  
416  C CD  . PRO A 59  ? 1.3324 1.4385 0.9449 -0.1181 0.1867  0.5558  56  PRO A CD  
417  N N   . PRO A 60  ? 1.4976 1.3985 1.2048 -0.1041 0.1248  0.6141  57  PRO A N   
418  C CA  . PRO A 60  ? 1.5211 1.3841 1.2449 -0.0785 0.0961  0.6137  57  PRO A CA  
419  C C   . PRO A 60  ? 1.5716 1.4262 1.2485 -0.0459 0.0740  0.6383  57  PRO A C   
420  O O   . PRO A 60  ? 1.5694 1.4227 1.2605 -0.0185 0.0474  0.6303  57  PRO A O   
421  C CB  . PRO A 60  ? 1.5259 1.3120 1.2910 -0.0979 0.1065  0.6248  57  PRO A CB  
422  C CG  . PRO A 60  ? 1.5203 1.2970 1.2743 -0.1287 0.1360  0.6464  57  PRO A CG  
423  C CD  . PRO A 60  ? 1.4791 1.3371 1.2166 -0.1372 0.1502  0.6298  57  PRO A CD  
424  N N   . ASP A 61  ? 1.6129 1.4639 1.2364 -0.0481 0.0839  0.6682  58  ASP A N   
425  C CA  . ASP A 61  ? 1.6249 1.4757 1.1984 -0.0187 0.0592  0.6916  58  ASP A CA  
426  C C   . ASP A 61  ? 1.5862 1.5021 1.1447 0.0021  0.0319  0.6623  58  ASP A C   
427  O O   . ASP A 61  ? 1.6420 1.5601 1.1895 0.0302  0.0006  0.6714  58  ASP A O   
428  C CB  . ASP A 61  ? 1.6971 1.5419 1.2054 -0.0292 0.0772  0.7240  58  ASP A CB  
429  C CG  . ASP A 61  ? 1.8377 1.6097 1.3543 -0.0449 0.0975  0.7615  58  ASP A CG  
430  O OD1 . ASP A 61  ? 1.8776 1.5958 1.3984 -0.0258 0.0804  0.7879  58  ASP A OD1 
431  O OD2 . ASP A 61  ? 1.9408 1.7095 1.4646 -0.0771 0.1313  0.7635  58  ASP A OD2 
432  N N   . GLU A 62  ? 1.5621 1.5317 1.1227 -0.0116 0.0427  0.6267  59  GLU A N   
433  C CA  . GLU A 62  ? 1.5301 1.5572 1.0778 0.0044  0.0178  0.5945  59  GLU A CA  
434  C C   . GLU A 62  ? 1.5031 1.5277 1.1046 0.0247  -0.0097 0.5805  59  GLU A C   
435  O O   . GLU A 62  ? 1.5132 1.5695 1.1049 0.0456  -0.0403 0.5703  59  GLU A O   
436  C CB  . GLU A 62  ? 1.4780 1.5540 1.0244 -0.0143 0.0388  0.5580  59  GLU A CB  
437  C CG  . GLU A 62  ? 1.4939 1.5771 0.9908 -0.0320 0.0707  0.5685  59  GLU A CG  
438  C CD  . GLU A 62  ? 1.6207 1.7310 1.0386 -0.0201 0.0585  0.5644  59  GLU A CD  
439  O OE1 . GLU A 62  ? 1.6994 1.8504 1.1086 -0.0114 0.0405  0.5286  59  GLU A OE1 
440  O OE2 . GLU A 62  ? 1.6729 1.7604 1.0344 -0.0212 0.0667  0.5965  59  GLU A OE2 
441  N N   . ILE A 63  ? 1.4342 1.4203 1.0927 0.0180  0.0010  0.5790  60  ILE A N   
442  C CA  . ILE A 63  ? 1.3498 1.3262 1.0583 0.0390  -0.0197 0.5666  60  ILE A CA  
443  C C   . ILE A 63  ? 1.4491 1.3984 1.1557 0.0690  -0.0429 0.5949  60  ILE A C   
444  O O   . ILE A 63  ? 1.3936 1.3682 1.1234 0.0937  -0.0690 0.5841  60  ILE A O   
445  C CB  . ILE A 63  ? 1.3337 1.2632 1.0939 0.0233  -0.0008 0.5587  60  ILE A CB  
446  C CG1 . ILE A 63  ? 1.2891 1.2585 1.0590 -0.0035 0.0159  0.5282  60  ILE A CG1 
447  C CG2 . ILE A 63  ? 1.3086 1.2137 1.1152 0.0487  -0.0171 0.5498  60  ILE A CG2 
448  C CD1 . ILE A 63  ? 1.2464 1.1762 1.0655 -0.0234 0.0297  0.5164  60  ILE A CD1 
449  N N   . LEU A 64  ? 1.5021 1.4017 1.1845 0.0670  -0.0335 0.6323  61  LEU A N   
450  C CA  . LEU A 64  ? 1.5337 1.4022 1.2149 0.0962  -0.0542 0.6638  61  LEU A CA  
451  C C   . LEU A 64  ? 1.5519 1.4765 1.1942 0.1151  -0.0862 0.6675  61  LEU A C   
452  O O   . LEU A 64  ? 1.4800 1.4018 1.1394 0.1444  -0.1124 0.6829  61  LEU A O   
453  C CB  . LEU A 64  ? 1.6072 1.4085 1.2636 0.0860  -0.0351 0.7043  61  LEU A CB  
454  C CG  . LEU A 64  ? 1.6329 1.3529 1.3347 0.0795  -0.0159 0.7110  61  LEU A CG  
455  C CD1 . LEU A 64  ? 1.6026 1.2582 1.2776 0.0815  -0.0095 0.7564  61  LEU A CD1 
456  C CD2 . LEU A 64  ? 1.6160 1.3220 1.3758 0.1073  -0.0305 0.6922  61  LEU A CD2 
457  N N   . LYS A 65  ? 1.5429 1.5165 1.1341 0.0988  -0.0845 0.6525  62  LYS A N   
458  C CA  . LYS A 65  ? 1.5263 1.5501 1.0724 0.1112  -0.1157 0.6493  62  LYS A CA  
459  C C   . LYS A 65  ? 1.4093 1.4902 0.9912 0.1194  -0.1392 0.6085  62  LYS A C   
460  O O   . LYS A 65  ? 1.4118 1.5370 0.9639 0.1267  -0.1686 0.5986  62  LYS A O   
461  C CB  . LYS A 65  ? 1.6050 1.6469 1.0727 0.0897  -0.0998 0.6481  62  LYS A CB  
462  C CG  . LYS A 65  ? 1.5893 1.5803 1.0123 0.0799  -0.0760 0.6909  62  LYS A CG  
463  C CD  . LYS A 65  ? 1.8039 1.7835 1.1759 0.1003  -0.1040 0.7282  62  LYS A CD  
464  C CE  . LYS A 65  ? 1.8940 1.8037 1.2545 0.0997  -0.0861 0.7786  62  LYS A CE  
465  N NZ  . LYS A 65  ? 1.9303 1.7917 1.3647 0.0935  -0.0638 0.7790  62  LYS A NZ  
466  N N   . SER A 66  ? 1.4044 1.4826 1.0474 0.1165  -0.1273 0.5845  63  SER A N   
467  C CA  . SER A 66  ? 1.2915 1.4207 0.9696 0.1195  -0.1428 0.5446  63  SER A CA  
468  C C   . SER A 66  ? 1.2869 1.4092 1.0349 0.1467  -0.1599 0.5476  63  SER A C   
469  O O   . SER A 66  ? 1.3041 1.3881 1.0666 0.1667  -0.1652 0.5801  63  SER A O   
470  C CB  . SER A 66  ? 1.2346 1.3696 0.9248 0.0958  -0.1147 0.5144  63  SER A CB  
471  O OG  . SER A 66  ? 1.1491 1.3400 0.8431 0.0919  -0.1279 0.4746  63  SER A OG  
472  N N   . SER A 67  ? 1.1636 1.3219 0.9564 0.1483  -0.1660 0.5131  64  SER A N   
473  C CA  . SER A 67  ? 1.0869 1.2459 0.9501 0.1736  -0.1771 0.5104  64  SER A CA  
474  C C   . SER A 67  ? 1.0664 1.2396 0.9699 0.1654  -0.1634 0.4745  64  SER A C   
475  O O   . SER A 67  ? 1.1014 1.3102 0.9792 0.1441  -0.1617 0.4473  64  SER A O   
476  C CB  . SER A 67  ? 1.1653 1.3768 1.0399 0.1908  -0.2152 0.5101  64  SER A CB  
477  O OG  . SER A 67  ? 1.2015 1.4281 1.1535 0.2123  -0.2218 0.4995  64  SER A OG  
478  N N   . PRO A 68  ? 1.1384 1.2796 1.1005 0.1823  -0.1511 0.4729  65  PRO A N   
479  C CA  . PRO A 68  ? 1.0640 1.2218 1.0644 0.1781  -0.1406 0.4393  65  PRO A CA  
480  C C   . PRO A 68  ? 0.9683 1.2001 0.9886 0.1779  -0.1637 0.4112  65  PRO A C   
481  O O   . PRO A 68  ? 0.8829 1.1304 0.9169 0.1637  -0.1534 0.3737  65  PRO A O   
482  C CB  . PRO A 68  ? 1.0553 1.1620 1.1122 0.2034  -0.1245 0.4447  65  PRO A CB  
483  C CG  . PRO A 68  ? 1.1187 1.1721 1.1631 0.2168  -0.1234 0.4813  65  PRO A CG  
484  C CD  . PRO A 68  ? 1.1877 1.2568 1.1673 0.1985  -0.1356 0.5007  65  PRO A CD  
485  N N   . PHE A 69  ? 0.9838 1.2532 1.0057 0.1880  -0.1925 0.4193  66  PHE A N   
486  C CA  . PHE A 69  ? 0.9336 1.2693 0.9802 0.1835  -0.2157 0.3906  66  PHE A CA  
487  C C   . PHE A 69  ? 0.9303 1.2955 0.9166 0.1543  -0.2229 0.3666  66  PHE A C   
488  O O   . PHE A 69  ? 0.9427 1.3488 0.9468 0.1423  -0.2312 0.3330  66  PHE A O   
489  C CB  . PHE A 69  ? 1.0337 1.3982 1.1067 0.2033  -0.2463 0.4074  66  PHE A CB  
490  C CG  . PHE A 69  ? 1.0854 1.4210 1.2205 0.2354  -0.2362 0.4290  66  PHE A CG  
491  C CD1 . PHE A 69  ? 0.9984 1.3190 1.1917 0.2455  -0.2098 0.4127  66  PHE A CD1 
492  C CD2 . PHE A 69  ? 1.1261 1.4442 1.2569 0.2569  -0.2503 0.4651  66  PHE A CD2 
493  C CE1 . PHE A 69  ? 1.0498 1.3377 1.2957 0.2763  -0.1952 0.4277  66  PHE A CE1 
494  C CE2 . PHE A 69  ? 1.1348 1.4217 1.3226 0.2883  -0.2380 0.4827  66  PHE A CE2 
495  C CZ  . PHE A 69  ? 1.1854 1.4561 1.4303 0.2979  -0.2089 0.4620  66  PHE A CZ  
496  N N   . VAL A 70  ? 1.0148 1.3567 0.9307 0.1424  -0.2166 0.3821  67  VAL A N   
497  C CA  . VAL A 70  ? 0.9219 1.2804 0.7795 0.1161  -0.2104 0.3568  67  VAL A CA  
498  C C   . VAL A 70  ? 0.8986 1.2488 0.7741 0.1042  -0.1835 0.3341  67  VAL A C   
499  O O   . VAL A 70  ? 0.8687 1.2457 0.7437 0.0893  -0.1831 0.2953  67  VAL A O   
500  C CB  . VAL A 70  ? 0.9735 1.3053 0.7571 0.1080  -0.2010 0.3812  67  VAL A CB  
501  C CG1 . VAL A 70  ? 0.8769 1.2267 0.6012 0.0842  -0.1905 0.3524  67  VAL A CG1 
502  C CG2 . VAL A 70  ? 0.9415 1.2759 0.7053 0.1232  -0.2292 0.4096  67  VAL A CG2 
503  N N   . TRP A 71  ? 0.9148 1.2137 0.8089 0.1078  -0.1575 0.3486  68  TRP A N   
504  C CA  . TRP A 71  ? 0.8324 1.1036 0.7424 0.0913  -0.1273 0.3154  68  TRP A CA  
505  C C   . TRP A 71  ? 0.8268 1.1203 0.7844 0.0915  -0.1293 0.2759  68  TRP A C   
506  O O   . TRP A 71  ? 0.7082 1.0004 0.6641 0.0747  -0.1131 0.2429  68  TRP A O   
507  C CB  . TRP A 71  ? 0.9058 1.1141 0.8341 0.0956  -0.1057 0.3352  68  TRP A CB  
508  C CG  . TRP A 71  ? 0.9872 1.1679 0.8741 0.0941  -0.1017 0.3793  68  TRP A CG  
509  C CD1 . TRP A 71  ? 1.0081 1.2132 0.8362 0.0839  -0.1059 0.3962  68  TRP A CD1 
510  C CD2 . TRP A 71  ? 1.0436 1.1627 0.9418 0.1021  -0.0899 0.4122  68  TRP A CD2 
511  N NE1 . TRP A 71  ? 1.0856 1.2500 0.8900 0.0842  -0.0965 0.4381  68  TRP A NE1 
512  C CE2 . TRP A 71  ? 1.0921 1.2029 0.9401 0.0952  -0.0879 0.4521  68  TRP A CE2 
513  C CE3 . TRP A 71  ? 1.0391 1.1046 0.9814 0.1141  -0.0786 0.4107  68  TRP A CE3 
514  C CZ2 . TRP A 71  ? 1.0769 1.1243 0.9241 0.0973  -0.0753 0.4864  68  TRP A CZ2 
515  C CZ3 . TRP A 71  ? 1.0586 1.0599 0.9972 0.1183  -0.0676 0.4472  68  TRP A CZ3 
516  C CH2 . TRP A 71  ? 1.0755 1.0687 0.9691 0.1098  -0.0670 0.4892  68  TRP A CH2 
517  N N   . PHE A 72  ? 0.8053 1.1211 0.8097 0.1109  -0.1475 0.2809  69  PHE A N   
518  C CA  . PHE A 72  ? 0.7133 1.0533 0.7635 0.1083  -0.1464 0.2458  69  PHE A CA  
519  C C   . PHE A 72  ? 0.7213 1.1066 0.7485 0.0897  -0.1624 0.2189  69  PHE A C   
520  O O   . PHE A 72  ? 0.6256 1.0120 0.6641 0.0760  -0.1495 0.1846  69  PHE A O   
521  C CB  . PHE A 72  ? 0.6365 0.9955 0.7518 0.1332  -0.1579 0.2586  69  PHE A CB  
522  C CG  . PHE A 72  ? 0.6700 1.0533 0.8370 0.1294  -0.1512 0.2262  69  PHE A CG  
523  C CD1 . PHE A 72  ? 0.5930 0.9396 0.7654 0.1212  -0.1203 0.2009  69  PHE A CD1 
524  C CD2 . PHE A 72  ? 0.5865 1.0307 0.7970 0.1322  -0.1769 0.2231  69  PHE A CD2 
525  C CE1 . PHE A 72  ? 0.5215 0.8871 0.7362 0.1175  -0.1113 0.1757  69  PHE A CE1 
526  C CE2 . PHE A 72  ? 0.5388 1.0039 0.8003 0.1260  -0.1670 0.1963  69  PHE A CE2 
527  C CZ  . PHE A 72  ? 0.4805 0.9036 0.7410 0.1193  -0.1321 0.1738  69  PHE A CZ  
528  N N   . LYS A 73  ? 0.6966 1.1148 0.6860 0.0889  -0.1903 0.2337  70  LYS A N   
529  C CA  . LYS A 73  ? 0.6553 1.1083 0.6118 0.0697  -0.2054 0.2040  70  LYS A CA  
530  C C   . LYS A 73  ? 0.6913 1.1184 0.6019 0.0515  -0.1770 0.1797  70  LYS A C   
531  O O   . LYS A 73  ? 0.7043 1.1424 0.6116 0.0369  -0.1744 0.1430  70  LYS A O   
532  C CB  . LYS A 73  ? 0.7960 1.2759 0.7074 0.0711  -0.2381 0.2220  70  LYS A CB  
533  C CG  . LYS A 73  ? 0.8915 1.3990 0.7724 0.0506  -0.2569 0.1842  70  LYS A CG  
534  C CD  . LYS A 73  ? 1.1031 1.5973 0.8913 0.0419  -0.2576 0.1866  70  LYS A CD  
535  C CE  . LYS A 73  ? 1.1643 1.6799 0.9162 0.0260  -0.2859 0.1548  70  LYS A CE  
536  N NZ  . LYS A 73  ? 1.2074 1.7461 1.0110 0.0122  -0.2954 0.1156  70  LYS A NZ  
537  N N   . ASP A 74  ? 0.6978 1.0908 0.5779 0.0521  -0.1549 0.2006  71  ASP A N   
538  C CA  . ASP A 74  ? 0.7487 1.1238 0.6014 0.0368  -0.1258 0.1800  71  ASP A CA  
539  C C   . ASP A 74  ? 0.7491 1.1111 0.6495 0.0322  -0.1089 0.1495  71  ASP A C   
540  O O   . ASP A 74  ? 0.7335 1.0964 0.6221 0.0209  -0.0945 0.1218  71  ASP A O   
541  C CB  . ASP A 74  ? 0.7611 1.1049 0.5896 0.0361  -0.1046 0.2109  71  ASP A CB  
542  C CG  . ASP A 74  ? 0.8581 1.2121 0.6273 0.0387  -0.1159 0.2433  71  ASP A CG  
543  O OD1 . ASP A 74  ? 0.8540 1.2393 0.5783 0.0346  -0.1319 0.2307  71  ASP A OD1 
544  O OD2 . ASP A 74  ? 0.8865 1.2137 0.6502 0.0442  -0.1093 0.2816  71  ASP A OD2 
545  N N   . ALA A 75  ? 0.6814 1.0307 0.6340 0.0427  -0.1096 0.1548  72  ALA A N   
546  C CA  . ALA A 75  ? 0.6457 0.9831 0.6367 0.0391  -0.0947 0.1284  72  ALA A CA  
547  C C   . ALA A 75  ? 0.6518 1.0198 0.6613 0.0331  -0.1073 0.1007  72  ALA A C   
548  O O   . ALA A 75  ? 0.5751 0.9364 0.5899 0.0234  -0.0940 0.0744  72  ALA A O   
549  C CB  . ALA A 75  ? 0.5659 0.8773 0.5980 0.0526  -0.0875 0.1412  72  ALA A CB  
550  N N   . LEU A 76  ? 0.5811 0.9828 0.6045 0.0379  -0.1341 0.1074  73  LEU A N   
551  C CA  . LEU A 76  ? 0.5464 0.9773 0.5928 0.0271  -0.1479 0.0800  73  LEU A CA  
552  C C   . LEU A 76  ? 0.6005 1.0325 0.5960 0.0104  -0.1478 0.0532  73  LEU A C   
553  O O   . LEU A 76  ? 0.5843 1.0120 0.5928 -0.0013 -0.1404 0.0230  73  LEU A O   
554  C CB  . LEU A 76  ? 0.6128 1.0876 0.6891 0.0334  -0.1814 0.0941  73  LEU A CB  
555  C CG  . LEU A 76  ? 0.5731 1.0558 0.7164 0.0530  -0.1807 0.1163  73  LEU A CG  
556  C CD1 . LEU A 76  ? 0.4458 0.9828 0.6206 0.0585  -0.2179 0.1305  73  LEU A CD1 
557  C CD2 . LEU A 76  ? 0.4912 0.9624 0.6868 0.0508  -0.1563 0.0978  73  LEU A CD2 
558  N N   . ASP A 77  ? 0.6705 1.1042 0.6057 0.0102  -0.1525 0.0646  74  ASP A N   
559  C CA  . ASP A 77  ? 0.6597 1.0898 0.5397 -0.0023 -0.1447 0.0386  74  ASP A CA  
560  C C   . ASP A 77  ? 0.6576 1.0577 0.5457 -0.0046 -0.1099 0.0219  74  ASP A C   
561  O O   . ASP A 77  ? 0.6666 1.0607 0.5368 -0.0131 -0.1003 -0.0090 74  ASP A O   
562  C CB  . ASP A 77  ? 0.6678 1.1034 0.4796 0.0003  -0.1490 0.0602  74  ASP A CB  
563  C CG  . ASP A 77  ? 0.7865 1.2559 0.5752 0.0000  -0.1888 0.0700  74  ASP A CG  
564  O OD1 . ASP A 77  ? 0.8651 1.3572 0.6826 -0.0084 -0.2128 0.0476  74  ASP A OD1 
565  O OD2 . ASP A 77  ? 0.9440 1.4190 0.6885 0.0073  -0.1978 0.1022  74  ASP A OD2 
566  N N   . GLY A 78  ? 0.6165 0.9965 0.5319 0.0031  -0.0921 0.0414  75  GLY A N   
567  C CA  . GLY A 78  ? 0.5950 0.9528 0.5257 0.0011  -0.0655 0.0278  75  GLY A CA  
568  C C   . GLY A 78  ? 0.6395 0.9925 0.6061 -0.0032 -0.0647 0.0011  75  GLY A C   
569  O O   . GLY A 78  ? 0.6381 0.9808 0.5989 -0.0072 -0.0503 -0.0216 75  GLY A O   
570  N N   . TYR A 79  ? 0.5790 0.9392 0.5860 -0.0013 -0.0780 0.0052  76  TYR A N   
571  C CA  . TYR A 79  ? 0.5456 0.9008 0.5907 -0.0073 -0.0746 -0.0154 76  TYR A CA  
572  C C   . TYR A 79  ? 0.5990 0.9629 0.6287 -0.0207 -0.0849 -0.0450 76  TYR A C   
573  O O   . TYR A 79  ? 0.5654 0.9090 0.6021 -0.0264 -0.0712 -0.0670 76  TYR A O   
574  C CB  . TYR A 79  ? 0.5402 0.9082 0.6343 -0.0026 -0.0835 -0.0026 76  TYR A CB  
575  C CG  . TYR A 79  ? 0.5443 0.9128 0.6828 -0.0113 -0.0793 -0.0196 76  TYR A CG  
576  C CD1 . TYR A 79  ? 0.5062 0.8975 0.6592 -0.0265 -0.0979 -0.0387 76  TYR A CD1 
577  C CD2 . TYR A 79  ? 0.4522 0.7976 0.6161 -0.0066 -0.0576 -0.0154 76  TYR A CD2 
578  C CE1 . TYR A 79  ? 0.4434 0.8334 0.6417 -0.0377 -0.0922 -0.0516 76  TYR A CE1 
579  C CE2 . TYR A 79  ? 0.4399 0.7842 0.6423 -0.0151 -0.0503 -0.0259 76  TYR A CE2 
580  C CZ  . TYR A 79  ? 0.4746 0.8409 0.6980 -0.0311 -0.0663 -0.0430 76  TYR A CZ  
581  O OH  . TYR A 79  ? 0.4497 0.8122 0.7163 -0.0425 -0.0563 -0.0510 76  TYR A OH  
582  N N   . ASP A 80  ? 0.5815 0.9724 0.5873 -0.0258 -0.1105 -0.0458 77  ASP A N   
583  C CA  . ASP A 80  ? 0.5820 0.9781 0.5649 -0.0417 -0.1241 -0.0783 77  ASP A CA  
584  C C   . ASP A 80  ? 0.6411 1.0105 0.5746 -0.0420 -0.1015 -0.0999 77  ASP A C   
585  O O   . ASP A 80  ? 0.6902 1.0437 0.6144 -0.0532 -0.0996 -0.1338 77  ASP A O   
586  C CB  . ASP A 80  ? 0.5652 0.9979 0.5209 -0.0468 -0.1600 -0.0726 77  ASP A CB  
587  C CG  . ASP A 80  ? 0.6172 1.0852 0.6341 -0.0454 -0.1848 -0.0532 77  ASP A CG  
588  O OD1 . ASP A 80  ? 0.5228 0.9854 0.6014 -0.0437 -0.1716 -0.0503 77  ASP A OD1 
589  O OD2 . ASP A 80  ? 0.6595 1.1629 0.6622 -0.0449 -0.2171 -0.0394 77  ASP A OD2 
590  N N   . TYR A 81  ? 0.6361 0.9996 0.5410 -0.0299 -0.0828 -0.0813 78  TYR A N   
591  C CA  . TYR A 81  ? 0.6959 1.0408 0.5648 -0.0269 -0.0563 -0.0985 78  TYR A CA  
592  C C   . TYR A 81  ? 0.7312 1.0486 0.6403 -0.0239 -0.0344 -0.1131 78  TYR A C   
593  O O   . TYR A 81  ? 0.7786 1.0760 0.6731 -0.0252 -0.0206 -0.1423 78  TYR A O   
594  C CB  . TYR A 81  ? 0.7246 1.0757 0.5689 -0.0168 -0.0399 -0.0703 78  TYR A CB  
595  C CG  . TYR A 81  ? 0.7007 1.0423 0.5167 -0.0117 -0.0088 -0.0842 78  TYR A CG  
596  C CD1 . TYR A 81  ? 0.8326 1.1748 0.5877 -0.0149 -0.0046 -0.1083 78  TYR A CD1 
597  C CD2 . TYR A 81  ? 0.7067 1.0411 0.5568 -0.0032 0.0163  -0.0738 78  TYR A CD2 
598  C CE1 . TYR A 81  ? 0.8764 1.2113 0.6074 -0.0069 0.0295  -0.1217 78  TYR A CE1 
599  C CE2 . TYR A 81  ? 0.7749 1.1082 0.6101 0.0042  0.0465  -0.0846 78  TYR A CE2 
600  C CZ  . TYR A 81  ? 0.8715 1.2047 0.6483 0.0036  0.0558  -0.1085 78  TYR A CZ  
601  O OH  . TYR A 81  ? 0.9024 1.2356 0.6656 0.0140  0.0910  -0.1204 78  TYR A OH  
602  N N   . LEU A 82  ? 0.6421 0.9549 0.5985 -0.0186 -0.0305 -0.0924 79  LEU A N   
603  C CA  . LEU A 82  ? 0.6922 0.9796 0.6836 -0.0150 -0.0129 -0.1004 79  LEU A CA  
604  C C   . LEU A 82  ? 0.6903 0.9610 0.6965 -0.0264 -0.0186 -0.1286 79  LEU A C   
605  O O   . LEU A 82  ? 0.6934 0.9363 0.7037 -0.0239 -0.0017 -0.1473 79  LEU A O   
606  C CB  . LEU A 82  ? 0.5932 0.8783 0.6214 -0.0097 -0.0117 -0.0742 79  LEU A CB  
607  C CG  . LEU A 82  ? 0.5738 0.8618 0.5949 -0.0008 -0.0005 -0.0522 79  LEU A CG  
608  C CD1 . LEU A 82  ? 0.5632 0.8480 0.6058 0.0013  -0.0058 -0.0294 79  LEU A CD1 
609  C CD2 . LEU A 82  ? 0.5830 0.8581 0.6139 0.0066  0.0194  -0.0583 79  LEU A CD2 
610  N N   . VAL A 83  ? 0.6517 0.9395 0.6706 -0.0392 -0.0424 -0.1313 80  VAL A N   
611  C CA  . VAL A 83  ? 0.7349 1.0094 0.7756 -0.0559 -0.0501 -0.1576 80  VAL A CA  
612  C C   . VAL A 83  ? 0.7922 1.0505 0.7864 -0.0642 -0.0511 -0.1942 80  VAL A C   
613  O O   . VAL A 83  ? 0.7401 0.9633 0.7432 -0.0717 -0.0411 -0.2209 80  VAL A O   
614  C CB  . VAL A 83  ? 0.6962 1.0042 0.7710 -0.0685 -0.0772 -0.1490 80  VAL A CB  
615  C CG1 . VAL A 83  ? 0.6043 0.9032 0.7062 -0.0917 -0.0878 -0.1773 80  VAL A CG1 
616  C CG2 . VAL A 83  ? 0.6215 0.9376 0.7405 -0.0577 -0.0688 -0.1170 80  VAL A CG2 
617  N N   . GLU A 84  ? 0.8559 1.1352 0.7959 -0.0628 -0.0616 -0.1961 81  GLU A N   
618  C CA  . GLU A 84  ? 0.8825 1.1436 0.7641 -0.0680 -0.0574 -0.2321 81  GLU A CA  
619  C C   . GLU A 84  ? 0.9059 1.1279 0.7851 -0.0529 -0.0194 -0.2456 81  GLU A C   
620  O O   . GLU A 84  ? 0.9399 1.1255 0.8041 -0.0586 -0.0101 -0.2826 81  GLU A O   
621  C CB  . GLU A 84  ? 0.9117 1.2022 0.7294 -0.0645 -0.0682 -0.2221 81  GLU A CB  
622  C CG  . GLU A 84  ? 1.0495 1.3233 0.7925 -0.0693 -0.0628 -0.2592 81  GLU A CG  
623  C CD  . GLU A 84  ? 1.3133 1.6050 1.0186 -0.0917 -0.1039 -0.2793 81  GLU A CD  
624  O OE1 . GLU A 84  ? 1.4158 1.7041 1.0393 -0.0954 -0.1064 -0.3019 81  GLU A OE1 
625  O OE2 . GLU A 84  ? 1.3313 1.6434 1.0885 -0.1056 -0.1341 -0.2718 81  GLU A OE2 
626  N N   . GLN A 85  ? 0.8199 1.0482 0.7183 -0.0336 0.0017  -0.2160 82  GLN A N   
627  C CA  . GLN A 85  ? 0.8230 1.0266 0.7292 -0.0155 0.0357  -0.2212 82  GLN A CA  
628  C C   . GLN A 85  ? 0.8211 0.9879 0.7780 -0.0134 0.0453  -0.2269 82  GLN A C   
629  O O   . GLN A 85  ? 0.8491 0.9923 0.8162 0.0035  0.0715  -0.2325 82  GLN A O   
630  C CB  . GLN A 85  ? 0.7903 1.0205 0.7080 0.0003  0.0486  -0.1848 82  GLN A CB  
631  C CG  . GLN A 85  ? 0.7961 1.0526 0.6624 0.0032  0.0545  -0.1788 82  GLN A CG  
632  C CD  . GLN A 85  ? 0.8689 1.1094 0.6883 0.0089  0.0774  -0.2125 82  GLN A CD  
633  O OE1 . GLN A 85  ? 0.8993 1.1482 0.6569 0.0012  0.0705  -0.2257 82  GLN A OE1 
634  N NE2 . GLN A 85  ? 0.9909 1.2089 0.8367 0.0251  0.1067  -0.2245 82  GLN A NE2 
635  N N   . GLY A 86  ? 0.7611 0.9244 0.7532 -0.0283 0.0270  -0.2216 83  GLY A N   
636  C CA  . GLY A 86  ? 0.7623 0.8858 0.7957 -0.0297 0.0372  -0.2270 83  GLY A CA  
637  C C   . GLY A 86  ? 0.7907 0.9197 0.8701 -0.0259 0.0371  -0.1922 83  GLY A C   
638  O O   . GLY A 86  ? 0.8447 0.9396 0.9531 -0.0209 0.0510  -0.1880 83  GLY A O   
639  N N   . TYR A 87  ? 0.7762 0.9432 0.8592 -0.0277 0.0225  -0.1673 84  TYR A N   
640  C CA  . TYR A 87  ? 0.6968 0.8689 0.8100 -0.0212 0.0253  -0.1353 84  TYR A CA  
641  C C   . TYR A 87  ? 0.6986 0.8892 0.8374 -0.0361 0.0097  -0.1271 84  TYR A C   
642  O O   . TYR A 87  ? 0.7162 0.9402 0.8473 -0.0372 -0.0053 -0.1169 84  TYR A O   
643  C CB  . TYR A 87  ? 0.6423 0.8373 0.7392 -0.0065 0.0279  -0.1127 84  TYR A CB  
644  C CG  . TYR A 87  ? 0.6823 0.8692 0.7676 0.0089  0.0455  -0.1171 84  TYR A CG  
645  C CD1 . TYR A 87  ? 0.7179 0.8851 0.8265 0.0223  0.0590  -0.1058 84  TYR A CD1 
646  C CD2 . TYR A 87  ? 0.7273 0.9288 0.7797 0.0115  0.0496  -0.1304 84  TYR A CD2 
647  C CE1 . TYR A 87  ? 0.6532 0.8201 0.7628 0.0393  0.0753  -0.1077 84  TYR A CE1 
648  C CE2 . TYR A 87  ? 0.7516 0.9507 0.8012 0.0275  0.0707  -0.1340 84  TYR A CE2 
649  C CZ  . TYR A 87  ? 0.6974 0.8815 0.7811 0.0421  0.0830  -0.1224 84  TYR A CZ  
650  O OH  . TYR A 87  ? 0.7401 0.9287 0.8318 0.0607  0.1039  -0.1240 84  TYR A OH  
651  N N   . ASP A 88  ? 0.6789 0.8478 0.8523 -0.0463 0.0155  -0.1289 85  ASP A N   
652  C CA  . ASP A 88  ? 0.7020 0.8915 0.9121 -0.0597 0.0071  -0.1190 85  ASP A CA  
653  C C   . ASP A 88  ? 0.6370 0.8414 0.8541 -0.0466 0.0133  -0.0881 85  ASP A C   
654  O O   . ASP A 88  ? 0.5857 0.8204 0.8246 -0.0503 0.0048  -0.0783 85  ASP A O   
655  C CB  . ASP A 88  ? 0.6737 0.8326 0.9207 -0.0741 0.0190  -0.1240 85  ASP A CB  
656  C CG  . ASP A 88  ? 0.8624 0.9925 1.1051 -0.0889 0.0161  -0.1569 85  ASP A CG  
657  O OD1 . ASP A 88  ? 0.9098 1.0617 1.1434 -0.1041 -0.0056 -0.1800 85  ASP A OD1 
658  O OD2 . ASP A 88  ? 0.9923 1.0747 1.2391 -0.0850 0.0351  -0.1595 85  ASP A OD2 
659  N N   . GLU A 89  ? 0.7304 0.7538 0.7873 -0.0724 0.0278  -0.0584 86  GLU A N   
660  C CA  . GLU A 89  ? 0.7185 0.7427 0.7690 -0.0673 0.0254  -0.0241 86  GLU A CA  
661  C C   . GLU A 89  ? 0.6319 0.6991 0.6867 -0.0438 0.0202  -0.0157 86  GLU A C   
662  O O   . GLU A 89  ? 0.6547 0.7109 0.7156 -0.0203 0.0159  -0.0181 86  GLU A O   
663  C CB  . GLU A 89  ? 0.7591 0.7085 0.7962 -0.0617 0.0238  -0.0058 86  GLU A CB  
664  C CG  . GLU A 89  ? 0.8562 0.7455 0.8898 -0.0841 0.0295  -0.0201 86  GLU A CG  
665  C CD  . GLU A 89  ? 0.9565 0.7618 0.9684 -0.0869 0.0283  0.0069  86  GLU A CD  
666  O OE1 . GLU A 89  ? 0.9077 0.7126 0.9001 -0.0833 0.0256  0.0392  86  GLU A OE1 
667  O OE2 . GLU A 89  ? 1.1148 0.8492 1.1246 -0.0943 0.0301  -0.0050 86  GLU A OE2 
668  N N   . ILE A 90  ? 0.6085 0.7238 0.6640 -0.0502 0.0204  -0.0057 87  ILE A N   
669  C CA  . ILE A 90  ? 0.5752 0.7308 0.6336 -0.0366 0.0168  -0.0009 87  ILE A CA  
670  C C   . ILE A 90  ? 0.5758 0.7403 0.6297 -0.0350 0.0165  0.0208  87  ILE A C   
671  O O   . ILE A 90  ? 0.5458 0.7228 0.6028 -0.0468 0.0207  0.0256  87  ILE A O   
672  C CB  . ILE A 90  ? 0.5543 0.7563 0.6144 -0.0456 0.0164  -0.0143 87  ILE A CB  
673  C CG1 . ILE A 90  ? 0.5251 0.7203 0.5842 -0.0478 0.0201  -0.0434 87  ILE A CG1 
674  C CG2 . ILE A 90  ? 0.4828 0.7179 0.5402 -0.0369 0.0135  -0.0010 87  ILE A CG2 
675  C CD1 . ILE A 90  ? 0.5998 0.8347 0.6502 -0.0669 0.0183  -0.0602 87  ILE A CD1 
676  N N   . VAL A 91  ? 0.5238 0.6857 0.5738 -0.0212 0.0124  0.0300  88  VAL A N   
677  C CA  . VAL A 91  ? 0.4791 0.6505 0.5233 -0.0190 0.0126  0.0431  88  VAL A CA  
678  C C   . VAL A 91  ? 0.4998 0.7019 0.5506 -0.0168 0.0106  0.0429  88  VAL A C   
679  O O   . VAL A 91  ? 0.4984 0.7146 0.5535 -0.0154 0.0093  0.0348  88  VAL A O   
680  C CB  . VAL A 91  ? 0.5193 0.6663 0.5497 -0.0111 0.0071  0.0517  88  VAL A CB  
681  C CG1 . VAL A 91  ? 0.4622 0.6173 0.4851 -0.0103 0.0071  0.0571  88  VAL A CG1 
682  C CG2 . VAL A 91  ? 0.5381 0.6504 0.5505 -0.0166 0.0093  0.0598  88  VAL A CG2 
683  N N   . VAL A 92  ? 0.5062 0.7176 0.5574 -0.0165 0.0117  0.0518  89  VAL A N   
684  C CA  . VAL A 92  ? 0.5133 0.7397 0.5643 -0.0152 0.0085  0.0592  89  VAL A CA  
685  C C   . VAL A 92  ? 0.4475 0.6519 0.4921 -0.0117 0.0090  0.0656  89  VAL A C   
686  O O   . VAL A 92  ? 0.4900 0.6784 0.5319 -0.0075 0.0131  0.0656  89  VAL A O   
687  C CB  . VAL A 92  ? 0.4487 0.6980 0.5073 -0.0144 0.0050  0.0660  89  VAL A CB  
688  C CG1 . VAL A 92  ? 0.4391 0.6850 0.5108 -0.0070 0.0096  0.0682  89  VAL A CG1 
689  C CG2 . VAL A 92  ? 0.4504 0.7055 0.5008 -0.0133 -0.0008 0.0805  89  VAL A CG2 
690  N N   . ALA A 93  ? 0.4213 0.6274 0.4628 -0.0168 0.0069  0.0680  90  ALA A N   
691  C CA  . ALA A 93  ? 0.5595 0.7442 0.5947 -0.0204 0.0062  0.0702  90  ALA A CA  
692  C C   . ALA A 93  ? 0.5787 0.7602 0.6105 -0.0289 0.0065  0.0824  90  ALA A C   
693  O O   . ALA A 93  ? 0.5475 0.7538 0.5793 -0.0383 0.0078  0.0852  90  ALA A O   
694  C CB  . ALA A 93  ? 0.4280 0.6199 0.4660 -0.0246 0.0016  0.0612  90  ALA A CB  
695  N N   . GLY A 94  ? 0.5948 0.7425 0.6209 -0.0265 0.0070  0.0895  91  GLY A N   
696  C CA  . GLY A 94  ? 0.5663 0.6966 0.5850 -0.0322 0.0056  0.1084  91  GLY A CA  
697  C C   . GLY A 94  ? 0.6299 0.7135 0.6410 -0.0423 0.0076  0.1083  91  GLY A C   
698  O O   . GLY A 94  ? 0.5859 0.6434 0.5969 -0.0349 0.0098  0.0939  91  GLY A O   
699  N N   . LEU A 95  ? 0.6639 0.7369 0.6653 -0.0632 0.0085  0.1228  92  LEU A N   
700  C CA  . LEU A 95  ? 0.6846 0.7114 0.6785 -0.0831 0.0110  0.1218  92  LEU A CA  
701  C C   . LEU A 95  ? 0.7371 0.7038 0.7178 -0.0782 0.0093  0.1471  92  LEU A C   
702  O O   . LEU A 95  ? 0.6769 0.6501 0.6453 -0.0818 0.0065  0.1748  92  LEU A O   
703  C CB  . LEU A 95  ? 0.6089 0.6683 0.6053 -0.1170 0.0153  0.1200  92  LEU A CB  
704  C CG  . LEU A 95  ? 0.6953 0.7120 0.6848 -0.1498 0.0187  0.1209  92  LEU A CG  
705  C CD1 . LEU A 95  ? 0.6855 0.6677 0.6758 -0.1480 0.0145  0.0947  92  LEU A CD1 
706  C CD2 . LEU A 95  ? 0.6512 0.7204 0.6531 -0.1855 0.0253  0.1179  92  LEU A CD2 
707  N N   . SER A 96  ? 0.6873 0.5928 0.6676 -0.0693 0.0105  0.1374  93  SER A N   
708  C CA  . SER A 96  ? 0.7648 0.5973 0.7369 -0.0592 0.0079  0.1594  93  SER A CA  
709  C C   . SER A 96  ? 0.7964 0.6498 0.7768 -0.0252 -0.0019 0.1832  93  SER A C   
710  O O   . SER A 96  ? 0.7576 0.6460 0.7595 0.0024  -0.0021 0.1670  93  SER A O   
711  C CB  . SER A 96  ? 0.8188 0.6170 0.7700 -0.0996 0.0105  0.1793  93  SER A CB  
712  O OG  . SER A 96  ? 0.9078 0.6148 0.8462 -0.0940 0.0077  0.2020  93  SER A OG  
713  N N   . LEU A 97  ? 0.8168 0.6544 0.7798 -0.0284 -0.0110 0.2217  94  LEU A N   
714  C CA  . LEU A 97  ? 0.8152 0.6875 0.7840 0.0003  -0.0258 0.2447  94  LEU A CA  
715  C C   . LEU A 97  ? 0.7493 0.7106 0.7309 0.0020  -0.0250 0.2250  94  LEU A C   
716  O O   . LEU A 97  ? 0.7179 0.7133 0.7233 0.0305  -0.0327 0.2208  94  LEU A O   
717  C CB  . LEU A 97  ? 0.7573 0.6096 0.6899 -0.0151 -0.0365 0.2911  94  LEU A CB  
718  C CG  . LEU A 97  ? 0.8713 0.7739 0.8008 0.0074  -0.0567 0.3161  94  LEU A CG  
719  C CD1 . LEU A 97  ? 0.7885 0.6611 0.7475 0.0560  -0.0746 0.3300  94  LEU A CD1 
720  C CD2 . LEU A 97  ? 0.9300 0.8334 0.8082 -0.0208 -0.0635 0.3573  94  LEU A CD2 
721  N N   . GLY A 98  ? 0.6859 0.6856 0.6565 -0.0281 -0.0153 0.2113  95  GLY A N   
722  C CA  . GLY A 98  ? 0.6250 0.6935 0.6078 -0.0253 -0.0137 0.1906  95  GLY A CA  
723  C C   . GLY A 98  ? 0.6658 0.7419 0.6764 -0.0036 -0.0106 0.1642  95  GLY A C   
724  O O   . GLY A 98  ? 0.5805 0.7016 0.6043 0.0060  -0.0129 0.1546  95  GLY A O   
725  N N   . GLY A 99  ? 0.6824 0.7144 0.6984 0.0004  -0.0036 0.1504  96  GLY A N   
726  C CA  . GLY A 99  ? 0.5836 0.6230 0.6183 0.0188  0.0028  0.1266  96  GLY A CA  
727  C C   . GLY A 99  ? 0.5928 0.6424 0.6526 0.0499  -0.0018 0.1337  96  GLY A C   
728  O O   . GLY A 99  ? 0.5876 0.6756 0.6671 0.0603  0.0032  0.1186  96  GLY A O   
729  N N   . ASP A 100 ? 0.6677 0.6847 0.7298 0.0649  -0.0121 0.1581  97  ASP A N   
730  C CA  . ASP A 100 ? 0.6990 0.7410 0.7934 0.0984  -0.0225 0.1686  97  ASP A CA  
731  C C   . ASP A 100 ? 0.6680 0.7837 0.7671 0.0926  -0.0344 0.1762  97  ASP A C   
732  O O   . ASP A 100 ? 0.6343 0.7998 0.7680 0.1090  -0.0360 0.1661  97  ASP A O   
733  C CB  . ASP A 100 ? 0.6725 0.6593 0.7659 0.1189  -0.0368 0.1999  97  ASP A CB  
734  C CG  . ASP A 100 ? 0.6998 0.6160 0.8065 0.1388  -0.0246 0.1839  97  ASP A CG  
735  O OD1 . ASP A 100 ? 0.8001 0.7062 0.9421 0.1790  -0.0304 0.1885  97  ASP A OD1 
736  O OD2 . ASP A 100 ? 0.8108 0.6851 0.8952 0.1155  -0.0096 0.1634  97  ASP A OD2 
737  N N   . PHE A 101 ? 0.6105 0.7368 0.6758 0.0666  -0.0410 0.1906  98  PHE A N   
738  C CA  . PHE A 101 ? 0.6056 0.7969 0.6681 0.0572  -0.0510 0.1916  98  PHE A CA  
739  C C   . PHE A 101 ? 0.6218 0.8498 0.7005 0.0481  -0.0380 0.1591  98  PHE A C   
740  O O   . PHE A 101 ? 0.5449 0.8243 0.6408 0.0487  -0.0447 0.1521  98  PHE A O   
741  C CB  . PHE A 101 ? 0.6251 0.8178 0.6439 0.0295  -0.0536 0.2065  98  PHE A CB  
742  C CG  . PHE A 101 ? 0.7209 0.8919 0.7141 0.0336  -0.0713 0.2467  98  PHE A CG  
743  C CD1 . PHE A 101 ? 0.7440 0.9088 0.7597 0.0664  -0.0910 0.2681  98  PHE A CD1 
744  C CD2 . PHE A 101 ? 0.7513 0.9112 0.6987 0.0051  -0.0683 0.2649  98  PHE A CD2 
745  C CE1 . PHE A 101 ? 0.8097 0.9474 0.7971 0.0725  -0.1117 0.3121  98  PHE A CE1 
746  C CE2 . PHE A 101 ? 0.7654 0.8996 0.6788 0.0047  -0.0847 0.3082  98  PHE A CE2 
747  C CZ  . PHE A 101 ? 0.8410 0.9592 0.7718 0.0394  -0.1086 0.3343  98  PHE A CZ  
748  N N   . ALA A 102 ? 0.5706 0.7715 0.6421 0.0373  -0.0213 0.1405  99  ALA A N   
749  C CA  . ALA A 102 ? 0.5449 0.7679 0.6249 0.0292  -0.0105 0.1162  99  ALA A CA  
750  C C   . ALA A 102 ? 0.5223 0.7679 0.6354 0.0450  -0.0059 0.1068  99  ALA A C   
751  O O   . ALA A 102 ? 0.4366 0.7203 0.5627 0.0368  -0.0044 0.0964  99  ALA A O   
752  C CB  . ALA A 102 ? 0.5114 0.7009 0.5754 0.0184  0.0010  0.1036  99  ALA A CB  
753  N N   . LEU A 103 ? 0.5498 0.7726 0.6790 0.0663  -0.0015 0.1081  100 LEU A N   
754  C CA  . LEU A 103 ? 0.5481 0.8033 0.7169 0.0841  0.0066  0.0966  100 LEU A CA  
755  C C   . LEU A 103 ? 0.5033 0.8213 0.7035 0.0899  -0.0100 0.1059  100 LEU A C   
756  O O   . LEU A 103 ? 0.4541 0.8214 0.6800 0.0818  -0.0034 0.0919  100 LEU A O   
757  C CB  . LEU A 103 ? 0.5451 0.7639 0.7303 0.1124  0.0130  0.0948  100 LEU A CB  
758  C CG  . LEU A 103 ? 0.6298 0.7927 0.7879 0.1063  0.0314  0.0765  100 LEU A CG  
759  C CD1 . LEU A 103 ? 0.5547 0.6641 0.7227 0.1331  0.0329  0.0768  100 LEU A CD1 
760  C CD2 . LEU A 103 ? 0.4573 0.6442 0.6166 0.0979  0.0541  0.0510  100 LEU A CD2 
761  N N   . LYS A 104 ? 0.4993 0.8170 0.6951 0.1005  -0.0328 0.1307  101 LYS A N   
762  C CA  . LYS A 104 ? 0.4309 0.8123 0.6524 0.1072  -0.0555 0.1420  101 LYS A CA  
763  C C   . LYS A 104 ? 0.4489 0.8695 0.6532 0.0741  -0.0585 0.1305  101 LYS A C   
764  O O   . LYS A 104 ? 0.4465 0.9308 0.6818 0.0691  -0.0671 0.1223  101 LYS A O   
765  C CB  . LYS A 104 ? 0.4942 0.8563 0.6990 0.1235  -0.0813 0.1769  101 LYS A CB  
766  C CG  . LYS A 104 ? 0.5425 0.9746 0.7782 0.1386  -0.1112 0.1924  101 LYS A CG  
767  C CD  . LYS A 104 ? 0.5319 0.9409 0.7385 0.1527  -0.1407 0.2344  101 LYS A CD  
768  C CE  . LYS A 104 ? 0.6145 1.0780 0.8371 0.1594  -0.1694 0.2382  101 LYS A CE  
769  N NZ  . LYS A 104 ? 0.6830 1.1616 0.9695 0.2017  -0.1801 0.2374  101 LYS A NZ  
770  N N   . LEU A 105 ? 0.4256 0.8105 0.5847 0.0511  -0.0508 0.1266  102 LEU A N   
771  C CA  . LEU A 105 ? 0.4577 0.8682 0.5998 0.0231  -0.0512 0.1111  102 LEU A CA  
772  C C   . LEU A 105 ? 0.4875 0.9161 0.6551 0.0106  -0.0361 0.0871  102 LEU A C   
773  O O   . LEU A 105 ? 0.4716 0.9376 0.6462 -0.0090 -0.0412 0.0737  102 LEU A O   
774  C CB  . LEU A 105 ? 0.5154 0.8848 0.6148 0.0078  -0.0422 0.1086  102 LEU A CB  
775  C CG  . LEU A 105 ? 0.5675 0.9561 0.6479 -0.0162 -0.0414 0.0896  102 LEU A CG  
776  C CD1 . LEU A 105 ? 0.5250 0.9051 0.5657 -0.0255 -0.0428 0.0965  102 LEU A CD1 
777  C CD2 . LEU A 105 ? 0.5397 0.9040 0.6264 -0.0254 -0.0236 0.0675  102 LEU A CD2 
778  N N   . SER A 106 ? 0.4567 0.8560 0.6328 0.0175  -0.0165 0.0808  103 SER A N   
779  C CA  . SER A 106 ? 0.4716 0.8827 0.6639 0.0024  0.0007  0.0634  103 SER A CA  
780  C C   . SER A 106 ? 0.4281 0.9091 0.6699 0.0014  -0.0034 0.0578  103 SER A C   
781  O O   . SER A 106 ? 0.3108 0.8129 0.5652 -0.0233 0.0074  0.0434  103 SER A O   
782  C CB  . SER A 106 ? 0.4072 0.7793 0.5918 0.0108  0.0216  0.0600  103 SER A CB  
783  O OG  . SER A 106 ? 0.4548 0.8552 0.6777 0.0319  0.0285  0.0584  103 SER A OG  
784  N N   . LEU A 107 ? 0.3925 0.9102 0.6653 0.0273  -0.0199 0.0701  104 LEU A N   
785  C CA  . LEU A 107 ? 0.3645 0.9641 0.6941 0.0302  -0.0301 0.0656  104 LEU A CA  
786  C C   . LEU A 107 ? 0.3448 0.9814 0.6651 0.0079  -0.0551 0.0636  104 LEU A C   
787  O O   . LEU A 107 ? 0.2713 0.9550 0.6245 0.0014  -0.0634 0.0537  104 LEU A O   
788  C CB  . LEU A 107 ? 0.3286 0.9487 0.6977 0.0739  -0.0418 0.0809  104 LEU A CB  
789  C CG  . LEU A 107 ? 0.3550 0.9280 0.7299 0.1015  -0.0189 0.0783  104 LEU A CG  
790  C CD1 . LEU A 107 ? 0.3357 0.9234 0.7523 0.1482  -0.0365 0.0944  104 LEU A CD1 
791  C CD2 . LEU A 107 ? 0.3896 0.9863 0.7906 0.0896  0.0150  0.0531  104 LEU A CD2 
792  N N   . ASN A 108 ? 0.4052 1.0102 0.6744 -0.0052 -0.0646 0.0685  105 ASN A N   
793  C CA  . ASN A 108 ? 0.4244 1.0585 0.6722 -0.0264 -0.0864 0.0629  105 ASN A CA  
794  C C   . ASN A 108 ? 0.4476 1.0588 0.6637 -0.0623 -0.0751 0.0390  105 ASN A C   
795  O O   . ASN A 108 ? 0.4306 1.0687 0.6336 -0.0854 -0.0885 0.0239  105 ASN A O   
796  C CB  . ASN A 108 ? 0.4051 1.0286 0.6151 -0.0101 -0.1091 0.0885  105 ASN A CB  
797  C CG  . ASN A 108 ? 0.4363 1.0755 0.6749 0.0247  -0.1274 0.1121  105 ASN A CG  
798  O OD1 . ASN A 108 ? 0.3763 1.0560 0.6260 0.0255  -0.1498 0.1138  105 ASN A OD1 
799  N ND2 . ASN A 108 ? 0.3885 0.9937 0.6411 0.0547  -0.1189 0.1291  105 ASN A ND2 
800  N N   . ARG A 109 ? 0.3820 0.9273 0.5781 -0.0648 -0.0502 0.0333  106 ARG A N   
801  C CA  . ARG A 109 ? 0.4275 0.9338 0.5970 -0.0913 -0.0382 0.0112  106 ARG A CA  
802  C C   . ARG A 109 ? 0.4714 0.9338 0.6482 -0.0958 -0.0138 0.0083  106 ARG A C   
803  O O   . ARG A 109 ? 0.5048 0.9560 0.6911 -0.0764 -0.0039 0.0220  106 ARG A O   
804  C CB  . ARG A 109 ? 0.4989 0.9642 0.6226 -0.0859 -0.0381 0.0116  106 ARG A CB  
805  C CG  . ARG A 109 ? 0.4375 0.9391 0.5394 -0.0836 -0.0584 0.0196  106 ARG A CG  
806  C CD  . ARG A 109 ? 0.5002 1.0423 0.5967 -0.1118 -0.0705 -0.0052 106 ARG A CD  
807  N NE  . ARG A 109 ? 0.5096 1.0757 0.5639 -0.1160 -0.0857 -0.0032 106 ARG A NE  
808  C CZ  . ARG A 109 ? 0.5530 1.1747 0.6036 -0.1128 -0.1127 0.0148  106 ARG A CZ  
809  N NH1 . ARG A 109 ? 0.5066 1.1542 0.6000 -0.0990 -0.1236 0.0288  106 ARG A NH1 
810  N NH2 . ARG A 109 ? 0.4927 1.1196 0.4913 -0.1184 -0.1204 0.0190  106 ARG A NH2 
811  N N   . ASP A 110 ? 0.4704 0.9023 0.6370 -0.1224 -0.0042 -0.0099 107 ASP A N   
812  C CA  . ASP A 110 ? 0.4452 0.8243 0.6054 -0.1301 0.0165  -0.0078 107 ASP A CA  
813  C C   . ASP A 110 ? 0.5016 0.8201 0.6286 -0.1083 0.0207  0.0021  107 ASP A C   
814  O O   . ASP A 110 ? 0.4900 0.7771 0.5960 -0.1075 0.0170  -0.0080 107 ASP A O   
815  C CB  . ASP A 110 ? 0.4278 0.7818 0.5846 -0.1655 0.0221  -0.0273 107 ASP A CB  
816  C CG  . ASP A 110 ? 0.5396 0.9604 0.7344 -0.1959 0.0183  -0.0404 107 ASP A CG  
817  O OD1 . ASP A 110 ? 0.5036 0.9836 0.7359 -0.1926 0.0216  -0.0316 107 ASP A OD1 
818  O OD2 . ASP A 110 ? 0.6365 1.0533 0.8270 -0.2248 0.0124  -0.0634 107 ASP A OD2 
819  N N   . VAL A 111 ? 0.4710 0.7771 0.5956 -0.0911 0.0289  0.0182  108 VAL A N   
820  C CA  . VAL A 111 ? 0.4928 0.7485 0.5892 -0.0750 0.0306  0.0266  108 VAL A CA  
821  C C   . VAL A 111 ? 0.5323 0.7485 0.6129 -0.0826 0.0441  0.0348  108 VAL A C   
822  O O   . VAL A 111 ? 0.5063 0.7399 0.5974 -0.0964 0.0570  0.0367  108 VAL A O   
823  C CB  . VAL A 111 ? 0.4907 0.7571 0.5854 -0.0513 0.0254  0.0376  108 VAL A CB  
824  C CG1 . VAL A 111 ? 0.4362 0.7352 0.5355 -0.0463 0.0115  0.0366  108 VAL A CG1 
825  C CG2 . VAL A 111 ? 0.3663 0.6496 0.4756 -0.0435 0.0349  0.0443  108 VAL A CG2 
826  N N   . LYS A 112 ? 0.5725 0.7401 0.6274 -0.0738 0.0406  0.0405  109 LYS A N   
827  C CA  . LYS A 112 ? 0.5437 0.6704 0.5718 -0.0785 0.0481  0.0543  109 LYS A CA  
828  C C   . LYS A 112 ? 0.5469 0.6845 0.5628 -0.0669 0.0526  0.0624  109 LYS A C   
829  O O   . LYS A 112 ? 0.5723 0.6918 0.5627 -0.0764 0.0633  0.0720  109 LYS A O   
830  C CB  . LYS A 112 ? 0.6353 0.7095 0.6438 -0.0683 0.0370  0.0594  109 LYS A CB  
831  C CG  . LYS A 112 ? 0.6890 0.7344 0.7050 -0.0773 0.0349  0.0479  109 LYS A CG  
832  C CD  . LYS A 112 ? 0.8106 0.8331 0.8196 -0.1082 0.0477  0.0525  109 LYS A CD  
833  C CE  . LYS A 112 ? 0.8650 0.8205 0.8378 -0.1102 0.0474  0.0765  109 LYS A CE  
834  N NZ  . LYS A 112 ? 0.9869 0.8932 0.9523 -0.1410 0.0566  0.0783  109 LYS A NZ  
835  N N   . GLY A 113 ? 0.4667 0.6274 0.4942 -0.0491 0.0452  0.0584  110 GLY A N   
836  C CA  . GLY A 113 ? 0.4498 0.6106 0.4646 -0.0386 0.0485  0.0609  110 GLY A CA  
837  C C   . GLY A 113 ? 0.4817 0.6598 0.5132 -0.0236 0.0397  0.0577  110 GLY A C   
838  O O   . GLY A 113 ? 0.4571 0.6456 0.5005 -0.0215 0.0298  0.0565  110 GLY A O   
839  N N   . ILE A 114 ? 0.4555 0.6319 0.4829 -0.0153 0.0452  0.0557  111 ILE A N   
840  C CA  . ILE A 114 ? 0.4587 0.6368 0.4970 -0.0033 0.0389  0.0560  111 ILE A CA  
841  C C   . ILE A 114 ? 0.5099 0.6588 0.5233 -0.0034 0.0362  0.0529  111 ILE A C   
842  O O   . ILE A 114 ? 0.5132 0.6478 0.5026 -0.0075 0.0436  0.0469  111 ILE A O   
843  C CB  . ILE A 114 ? 0.4736 0.6711 0.5380 0.0093  0.0475  0.0532  111 ILE A CB  
844  C CG1 . ILE A 114 ? 0.4755 0.7151 0.5697 0.0063  0.0474  0.0544  111 ILE A CG1 
845  C CG2 . ILE A 114 ? 0.4701 0.6538 0.5411 0.0225  0.0391  0.0590  111 ILE A CG2 
846  C CD1 . ILE A 114 ? 0.4714 0.7416 0.5937 0.0133  0.0632  0.0463  111 ILE A CD1 
847  N N   . VAL A 115 ? 0.5002 0.6433 0.5167 -0.0028 0.0261  0.0562  112 VAL A N   
848  C CA  . VAL A 115 ? 0.5921 0.7114 0.5919 -0.0076 0.0226  0.0507  112 VAL A CA  
849  C C   . VAL A 115 ? 0.5965 0.7016 0.6075 -0.0045 0.0219  0.0552  112 VAL A C   
850  O O   . VAL A 115 ? 0.5548 0.6717 0.5751 -0.0086 0.0153  0.0664  112 VAL A O   
851  C CB  . VAL A 115 ? 0.5331 0.6595 0.5264 -0.0169 0.0096  0.0514  112 VAL A CB  
852  C CG1 . VAL A 115 ? 0.5323 0.6414 0.5096 -0.0271 0.0045  0.0424  112 VAL A CG1 
853  C CG2 . VAL A 115 ? 0.4752 0.6062 0.4582 -0.0156 0.0064  0.0538  112 VAL A CG2 
854  N N   . THR A 116 ? 0.5585 0.6340 0.5650 0.0020  0.0299  0.0464  113 THR A N   
855  C CA  . THR A 116 ? 0.5560 0.5994 0.5686 0.0050  0.0281  0.0526  113 THR A CA  
856  C C   . THR A 116 ? 0.6147 0.6243 0.6065 -0.0140 0.0261  0.0404  113 THR A C   
857  O O   . THR A 116 ? 0.6645 0.6658 0.6363 -0.0195 0.0299  0.0207  113 THR A O   
858  C CB  . THR A 116 ? 0.5493 0.5766 0.5797 0.0297  0.0375  0.0495  113 THR A CB  
859  O OG1 . THR A 116 ? 0.6211 0.6236 0.6377 0.0325  0.0514  0.0238  113 THR A OG1 
860  C CG2 . THR A 116 ? 0.5578 0.6339 0.6134 0.0439  0.0393  0.0557  113 THR A CG2 
861  N N   . MET A 117 ? 0.6946 0.6884 0.6880 -0.0283 0.0198  0.0523  114 MET A N   
862  C CA  . MET A 117 ? 0.7080 0.6753 0.6876 -0.0541 0.0167  0.0411  114 MET A CA  
863  C C   . MET A 117 ? 0.6975 0.6027 0.6757 -0.0576 0.0201  0.0491  114 MET A C   
864  O O   . MET A 117 ? 0.6825 0.5842 0.6660 -0.0632 0.0171  0.0748  114 MET A O   
865  C CB  . MET A 117 ? 0.6495 0.6617 0.6364 -0.0760 0.0078  0.0475  114 MET A CB  
866  C CG  . MET A 117 ? 0.6469 0.7001 0.6315 -0.0773 -0.0003 0.0345  114 MET A CG  
867  S SD  . MET A 117 ? 0.6598 0.7781 0.6699 -0.0856 -0.0088 0.0421  114 MET A SD  
868  C CE  . MET A 117 ? 0.6075 0.7371 0.6282 -0.0744 0.0004  0.0623  114 MET A CE  
869  N N   . CYS A 118 ? 0.7107 0.5627 0.6770 -0.0559 0.0267  0.0270  115 CYS A N   
870  C CA  . CYS A 118 ? 0.7795 0.5544 0.7437 -0.0562 0.0305  0.0312  115 CYS A CA  
871  C C   . CYS A 118 ? 0.8486 0.6121 0.8309 -0.0260 0.0285  0.0631  115 CYS A C   
872  O O   . CYS A 118 ? 0.9256 0.6482 0.9042 -0.0345 0.0235  0.0902  115 CYS A O   
873  C CB  . CYS A 118 ? 0.8702 0.6219 0.8240 -0.0991 0.0255  0.0362  115 CYS A CB  
874  S SG  . CYS A 118 ? 0.8867 0.6667 0.8258 -0.1370 0.0201  -0.0003 115 CYS A SG  
875  N N   . ALA A 119 ? 0.7626 0.5645 0.7635 0.0077  0.0315  0.0611  116 ALA A N   
876  C CA  . ALA A 119 ? 0.7807 0.5878 0.8036 0.0376  0.0245  0.0901  116 ALA A CA  
877  C C   . ALA A 119 ? 0.8582 0.6010 0.8972 0.0705  0.0299  0.0835  116 ALA A C   
878  O O   . ALA A 119 ? 0.9109 0.6481 0.9572 0.0854  0.0449  0.0488  116 ALA A O   
879  C CB  . ALA A 119 ? 0.7350 0.6209 0.7780 0.0546  0.0238  0.0900  116 ALA A CB  
880  N N   . PRO A 120 ? 0.9405 0.6334 0.9839 0.0840  0.0185  0.1159  117 PRO A N   
881  C CA  . PRO A 120 ? 0.9561 0.5781 1.0206 0.1224  0.0217  0.1111  117 PRO A CA  
882  C C   . PRO A 120 ? 0.8968 0.5703 1.0093 0.1732  0.0201  0.1105  117 PRO A C   
883  O O   . PRO A 120 ? 0.8682 0.6200 0.9952 0.1785  0.0082  0.1305  117 PRO A O   
884  C CB  . PRO A 120 ? 1.0311 0.5814 1.0779 0.1151  0.0055  0.1564  117 PRO A CB  
885  C CG  . PRO A 120 ? 0.9591 0.5799 0.9893 0.0906  -0.0078 0.1898  117 PRO A CG  
886  C CD  . PRO A 120 ? 0.8512 0.5378 0.8726 0.0592  0.0041  0.1577  117 PRO A CD  
887  N N   . MET A 121 ? 0.8734 0.5030 1.0137 0.2103  0.0329  0.0843  118 MET A N   
888  C CA  . MET A 121 ? 0.9520 0.6290 1.1508 0.2637  0.0339  0.0794  118 MET A CA  
889  C C   . MET A 121 ? 1.0477 0.6377 1.2726 0.3087  0.0240  0.0958  118 MET A C   
890  O O   . MET A 121 ? 1.1439 0.6523 1.3688 0.3211  0.0419  0.0633  118 MET A O   
891  C CB  . MET A 121 ? 0.8219 0.5411 1.0383 0.2721  0.0647  0.0253  118 MET A CB  
892  C CG  . MET A 121 ? 0.9102 0.7280 1.1179 0.2440  0.0712  0.0174  118 MET A CG  
893  S SD  . MET A 121 ? 0.8312 0.7583 1.0907 0.2654  0.0531  0.0469  118 MET A SD  
894  C CE  . MET A 121 ? 0.6621 0.6098 0.8681 0.2120  0.0342  0.0771  118 MET A CE  
895  N N   . GLY A 122 ? 1.0836 0.6890 1.3294 0.3345  -0.0054 0.1450  119 GLY A N   
896  C CA  . GLY A 122 ? 1.2641 0.7760 1.5297 0.3788  -0.0213 0.1718  119 GLY A CA  
897  C C   . GLY A 122 ? 1.4346 0.8897 1.6493 0.3512  -0.0491 0.2329  119 GLY A C   
898  O O   . GLY A 122 ? 1.4663 0.8926 1.6241 0.2938  -0.0428 0.2369  119 GLY A O   
899  N N   . GLY A 123 ? 1.6857 1.1413 1.9007 0.3813  -0.0830 0.2681  120 GLY A N   
900  C CA  . GLY A 123 ? 1.7788 1.1895 1.9297 0.3534  -0.1088 0.3233  120 GLY A CA  
901  C C   . GLY A 123 ? 2.0150 1.2793 2.1181 0.3459  -0.1087 0.3359  120 GLY A C   
902  O O   . GLY A 123 ? 2.1509 1.3689 2.2060 0.3463  -0.1309 0.3823  120 GLY A O   
903  N N   . LYS A 124 ? 1.9923 1.1812 2.1015 0.3367  -0.0817 0.2938  121 LYS A N   
904  C CA  . LYS A 124 ? 2.1789 1.2237 2.2371 0.3174  -0.0790 0.3003  121 LYS A CA  
905  C C   . LYS A 124 ? 2.3671 1.3853 2.3579 0.2474  -0.0758 0.3381  121 LYS A C   
906  O O   . LYS A 124 ? 2.2424 1.2678 2.2270 0.1958  -0.0550 0.3152  121 LYS A O   
907  C CB  . LYS A 124 ? 2.0693 1.0529 2.1485 0.3150  -0.0515 0.2366  121 LYS A CB  
908  C CG  . LYS A 124 ? 2.2538 1.0914 2.2795 0.2802  -0.0511 0.2378  121 LYS A CG  
909  C CD  . LYS A 124 ? 2.2018 1.0031 2.2421 0.2529  -0.0240 0.1715  121 LYS A CD  
910  C CE  . LYS A 124 ? 2.3005 0.9769 2.3073 0.2071  -0.0310 0.1740  121 LYS A CE  
911  N NZ  . LYS A 124 ? 2.3419 0.9863 2.3570 0.1776  -0.0038 0.1053  121 LYS A NZ  
912  N N   . THR A 125 ? 2.5901 1.5850 2.5319 0.2452  -0.0919 0.3944  122 THR A N   
913  C CA  . THR A 125 ? 2.6072 1.5973 2.4908 0.1809  -0.0816 0.4317  122 THR A CA  
914  C C   . THR A 125 ? 2.7095 1.5702 2.5553 0.1525  -0.0585 0.4482  122 THR A C   
915  O O   . THR A 125 ? 2.7161 1.5799 2.5310 0.0948  -0.0451 0.4768  122 THR A O   
916  C CB  . THR A 125 ? 2.5546 1.6172 2.4109 0.1879  -0.1058 0.4820  122 THR A CB  
917  O OG1 . THR A 125 ? 2.6552 1.6739 2.5114 0.2487  -0.1288 0.5070  122 THR A OG1 
918  C CG2 . THR A 125 ? 2.3913 1.5976 2.2834 0.1907  -0.1177 0.4668  122 THR A CG2 
919  N N   . GLU A 126 ? 2.7477 1.5131 2.6089 0.1877  -0.0536 0.4266  123 GLU A N   
920  C CA  . GLU A 126 ? 2.8462 1.5025 2.6987 0.1608  -0.0285 0.4453  123 GLU A CA  
921  C C   . GLU A 126 ? 2.7650 1.4109 2.6614 0.0980  -0.0010 0.4028  123 GLU A C   
922  O O   . GLU A 126 ? 2.6748 1.3745 2.6054 0.0919  0.0016  0.3509  123 GLU A O   
923  C CB  . GLU A 126 ? 2.9521 1.5090 2.8091 0.2259  -0.0341 0.4424  123 GLU A CB  
924  C CG  . GLU A 126 ? 3.0207 1.5818 2.8566 0.2813  -0.0662 0.4981  123 GLU A CG  
925  C CD  . GLU A 126 ? 3.0078 1.6993 2.8604 0.3149  -0.1010 0.4960  123 GLU A CD  
926  O OE1 . GLU A 126 ? 2.9628 1.7041 2.8666 0.3487  -0.1096 0.4445  123 GLU A OE1 
927  O OE2 . GLU A 126 ? 3.0070 1.7574 2.8292 0.3052  -0.1182 0.5445  123 GLU A OE2 
928  N N   . GLY A 127 ? 2.5725 1.1516 2.4721 0.0475  0.0082  0.4253  124 GLY A N   
929  C CA  . GLY A 127 ? 2.3821 0.9444 2.3051 -0.0203 0.0147  0.3847  124 GLY A CA  
930  C C   . GLY A 127 ? 2.2106 0.8670 2.1011 -0.0778 0.0196  0.3805  124 GLY A C   
931  O O   . GLY A 127 ? 2.1911 0.8654 2.0434 -0.1244 0.0262  0.4172  124 GLY A O   
932  N N   . ALA A 128 ? 2.1412 1.1619 1.7660 0.0076  0.2919  0.0808  125 ALA A N   
933  C CA  . ALA A 128 ? 1.9791 1.1060 1.6246 -0.0337 0.2570  0.0969  125 ALA A CA  
934  C C   . ALA A 128 ? 1.8986 1.1541 1.6355 0.0018  0.2424  0.1284  125 ALA A C   
935  O O   . ALA A 128 ? 1.8404 1.1640 1.6002 -0.0273 0.2158  0.1582  125 ALA A O   
936  C CB  . ALA A 128 ? 1.8870 1.0262 1.5020 -0.0471 0.2622  0.0683  125 ALA A CB  
937  N N   . ILE A 129 ? 1.8966 1.1888 1.6849 0.0621  0.2605  0.1222  126 ILE A N   
938  C CA  . ILE A 129 ? 1.8010 1.2058 1.6614 0.0903  0.2472  0.1473  126 ILE A CA  
939  C C   . ILE A 129 ? 1.8457 1.2492 1.7218 0.0944  0.2355  0.1813  126 ILE A C   
940  O O   . ILE A 129 ? 1.7435 1.2287 1.6555 0.0920  0.2191  0.2082  126 ILE A O   
941  C CB  . ILE A 129 ? 1.7585 1.2026 1.6647 0.1444  0.2667  0.1306  126 ILE A CB  
942  C CG1 . ILE A 129 ? 1.7374 1.1871 1.6254 0.1353  0.2804  0.1001  126 ILE A CG1 
943  C CG2 . ILE A 129 ? 1.6290 1.1738 1.5956 0.1691  0.2532  0.1535  126 ILE A CG2 
944  C CD1 . ILE A 129 ? 1.5767 1.0589 1.4382 0.0888  0.2599  0.1065  126 ILE A CD1 
945  N N   . TYR A 130 ? 1.9246 1.2279 1.7677 0.1008  0.2471  0.1817  127 TYR A N   
946  C CA  . TYR A 130 ? 1.9040 1.1938 1.7561 0.1102  0.2393  0.2159  127 TYR A CA  
947  C C   . TYR A 130 ? 1.8705 1.1703 1.7021 0.0503  0.2187  0.2411  127 TYR A C   
948  O O   . TYR A 130 ? 1.8191 1.1988 1.6875 0.0506  0.2052  0.2713  127 TYR A O   
949  C CB  . TYR A 130 ? 2.0631 1.2302 1.8802 0.1370  0.2615  0.2108  127 TYR A CB  
950  C CG  . TYR A 130 ? 2.0744 1.2095 1.8906 0.1503  0.2556  0.2486  127 TYR A CG  
951  C CD1 . TYR A 130 ? 2.0288 1.2168 1.8958 0.2083  0.2526  0.2704  127 TYR A CD1 
952  C CD2 . TYR A 130 ? 2.1512 1.2008 1.9108 0.1008  0.2522  0.2639  127 TYR A CD2 
953  C CE1 . TYR A 130 ? 2.0934 1.2483 1.9512 0.2210  0.2463  0.3084  127 TYR A CE1 
954  C CE2 . TYR A 130 ? 2.1881 1.1998 1.9398 0.1113  0.2496  0.3008  127 TYR A CE2 
955  C CZ  . TYR A 130 ? 2.2021 1.2650 2.0012 0.1739  0.2469  0.3239  127 TYR A CZ  
956  O OH  . TYR A 130 ? 2.2441 1.2657 2.0274 0.1847  0.2432  0.3642  127 TYR A OH  
957  N N   . GLU A 131 ? 1.9364 1.1567 1.7073 -0.0044 0.2174  0.2292  128 GLU A N   
958  C CA  . GLU A 131 ? 1.9252 1.1655 1.6823 -0.0700 0.1958  0.2539  128 GLU A CA  
959  C C   . GLU A 131 ? 1.8663 1.2517 1.6819 -0.0793 0.1765  0.2730  128 GLU A C   
960  O O   . GLU A 131 ? 1.8368 1.2764 1.6739 -0.1094 0.1634  0.3067  128 GLU A O   
961  C CB  . GLU A 131 ? 2.0044 1.1488 1.6837 -0.1346 0.1930  0.2310  128 GLU A CB  
962  C CG  . GLU A 131 ? 2.1434 1.2929 1.7976 -0.1449 0.1934  0.1943  128 GLU A CG  
963  C CD  . GLU A 131 ? 2.0973 1.3828 1.7947 -0.1669 0.1672  0.2065  128 GLU A CD  
964  O OE1 . GLU A 131 ? 2.0771 1.3755 1.7607 -0.1620 0.1693  0.1815  128 GLU A OE1 
965  O OE2 . GLU A 131 ? 2.0614 1.4355 1.8017 -0.1912 0.1464  0.2425  128 GLU A OE2 
966  N N   . GLY A 132 ? 1.8419 1.2884 1.6839 -0.0516 0.1789  0.2537  129 GLY A N   
967  C CA  . GLY A 132 ? 1.6919 1.2602 1.5805 -0.0579 0.1649  0.2709  129 GLY A CA  
968  C C   . GLY A 132 ? 1.6160 1.2628 1.5586 -0.0210 0.1684  0.2986  129 GLY A C   
969  O O   . GLY A 132 ? 1.5541 1.2817 1.5284 -0.0382 0.1598  0.3282  129 GLY A O   
970  N N   . PHE A 133 ? 1.5750 1.2026 1.5279 0.0303  0.1819  0.2900  130 PHE A N   
971  C CA  . PHE A 133 ? 1.4761 1.1567 1.4608 0.0598  0.1839  0.3157  130 PHE A CA  
972  C C   . PHE A 133 ? 1.5380 1.2020 1.5116 0.0293  0.1787  0.3509  130 PHE A C   
973  O O   . PHE A 133 ? 1.5430 1.2758 1.5415 0.0291  0.1792  0.3793  130 PHE A O   
974  C CB  . PHE A 133 ? 1.4375 1.0912 1.4278 0.1118  0.1928  0.3018  130 PHE A CB  
975  C CG  . PHE A 133 ? 1.3458 1.0712 1.3653 0.1450  0.1929  0.3145  130 PHE A CG  
976  C CD1 . PHE A 133 ? 1.3114 1.1132 1.3484 0.1363  0.1936  0.3280  130 PHE A CD1 
977  C CD2 . PHE A 133 ? 1.4178 1.1328 1.4443 0.1855  0.1929  0.3137  130 PHE A CD2 
978  C CE1 . PHE A 133 ? 1.3189 1.1705 1.3671 0.1638  0.1975  0.3356  130 PHE A CE1 
979  C CE2 . PHE A 133 ? 1.3809 1.1569 1.4221 0.2084  0.1897  0.3232  130 PHE A CE2 
980  C CZ  . PHE A 133 ? 1.3415 1.1784 1.3871 0.1958  0.1936  0.3317  130 PHE A CZ  
981  N N   . LEU A 134 ? 1.6437 1.2109 1.5748 0.0005  0.1776  0.3492  131 LEU A N   
982  C CA  . LEU A 134 ? 1.6664 1.2049 1.5799 -0.0366 0.1745  0.3825  131 LEU A CA  
983  C C   . LEU A 134 ? 1.6612 1.2794 1.5974 -0.0911 0.1632  0.4038  131 LEU A C   
984  O O   . LEU A 134 ? 1.5553 1.2284 1.5147 -0.1026 0.1652  0.4391  131 LEU A O   
985  C CB  . LEU A 134 ? 1.6233 1.0236 1.4759 -0.0592 0.1790  0.3715  131 LEU A CB  
986  C CG  . LEU A 134 ? 1.7148 1.0292 1.5468 -0.0078 0.1924  0.3730  131 LEU A CG  
987  C CD1 . LEU A 134 ? 1.8829 1.0478 1.6469 -0.0337 0.2026  0.3627  131 LEU A CD1 
988  C CD2 . LEU A 134 ? 1.7469 1.0980 1.5953 0.0111  0.1912  0.4136  131 LEU A CD2 
989  N N   . GLU A 135 ? 1.6477 1.2764 1.5774 -0.1252 0.1514  0.3850  132 GLU A N   
990  C CA  . GLU A 135 ? 1.6015 1.3243 1.5632 -0.1737 0.1360  0.4084  132 GLU A CA  
991  C C   . GLU A 135 ? 1.5129 1.3619 1.5390 -0.1356 0.1427  0.4279  132 GLU A C   
992  O O   . GLU A 135 ? 1.4998 1.4379 1.5676 -0.1592 0.1403  0.4630  132 GLU A O   
993  C CB  . GLU A 135 ? 1.6807 1.3872 1.6146 -0.2130 0.1183  0.3836  132 GLU A CB  
994  C CG  . GLU A 135 ? 1.8192 1.4344 1.6928 -0.2848 0.1059  0.3790  132 GLU A CG  
995  C CD  . GLU A 135 ? 1.9415 1.6292 1.8237 -0.3517 0.0763  0.3904  132 GLU A CD  
996  O OE1 . GLU A 135 ? 2.0744 1.6812 1.8913 -0.4156 0.0616  0.3739  132 GLU A OE1 
997  O OE2 . GLU A 135 ? 1.8480 1.6721 1.7993 -0.3397 0.0678  0.4164  132 GLU A OE2 
998  N N   . TYR A 136 ? 1.3998 1.2568 1.4340 -0.0777 0.1540  0.4058  133 TYR A N   
999  C CA  . TYR A 136 ? 1.3284 1.2823 1.4088 -0.0396 0.1660  0.4205  133 TYR A CA  
1000 C C   . TYR A 136 ? 1.3608 1.3449 1.4566 -0.0336 0.1792  0.4547  133 TYR A C   
1001 O O   . TYR A 136 ? 1.2923 1.3665 1.4286 -0.0327 0.1887  0.4829  133 TYR A O   
1002 C CB  . TYR A 136 ? 1.2367 1.1736 1.3108 0.0140  0.1767  0.3882  133 TYR A CB  
1003 C CG  . TYR A 136 ? 1.0853 1.0951 1.1889 0.0538  0.1934  0.3973  133 TYR A CG  
1004 C CD1 . TYR A 136 ? 1.0394 1.1214 1.1724 0.0579  0.1972  0.4058  133 TYR A CD1 
1005 C CD2 . TYR A 136 ? 1.1877 1.1873 1.2827 0.0876  0.2058  0.3977  133 TYR A CD2 
1006 C CE1 . TYR A 136 ? 0.9986 1.1291 1.1482 0.0963  0.2189  0.4122  133 TYR A CE1 
1007 C CE2 . TYR A 136 ? 1.1508 1.2013 1.2572 0.1191  0.2237  0.4017  133 TYR A CE2 
1008 C CZ  . TYR A 136 ? 1.0680 1.1775 1.1997 0.1242  0.2332  0.4074  133 TYR A CZ  
1009 O OH  . TYR A 136 ? 1.0856 1.2277 1.2182 0.1574  0.2570  0.4094  133 TYR A OH  
1010 N N   . ALA A 137 ? 1.4676 1.3756 1.5295 -0.0285 0.1823  0.4556  134 ALA A N   
1011 C CA  . ALA A 137 ? 1.3983 1.3232 1.4618 -0.0254 0.1950  0.4892  134 ALA A CA  
1012 C C   . ALA A 137 ? 1.5281 1.4718 1.6015 -0.0848 0.1922  0.5234  134 ALA A C   
1013 O O   . ALA A 137 ? 1.4907 1.4959 1.5872 -0.0882 0.2077  0.5571  134 ALA A O   
1014 C CB  . ALA A 137 ? 1.4834 1.3213 1.5050 0.0031  0.1964  0.4832  134 ALA A CB  
1015 N N   . ARG A 138 ? 1.5856 1.4773 1.6388 -0.1352 0.1746  0.5150  135 ARG A N   
1016 C CA  . ARG A 138 ? 1.5963 1.5105 1.6594 -0.2035 0.1683  0.5463  135 ARG A CA  
1017 C C   . ARG A 138 ? 1.5406 1.6008 1.6754 -0.2159 0.1691  0.5738  135 ARG A C   
1018 O O   . ARG A 138 ? 1.5373 1.6650 1.7062 -0.2284 0.1846  0.6121  135 ARG A O   
1019 C CB  . ARG A 138 ? 1.6856 1.5133 1.7039 -0.2603 0.1472  0.5253  135 ARG A CB  
1020 C CG  . ARG A 138 ? 1.8122 1.4881 1.7589 -0.2672 0.1527  0.5149  135 ARG A CG  
1021 C CD  . ARG A 138 ? 1.9692 1.5680 1.8692 -0.3491 0.1382  0.5112  135 ARG A CD  
1022 N NE  . ARG A 138 ? 2.1109 1.5454 1.9341 -0.3493 0.1492  0.4994  135 ARG A NE  
1023 C CZ  . ARG A 138 ? 2.1521 1.5325 1.9550 -0.3394 0.1650  0.5268  135 ARG A CZ  
1024 N NH1 . ARG A 138 ? 2.0985 1.5732 1.9466 -0.3342 0.1733  0.5659  135 ARG A NH1 
1025 N NH2 . ARG A 138 ? 2.2506 1.4735 1.9817 -0.3326 0.1757  0.5163  135 ARG A NH2 
1026 N N   . ASN A 139 ? 1.4767 1.5877 1.6356 -0.2107 0.1547  0.5574  136 ASN A N   
1027 C CA  . ASN A 139 ? 1.4499 1.7021 1.6815 -0.2153 0.1545  0.5875  136 ASN A CA  
1028 C C   . ASN A 139 ? 1.4173 1.7381 1.6858 -0.1545 0.1883  0.6055  136 ASN A C   
1029 O O   . ASN A 139 ? 1.4354 1.8702 1.7670 -0.1574 0.2011  0.6433  136 ASN A O   
1030 C CB  . ASN A 139 ? 1.5268 1.8059 1.7653 -0.2139 0.1321  0.5670  136 ASN A CB  
1031 C CG  . ASN A 139 ? 1.5879 1.7928 1.7762 -0.2779 0.1004  0.5460  136 ASN A CG  
1032 O OD1 . ASN A 139 ? 1.6073 1.6918 1.7338 -0.2969 0.1011  0.5255  136 ASN A OD1 
1033 N ND2 . ASN A 139 ? 1.5455 1.8167 1.7541 -0.3104 0.0731  0.5519  136 ASN A ND2 
1034 N N   . PHE A 140 ? 1.3812 1.6366 1.6108 -0.1003 0.2042  0.5796  137 PHE A N   
1035 C CA  . PHE A 140 ? 1.3716 1.6749 1.6174 -0.0492 0.2374  0.5929  137 PHE A CA  
1036 C C   . PHE A 140 ? 1.4529 1.7624 1.6953 -0.0659 0.2574  0.6272  137 PHE A C   
1037 O O   . PHE A 140 ? 1.4316 1.8276 1.7147 -0.0549 0.2853  0.6588  137 PHE A O   
1038 C CB  . PHE A 140 ? 1.2999 1.5364 1.5010 0.0043  0.2444  0.5558  137 PHE A CB  
1039 C CG  . PHE A 140 ? 1.3014 1.5790 1.5062 0.0518  0.2778  0.5634  137 PHE A CG  
1040 C CD1 . PHE A 140 ? 1.3317 1.6698 1.5672 0.0836  0.2934  0.5614  137 PHE A CD1 
1041 C CD2 . PHE A 140 ? 1.3186 1.5706 1.4900 0.0621  0.2962  0.5761  137 PHE A CD2 
1042 C CE1 . PHE A 140 ? 1.2455 1.6058 1.4728 0.1258  0.3298  0.5662  137 PHE A CE1 
1043 C CE2 . PHE A 140 ? 1.2812 1.5613 1.4421 0.1008  0.3294  0.5807  137 PHE A CE2 
1044 C CZ  . PHE A 140 ? 1.2137 1.5441 1.4010 0.1324  0.3481  0.5740  137 PHE A CZ  
1045 N N   . LYS A 141 ? 1.5087 1.7218 1.6990 -0.0880 0.2480  0.6227  138 LYS A N   
1046 C CA  . LYS A 141 ? 1.4950 1.7033 1.6736 -0.1107 0.2660  0.6582  138 LYS A CA  
1047 C C   . LYS A 141 ? 1.5486 1.8490 1.7862 -0.1669 0.2686  0.6972  138 LYS A C   
1048 O O   . LYS A 141 ? 1.6048 1.9559 1.8611 -0.1756 0.2963  0.7340  138 LYS A O   
1049 C CB  . LYS A 141 ? 1.5460 1.6255 1.6574 -0.1274 0.2522  0.6495  138 LYS A CB  
1050 C CG  . LYS A 141 ? 1.5536 1.5628 1.6151 -0.0694 0.2535  0.6254  138 LYS A CG  
1051 C CD  . LYS A 141 ? 1.5761 1.4615 1.5858 -0.0765 0.2337  0.6090  138 LYS A CD  
1052 C CE  . LYS A 141 ? 1.6541 1.4831 1.6202 -0.0233 0.2344  0.6012  138 LYS A CE  
1053 N NZ  . LYS A 141 ? 1.6738 1.5721 1.6439 0.0110  0.2533  0.6110  138 LYS A NZ  
1054 N N   . LYS A 142 ? 1.4746 1.8034 1.7420 -0.2075 0.2399  0.6911  139 LYS A N   
1055 C CA  . LYS A 142 ? 1.4742 1.9217 1.8137 -0.2589 0.2370  0.7300  139 LYS A CA  
1056 C C   . LYS A 142 ? 1.4555 2.0392 1.8698 -0.2117 0.2638  0.7532  139 LYS A C   
1057 O O   . LYS A 142 ? 1.3875 2.0682 1.8571 -0.2243 0.2896  0.7962  139 LYS A O   
1058 C CB  . LYS A 142 ? 1.4858 1.9280 1.8282 -0.3149 0.1943  0.7157  139 LYS A CB  
1059 C CG  . LYS A 142 ? 1.5298 1.8915 1.8289 -0.3964 0.1755  0.7195  139 LYS A CG  
1060 C CD  . LYS A 142 ? 1.5160 1.8512 1.7958 -0.4495 0.1338  0.6958  139 LYS A CD  
1061 C CE  . LYS A 142 ? 1.5178 1.9952 1.8729 -0.5158 0.1122  0.7334  139 LYS A CE  
1062 N NZ  . LYS A 142 ? 1.4176 2.0648 1.8732 -0.4679 0.1294  0.7681  139 LYS A NZ  
1063 N N   . TYR A 143 ? 1.4934 2.0821 1.9089 -0.1559 0.2622  0.7261  140 TYR A N   
1064 C CA  . TYR A 143 ? 1.4316 2.1248 1.9045 -0.1008 0.2938  0.7449  140 TYR A CA  
1065 C C   . TYR A 143 ? 1.4186 2.1207 1.8826 -0.0691 0.3430  0.7649  140 TYR A C   
1066 O O   . TYR A 143 ? 1.3696 2.1807 1.8974 -0.0532 0.3770  0.8025  140 TYR A O   
1067 C CB  . TYR A 143 ? 1.4507 2.1057 1.8984 -0.0442 0.2898  0.7060  140 TYR A CB  
1068 C CG  . TYR A 143 ? 1.5407 2.2721 2.0287 0.0205  0.3281  0.7199  140 TYR A CG  
1069 C CD1 . TYR A 143 ? 1.5381 2.2428 1.9938 0.0687  0.3735  0.7165  140 TYR A CD1 
1070 C CD2 . TYR A 143 ? 1.5175 2.3398 2.0680 0.0338  0.3197  0.7370  140 TYR A CD2 
1071 C CE1 . TYR A 143 ? 1.5549 2.3113 2.0357 0.1283  0.4148  0.7265  140 TYR A CE1 
1072 C CE2 . TYR A 143 ? 1.4817 2.3618 2.0655 0.0987  0.3597  0.7520  140 TYR A CE2 
1073 C CZ  . TYR A 143 ? 1.4965 2.3376 2.0430 0.1457  0.4098  0.7447  140 TYR A CZ  
1074 O OH  . TYR A 143 ? 1.2976 2.1773 1.8649 0.2102  0.4554  0.7565  140 TYR A OH  
1075 N N   . GLU A 144 ? 1.4681 2.0577 1.8520 -0.0587 0.3484  0.7423  141 GLU A N   
1076 C CA  . GLU A 144 ? 1.4479 2.0308 1.8035 -0.0340 0.3917  0.7594  141 GLU A CA  
1077 C C   . GLU A 144 ? 1.5173 2.1685 1.9142 -0.0809 0.4116  0.8089  141 GLU A C   
1078 O O   . GLU A 144 ? 1.5242 2.1850 1.9029 -0.0627 0.4544  0.8294  141 GLU A O   
1079 C CB  . GLU A 144 ? 1.4347 1.8858 1.6953 -0.0218 0.3818  0.7297  141 GLU A CB  
1080 C CG  . GLU A 144 ? 1.4189 1.8260 1.6375 0.0377  0.3860  0.6903  141 GLU A CG  
1081 C CD  . GLU A 144 ? 1.4894 1.7883 1.6246 0.0497  0.3740  0.6682  141 GLU A CD  
1082 O OE1 . GLU A 144 ? 1.5649 1.7951 1.6786 0.0239  0.3409  0.6579  141 GLU A OE1 
1083 O OE2 . GLU A 144 ? 1.4326 1.7138 1.5213 0.0857  0.3978  0.6617  141 GLU A OE2 
1084 N N   . GLY A 145 ? 1.4789 2.1780 1.9267 -0.1443 0.3831  0.8285  142 GLY A N   
1085 C CA  . GLY A 145 ? 1.4345 2.2039 1.9264 -0.1989 0.4001  0.8764  142 GLY A CA  
1086 C C   . GLY A 145 ? 1.5613 2.2174 1.9742 -0.2340 0.4021  0.8790  142 GLY A C   
1087 O O   . GLY A 145 ? 1.5967 2.2712 2.0047 -0.2407 0.4359  0.9038  142 GLY A O   
1088 N N   . LYS A 146 ? 1.6504 2.1780 1.9942 -0.2504 0.3643  0.8451  143 LYS A N   
1089 C CA  . LYS A 146 ? 1.8009 2.2034 2.0634 -0.2771 0.3627  0.8476  143 LYS A CA  
1090 C C   . LYS A 146 ? 1.9123 2.2891 2.1800 -0.3650 0.3366  0.8611  143 LYS A C   
1091 O O   . LYS A 146 ? 1.8847 2.2600 2.1690 -0.3938 0.3002  0.8397  143 LYS A O   
1092 C CB  . LYS A 146 ? 1.8109 2.0819 1.9921 -0.2306 0.3429  0.8039  143 LYS A CB  
1093 C CG  . LYS A 146 ? 1.7336 2.0116 1.8911 -0.1544 0.3663  0.7893  143 LYS A CG  
1094 C CD  . LYS A 146 ? 1.7281 1.8922 1.8164 -0.1156 0.3422  0.7500  143 LYS A CD  
1095 C CE  . LYS A 146 ? 1.6972 1.8636 1.7502 -0.0532 0.3634  0.7386  143 LYS A CE  
1096 N NZ  . LYS A 146 ? 1.7355 1.8096 1.7326 -0.0187 0.3366  0.7041  143 LYS A NZ  
1097 N N   . ASP A 147 ? 1.9750 2.3238 2.2191 -0.4108 0.3561  0.8959  144 ASP A N   
1098 C CA  . ASP A 147 ? 2.0447 2.3539 2.2816 -0.5026 0.3352  0.9094  144 ASP A CA  
1099 C C   . ASP A 147 ? 2.1573 2.3049 2.3131 -0.5111 0.2989  0.8674  144 ASP A C   
1100 O O   . ASP A 147 ? 2.2036 2.2667 2.3076 -0.4451 0.2941  0.8354  144 ASP A O   
1101 C CB  . ASP A 147 ? 2.1315 2.4187 2.3419 -0.5389 0.3653  0.9404  144 ASP A CB  
1102 C CG  . ASP A 147 ? 2.2505 2.3699 2.3489 -0.5179 0.3753  0.9412  144 ASP A CG  
1103 O OD1 . ASP A 147 ? 2.2759 2.3881 2.3454 -0.5115 0.4072  0.9598  144 ASP A OD1 
1104 O OD2 . ASP A 147 ? 2.3052 2.2946 2.3393 -0.5041 0.3502  0.9162  144 ASP A OD2 
1105 N N   . GLN A 148 ? 2.1685 2.2778 2.3152 -0.5952 0.2739  0.8672  145 GLN A N   
1106 C CA  . GLN A 148 ? 2.2385 2.1972 2.3097 -0.6064 0.2434  0.8245  145 GLN A CA  
1107 C C   . GLN A 148 ? 2.3381 2.1204 2.3091 -0.5809 0.2565  0.8203  145 GLN A C   
1108 O O   . GLN A 148 ? 2.3868 2.0506 2.3000 -0.5440 0.2422  0.7827  145 GLN A O   
1109 C CB  . GLN A 148 ? 2.2190 2.1734 2.2930 -0.7106 0.2157  0.8251  145 GLN A CB  
1110 C CG  . GLN A 148 ? 2.2779 2.0741 2.2676 -0.7289 0.1882  0.7776  145 GLN A CG  
1111 C CD  . GLN A 148 ? 2.2453 2.0442 2.2387 -0.6511 0.1744  0.7341  145 GLN A CD  
1112 O OE1 . GLN A 148 ? 2.3031 1.9696 2.2292 -0.5997 0.1779  0.7032  145 GLN A OE1 
1113 N NE2 . GLN A 148 ? 2.2145 2.1668 2.2892 -0.6407 0.1602  0.7347  145 GLN A NE2 
1114 N N   . GLU A 149 ? 2.3862 2.1517 2.3366 -0.5965 0.2851  0.8613  146 GLU A N   
1115 C CA  . GLU A 149 ? 2.4617 2.0676 2.3175 -0.5638 0.2970  0.8654  146 GLU A CA  
1116 C C   . GLU A 149 ? 2.4263 2.0351 2.2718 -0.4601 0.3007  0.8484  146 GLU A C   
1117 O O   . GLU A 149 ? 2.4664 1.9476 2.2451 -0.4158 0.2932  0.8322  146 GLU A O   
1118 C CB  . GLU A 149 ? 2.4796 2.0721 2.3123 -0.6092 0.3276  0.9175  146 GLU A CB  
1119 C CG  . GLU A 149 ? 2.5237 2.0381 2.2895 -0.5440 0.3483  0.9360  146 GLU A CG  
1120 C CD  . GLU A 149 ? 2.6011 2.1303 2.3480 -0.5739 0.3824  0.9712  146 GLU A CD  
1121 O OE1 . GLU A 149 ? 2.6739 2.1027 2.3716 -0.6322 0.3895  0.9801  146 GLU A OE1 
1122 O OE2 . GLU A 149 ? 2.5765 2.2121 2.3535 -0.5361 0.4051  0.9826  146 GLU A OE2 
1123 N N   . THR A 150 ? 2.3564 2.1099 2.2675 -0.4209 0.3129  0.8523  147 THR A N   
1124 C CA  . THR A 150 ? 2.3071 2.0671 2.2041 -0.3320 0.3163  0.8347  147 THR A CA  
1125 C C   . THR A 150 ? 2.2720 1.9981 2.1703 -0.2914 0.2871  0.7844  147 THR A C   
1126 O O   . THR A 150 ? 2.2863 1.9278 2.1359 -0.2380 0.2787  0.7672  147 THR A O   
1127 C CB  . THR A 150 ? 2.2324 2.1421 2.1901 -0.3056 0.3427  0.8497  147 THR A CB  
1128 O OG1 . THR A 150 ? 2.2506 2.1926 2.2062 -0.3424 0.3760  0.8975  147 THR A OG1 
1129 C CG2 . THR A 150 ? 2.1926 2.0971 2.1212 -0.2234 0.3464  0.8296  147 THR A CG2 
1130 N N   . ILE A 151 ? 2.2191 2.0147 2.1737 -0.3172 0.2713  0.7631  148 ILE A N   
1131 C CA  . ILE A 151 ? 2.1608 1.9371 2.1196 -0.2817 0.2479  0.7160  148 ILE A CA  
1132 C C   . ILE A 151 ? 2.2373 1.8560 2.1234 -0.2647 0.2357  0.6933  148 ILE A C   
1133 O O   . ILE A 151 ? 2.1729 1.7653 2.0512 -0.2083 0.2263  0.6606  148 ILE A O   
1134 C CB  . ILE A 151 ? 2.0297 1.8771 2.0402 -0.3325 0.2291  0.7039  148 ILE A CB  
1135 C CG1 . ILE A 151 ? 1.9477 1.9596 2.0407 -0.3462 0.2432  0.7352  148 ILE A CG1 
1136 C CG2 . ILE A 151 ? 1.9089 1.7495 1.9238 -0.2921 0.2101  0.6577  148 ILE A CG2 
1137 C CD1 . ILE A 151 ? 1.8546 1.9495 2.0026 -0.4045 0.2205  0.7362  148 ILE A CD1 
1138 N N   . ASP A 152 ? 2.3160 1.8266 2.1487 -0.3114 0.2390  0.7122  149 ASP A N   
1139 C CA  . ASP A 152 ? 2.3874 1.7375 2.1479 -0.2889 0.2344  0.6970  149 ASP A CA  
1140 C C   . ASP A 152 ? 2.3791 1.6910 2.1076 -0.2181 0.2426  0.7135  149 ASP A C   
1141 O O   . ASP A 152 ? 2.4231 1.6361 2.1139 -0.1728 0.2363  0.6975  149 ASP A O   
1142 C CB  . ASP A 152 ? 2.5289 1.7614 2.2332 -0.3637 0.2388  0.7136  149 ASP A CB  
1143 C CG  . ASP A 152 ? 2.5680 1.8226 2.2898 -0.4414 0.2239  0.6939  149 ASP A CG  
1144 O OD1 . ASP A 152 ? 2.4560 1.8569 2.2506 -0.4502 0.2140  0.6888  149 ASP A OD1 
1145 O OD2 . ASP A 152 ? 2.7016 1.8241 2.3595 -0.4952 0.2221  0.6855  149 ASP A OD2 
1146 N N   . ASN A 153 ? 2.3503 1.7401 2.0916 -0.2070 0.2568  0.7463  150 ASN A N   
1147 C CA  . ASN A 153 ? 2.3574 1.7072 2.0548 -0.1495 0.2607  0.7669  150 ASN A CA  
1148 C C   . ASN A 153 ? 2.2792 1.6797 1.9991 -0.0764 0.2469  0.7366  150 ASN A C   
1149 O O   . ASN A 153 ? 2.3413 1.6691 2.0324 -0.0283 0.2342  0.7286  150 ASN A O   
1150 C CB  . ASN A 153 ? 2.3943 1.7994 2.0827 -0.1682 0.2838  0.8115  150 ASN A CB  
1151 C CG  . ASN A 153 ? 2.5220 1.8671 2.1821 -0.2423 0.2991  0.8464  150 ASN A CG  
1152 O OD1 . ASN A 153 ? 2.5327 1.9662 2.2333 -0.2944 0.3158  0.8649  150 ASN A OD1 
1153 N ND2 . ASN A 153 ? 2.5192 1.7127 2.1110 -0.2474 0.2955  0.8572  150 ASN A ND2 
1154 N N   . GLU A 154 ? 2.2113 1.7363 1.9835 -0.0665 0.2506  0.7215  151 GLU A N   
1155 C CA  . GLU A 154 ? 2.1434 1.7065 1.9324 -0.0060 0.2375  0.6892  151 GLU A CA  
1156 C C   . GLU A 154 ? 2.0993 1.6277 1.9094 0.0037  0.2210  0.6476  151 GLU A C   
1157 O O   . GLU A 154 ? 2.0800 1.6267 1.9028 0.0521  0.2100  0.6210  151 GLU A O   
1158 C CB  . GLU A 154 ? 2.0131 1.6999 1.8423 0.0040  0.2502  0.6815  151 GLU A CB  
1159 C CG  . GLU A 154 ? 2.0021 1.7423 1.8293 -0.0253 0.2777  0.7194  151 GLU A CG  
1160 C CD  . GLU A 154 ? 2.0009 1.8057 1.8853 -0.0777 0.2880  0.7248  151 GLU A CD  
1161 O OE1 . GLU A 154 ? 2.0538 1.8097 1.9443 -0.1159 0.2730  0.7174  151 GLU A OE1 
1162 O OE2 . GLU A 154 ? 1.9395 1.8439 1.8612 -0.0804 0.3114  0.7370  151 GLU A OE2 
1163 N N   . MET A 155 ? 2.1101 1.5872 1.9192 -0.0445 0.2200  0.6409  152 MET A N   
1164 C CA  . MET A 155 ? 2.1315 1.5605 1.9457 -0.0365 0.2086  0.6005  152 MET A CA  
1165 C C   . MET A 155 ? 2.2382 1.5466 2.0080 0.0032  0.2057  0.5990  152 MET A C   
1166 O O   . MET A 155 ? 2.2323 1.5312 2.0155 0.0475  0.1993  0.5686  152 MET A O   
1167 C CB  . MET A 155 ? 2.0908 1.5024 1.9074 -0.1065 0.2071  0.5921  152 MET A CB  
1168 C CG  . MET A 155 ? 2.0691 1.4820 1.9020 -0.1056 0.1967  0.5468  152 MET A CG  
1169 S SD  . MET A 155 ? 1.9199 1.4771 1.8185 -0.0635 0.1928  0.5253  152 MET A SD  
1170 C CE  . MET A 155 ? 1.7363 1.4006 1.6795 -0.1269 0.1907  0.5422  152 MET A CE  
1171 N N   . ASP A 156 ? 2.3028 1.5196 2.0215 -0.0093 0.2129  0.6343  153 ASP A N   
1172 C CA  . ASP A 156 ? 2.3939 1.4999 2.0722 0.0403  0.2120  0.6432  153 ASP A CA  
1173 C C   . ASP A 156 ? 2.3985 1.5640 2.0922 0.1097  0.2000  0.6540  153 ASP A C   
1174 O O   . ASP A 156 ? 2.4672 1.5648 2.1416 0.1606  0.1951  0.6646  153 ASP A O   
1175 C CB  . ASP A 156 ? 2.5163 1.5021 2.1287 0.0092  0.2241  0.6837  153 ASP A CB  
1176 C CG  . ASP A 156 ? 2.5409 1.4470 2.1255 -0.0664 0.2341  0.6719  153 ASP A CG  
1177 O OD1 . ASP A 156 ? 2.5147 1.4629 2.1300 -0.0936 0.2288  0.6335  153 ASP A OD1 
1178 O OD2 . ASP A 156 ? 2.5611 1.3584 2.0870 -0.1022 0.2463  0.7018  153 ASP A OD2 
1179 N N   . HIS A 157 ? 2.4339 1.7220 2.1592 0.1122  0.1956  0.6532  154 HIS A N   
1180 C CA  . HIS A 157 ? 2.3743 1.7276 2.1110 0.1676  0.1811  0.6549  154 HIS A CA  
1181 C C   . HIS A 157 ? 2.2946 1.7348 2.0861 0.1867  0.1741  0.6095  154 HIS A C   
1182 O O   . HIS A 157 ? 2.2626 1.7728 2.0655 0.2189  0.1628  0.6051  154 HIS A O   
1183 C CB  . HIS A 157 ? 2.3767 1.7848 2.0873 0.1566  0.1857  0.6883  154 HIS A CB  
1184 C CG  . HIS A 157 ? 2.5036 1.8275 2.1527 0.1459  0.1917  0.7380  154 HIS A CG  
1185 N ND1 . HIS A 157 ? 2.5234 1.8060 2.1512 0.0878  0.2119  0.7597  154 HIS A ND1 
1186 C CD2 . HIS A 157 ? 2.5546 1.8299 2.1574 0.1839  0.1795  0.7733  154 HIS A CD2 
1187 C CE1 . HIS A 157 ? 2.6031 1.8056 2.1699 0.0897  0.2154  0.8046  154 HIS A CE1 
1188 N NE2 . HIS A 157 ? 2.6087 1.8040 2.1575 0.1502  0.1952  0.8149  154 HIS A NE2 
1189 N N   . PHE A 158 ? 2.1318 1.5636 1.9497 0.1634  0.1802  0.5760  155 PHE A N   
1190 C CA  . PHE A 158 ? 1.9761 1.4768 1.8401 0.1777  0.1765  0.5337  155 PHE A CA  
1191 C C   . PHE A 158 ? 1.9911 1.4467 1.8669 0.2228  0.1707  0.5129  155 PHE A C   
1192 O O   . PHE A 158 ? 1.9322 1.2988 1.7930 0.2161  0.1793  0.5029  155 PHE A O   
1193 C CB  . PHE A 158 ? 1.8639 1.3801 1.7446 0.1279  0.1851  0.5134  155 PHE A CB  
1194 C CG  . PHE A 158 ? 1.7282 1.3420 1.6502 0.1317  0.1851  0.4858  155 PHE A CG  
1195 C CD1 . PHE A 158 ? 1.6789 1.3724 1.6110 0.1500  0.1866  0.4928  155 PHE A CD1 
1196 C CD2 . PHE A 158 ? 1.6948 1.3106 1.6359 0.1158  0.1857  0.4530  155 PHE A CD2 
1197 C CE1 . PHE A 158 ? 1.5724 1.3401 1.5350 0.1548  0.1909  0.4678  155 PHE A CE1 
1198 C CE2 . PHE A 158 ? 1.5478 1.2448 1.5220 0.1210  0.1871  0.4311  155 PHE A CE2 
1199 C CZ  . PHE A 158 ? 1.5567 1.3270 1.5428 0.1417  0.1908  0.4387  155 PHE A CZ  
1200 N N   . LYS A 159 ? 2.0255 1.5421 1.9267 0.2672  0.1581  0.5062  156 LYS A N   
1201 C CA  . LYS A 159 ? 2.0467 1.5444 1.9747 0.3135  0.1542  0.4893  156 LYS A CA  
1202 C C   . LYS A 159 ? 1.9697 1.5367 1.9421 0.3151  0.1568  0.4452  156 LYS A C   
1203 O O   . LYS A 159 ? 1.9237 1.5763 1.9191 0.3285  0.1454  0.4378  156 LYS A O   
1204 C CB  . LYS A 159 ? 2.1140 1.6352 2.0449 0.3620  0.1342  0.5187  156 LYS A CB  
1205 C CG  . LYS A 159 ? 2.1279 1.6701 2.1088 0.4120  0.1294  0.5009  156 LYS A CG  
1206 C CD  . LYS A 159 ? 2.1865 1.8041 2.1876 0.4515  0.1010  0.5236  156 LYS A CD  
1207 C CE  . LYS A 159 ? 2.0727 1.7451 2.1413 0.4910  0.0975  0.5007  156 LYS A CE  
1208 N NZ  . LYS A 159 ? 2.0749 1.8218 2.1686 0.5301  0.0647  0.5298  156 LYS A NZ  
1209 N N   . PRO A 160 ? 1.9125 1.4395 1.8901 0.2986  0.1720  0.4147  157 PRO A N   
1210 C CA  . PRO A 160 ? 1.8329 1.4186 1.8457 0.2980  0.1768  0.3748  157 PRO A CA  
1211 C C   . PRO A 160 ? 1.7753 1.3622 1.8237 0.3421  0.1818  0.3544  157 PRO A C   
1212 O O   . PRO A 160 ? 1.7164 1.3494 1.7923 0.3406  0.1884  0.3218  157 PRO A O   
1213 C CB  . PRO A 160 ? 1.8264 1.3641 1.8157 0.2518  0.1895  0.3571  157 PRO A CB  
1214 C CG  . PRO A 160 ? 1.8843 1.3092 1.8341 0.2483  0.1968  0.3730  157 PRO A CG  
1215 C CD  . PRO A 160 ? 1.9282 1.3547 1.8666 0.2646  0.1854  0.4160  157 PRO A CD  
1216 N N   . THR A 161 ? 2.0794 1.5087 1.7037 0.2098  0.1631  0.7887  158 THR A N   
1217 C CA  . THR A 161 ? 2.0256 1.4535 1.6849 0.2495  0.1417  0.7811  158 THR A CA  
1218 C C   . THR A 161 ? 1.9202 1.4449 1.5651 0.2744  0.1037  0.7649  158 THR A C   
1219 O O   . THR A 161 ? 1.7768 1.3261 1.4613 0.2898  0.0870  0.7345  158 THR A O   
1220 C CB  . THR A 161 ? 1.9893 1.3575 1.6462 0.2828  0.1463  0.8307  158 THR A CB  
1221 O OG1 . THR A 161 ? 2.0447 1.3181 1.7166 0.2553  0.1823  0.8430  158 THR A OG1 
1222 C CG2 . THR A 161 ? 1.9531 1.3203 1.6537 0.3254  0.1280  0.8221  158 THR A CG2 
1223 N N   . GLU A 162 ? 2.0521 1.6319 1.6399 0.2773  0.0901  0.7838  159 GLU A N   
1224 C CA  . GLU A 162 ? 1.9902 1.6629 1.5568 0.2933  0.0532  0.7652  159 GLU A CA  
1225 C C   . GLU A 162 ? 1.8950 1.6065 1.4887 0.2689  0.0496  0.7094  159 GLU A C   
1226 O O   . GLU A 162 ? 1.8151 1.5577 1.4476 0.2843  0.0289  0.6826  159 GLU A O   
1227 C CB  . GLU A 162 ? 2.0603 1.7706 1.5521 0.2901  0.0481  0.7904  159 GLU A CB  
1228 C CG  . GLU A 162 ? 2.0106 1.8134 1.4662 0.2920  0.0156  0.7627  159 GLU A CG  
1229 C CD  . GLU A 162 ? 1.9979 1.8524 1.4950 0.3143  -0.0205 0.7341  159 GLU A CD  
1230 O OE1 . GLU A 162 ? 2.0737 1.9434 1.5764 0.3497  -0.0453 0.7594  159 GLU A OE1 
1231 O OE2 . GLU A 162 ? 1.9201 1.8036 1.4449 0.2963  -0.0240 0.6876  159 GLU A OE2 
1232 N N   . THR A 163 ? 1.8695 1.5800 1.4453 0.2312  0.0714  0.6933  160 THR A N   
1233 C CA  . THR A 163 ? 1.6744 1.4284 1.2668 0.2093  0.0668  0.6442  160 THR A CA  
1234 C C   . THR A 163 ? 1.6951 1.4174 1.3517 0.2065  0.0713  0.6166  160 THR A C   
1235 O O   . THR A 163 ? 1.6020 1.3691 1.2815 0.2131  0.0510  0.5842  160 THR A O   
1236 C CB  . THR A 163 ? 1.6602 1.4141 1.2275 0.1713  0.0938  0.6369  160 THR A CB  
1237 O OG1 . THR A 163 ? 1.6605 1.4682 1.1654 0.1759  0.0831  0.6444  160 THR A OG1 
1238 C CG2 . THR A 163 ? 1.5237 1.2972 1.1255 0.1454  0.0987  0.5901  160 THR A CG2 
1239 N N   . LEU A 164 ? 1.7144 1.3573 1.3994 0.1963  0.0979  0.6282  161 LEU A N   
1240 C CA  . LEU A 164 ? 1.6700 1.2749 1.4099 0.1910  0.1053  0.5988  161 LEU A CA  
1241 C C   . LEU A 164 ? 1.6704 1.2900 1.4400 0.2314  0.0831  0.5947  161 LEU A C   
1242 O O   . LEU A 164 ? 1.6457 1.2560 1.4560 0.2307  0.0844  0.5633  161 LEU A O   
1243 C CB  . LEU A 164 ? 1.7403 1.2524 1.4998 0.1695  0.1377  0.6100  161 LEU A CB  
1244 C CG  . LEU A 164 ? 1.8168 1.3075 1.5971 0.1213  0.1592  0.5786  161 LEU A CG  
1245 C CD1 . LEU A 164 ? 1.7183 1.2532 1.4658 0.0926  0.1671  0.5831  161 LEU A CD1 
1246 C CD2 . LEU A 164 ? 1.8636 1.2597 1.6705 0.1019  0.1855  0.5838  161 LEU A CD2 
1247 N N   . LYS A 165 ? 1.6911 1.3380 1.4420 0.2663  0.0628  0.6256  162 LYS A N   
1248 C CA  . LYS A 165 ? 1.6101 1.2814 1.3949 0.3061  0.0409  0.6250  162 LYS A CA  
1249 C C   . LYS A 165 ? 1.5146 1.2820 1.3011 0.3129  0.0073  0.5987  162 LYS A C   
1250 O O   . LYS A 165 ? 1.4988 1.2900 1.3303 0.3314  -0.0045 0.5795  162 LYS A O   
1251 C CB  . LYS A 165 ? 1.6356 1.2906 1.4055 0.3412  0.0338  0.6733  162 LYS A CB  
1252 C CG  . LYS A 165 ? 1.7278 1.3898 1.5446 0.3841  0.0199  0.6776  162 LYS A CG  
1253 C CD  . LYS A 165 ? 1.6433 1.3920 1.4471 0.4151  -0.0201 0.6950  162 LYS A CD  
1254 C CE  . LYS A 165 ? 1.6064 1.3788 1.4696 0.4544  -0.0346 0.6912  162 LYS A CE  
1255 N NZ  . LYS A 165 ? 1.5951 1.3974 1.5044 0.4426  -0.0345 0.6413  162 LYS A NZ  
1256 N N   . GLU A 166 ? 1.5095 1.3318 1.2487 0.2978  -0.0071 0.5961  163 GLU A N   
1257 C CA  . GLU A 166 ? 1.4778 1.3825 1.2191 0.2938  -0.0354 0.5618  163 GLU A CA  
1258 C C   . GLU A 166 ? 1.4216 1.3197 1.1967 0.2699  -0.0225 0.5216  163 GLU A C   
1259 O O   . GLU A 166 ? 1.2662 1.2141 1.0713 0.2744  -0.0414 0.4935  163 GLU A O   
1260 C CB  . GLU A 166 ? 1.5174 1.4687 1.1959 0.2786  -0.0474 0.5617  163 GLU A CB  
1261 C CG  . GLU A 166 ? 1.5836 1.5473 1.2163 0.2995  -0.0619 0.6007  163 GLU A CG  
1262 C CD  . GLU A 166 ? 1.6434 1.6732 1.2190 0.2892  -0.0845 0.5866  163 GLU A CD  
1263 O OE1 . GLU A 166 ? 1.5983 1.6919 1.1869 0.2911  -0.1150 0.5556  163 GLU A OE1 
1264 O OE2 . GLU A 166 ? 1.7600 1.7768 1.2778 0.2780  -0.0706 0.6045  163 GLU A OE2 
1265 N N   . LEU A 167 ? 1.4369 1.2767 1.2073 0.2421  0.0091  0.5190  164 LEU A N   
1266 C CA  . LEU A 167 ? 1.4110 1.2358 1.2120 0.2187  0.0232  0.4848  164 LEU A CA  
1267 C C   . LEU A 167 ? 1.3924 1.1905 1.2467 0.2380  0.0257  0.4732  164 LEU A C   
1268 O O   . LEU A 167 ? 1.2729 1.0918 1.1544 0.2320  0.0225  0.4425  164 LEU A O   
1269 C CB  . LEU A 167 ? 1.4360 1.2009 1.2267 0.1849  0.0559  0.4884  164 LEU A CB  
1270 C CG  . LEU A 167 ? 1.3513 1.1202 1.1542 0.1506  0.0681  0.4557  164 LEU A CG  
1271 C CD1 . LEU A 167 ? 1.2388 1.0858 1.0343 0.1531  0.0437  0.4309  164 LEU A CD1 
1272 C CD2 . LEU A 167 ? 1.3053 1.0543 1.0847 0.1182  0.0915  0.4656  164 LEU A CD2 
1273 N N   . SER A 168 ? 1.4925 1.2419 1.3613 0.2622  0.0339  0.4977  165 SER A N   
1274 C CA  . SER A 168 ? 1.4657 1.1846 1.3840 0.2832  0.0415  0.4848  165 SER A CA  
1275 C C   . SER A 168 ? 1.3385 1.1366 1.2860 0.3115  0.0129  0.4745  165 SER A C   
1276 O O   . SER A 168 ? 1.2825 1.0876 1.2696 0.3159  0.0169  0.4469  165 SER A O   
1277 C CB  . SER A 168 ? 1.5417 1.1857 1.4669 0.3028  0.0593  0.5133  165 SER A CB  
1278 O OG  . SER A 168 ? 1.5419 1.1618 1.5134 0.3290  0.0667  0.4997  165 SER A OG  
1279 N N   . GLU A 169 ? 1.2780 1.1383 1.2075 0.3288  -0.0159 0.4949  166 GLU A N   
1280 C CA  . GLU A 169 ? 1.2104 1.1557 1.1715 0.3480  -0.0464 0.4819  166 GLU A CA  
1281 C C   . GLU A 169 ? 1.1548 1.1520 1.1200 0.3217  -0.0564 0.4442  166 GLU A C   
1282 O O   . GLU A 169 ? 1.0218 1.0540 1.0339 0.3281  -0.0616 0.4208  166 GLU A O   
1283 C CB  . GLU A 169 ? 1.2219 1.2246 1.1573 0.3655  -0.0785 0.5076  166 GLU A CB  
1284 C CG  . GLU A 169 ? 1.4337 1.3866 1.3413 0.3844  -0.0706 0.5523  166 GLU A CG  
1285 C CD  . GLU A 169 ? 1.4630 1.4788 1.3359 0.3988  -0.1052 0.5759  166 GLU A CD  
1286 O OE1 . GLU A 169 ? 1.4864 1.5801 1.3519 0.3880  -0.1346 0.5529  166 GLU A OE1 
1287 O OE2 . GLU A 169 ? 1.5277 1.5130 1.3795 0.4202  -0.1036 0.6169  166 GLU A OE2 
1288 N N   . ALA A 170 ? 1.1858 1.1900 1.1032 0.2924  -0.0577 0.4384  167 ALA A N   
1289 C CA  . ALA A 170 ? 1.0864 1.1392 1.0034 0.2679  -0.0682 0.4040  167 ALA A CA  
1290 C C   . ALA A 170 ? 1.0830 1.1089 1.0416 0.2610  -0.0487 0.3804  167 ALA A C   
1291 O O   . ALA A 170 ? 0.9886 1.0661 0.9799 0.2595  -0.0618 0.3556  167 ALA A O   
1292 C CB  . ALA A 170 ? 1.0322 1.0788 0.8921 0.2391  -0.0621 0.4022  167 ALA A CB  
1293 N N   . LEU A 171 ? 1.1313 1.0749 1.0897 0.2548  -0.0169 0.3867  168 LEU A N   
1294 C CA  . LEU A 171 ? 1.0674 0.9763 1.0567 0.2434  0.0034  0.3580  168 LEU A CA  
1295 C C   . LEU A 171 ? 1.0772 1.0040 1.1195 0.2737  0.0021  0.3492  168 LEU A C   
1296 O O   . LEU A 171 ? 1.0183 0.9709 1.0863 0.2593  0.0033  0.3106  168 LEU A O   
1297 C CB  . LEU A 171 ? 1.1399 0.9534 1.1173 0.2275  0.0361  0.3627  168 LEU A CB  
1298 C CG  . LEU A 171 ? 1.1473 0.9441 1.0887 0.1866  0.0455  0.3577  168 LEU A CG  
1299 C CD1 . LEU A 171 ? 1.2145 0.9188 1.1569 0.1710  0.0763  0.3631  168 LEU A CD1 
1300 C CD2 . LEU A 171 ? 0.9778 0.8189 0.9227 0.1539  0.0376  0.3115  168 LEU A CD2 
1301 N N   . ASP A 172 ? 1.1058 1.0232 1.1641 0.3064  0.0009  0.3732  169 ASP A N   
1302 C CA  . ASP A 172 ? 1.0530 0.9937 1.1666 0.3359  0.0026  0.3637  169 ASP A CA  
1303 C C   . ASP A 172 ? 0.9751 1.0208 1.1187 0.3362  -0.0267 0.3490  169 ASP A C   
1304 O O   . ASP A 172 ? 0.9419 1.0145 1.1316 0.3420  -0.0191 0.3265  169 ASP A O   
1305 C CB  . ASP A 172 ? 0.9729 0.8896 1.0971 0.3693  0.0042  0.3923  169 ASP A CB  
1306 C CG  . ASP A 172 ? 1.1532 0.9597 1.2589 0.3676  0.0369  0.4013  169 ASP A CG  
1307 O OD1 . ASP A 172 ? 1.2505 1.0037 1.3356 0.3372  0.0565  0.3830  169 ASP A OD1 
1308 O OD2 . ASP A 172 ? 1.1426 0.9160 1.2555 0.3948  0.0420  0.4261  169 ASP A OD2 
1309 N N   . THR A 173 ? 0.9120 1.0159 1.0285 0.3263  -0.0584 0.3578  170 THR A N   
1310 C CA  . THR A 173 ? 0.8419 1.0404 0.9834 0.3169  -0.0878 0.3378  170 THR A CA  
1311 C C   . THR A 173 ? 0.8774 1.0870 1.0304 0.2896  -0.0792 0.3050  170 THR A C   
1312 O O   . THR A 173 ? 0.8434 1.1072 1.0443 0.2851  -0.0845 0.2819  170 THR A O   
1313 C CB  . THR A 173 ? 0.7913 1.0319 0.8864 0.3047  -0.1196 0.3458  170 THR A CB  
1314 O OG1 . THR A 173 ? 0.8837 1.1147 0.9664 0.3310  -0.1278 0.3786  170 THR A OG1 
1315 C CG2 . THR A 173 ? 0.8241 1.1554 0.9463 0.2909  -0.1508 0.3201  170 THR A CG2 
1316 N N   . ILE A 174 ? 0.8812 1.0337 0.9871 0.2580  -0.0631 0.2908  171 ILE A N   
1317 C CA  . ILE A 174 ? 0.8393 0.9908 0.9449 0.2204  -0.0540 0.2488  171 ILE A CA  
1318 C C   . ILE A 174 ? 0.8619 0.9799 1.0015 0.2235  -0.0262 0.2296  171 ILE A C   
1319 O O   . ILE A 174 ? 0.8438 0.9879 1.0042 0.2055  -0.0227 0.2006  171 ILE A O   
1320 C CB  . ILE A 174 ? 0.8166 0.9251 0.8678 0.1903  -0.0459 0.2431  171 ILE A CB  
1321 C CG1 . ILE A 174 ? 0.7532 0.9082 0.7694 0.1837  -0.0717 0.2506  171 ILE A CG1 
1322 C CG2 . ILE A 174 ? 0.7396 0.8310 0.7921 0.1578  -0.0312 0.2059  171 ILE A CG2 
1323 C CD1 . ILE A 174 ? 0.7623 0.8918 0.7337 0.1544  -0.0623 0.2395  171 ILE A CD1 
1324 N N   . LYS A 175 ? 0.8580 0.9145 1.0008 0.2467  -0.0042 0.2451  172 LYS A N   
1325 C CA  . LYS A 175 ? 0.9061 0.9279 1.0739 0.2519  0.0242  0.2227  172 LYS A CA  
1326 C C   . LYS A 175 ? 0.8390 0.9310 1.0646 0.2712  0.0207  0.2159  172 LYS A C   
1327 O O   . LYS A 175 ? 0.7945 0.8938 1.0346 0.2575  0.0368  0.1870  172 LYS A O   
1328 C CB  . LYS A 175 ? 0.9304 0.8703 1.0941 0.2775  0.0484  0.2401  172 LYS A CB  
1329 C CG  . LYS A 175 ? 0.8830 0.7748 1.0608 0.2820  0.0811  0.2108  172 LYS A CG  
1330 C CD  . LYS A 175 ? 0.9689 0.7684 1.1389 0.3042  0.1047  0.2258  172 LYS A CD  
1331 C CE  . LYS A 175 ? 1.0906 0.8569 1.2895 0.3317  0.1361  0.2057  172 LYS A CE  
1332 N NZ  . LYS A 175 ? 1.3137 0.9696 1.4802 0.3183  0.1657  0.1838  172 LYS A NZ  
1333 N N   . GLU A 176 ? 0.8646 1.0149 1.1248 0.3025  -0.0007 0.2442  173 GLU A N   
1334 C CA  . GLU A 176 ? 0.8358 1.0667 1.1625 0.3192  -0.0061 0.2400  173 GLU A CA  
1335 C C   . GLU A 176 ? 0.7946 1.0913 1.1303 0.2814  -0.0241 0.2149  173 GLU A C   
1336 O O   . GLU A 176 ? 0.7722 1.1341 1.1665 0.2849  -0.0234 0.2062  173 GLU A O   
1337 C CB  . GLU A 176 ? 0.9005 1.1816 1.2574 0.3531  -0.0308 0.2712  173 GLU A CB  
1338 C CG  . GLU A 176 ? 1.0075 1.2186 1.3303 0.3769  -0.0258 0.3000  173 GLU A CG  
1339 C CD  . GLU A 176 ? 1.1670 1.3326 1.5215 0.4107  0.0050  0.3017  173 GLU A CD  
1340 O OE1 . GLU A 176 ? 1.2020 1.3776 1.5938 0.4133  0.0290  0.2770  173 GLU A OE1 
1341 O OE2 . GLU A 176 ? 1.1986 1.3210 1.5403 0.4345  0.0059  0.3276  173 GLU A OE2 
1342 N N   . GLN A 177 ? 0.7242 1.0040 1.0075 0.2461  -0.0374 0.2041  174 GLN A N   
1343 C CA  . GLN A 177 ? 0.7138 1.0421 1.0005 0.2104  -0.0535 0.1804  174 GLN A CA  
1344 C C   . GLN A 177 ? 0.6882 0.9760 0.9554 0.1793  -0.0293 0.1516  174 GLN A C   
1345 O O   . GLN A 177 ? 0.5907 0.9109 0.8668 0.1516  -0.0365 0.1332  174 GLN A O   
1346 C CB  . GLN A 177 ? 0.6982 1.0389 0.9398 0.1952  -0.0838 0.1859  174 GLN A CB  
1347 C CG  . GLN A 177 ? 0.6977 1.1106 0.9616 0.2168  -0.1189 0.2078  174 GLN A CG  
1348 C CD  . GLN A 177 ? 0.7742 1.2060 0.9865 0.1981  -0.1486 0.2054  174 GLN A CD  
1349 O OE1 . GLN A 177 ? 0.7859 1.1634 0.9376 0.1887  -0.1404 0.2083  174 GLN A OE1 
1350 N NE2 . GLN A 177 ? 0.7820 1.2937 1.0193 0.1915  -0.1824 0.1979  174 GLN A NE2 
1351 N N   . VAL A 178 ? 0.7242 0.9418 0.9646 0.1826  -0.0017 0.1472  175 VAL A N   
1352 C CA  . VAL A 178 ? 0.7155 0.9001 0.9296 0.1533  0.0156  0.1222  175 VAL A CA  
1353 C C   . VAL A 178 ? 0.6378 0.8645 0.8918 0.1464  0.0278  0.1077  175 VAL A C   
1354 O O   . VAL A 178 ? 0.5470 0.7727 0.7866 0.1185  0.0313  0.0923  175 VAL A O   
1355 C CB  . VAL A 178 ? 0.6978 0.8046 0.8771 0.1569  0.0400  0.1172  175 VAL A CB  
1356 C CG1 . VAL A 178 ? 0.7450 0.8291 0.8993 0.1306  0.0552  0.0923  175 VAL A CG1 
1357 C CG2 . VAL A 178 ? 0.7410 0.8075 0.8813 0.1520  0.0300  0.1309  175 VAL A CG2 
1358 N N   . ASP A 179 ? 0.6343 0.9023 0.9427 0.1724  0.0354  0.1157  176 ASP A N   
1359 C CA  . ASP A 179 ? 0.5581 0.8700 0.9100 0.1658  0.0530  0.1046  176 ASP A CA  
1360 C C   . ASP A 179 ? 0.5465 0.9224 0.9298 0.1385  0.0306  0.1010  176 ASP A C   
1361 O O   . ASP A 179 ? 0.5261 0.9384 0.9480 0.1266  0.0462  0.0939  176 ASP A O   
1362 C CB  . ASP A 179 ? 0.5502 0.8912 0.9580 0.2043  0.0725  0.1140  176 ASP A CB  
1363 C CG  . ASP A 179 ? 0.7672 1.1649 1.2226 0.2318  0.0446  0.1382  176 ASP A CG  
1364 O OD1 . ASP A 179 ? 0.7928 1.2732 1.3017 0.2231  0.0237  0.1415  176 ASP A OD1 
1365 O OD2 . ASP A 179 ? 0.8451 1.2050 1.2856 0.2624  0.0431  0.1552  176 ASP A OD2 
1366 N N   . GLU A 180 ? 0.5814 0.9669 0.9456 0.1255  -0.0024 0.1036  177 GLU A N   
1367 C CA  . GLU A 180 ? 0.4992 0.9309 0.8842 0.0952  -0.0233 0.0930  177 GLU A CA  
1368 C C   . GLU A 180 ? 0.4676 0.8524 0.8017 0.0636  -0.0224 0.0778  177 GLU A C   
1369 O O   . GLU A 180 ? 0.4893 0.8980 0.8383 0.0370  -0.0343 0.0660  177 GLU A O   
1370 C CB  . GLU A 180 ? 0.4608 0.9434 0.8592 0.1025  -0.0624 0.1018  177 GLU A CB  
1371 C CG  . GLU A 180 ? 0.5668 1.1023 1.0191 0.1396  -0.0681 0.1227  177 GLU A CG  
1372 C CD  . GLU A 180 ? 0.6478 1.2194 1.0909 0.1555  -0.1078 0.1393  177 GLU A CD  
1373 O OE1 . GLU A 180 ? 0.5757 1.1522 0.9826 0.1310  -0.1340 0.1278  177 GLU A OE1 
1374 O OE2 . GLU A 180 ? 0.6819 1.2765 1.1517 0.1948  -0.1118 0.1646  177 GLU A OE2 
1375 N N   . VAL A 181 ? 0.4928 0.8128 0.7719 0.0658  -0.0089 0.0774  178 VAL A N   
1376 C CA  . VAL A 181 ? 0.5198 0.8011 0.7560 0.0415  -0.0086 0.0664  178 VAL A CA  
1377 C C   . VAL A 181 ? 0.5322 0.8119 0.7820 0.0233  0.0120  0.0589  178 VAL A C   
1378 O O   . VAL A 181 ? 0.4556 0.7317 0.7147 0.0318  0.0365  0.0612  178 VAL A O   
1379 C CB  . VAL A 181 ? 0.5575 0.7814 0.7412 0.0487  -0.0009 0.0698  178 VAL A CB  
1380 C CG1 . VAL A 181 ? 0.5123 0.7040 0.6625 0.0279  0.0048  0.0605  178 VAL A CG1 
1381 C CG2 . VAL A 181 ? 0.5361 0.7567 0.6991 0.0600  -0.0200 0.0804  178 VAL A CG2 
1382 N N   . LEU A 182 ? 0.5016 0.7799 0.7494 -0.0010 0.0046  0.0504  179 LEU A N   
1383 C CA  . LEU A 182 ? 0.5247 0.8011 0.7889 -0.0191 0.0242  0.0489  179 LEU A CA  
1384 C C   . LEU A 182 ? 0.4709 0.6995 0.6926 -0.0319 0.0298  0.0474  179 LEU A C   
1385 O O   . LEU A 182 ? 0.4797 0.6967 0.7013 -0.0405 0.0501  0.0531  179 LEU A O   
1386 C CB  . LEU A 182 ? 0.4390 0.7615 0.7597 -0.0393 0.0153  0.0428  179 LEU A CB  
1387 C CG  . LEU A 182 ? 0.4409 0.8315 0.8250 -0.0316 0.0089  0.0456  179 LEU A CG  
1388 C CD1 . LEU A 182 ? 0.3266 0.7631 0.7596 -0.0587 -0.0125 0.0333  179 LEU A CD1 
1389 C CD2 . LEU A 182 ? 0.4810 0.8922 0.8995 -0.0232 0.0420  0.0557  179 LEU A CD2 
1390 N N   . ASP A 183 ? 0.5096 0.7136 0.6967 -0.0311 0.0140  0.0426  180 ASP A N   
1391 C CA  . ASP A 183 ? 0.4956 0.6633 0.6540 -0.0404 0.0167  0.0416  180 ASP A CA  
1392 C C   . ASP A 183 ? 0.5358 0.6760 0.6564 -0.0314 0.0283  0.0503  180 ASP A C   
1393 O O   . ASP A 183 ? 0.5210 0.6614 0.6302 -0.0194 0.0316  0.0518  180 ASP A O   
1394 C CB  . ASP A 183 ? 0.4779 0.6388 0.6197 -0.0415 -0.0024 0.0311  180 ASP A CB  
1395 C CG  . ASP A 183 ? 0.5229 0.7119 0.6940 -0.0535 -0.0180 0.0172  180 ASP A CG  
1396 O OD1 . ASP A 183 ? 0.5145 0.7025 0.7132 -0.0722 -0.0131 0.0108  180 ASP A OD1 
1397 O OD2 . ASP A 183 ? 0.5419 0.7545 0.7080 -0.0458 -0.0360 0.0131  180 ASP A OD2 
1398 N N   . PRO A 184 ? 0.5284 0.6444 0.6301 -0.0369 0.0341  0.0558  181 PRO A N   
1399 C CA  . PRO A 184 ? 0.5469 0.6462 0.6123 -0.0304 0.0396  0.0630  181 PRO A CA  
1400 C C   . PRO A 184 ? 0.5220 0.6172 0.5678 -0.0230 0.0280  0.0576  181 PRO A C   
1401 O O   . PRO A 184 ? 0.5072 0.6045 0.5564 -0.0222 0.0163  0.0532  181 PRO A O   
1402 C CB  . PRO A 184 ? 0.5005 0.5812 0.5560 -0.0343 0.0406  0.0724  181 PRO A CB  
1403 C CG  . PRO A 184 ? 0.5189 0.5985 0.6067 -0.0457 0.0478  0.0730  181 PRO A CG  
1404 C CD  . PRO A 184 ? 0.4944 0.5974 0.6102 -0.0493 0.0373  0.0574  181 PRO A CD  
1405 N N   . ILE A 185 ? 0.5101 0.5977 0.5333 -0.0192 0.0332  0.0568  182 ILE A N   
1406 C CA  . ILE A 185 ? 0.5438 0.6228 0.5543 -0.0160 0.0256  0.0519  182 ILE A CA  
1407 C C   . ILE A 185 ? 0.5578 0.6244 0.5378 -0.0211 0.0252  0.0494  182 ILE A C   
1408 O O   . ILE A 185 ? 0.5242 0.5878 0.4850 -0.0227 0.0332  0.0484  182 ILE A O   
1409 C CB  . ILE A 185 ? 0.5133 0.5928 0.5369 -0.0062 0.0304  0.0487  182 ILE A CB  
1410 C CG1 . ILE A 185 ? 0.5431 0.6033 0.5532 -0.0038 0.0261  0.0475  182 ILE A CG1 
1411 C CG2 . ILE A 185 ? 0.5435 0.6209 0.5654 -0.0015 0.0481  0.0450  182 ILE A CG2 
1412 C CD1 . ILE A 185 ? 0.5543 0.6154 0.5818 0.0107  0.0264  0.0523  182 ILE A CD1 
1413 N N   . LEU A 186 ? 0.6041 0.6671 0.5790 -0.0254 0.0155  0.0481  183 LEU A N   
1414 C CA  . LEU A 186 ? 0.6078 0.6639 0.5615 -0.0350 0.0110  0.0420  183 LEU A CA  
1415 C C   . LEU A 186 ? 0.5917 0.6281 0.5474 -0.0379 0.0125  0.0362  183 LEU A C   
1416 O O   . LEU A 186 ? 0.5687 0.6087 0.5387 -0.0365 0.0093  0.0437  183 LEU A O   
1417 C CB  . LEU A 186 ? 0.5557 0.6322 0.5121 -0.0399 -0.0012 0.0495  183 LEU A CB  
1418 C CG  . LEU A 186 ? 0.6053 0.6895 0.5549 -0.0537 -0.0117 0.0441  183 LEU A CG  
1419 C CD1 . LEU A 186 ? 0.6565 0.7321 0.5741 -0.0624 -0.0134 0.0315  183 LEU A CD1 
1420 C CD2 . LEU A 186 ? 0.5648 0.6806 0.5299 -0.0525 -0.0226 0.0554  183 LEU A CD2 
1421 N N   . VAL A 187 ? 0.6444 0.6558 0.5828 -0.0411 0.0199  0.0232  184 VAL A N   
1422 C CA  . VAL A 187 ? 0.6175 0.5970 0.5571 -0.0440 0.0249  0.0181  184 VAL A CA  
1423 C C   . VAL A 187 ? 0.6567 0.6290 0.5842 -0.0672 0.0166  0.0071  184 VAL A C   
1424 O O   . VAL A 187 ? 0.6744 0.6465 0.5774 -0.0774 0.0130  -0.0087 184 VAL A O   
1425 C CB  . VAL A 187 ? 0.6786 0.6285 0.6113 -0.0308 0.0416  0.0077  184 VAL A CB  
1426 C CG1 . VAL A 187 ? 0.7215 0.6276 0.6581 -0.0292 0.0495  0.0060  184 VAL A CG1 
1427 C CG2 . VAL A 187 ? 0.6439 0.6166 0.5987 -0.0106 0.0474  0.0190  184 VAL A CG2 
1428 N N   . ILE A 188 ? 0.6596 0.6299 0.6035 -0.0775 0.0134  0.0154  185 ILE A N   
1429 C CA  . ILE A 188 ? 0.7417 0.7126 0.6868 -0.1043 0.0054  0.0061  185 ILE A CA  
1430 C C   . ILE A 188 ? 0.7273 0.6473 0.6751 -0.1146 0.0173  0.0019  185 ILE A C   
1431 O O   . ILE A 188 ? 0.7411 0.6447 0.7007 -0.1021 0.0272  0.0204  185 ILE A O   
1432 C CB  . ILE A 188 ? 0.6487 0.6661 0.6185 -0.1106 -0.0044 0.0215  185 ILE A CB  
1433 C CG1 . ILE A 188 ? 0.6419 0.7018 0.6079 -0.1059 -0.0181 0.0220  185 ILE A CG1 
1434 C CG2 . ILE A 188 ? 0.6639 0.6817 0.6509 -0.1389 -0.0068 0.0181  185 ILE A CG2 
1435 C CD1 . ILE A 188 ? 0.5886 0.6908 0.5812 -0.0983 -0.0223 0.0393  185 ILE A CD1 
1436 N N   . GLN A 189 ? 0.7798 0.6719 0.7143 -0.1376 0.0159  -0.0221 186 GLN A N   
1437 C CA  . GLN A 189 ? 0.8405 0.6714 0.7785 -0.1488 0.0302  -0.0273 186 GLN A CA  
1438 C C   . GLN A 189 ? 0.8814 0.7036 0.8212 -0.1893 0.0214  -0.0502 186 GLN A C   
1439 O O   . GLN A 189 ? 0.8339 0.6741 0.7523 -0.2035 0.0069  -0.0759 186 GLN A O   
1440 C CB  . GLN A 189 ? 0.8858 0.6612 0.8031 -0.1275 0.0474  -0.0402 186 GLN A CB  
1441 C CG  . GLN A 189 ? 0.9599 0.6586 0.8798 -0.1367 0.0647  -0.0472 186 GLN A CG  
1442 C CD  . GLN A 189 ? 0.9804 0.6643 0.9263 -0.1290 0.0738  -0.0108 186 GLN A CD  
1443 O OE1 . GLN A 189 ? 0.9022 0.6111 0.8558 -0.0992 0.0748  0.0163  186 GLN A OE1 
1444 N NE2 . GLN A 189 ? 1.0039 0.6463 0.9615 -0.1574 0.0810  -0.0101 186 GLN A NE2 
1445 N N   . ALA A 190 ? 0.9414 0.7385 0.9064 -0.2092 0.0298  -0.0395 187 ALA A N   
1446 C CA  . ALA A 190 ? 1.0249 0.8064 1.0004 -0.2535 0.0240  -0.0622 187 ALA A CA  
1447 C C   . ALA A 190 ? 1.1125 0.8070 1.0616 -0.2608 0.0378  -0.0931 187 ALA A C   
1448 O O   . ALA A 190 ? 1.1216 0.7545 1.0663 -0.2366 0.0604  -0.0811 187 ALA A O   
1449 C CB  . ALA A 190 ? 1.0130 0.8008 1.0300 -0.2743 0.0326  -0.0358 187 ALA A CB  
1450 N N   . GLU A 191 ? 1.2969 0.9874 1.2267 -0.2921 0.0236  -0.1338 188 GLU A N   
1451 C CA  . GLU A 191 ? 1.3867 0.9927 1.2825 -0.2983 0.0374  -0.1725 188 GLU A CA  
1452 C C   . GLU A 191 ? 1.4503 0.9717 1.3700 -0.3175 0.0598  -0.1693 188 GLU A C   
1453 O O   . GLU A 191 ? 1.5104 0.9541 1.4198 -0.2909 0.0862  -0.1660 188 GLU A O   
1454 C CB  . GLU A 191 ? 1.4229 1.0501 1.2864 -0.3320 0.0133  -0.2198 188 GLU A CB  
1455 C CG  . GLU A 191 ? 1.4555 1.0643 1.2581 -0.3075 0.0180  -0.2499 188 GLU A CG  
1456 C CD  . GLU A 191 ? 1.5359 1.1748 1.2964 -0.3404 -0.0094 -0.2942 188 GLU A CD  
1457 O OE1 . GLU A 191 ? 1.4546 1.1807 1.2279 -0.3548 -0.0406 -0.2827 188 GLU A OE1 
1458 O OE2 . GLU A 191 ? 1.6966 1.2718 1.4106 -0.3516 -0.0002 -0.3414 188 GLU A OE2 
1459 N N   . ASN A 192 ? 1.3606 0.8972 1.3170 -0.3627 0.0515  -0.1669 189 ASN A N   
1460 C CA  . ASN A 192 ? 1.4460 0.8991 1.4280 -0.3878 0.0748  -0.1612 189 ASN A CA  
1461 C C   . ASN A 192 ? 1.4219 0.8877 1.4381 -0.3673 0.0914  -0.1015 189 ASN A C   
1462 O O   . ASN A 192 ? 1.4225 0.9247 1.4791 -0.3973 0.0904  -0.0798 189 ASN A O   
1463 C CB  . ASN A 192 ? 1.5286 1.0049 1.5383 -0.4391 0.0545  -0.1865 189 ASN A CB  
1464 C CG  . ASN A 192 ? 1.5512 1.0453 1.5225 -0.4532 0.0286  -0.2408 189 ASN A CG  
1465 O OD1 . ASN A 192 ? 1.6261 1.0500 1.5552 -0.4395 0.0393  -0.2731 189 ASN A OD1 
1466 N ND2 . ASN A 192 ? 1.4805 1.0726 1.4656 -0.4765 -0.0051 -0.2488 189 ASN A ND2 
1467 N N   . ASP A 193 ? 1.4287 0.8679 1.4274 -0.3150 0.1074  -0.0752 190 ASP A N   
1468 C CA  . ASP A 193 ? 1.3705 0.8179 1.3880 -0.2895 0.1218  -0.0198 190 ASP A CA  
1469 C C   . ASP A 193 ? 1.4387 0.7800 1.4623 -0.2882 0.1522  -0.0006 190 ASP A C   
1470 O O   . ASP A 193 ? 1.4703 0.7338 1.4739 -0.2657 0.1664  -0.0163 190 ASP A O   
1471 C CB  . ASP A 193 ? 1.2548 0.7445 1.2531 -0.2346 0.1171  0.0001  190 ASP A CB  
1472 C CG  . ASP A 193 ? 1.2270 0.7598 1.2393 -0.2151 0.1207  0.0505  190 ASP A CG  
1473 O OD1 . ASP A 193 ? 1.3044 0.7912 1.3282 -0.2198 0.1403  0.0818  190 ASP A OD1 
1474 O OD2 . ASP A 193 ? 1.1092 0.7182 1.1178 -0.1956 0.1054  0.0586  190 ASP A OD2 
1475 N N   . ASN A 194 ? 1.4950 0.8387 1.5471 -0.3073 0.1623  0.0359  191 ASN A N   
1476 C CA  . ASN A 194 ? 1.5341 0.8057 1.5916 -0.2944 0.1810  0.0653  191 ASN A CA  
1477 C C   . ASN A 194 ? 1.5322 0.8046 1.5776 -0.2458 0.1936  0.1207  191 ASN A C   
1478 O O   . ASN A 194 ? 1.5572 0.7733 1.6008 -0.2285 0.2073  0.1499  191 ASN A O   
1479 C CB  . ASN A 194 ? 1.5900 0.8688 1.6822 -0.3408 0.1817  0.0762  191 ASN A CB  
1480 C CG  . ASN A 194 ? 1.6309 0.9297 1.7423 -0.3910 0.1625  0.0250  191 ASN A CG  
1481 O OD1 . ASN A 194 ? 1.6956 1.0571 1.8434 -0.4285 0.1527  0.0293  191 ASN A OD1 
1482 N ND2 . ASN A 194 ? 1.6096 0.8613 1.6969 -0.3897 0.1562  -0.0237 191 ASN A ND2 
1483 N N   . MET A 195 ? 1.4187 0.7556 1.4541 -0.2232 0.1873  0.1360  192 MET A N   
1484 C CA  . MET A 195 ? 1.3710 0.7256 1.3940 -0.1810 0.1932  0.1891  192 MET A CA  
1485 C C   . MET A 195 ? 1.3668 0.7155 1.3698 -0.1257 0.1876  0.1915  192 MET A C   
1486 O O   . MET A 195 ? 1.4362 0.7476 1.4317 -0.0893 0.1970  0.2265  192 MET A O   
1487 C CB  . MET A 195 ? 1.2102 0.6636 1.2367 -0.1883 0.1826  0.2071  192 MET A CB  
1488 C CG  . MET A 195 ? 1.2778 0.7452 1.2848 -0.1533 0.1907  0.2614  192 MET A CG  
1489 S SD  . MET A 195 ? 1.5080 0.9481 1.5177 -0.1749 0.2071  0.2976  192 MET A SD  
1490 C CE  . MET A 195 ? 1.3976 0.8328 1.4502 -0.2418 0.2089  0.2596  192 MET A CE  
1491 N N   . ILE A 196 ? 1.2703 0.6705 1.2670 -0.1167 0.1677  0.1547  193 ILE A N   
1492 C CA  . ILE A 196 ? 1.2465 0.6481 1.2329 -0.0692 0.1634  0.1507  193 ILE A CA  
1493 C C   . ILE A 196 ? 1.3037 0.6481 1.2862 -0.0747 0.1711  0.1032  193 ILE A C   
1494 O O   . ILE A 196 ? 1.3551 0.6616 1.3382 -0.1167 0.1752  0.0713  193 ILE A O   
1495 C CB  . ILE A 196 ? 1.2093 0.7112 1.1902 -0.0512 0.1395  0.1490  193 ILE A CB  
1496 C CG1 . ILE A 196 ? 1.1374 0.6898 1.1180 -0.0838 0.1238  0.1090  193 ILE A CG1 
1497 C CG2 . ILE A 196 ? 1.1878 0.7378 1.1651 -0.0444 0.1344  0.1908  193 ILE A CG2 
1498 C CD1 . ILE A 196 ? 1.0103 0.6120 0.9834 -0.0612 0.1098  0.0881  193 ILE A CD1 
1499 N N   . ASP A 197 ? 1.3095 0.6486 1.2881 -0.0319 0.1740  0.0978  194 ASP A N   
1500 C CA  . ASP A 197 ? 1.2746 0.5757 1.2425 -0.0318 0.1823  0.0493  194 ASP A CA  
1501 C C   . ASP A 197 ? 1.2205 0.6040 1.1756 -0.0441 0.1611  0.0188  194 ASP A C   
1502 O O   . ASP A 197 ? 1.2129 0.6636 1.1726 -0.0157 0.1501  0.0334  194 ASP A O   
1503 C CB  . ASP A 197 ? 1.3669 0.6328 1.3417 0.0223  0.1993  0.0579  194 ASP A CB  
1504 C CG  . ASP A 197 ? 1.4306 0.6624 1.3898 0.0262  0.2126  0.0054  194 ASP A CG  
1505 O OD1 . ASP A 197 ? 1.4047 0.6080 1.3422 -0.0160 0.2123  -0.0381 194 ASP A OD1 
1506 O OD2 . ASP A 197 ? 1.4848 0.7285 1.4531 0.0714  0.2223  0.0070  194 ASP A OD2 
1507 N N   . PRO A 198 ? 1.2539 0.6349 1.1933 -0.0854 0.1541  -0.0225 195 PRO A N   
1508 C CA  . PRO A 198 ? 1.2217 0.6859 1.1477 -0.0963 0.1317  -0.0421 195 PRO A CA  
1509 C C   . PRO A 198 ? 1.1720 0.6559 1.0835 -0.0623 0.1366  -0.0574 195 PRO A C   
1510 O O   . PRO A 198 ? 1.0710 0.6274 0.9769 -0.0599 0.1209  -0.0578 195 PRO A O   
1511 C CB  . PRO A 198 ? 1.2446 0.6936 1.1559 -0.1464 0.1230  -0.0821 195 PRO A CB  
1512 C CG  . PRO A 198 ? 1.2962 0.6503 1.2161 -0.1667 0.1421  -0.0871 195 PRO A CG  
1513 C CD  . PRO A 198 ? 1.2855 0.5854 1.2176 -0.1227 0.1656  -0.0542 195 PRO A CD  
1514 N N   . GLN A 199 ? 1.2180 0.6387 1.1270 -0.0340 0.1609  -0.0670 196 GLN A N   
1515 C CA  . GLN A 199 ? 1.2092 0.6523 1.1154 0.0043  0.1720  -0.0745 196 GLN A CA  
1516 C C   . GLN A 199 ? 1.1007 0.6204 1.0358 0.0341  0.1606  -0.0351 196 GLN A C   
1517 O O   . GLN A 199 ? 1.0465 0.6052 0.9863 0.0587  0.1660  -0.0395 196 GLN A O   
1518 C CB  . GLN A 199 ? 1.2578 0.6161 1.1677 0.0347  0.2036  -0.0848 196 GLN A CB  
1519 C CG  . GLN A 199 ? 1.3830 0.7428 1.2755 0.0587  0.2233  -0.1174 196 GLN A CG  
1520 C CD  . GLN A 199 ? 1.4926 0.8511 1.3341 0.0221  0.2188  -0.1673 196 GLN A CD  
1521 O OE1 . GLN A 199 ? 1.5067 0.8262 1.3270 -0.0195 0.2092  -0.1900 196 GLN A OE1 
1522 N NE2 . GLN A 199 ? 1.4507 0.8569 1.2726 0.0360  0.2250  -0.1828 196 GLN A NE2 
1523 N N   . SER A 200 ? 1.0974 0.6390 1.0513 0.0314  0.1465  0.0019  197 SER A N   
1524 C CA  . SER A 200 ? 0.9941 0.6085 0.9696 0.0545  0.1322  0.0333  197 SER A CA  
1525 C C   . SER A 200 ? 0.9642 0.6490 0.9316 0.0414  0.1171  0.0189  197 SER A C   
1526 O O   . SER A 200 ? 0.8766 0.6141 0.8614 0.0626  0.1129  0.0290  197 SER A O   
1527 C CB  . SER A 200 ? 1.0100 0.6338 0.9930 0.0476  0.1201  0.0695  197 SER A CB  
1528 O OG  . SER A 200 ? 1.0539 0.6045 1.0406 0.0552  0.1360  0.0869  197 SER A OG  
1529 N N   . ALA A 201 ? 0.9648 0.6527 0.9090 0.0057  0.1082  -0.0027 198 ALA A N   
1530 C CA  . ALA A 201 ? 0.9165 0.6651 0.8507 -0.0055 0.0943  -0.0119 198 ALA A CA  
1531 C C   . ALA A 201 ? 0.8974 0.6550 0.8226 0.0124  0.1080  -0.0297 198 ALA A C   
1532 O O   . ALA A 201 ? 0.8337 0.6446 0.7681 0.0205  0.1029  -0.0213 198 ALA A O   
1533 C CB  . ALA A 201 ? 0.8303 0.5807 0.7432 -0.0434 0.0814  -0.0303 198 ALA A CB  
1534 N N   . ASN A 202 ? 0.9443 0.6475 0.8521 0.0185  0.1288  -0.0547 199 ASN A N   
1535 C CA  . ASN A 202 ? 0.9766 0.6881 0.8773 0.0403  0.1491  -0.0701 199 ASN A CA  
1536 C C   . ASN A 202 ? 0.9368 0.6814 0.8837 0.0772  0.1572  -0.0435 199 ASN A C   
1537 O O   . ASN A 202 ? 0.8622 0.6549 0.8199 0.0885  0.1638  -0.0420 199 ASN A O   
1538 C CB  . ASN A 202 ? 1.0122 0.6513 0.8831 0.0421  0.1732  -0.1058 199 ASN A CB  
1539 C CG  . ASN A 202 ? 1.1350 0.7649 0.9513 0.0078  0.1660  -0.1416 199 ASN A CG  
1540 O OD1 . ASN A 202 ? 1.1206 0.8055 0.9223 -0.0095 0.1466  -0.1368 199 ASN A OD1 
1541 N ND2 . ASN A 202 ? 1.2260 0.7853 1.0109 -0.0012 0.1809  -0.1783 199 ASN A ND2 
1542 N N   . TYR A 203 ? 0.8823 0.6048 0.8585 0.0956  0.1565  -0.0205 200 TYR A N   
1543 C CA  . TYR A 203 ? 0.8520 0.6181 0.8747 0.1297  0.1569  0.0068  200 TYR A CA  
1544 C C   . TYR A 203 ? 0.8009 0.6454 0.8394 0.1193  0.1345  0.0222  200 TYR A C   
1545 O O   . TYR A 203 ? 0.7920 0.6882 0.8628 0.1361  0.1381  0.0287  200 TYR A O   
1546 C CB  . TYR A 203 ? 0.8750 0.6097 0.9191 0.1499  0.1536  0.0354  200 TYR A CB  
1547 C CG  . TYR A 203 ? 0.8459 0.6286 0.9392 0.1899  0.1534  0.0611  200 TYR A CG  
1548 C CD1 . TYR A 203 ? 0.9307 0.6938 1.0495 0.2271  0.1799  0.0568  200 TYR A CD1 
1549 C CD2 . TYR A 203 ? 0.8230 0.6760 0.9391 0.1903  0.1268  0.0866  200 TYR A CD2 
1550 C CE1 . TYR A 203 ? 0.9114 0.7313 1.0848 0.2648  0.1780  0.0814  200 TYR A CE1 
1551 C CE2 . TYR A 203 ? 0.8380 0.7459 1.0028 0.2235  0.1219  0.1076  200 TYR A CE2 
1552 C CZ  . TYR A 203 ? 0.9058 0.8013 1.1029 0.2611  0.1466  0.1069  200 TYR A CZ  
1553 O OH  . TYR A 203 ? 0.9239 0.8851 1.1790 0.2956  0.1399  0.1300  200 TYR A OH  
1554 N N   . ILE A 204 ? 0.7982 0.6520 0.8186 0.0914  0.1129  0.0274  201 ILE A N   
1555 C CA  . ILE A 204 ? 0.7399 0.6568 0.7734 0.0822  0.0936  0.0391  201 ILE A CA  
1556 C C   . ILE A 204 ? 0.7676 0.7121 0.7924 0.0719  0.1009  0.0231  201 ILE A C   
1557 O O   . ILE A 204 ? 0.6925 0.6845 0.7462 0.0794  0.1014  0.0302  201 ILE A O   
1558 C CB  . ILE A 204 ? 0.7143 0.6306 0.7305 0.0588  0.0738  0.0474  201 ILE A CB  
1559 C CG1 . ILE A 204 ? 0.7550 0.6463 0.7770 0.0698  0.0702  0.0691  201 ILE A CG1 
1560 C CG2 . ILE A 204 ? 0.6675 0.6392 0.6937 0.0501  0.0569  0.0542  201 ILE A CG2 
1561 C CD1 . ILE A 204 ? 0.7448 0.6384 0.7511 0.0484  0.0567  0.0789  201 ILE A CD1 
1562 N N   . TYR A 205 ? 0.7526 0.6693 0.7372 0.0529  0.1061  0.0027  202 TYR A N   
1563 C CA  . TYR A 205 ? 0.7138 0.6553 0.6795 0.0424  0.1114  -0.0070 202 TYR A CA  
1564 C C   . TYR A 205 ? 0.7271 0.6857 0.7105 0.0631  0.1367  -0.0105 202 TYR A C   
1565 O O   . TYR A 205 ? 0.6855 0.6831 0.6770 0.0592  0.1413  -0.0045 202 TYR A O   
1566 C CB  . TYR A 205 ? 0.7383 0.6482 0.6529 0.0215  0.1104  -0.0291 202 TYR A CB  
1567 C CG  . TYR A 205 ? 0.7346 0.6667 0.6170 0.0126  0.1156  -0.0363 202 TYR A CG  
1568 C CD1 . TYR A 205 ? 0.6788 0.6440 0.5579 -0.0013 0.0980  -0.0218 202 TYR A CD1 
1569 C CD2 . TYR A 205 ? 0.7572 0.6739 0.6087 0.0205  0.1406  -0.0563 202 TYR A CD2 
1570 C CE1 . TYR A 205 ? 0.6605 0.6430 0.5073 -0.0071 0.1029  -0.0216 202 TYR A CE1 
1571 C CE2 . TYR A 205 ? 0.7460 0.6837 0.5599 0.0132  0.1468  -0.0584 202 TYR A CE2 
1572 C CZ  . TYR A 205 ? 0.7509 0.7215 0.5631 -0.0006 0.1269  -0.0382 202 TYR A CZ  
1573 O OH  . TYR A 205 ? 0.6907 0.6799 0.4642 -0.0054 0.1333  -0.0332 202 TYR A OH  
1574 N N   . ASP A 206 ? 0.7414 0.6711 0.7354 0.0860  0.1559  -0.0181 203 ASP A N   
1575 C CA  . ASP A 206 ? 0.7646 0.7115 0.7785 0.1093  0.1855  -0.0235 203 ASP A CA  
1576 C C   . ASP A 206 ? 0.7265 0.7311 0.8083 0.1289  0.1831  0.0002  203 ASP A C   
1577 O O   . ASP A 206 ? 0.7299 0.7715 0.8395 0.1417  0.2057  0.0002  203 ASP A O   
1578 C CB  . ASP A 206 ? 0.8022 0.6899 0.8013 0.1299  0.2104  -0.0443 203 ASP A CB  
1579 C CG  . ASP A 206 ? 0.9135 0.7576 0.8448 0.1127  0.2233  -0.0779 203 ASP A CG  
1580 O OD1 . ASP A 206 ? 0.9123 0.7845 0.8118 0.0931  0.2198  -0.0811 203 ASP A OD1 
1581 O OD2 . ASP A 206 ? 1.0442 0.8239 0.9522 0.1190  0.2371  -0.1012 203 ASP A OD2 
1582 N N   . HIS A 207 ? 0.7232 0.7410 0.8325 0.1309  0.1568  0.0200  204 HIS A N   
1583 C CA  . HIS A 207 ? 0.6616 0.7343 0.8344 0.1523  0.1505  0.0402  204 HIS A CA  
1584 C C   . HIS A 207 ? 0.6171 0.7464 0.8138 0.1327  0.1239  0.0532  204 HIS A C   
1585 O O   . HIS A 207 ? 0.5970 0.7846 0.8494 0.1438  0.1190  0.0648  204 HIS A O   
1586 C CB  . HIS A 207 ? 0.6549 0.7016 0.8419 0.1779  0.1421  0.0549  204 HIS A CB  
1587 C CG  . HIS A 207 ? 0.7513 0.7494 0.9378 0.2071  0.1725  0.0449  204 HIS A CG  
1588 N ND1 . HIS A 207 ? 0.7987 0.7173 0.9335 0.1986  0.1853  0.0246  204 HIS A ND1 
1589 C CD2 . HIS A 207 ? 0.7614 0.7787 0.9952 0.2448  0.1944  0.0496  204 HIS A CD2 
1590 C CE1 . HIS A 207 ? 0.8584 0.7401 1.0034 0.2298  0.2149  0.0150  204 HIS A CE1 
1591 N NE2 . HIS A 207 ? 0.8087 0.7499 1.0147 0.2610  0.2222  0.0314  204 HIS A NE2 
1592 N N   . VAL A 208 ? 0.5754 0.6908 0.7356 0.1045  0.1065  0.0504  205 VAL A N   
1593 C CA  . VAL A 208 ? 0.6079 0.7680 0.7883 0.0855  0.0875  0.0569  205 VAL A CA  
1594 C C   . VAL A 208 ? 0.5577 0.7548 0.7661 0.0788  0.1071  0.0543  205 VAL A C   
1595 O O   . VAL A 208 ? 0.5909 0.7722 0.7819 0.0830  0.1347  0.0460  205 VAL A O   
1596 C CB  . VAL A 208 ? 0.6049 0.7394 0.7422 0.0609  0.0715  0.0536  205 VAL A CB  
1597 C CG1 . VAL A 208 ? 0.5401 0.6484 0.6574 0.0648  0.0548  0.0596  205 VAL A CG1 
1598 C CG2 . VAL A 208 ? 0.6005 0.7024 0.6948 0.0488  0.0872  0.0421  205 VAL A CG2 
1599 N N   . ASP A 209 ? 0.5218 0.7683 0.7728 0.0668  0.0942  0.0605  206 ASP A N   
1600 C CA  . ASP A 209 ? 0.5260 0.8073 0.8086 0.0534  0.1129  0.0613  206 ASP A CA  
1601 C C   . ASP A 209 ? 0.4985 0.7577 0.7490 0.0247  0.1108  0.0604  206 ASP A C   
1602 O O   . ASP A 209 ? 0.5254 0.8107 0.8062 0.0074  0.1202  0.0649  206 ASP A O   
1603 C CB  . ASP A 209 ? 0.4575 0.8084 0.8153 0.0530  0.1014  0.0676  206 ASP A CB  
1604 C CG  . ASP A 209 ? 0.5980 0.9943 1.0071 0.0513  0.1323  0.0710  206 ASP A CG  
1605 O OD1 . ASP A 209 ? 0.6940 1.0632 1.0706 0.0504  0.1639  0.0691  206 ASP A OD1 
1606 O OD2 . ASP A 209 ? 0.6001 1.0637 1.0820 0.0506  0.1252  0.0758  206 ASP A OD2 
1607 N N   . SER A 210 ? 0.5035 0.7161 0.6981 0.0199  0.1001  0.0568  207 SER A N   
1608 C CA  . SER A 210 ? 0.5598 0.7534 0.7286 -0.0011 0.0971  0.0594  207 SER A CA  
1609 C C   . SER A 210 ? 0.5197 0.7068 0.6695 -0.0060 0.1255  0.0649  207 SER A C   
1610 O O   . SER A 210 ? 0.5006 0.6793 0.6272 0.0068  0.1454  0.0604  207 SER A O   
1611 C CB  . SER A 210 ? 0.5217 0.6771 0.6423 -0.0020 0.0800  0.0559  207 SER A CB  
1612 O OG  . SER A 210 ? 0.5908 0.7509 0.7216 0.0050  0.0594  0.0534  207 SER A OG  
1613 N N   . ASP A 211 ? 0.5198 0.7069 0.6760 -0.0244 0.1286  0.0749  208 ASP A N   
1614 C CA  . ASP A 211 ? 0.5440 0.7213 0.6750 -0.0311 0.1537  0.0876  208 ASP A CA  
1615 C C   . ASP A 211 ? 0.5687 0.7084 0.6350 -0.0305 0.1456  0.0917  208 ASP A C   
1616 O O   . ASP A 211 ? 0.6240 0.7543 0.6565 -0.0333 0.1630  0.1053  208 ASP A O   
1617 C CB  . ASP A 211 ? 0.5229 0.7133 0.6968 -0.0520 0.1620  0.1007  208 ASP A CB  
1618 C CG  . ASP A 211 ? 0.5722 0.8113 0.8098 -0.0557 0.1807  0.1011  208 ASP A CG  
1619 O OD1 . ASP A 211 ? 0.5890 0.8521 0.8373 -0.0366 0.1882  0.0926  208 ASP A OD1 
1620 O OD2 . ASP A 211 ? 0.6346 0.8878 0.9151 -0.0776 0.1902  0.1107  208 ASP A OD2 
1621 N N   . ASP A 212 ? 0.5334 0.6567 0.5824 -0.0265 0.1199  0.0823  209 ASP A N   
1622 C CA  . ASP A 212 ? 0.6100 0.7091 0.6126 -0.0274 0.1070  0.0872  209 ASP A CA  
1623 C C   . ASP A 212 ? 0.5985 0.6889 0.5848 -0.0207 0.0890  0.0711  209 ASP A C   
1624 O O   . ASP A 212 ? 0.5445 0.6361 0.5528 -0.0209 0.0722  0.0666  209 ASP A O   
1625 C CB  . ASP A 212 ? 0.5665 0.6564 0.5861 -0.0357 0.0961  0.0989  209 ASP A CB  
1626 C CG  . ASP A 212 ? 0.6382 0.7113 0.6202 -0.0321 0.0830  0.1082  209 ASP A CG  
1627 O OD1 . ASP A 212 ? 0.6701 0.7435 0.6137 -0.0272 0.0770  0.1031  209 ASP A OD1 
1628 O OD2 . ASP A 212 ? 0.6628 0.7232 0.6575 -0.0341 0.0779  0.1193  209 ASP A OD2 
1629 N N   . LYS A 213 ? 0.6223 0.7021 0.5683 -0.0166 0.0939  0.0615  210 LYS A N   
1630 C CA  . LYS A 213 ? 0.6117 0.6777 0.5486 -0.0142 0.0802  0.0460  210 LYS A CA  
1631 C C   . LYS A 213 ? 0.6078 0.6597 0.4933 -0.0197 0.0745  0.0365  210 LYS A C   
1632 O O   . LYS A 213 ? 0.6470 0.7007 0.4958 -0.0209 0.0839  0.0387  210 LYS A O   
1633 C CB  . LYS A 213 ? 0.5587 0.6224 0.5179 -0.0026 0.0921  0.0350  210 LYS A CB  
1634 C CG  . LYS A 213 ? 0.6271 0.6906 0.5736 0.0059  0.1197  0.0277  210 LYS A CG  
1635 C CD  . LYS A 213 ? 0.6188 0.6925 0.6097 0.0224  0.1311  0.0245  210 LYS A CD  
1636 C CE  . LYS A 213 ? 0.6429 0.7061 0.6180 0.0367  0.1605  0.0104  210 LYS A CE  
1637 N NZ  . LYS A 213 ? 0.6316 0.7134 0.6615 0.0577  0.1716  0.0124  210 LYS A NZ  
1638 N N   . ASN A 214 ? 0.7963 0.8358 0.6788 -0.0242 0.0594  0.0253  211 ASN A N   
1639 C CA  . ASN A 214 ? 0.8168 0.8525 0.6648 -0.0360 0.0438  0.0169  211 ASN A CA  
1640 C C   . ASN A 214 ? 0.8250 0.8388 0.6802 -0.0422 0.0380  0.0008  211 ASN A C   
1641 O O   . ASN A 214 ? 0.8104 0.8229 0.6997 -0.0383 0.0352  0.0082  211 ASN A O   
1642 C CB  . ASN A 214 ? 0.8128 0.8715 0.6709 -0.0398 0.0248  0.0351  211 ASN A CB  
1643 C CG  . ASN A 214 ? 0.9146 0.9873 0.7346 -0.0474 0.0103  0.0356  211 ASN A CG  
1644 O OD1 . ASN A 214 ? 0.9771 1.0703 0.8012 -0.0439 -0.0008 0.0555  211 ASN A OD1 
1645 N ND2 . ASN A 214 ? 0.9361 0.9974 0.7172 -0.0568 0.0098  0.0130  211 ASN A ND2 
1646 N N   . ILE A 215 ? 0.7295 0.7241 0.5502 -0.0534 0.0362  -0.0209 212 ILE A N   
1647 C CA  . ILE A 215 ? 0.7122 0.6791 0.5412 -0.0644 0.0317  -0.0352 212 ILE A CA  
1648 C C   . ILE A 215 ? 0.7659 0.7399 0.5697 -0.0888 0.0117  -0.0501 212 ILE A C   
1649 O O   . ILE A 215 ? 0.7652 0.7442 0.5252 -0.0947 0.0087  -0.0643 212 ILE A O   
1650 C CB  . ILE A 215 ? 0.7930 0.7153 0.6166 -0.0540 0.0545  -0.0529 212 ILE A CB  
1651 C CG1 . ILE A 215 ? 0.8097 0.6923 0.6419 -0.0667 0.0520  -0.0646 212 ILE A CG1 
1652 C CG2 . ILE A 215 ? 0.7712 0.6809 0.5467 -0.0522 0.0692  -0.0757 212 ILE A CG2 
1653 C CD1 . ILE A 215 ? 0.8428 0.6749 0.6808 -0.0496 0.0758  -0.0744 212 ILE A CD1 
1654 N N   . LYS A 216 ? 0.7173 0.6970 0.5487 -0.1038 -0.0020 -0.0465 213 LYS A N   
1655 C CA  . LYS A 216 ? 0.7910 0.7881 0.6140 -0.1307 -0.0236 -0.0598 213 LYS A CA  
1656 C C   . LYS A 216 ? 0.7658 0.7248 0.6048 -0.1516 -0.0201 -0.0755 213 LYS A C   
1657 O O   . LYS A 216 ? 0.7669 0.7097 0.6388 -0.1451 -0.0095 -0.0599 213 LYS A O   
1658 C CB  . LYS A 216 ? 0.7565 0.8114 0.6091 -0.1321 -0.0438 -0.0360 213 LYS A CB  
1659 C CG  . LYS A 216 ? 0.6904 0.7817 0.5269 -0.1161 -0.0517 -0.0186 213 LYS A CG  
1660 C CD  . LYS A 216 ? 0.9101 1.0155 0.6979 -0.1271 -0.0666 -0.0339 213 LYS A CD  
1661 C CE  . LYS A 216 ? 1.0149 1.1756 0.8018 -0.1191 -0.0883 -0.0096 213 LYS A CE  
1662 N NZ  . LYS A 216 ? 1.0172 1.1793 0.8213 -0.0923 -0.0747 0.0209  213 LYS A NZ  
1663 N N   . TRP A 217 ? 0.7624 0.7083 0.5769 -0.1786 -0.0303 -0.1054 214 TRP A N   
1664 C CA  . TRP A 217 ? 0.7846 0.6842 0.6102 -0.2050 -0.0259 -0.1259 214 TRP A CA  
1665 C C   . TRP A 217 ? 0.9005 0.8426 0.7483 -0.2417 -0.0523 -0.1322 214 TRP A C   
1666 O O   . TRP A 217 ? 0.8850 0.8741 0.7115 -0.2532 -0.0768 -0.1431 214 TRP A O   
1667 C CB  . TRP A 217 ? 0.8805 0.7197 0.6578 -0.2108 -0.0133 -0.1657 214 TRP A CB  
1668 C CG  . TRP A 217 ? 0.9658 0.7629 0.7291 -0.1757 0.0162  -0.1632 214 TRP A CG  
1669 C CD1 . TRP A 217 ? 0.9590 0.7701 0.6885 -0.1517 0.0256  -0.1644 214 TRP A CD1 
1670 C CD2 . TRP A 217 ? 0.9843 0.7227 0.7712 -0.1596 0.0414  -0.1564 214 TRP A CD2 
1671 N NE1 . TRP A 217 ? 0.9748 0.7455 0.7120 -0.1227 0.0550  -0.1611 214 TRP A NE1 
1672 C CE2 . TRP A 217 ? 0.9766 0.7028 0.7483 -0.1248 0.0634  -0.1554 214 TRP A CE2 
1673 C CE3 . TRP A 217 ? 0.9876 0.6842 0.8082 -0.1703 0.0484  -0.1476 214 TRP A CE3 
1674 C CZ2 . TRP A 217 ? 0.9807 0.6604 0.7737 -0.0978 0.0886  -0.1466 214 TRP A CZ2 
1675 C CZ3 . TRP A 217 ? 1.0322 0.6750 0.8661 -0.1429 0.0739  -0.1365 214 TRP A CZ3 
1676 C CH2 . TRP A 217 ? 1.0241 0.6618 0.8463 -0.1056 0.0920  -0.1361 214 TRP A CH2 
1677 N N   . TYR A 218 ? 0.9445 0.8721 0.8354 -0.2613 -0.0471 -0.1249 215 TYR A N   
1678 C CA  . TYR A 218 ? 0.9119 0.8870 0.8394 -0.2984 -0.0685 -0.1278 215 TYR A CA  
1679 C C   . TYR A 218 ? 1.0156 0.9312 0.9493 -0.3378 -0.0617 -0.1564 215 TYR A C   
1680 O O   . TYR A 218 ? 1.0324 0.8854 0.9806 -0.3345 -0.0355 -0.1464 215 TYR A O   
1681 C CB  . TYR A 218 ? 0.9203 0.9437 0.9018 -0.2884 -0.0651 -0.0885 215 TYR A CB  
1682 C CG  . TYR A 218 ? 0.8493 0.9193 0.8238 -0.2512 -0.0703 -0.0651 215 TYR A CG  
1683 C CD1 . TYR A 218 ? 0.7555 0.7938 0.7136 -0.2159 -0.0507 -0.0499 215 TYR A CD1 
1684 C CD2 . TYR A 218 ? 0.8370 0.9821 0.8227 -0.2515 -0.0957 -0.0583 215 TYR A CD2 
1685 C CE1 . TYR A 218 ? 0.7569 0.8312 0.7104 -0.1864 -0.0543 -0.0310 215 TYR A CE1 
1686 C CE2 . TYR A 218 ? 0.7665 0.9432 0.7457 -0.2170 -0.0978 -0.0358 215 TYR A CE2 
1687 C CZ  . TYR A 218 ? 0.7408 0.8783 0.7034 -0.1870 -0.0761 -0.0238 215 TYR A CZ  
1688 O OH  . TYR A 218 ? 0.7043 0.8669 0.6638 -0.1580 -0.0769 -0.0037 215 TYR A OH  
1689 N N   . SER A 219 ? 1.0769 1.0127 1.0002 -0.3760 -0.0865 -0.1906 216 SER A N   
1690 C CA  . SER A 219 ? 1.1449 1.0134 1.0577 -0.4168 -0.0825 -0.2318 216 SER A CA  
1691 C C   . SER A 219 ? 1.1970 1.0744 1.1745 -0.4605 -0.0840 -0.2267 216 SER A C   
1692 O O   . SER A 219 ? 1.2071 1.0211 1.1884 -0.4815 -0.0756 -0.2504 216 SER A O   
1693 C CB  . SER A 219 ? 1.2547 1.1433 1.1169 -0.4364 -0.1111 -0.2760 216 SER A CB  
1694 O OG  . SER A 219 ? 1.1991 1.1889 1.0966 -0.4483 -0.1465 -0.2643 216 SER A OG  
1695 N N   . GLU A 220 ? 1.1193 1.0771 1.1528 -0.4612 -0.0922 -0.1908 217 GLU A N   
1696 C CA  . GLU A 220 ? 1.1006 1.0825 1.2023 -0.4900 -0.0915 -0.1796 217 GLU A CA  
1697 C C   . GLU A 220 ? 1.0735 1.0585 1.2200 -0.4815 -0.0632 -0.1343 217 GLU A C   
1698 O O   . GLU A 220 ? 1.0615 1.0716 1.2670 -0.5020 -0.0576 -0.1193 217 GLU A O   
1699 C CB  . GLU A 220 ? 1.0661 1.1559 1.2033 -0.5013 -0.1286 -0.1822 217 GLU A CB  
1700 C CG  . GLU A 220 ? 1.1588 1.2684 1.2429 -0.5002 -0.1615 -0.2174 217 GLU A CG  
1701 C CD  . GLU A 220 ? 1.2761 1.3417 1.3529 -0.5353 -0.1721 -0.2600 217 GLU A CD  
1702 O OE1 . GLU A 220 ? 1.3029 1.3736 1.4412 -0.5661 -0.1708 -0.2582 217 GLU A OE1 
1703 O OE2 . GLU A 220 ? 1.3141 1.3409 1.3238 -0.5320 -0.1809 -0.2955 217 GLU A OE2 
1704 N N   . SER A 221 ? 0.9574 0.9198 1.0775 -0.4373 -0.0443 -0.1081 218 SER A N   
1705 C CA  . SER A 221 ? 0.9550 0.9291 1.1074 -0.4172 -0.0201 -0.0631 218 SER A CA  
1706 C C   . SER A 221 ? 0.9938 0.8678 1.1336 -0.4125 0.0134  -0.0507 218 SER A C   
1707 O O   . SER A 221 ? 1.0785 0.8715 1.1811 -0.4106 0.0201  -0.0746 218 SER A O   
1708 C CB  . SER A 221 ? 0.9246 0.9430 1.0586 -0.3651 -0.0227 -0.0394 218 SER A CB  
1709 O OG  . SER A 221 ? 0.9171 1.0100 1.0509 -0.3630 -0.0533 -0.0513 218 SER A OG  
1710 N N   . GLY A 222 ? 0.9574 0.8388 1.1269 -0.4075 0.0360  -0.0112 219 GLY A N   
1711 C CA  . GLY A 222 ? 0.9644 0.7631 1.1188 -0.3912 0.0673  0.0145  219 GLY A CA  
1712 C C   . GLY A 222 ? 0.9152 0.7185 1.0363 -0.3344 0.0731  0.0400  219 GLY A C   
1713 O O   . GLY A 222 ? 0.9149 0.7661 1.0187 -0.3085 0.0548  0.0311  219 GLY A O   
1714 N N   . HIS A 223 ? 0.9805 0.7340 1.0933 -0.3164 0.0983  0.0739  220 HIS A N   
1715 C CA  . HIS A 223 ? 0.9164 0.6700 0.9969 -0.2649 0.1014  0.0960  220 HIS A CA  
1716 C C   . HIS A 223 ? 0.8846 0.7239 0.9718 -0.2475 0.0953  0.1146  220 HIS A C   
1717 O O   . HIS A 223 ? 0.8413 0.7077 0.9068 -0.2139 0.0835  0.1118  220 HIS A O   
1718 C CB  . HIS A 223 ? 1.0042 0.6848 1.0718 -0.2492 0.1267  0.1297  220 HIS A CB  
1719 C CG  . HIS A 223 ? 1.0211 0.7095 1.0587 -0.1984 0.1257  0.1527  220 HIS A CG  
1720 N ND1 . HIS A 223 ? 1.0230 0.7037 1.0399 -0.1678 0.1135  0.1341  220 HIS A ND1 
1721 C CD2 . HIS A 223 ? 0.9352 0.6444 0.9602 -0.1750 0.1343  0.1915  220 HIS A CD2 
1722 C CE1 . HIS A 223 ? 0.9940 0.6930 0.9939 -0.1299 0.1124  0.1599  220 HIS A CE1 
1723 N NE2 . HIS A 223 ? 0.8968 0.6122 0.8970 -0.1331 0.1233  0.1936  220 HIS A NE2 
1724 N N   . VAL A 224 ? 0.8621 0.7433 0.9811 -0.2698 0.1059  0.1328  221 VAL A N   
1725 C CA  . VAL A 224 ? 0.7926 0.7528 0.9193 -0.2525 0.1042  0.1462  221 VAL A CA  
1726 C C   . VAL A 224 ? 0.7737 0.7985 0.9242 -0.2619 0.0795  0.1184  221 VAL A C   
1727 O O   . VAL A 224 ? 0.7246 0.8059 0.9192 -0.2873 0.0791  0.1186  221 VAL A O   
1728 C CB  . VAL A 224 ? 0.8301 0.8133 0.9817 -0.2693 0.1304  0.1778  221 VAL A CB  
1729 C CG1 . VAL A 224 ? 0.8402 0.8980 0.9924 -0.2451 0.1334  0.1888  221 VAL A CG1 
1730 C CG2 . VAL A 224 ? 0.8871 0.8000 1.0104 -0.2608 0.1536  0.2092  221 VAL A CG2 
1731 N N   . ILE A 225 ? 0.7640 0.7846 0.8872 -0.2399 0.0596  0.0976  222 ILE A N   
1732 C CA  . ILE A 225 ? 0.7538 0.8165 0.8894 -0.2515 0.0343  0.0709  222 ILE A CA  
1733 C C   . ILE A 225 ? 0.7127 0.8597 0.8776 -0.2416 0.0272  0.0796  222 ILE A C   
1734 O O   . ILE A 225 ? 0.7024 0.9020 0.8981 -0.2601 0.0093  0.0676  222 ILE A O   
1735 C CB  . ILE A 225 ? 0.7796 0.8100 0.8733 -0.2297 0.0207  0.0507  222 ILE A CB  
1736 C CG1 . ILE A 225 ? 0.7181 0.7810 0.8135 -0.2467 -0.0048 0.0234  222 ILE A CG1 
1737 C CG2 . ILE A 225 ? 0.7162 0.7610 0.7888 -0.1884 0.0216  0.0637  222 ILE A CG2 
1738 C CD1 . ILE A 225 ? 0.7678 0.7888 0.8190 -0.2356 -0.0122 0.0004  222 ILE A CD1 
1739 N N   . THR A 226 ? 0.7144 0.8766 0.8707 -0.2118 0.0407  0.0994  223 THR A N   
1740 C CA  . THR A 226 ? 0.6357 0.8673 0.8170 -0.1956 0.0399  0.1067  223 THR A CA  
1741 C C   . THR A 226 ? 0.6172 0.9053 0.8537 -0.2200 0.0512  0.1178  223 THR A C   
1742 O O   . THR A 226 ? 0.6365 0.9866 0.9014 -0.2045 0.0536  0.1240  223 THR A O   
1743 C CB  . THR A 226 ? 0.6365 0.8585 0.7876 -0.1609 0.0546  0.1199  223 THR A CB  
1744 O OG1 . THR A 226 ? 0.7408 0.9295 0.8777 -0.1666 0.0771  0.1386  223 THR A OG1 
1745 C CG2 . THR A 226 ? 0.5349 0.7193 0.6449 -0.1372 0.0415  0.1087  223 THR A CG2 
1746 N N   . ILE A 227 ? 0.5956 0.8648 0.8529 -0.2569 0.0610  0.1210  224 ILE A N   
1747 C CA  . ILE A 227 ? 0.6611 0.9930 0.9813 -0.2851 0.0724  0.1316  224 ILE A CA  
1748 C C   . ILE A 227 ? 0.6764 1.0107 1.0324 -0.3340 0.0560  0.1135  224 ILE A C   
1749 O O   . ILE A 227 ? 0.5335 0.9118 0.9454 -0.3601 0.0642  0.1175  224 ILE A O   
1750 C CB  . ILE A 227 ? 0.6542 0.9726 0.9749 -0.2875 0.1111  0.1611  224 ILE A CB  
1751 C CG1 . ILE A 227 ? 0.6864 0.9247 0.9910 -0.3169 0.1227  0.1668  224 ILE A CG1 
1752 C CG2 . ILE A 227 ? 0.6333 0.9417 0.9057 -0.2416 0.1251  0.1740  224 ILE A CG2 
1753 C CD1 . ILE A 227 ? 0.6094 0.8297 0.9118 -0.3209 0.1611  0.1994  224 ILE A CD1 
1754 N N   . ASP A 228 ? 0.6717 0.9539 0.9921 -0.3410 0.0337  0.0880  225 ASP A N   
1755 C CA  . ASP A 228 ? 0.6761 0.9491 1.0191 -0.3895 0.0173  0.0633  225 ASP A CA  
1756 C C   . ASP A 228 ? 0.7060 1.0612 1.0771 -0.3950 -0.0192 0.0441  225 ASP A C   
1757 O O   . ASP A 228 ? 0.6642 1.0850 1.0473 -0.3640 -0.0273 0.0561  225 ASP A O   
1758 C CB  . ASP A 228 ? 0.7824 0.9546 1.0690 -0.3925 0.0152  0.0423  225 ASP A CB  
1759 C CG  . ASP A 228 ? 0.8639 0.9797 1.1692 -0.4422 0.0263  0.0316  225 ASP A CG  
1760 O OD1 . ASP A 228 ? 0.9120 1.0703 1.2693 -0.4688 0.0166  0.0206  225 ASP A OD1 
1761 O OD2 . ASP A 228 ? 0.8981 0.9190 1.1657 -0.4359 0.0446  0.0336  225 ASP A OD2 
1762 N N   . LYS A 229 ? 0.7461 1.0897 1.1219 -0.4267 -0.0415 0.0131  226 LYS A N   
1763 C CA  . LYS A 229 ? 0.7182 1.1398 1.1225 -0.4301 -0.0768 -0.0031 226 LYS A CA  
1764 C C   . LYS A 229 ? 0.7082 1.1546 1.0685 -0.4008 -0.1046 -0.0092 226 LYS A C   
1765 O O   . LYS A 229 ? 0.6726 1.1940 1.0566 -0.3882 -0.1301 -0.0083 226 LYS A O   
1766 C CB  . LYS A 229 ? 0.8212 1.2189 1.2359 -0.4727 -0.0940 -0.0363 226 LYS A CB  
1767 C CG  . LYS A 229 ? 0.8794 1.1673 1.2369 -0.4908 -0.0865 -0.0608 226 LYS A CG  
1768 C CD  . LYS A 229 ? 0.8889 1.1445 1.2747 -0.5353 -0.0914 -0.0868 226 LYS A CD  
1769 C CE  . LYS A 229 ? 0.8573 1.1787 1.2571 -0.5509 -0.1342 -0.1156 226 LYS A CE  
1770 N NZ  . LYS A 229 ? 1.1127 1.4449 1.5745 -0.5949 -0.1406 -0.1297 226 LYS A NZ  
1771 N N   . GLU A 230 ? 0.7590 1.1424 1.0570 -0.3855 -0.0987 -0.0126 227 GLU A N   
1772 C CA  . GLU A 230 ? 0.7528 1.1444 1.0027 -0.3518 -0.1199 -0.0179 227 GLU A CA  
1773 C C   . GLU A 230 ? 0.6894 1.0903 0.9325 -0.3003 -0.1044 0.0115  227 GLU A C   
1774 O O   . GLU A 230 ? 0.6786 1.0613 0.8754 -0.2703 -0.1117 0.0108  227 GLU A O   
1775 C CB  . GLU A 230 ? 0.7928 1.0972 0.9717 -0.3546 -0.1201 -0.0459 227 GLU A CB  
1776 C CG  . GLU A 230 ? 0.7814 1.0723 0.9515 -0.4038 -0.1408 -0.0853 227 GLU A CG  
1777 C CD  . GLU A 230 ? 0.9151 1.1200 1.0100 -0.3989 -0.1367 -0.1149 227 GLU A CD  
1778 O OE1 . GLU A 230 ? 0.9494 1.0692 1.0273 -0.3936 -0.1068 -0.1156 227 GLU A OE1 
1779 O OE2 . GLU A 230 ? 0.9575 1.1818 1.0091 -0.3975 -0.1622 -0.1357 227 GLU A OE2 
1780 N N   . LYS A 231 ? 0.6099 1.0394 0.8978 -0.2914 -0.0819 0.0359  228 LYS A N   
1781 C CA  . LYS A 231 ? 0.6745 1.0896 0.9456 -0.2469 -0.0611 0.0569  228 LYS A CA  
1782 C C   . LYS A 231 ? 0.5929 1.0563 0.8650 -0.2120 -0.0780 0.0657  228 LYS A C   
1783 O O   . LYS A 231 ? 0.5631 0.9901 0.7969 -0.1791 -0.0707 0.0709  228 LYS A O   
1784 C CB  . LYS A 231 ? 0.6281 1.0607 0.9386 -0.2472 -0.0305 0.0778  228 LYS A CB  
1785 C CG  . LYS A 231 ? 0.6015 1.1299 0.9839 -0.2509 -0.0316 0.0908  228 LYS A CG  
1786 C CD  . LYS A 231 ? 0.5190 1.0570 0.9340 -0.2588 0.0046  0.1095  228 LYS A CD  
1787 C CE  . LYS A 231 ? 0.5984 1.1740 1.0711 -0.2977 0.0038  0.1050  228 LYS A CE  
1788 N NZ  . LYS A 231 ? 0.6217 1.2833 1.1502 -0.2834 -0.0094 0.1065  228 LYS A NZ  
1789 N N   . GLU A 232 ? 0.5454 1.0893 0.8623 -0.2190 -0.1013 0.0686  229 GLU A N   
1790 C CA  . GLU A 232 ? 0.5379 1.1247 0.8566 -0.1831 -0.1181 0.0819  229 GLU A CA  
1791 C C   . GLU A 232 ? 0.6144 1.1546 0.8649 -0.1719 -0.1344 0.0723  229 GLU A C   
1792 O O   . GLU A 232 ? 0.5902 1.1179 0.8194 -0.1355 -0.1313 0.0861  229 GLU A O   
1793 C CB  . GLU A 232 ? 0.5351 1.2168 0.9131 -0.1924 -0.1438 0.0872  229 GLU A CB  
1794 C CG  . GLU A 232 ? 0.6447 1.3691 1.0901 -0.1951 -0.1221 0.0969  229 GLU A CG  
1795 C CD  . GLU A 232 ? 0.7372 1.4622 1.2072 -0.2436 -0.1242 0.0786  229 GLU A CD  
1796 O OE1 . GLU A 232 ? 0.8354 1.6063 1.3661 -0.2502 -0.1118 0.0851  229 GLU A OE1 
1797 O OE2 . GLU A 232 ? 0.7765 1.4518 1.2062 -0.2752 -0.1352 0.0568  229 GLU A OE2 
1798 N N   . GLN A 233 ? 0.5778 1.0909 0.7939 -0.2036 -0.1497 0.0478  230 GLN A N   
1799 C CA  . GLN A 233 ? 0.6572 1.1198 0.8032 -0.1932 -0.1567 0.0370  230 GLN A CA  
1800 C C   . GLN A 233 ? 0.6655 1.0550 0.7784 -0.1691 -0.1267 0.0418  230 GLN A C   
1801 O O   . GLN A 233 ? 0.6144 0.9834 0.6917 -0.1431 -0.1256 0.0493  230 GLN A O   
1802 C CB  . GLN A 233 ? 0.7272 1.1635 0.8394 -0.2319 -0.1711 0.0040  230 GLN A CB  
1803 C CG  . GLN A 233 ? 0.8788 1.2886 0.9191 -0.2229 -0.1841 -0.0084 230 GLN A CG  
1804 C CD  . GLN A 233 ? 0.9298 1.3975 0.9630 -0.1952 -0.2066 0.0151  230 GLN A CD  
1805 O OE1 . GLN A 233 ? 0.9614 1.3993 0.9489 -0.1677 -0.1990 0.0262  230 GLN A OE1 
1806 N NE2 . GLN A 233 ? 0.8484 1.4007 0.9279 -0.2033 -0.2350 0.0241  230 GLN A NE2 
1807 N N   . VAL A 234 ? 0.6350 0.9869 0.7598 -0.1787 -0.1028 0.0392  231 VAL A N   
1808 C CA  . VAL A 234 ? 0.6317 0.9229 0.7278 -0.1573 -0.0788 0.0434  231 VAL A CA  
1809 C C   . VAL A 234 ? 0.6236 0.9332 0.7325 -0.1229 -0.0703 0.0639  231 VAL A C   
1810 O O   . VAL A 234 ? 0.5646 0.8400 0.6442 -0.1017 -0.0631 0.0665  231 VAL A O   
1811 C CB  . VAL A 234 ? 0.6650 0.9172 0.7698 -0.1733 -0.0577 0.0411  231 VAL A CB  
1812 C CG1 . VAL A 234 ? 0.6052 0.8071 0.6829 -0.1492 -0.0383 0.0475  231 VAL A CG1 
1813 C CG2 . VAL A 234 ? 0.6623 0.8811 0.7540 -0.2071 -0.0630 0.0184  231 VAL A CG2 
1814 N N   . PHE A 235 ? 0.5776 0.9410 0.7336 -0.1176 -0.0692 0.0773  232 PHE A N   
1815 C CA  . PHE A 235 ? 0.5913 0.9675 0.7600 -0.0835 -0.0592 0.0930  232 PHE A CA  
1816 C C   . PHE A 235 ? 0.5947 0.9705 0.7421 -0.0627 -0.0740 0.0997  232 PHE A C   
1817 O O   . PHE A 235 ? 0.5297 0.8707 0.6578 -0.0403 -0.0630 0.1046  232 PHE A O   
1818 C CB  . PHE A 235 ? 0.4678 0.9091 0.6949 -0.0784 -0.0548 0.1053  232 PHE A CB  
1819 C CG  . PHE A 235 ? 0.5077 0.9541 0.7580 -0.0977 -0.0343 0.1045  232 PHE A CG  
1820 C CD1 . PHE A 235 ? 0.5400 0.9274 0.7558 -0.1111 -0.0201 0.0973  232 PHE A CD1 
1821 C CD2 . PHE A 235 ? 0.4458 0.9595 0.7554 -0.1008 -0.0276 0.1148  232 PHE A CD2 
1822 C CE1 . PHE A 235 ? 0.4637 0.8530 0.6971 -0.1278 0.0005  0.1028  232 PHE A CE1 
1823 C CE2 . PHE A 235 ? 0.4474 0.9668 0.7777 -0.1202 -0.0046 0.1180  232 PHE A CE2 
1824 C CZ  . PHE A 235 ? 0.4577 0.9111 0.7460 -0.1340 0.0096  0.1132  232 PHE A CZ  
1825 N N   . GLU A 236 ? 0.5710 0.9853 0.7200 -0.0720 -0.0994 0.1008  233 GLU A N   
1826 C CA  . GLU A 236 ? 0.6223 1.0406 0.7480 -0.0509 -0.1132 0.1139  233 GLU A CA  
1827 C C   . GLU A 236 ? 0.6010 0.9556 0.6697 -0.0492 -0.1048 0.1065  233 GLU A C   
1828 O O   . GLU A 236 ? 0.6134 0.9486 0.6665 -0.0260 -0.0995 0.1213  233 GLU A O   
1829 C CB  . GLU A 236 ? 0.6180 1.0962 0.7493 -0.0639 -0.1458 0.1156  233 GLU A CB  
1830 C CG  . GLU A 236 ? 0.6787 1.1669 0.7837 -0.0395 -0.1609 0.1360  233 GLU A CG  
1831 C CD  . GLU A 236 ? 0.8409 1.3721 0.9958 -0.0054 -0.1614 0.1649  233 GLU A CD  
1832 O OE1 . GLU A 236 ? 0.7788 1.3574 0.9934 -0.0071 -0.1587 0.1655  233 GLU A OE1 
1833 O OE2 . GLU A 236 ? 0.8931 1.4091 1.0290 0.0237  -0.1617 0.1882  233 GLU A OE2 
1834 N N   . ASP A 237 ? 0.5482 0.8692 0.5892 -0.0730 -0.1012 0.0847  234 ASP A N   
1835 C CA  . ASP A 237 ? 0.6442 0.9126 0.6387 -0.0693 -0.0902 0.0777  234 ASP A CA  
1836 C C   . ASP A 237 ? 0.6060 0.8386 0.6081 -0.0520 -0.0675 0.0834  234 ASP A C   
1837 O O   . ASP A 237 ? 0.6314 0.8357 0.6104 -0.0413 -0.0587 0.0873  234 ASP A O   
1838 C CB  . ASP A 237 ? 0.6771 0.9156 0.6455 -0.0943 -0.0885 0.0520  234 ASP A CB  
1839 C CG  . ASP A 237 ? 0.7010 0.9643 0.6459 -0.1142 -0.1116 0.0385  234 ASP A CG  
1840 O OD1 . ASP A 237 ? 0.7796 1.0786 0.7107 -0.1046 -0.1294 0.0515  234 ASP A OD1 
1841 O OD2 . ASP A 237 ? 0.7294 0.9742 0.6675 -0.1400 -0.1124 0.0144  234 ASP A OD2 
1842 N N   . ILE A 238 ? 0.5870 0.8233 0.6200 -0.0514 -0.0576 0.0832  235 ILE A N   
1843 C CA  . ILE A 238 ? 0.5808 0.7910 0.6190 -0.0361 -0.0403 0.0859  235 ILE A CA  
1844 C C   . ILE A 238 ? 0.5621 0.7768 0.6100 -0.0131 -0.0387 0.1005  235 ILE A C   
1845 O O   . ILE A 238 ? 0.5163 0.6987 0.5536 -0.0039 -0.0287 0.1010  235 ILE A O   
1846 C CB  . ILE A 238 ? 0.4895 0.7080 0.5504 -0.0406 -0.0303 0.0832  235 ILE A CB  
1847 C CG1 . ILE A 238 ? 0.5165 0.7126 0.5642 -0.0609 -0.0274 0.0726  235 ILE A CG1 
1848 C CG2 . ILE A 238 ? 0.4459 0.6474 0.5089 -0.0234 -0.0157 0.0839  235 ILE A CG2 
1849 C CD1 . ILE A 238 ? 0.4836 0.6844 0.5478 -0.0672 -0.0154 0.0756  235 ILE A CD1 
1850 N N   . TYR A 239 ? 0.5277 0.7826 0.6007 -0.0038 -0.0481 0.1131  236 TYR A N   
1851 C CA  . TYR A 239 ? 0.5482 0.8036 0.6329 0.0221  -0.0461 0.1309  236 TYR A CA  
1852 C C   . TYR A 239 ? 0.5494 0.7793 0.6012 0.0258  -0.0498 0.1417  236 TYR A C   
1853 O O   . TYR A 239 ? 0.5191 0.7141 0.5688 0.0395  -0.0372 0.1494  236 TYR A O   
1854 C CB  . TYR A 239 ? 0.5541 0.8677 0.6756 0.0333  -0.0589 0.1458  236 TYR A CB  
1855 C CG  . TYR A 239 ? 0.4549 0.7703 0.5924 0.0653  -0.0580 0.1693  236 TYR A CG  
1856 C CD1 . TYR A 239 ? 0.4531 0.7380 0.6082 0.0869  -0.0365 0.1690  236 TYR A CD1 
1857 C CD2 . TYR A 239 ? 0.5123 0.8571 0.6447 0.0749  -0.0785 0.1918  236 TYR A CD2 
1858 C CE1 . TYR A 239 ? 0.4972 0.7732 0.6691 0.1182  -0.0325 0.1908  236 TYR A CE1 
1859 C CE2 . TYR A 239 ? 0.5093 0.8515 0.6573 0.1084  -0.0768 0.2193  236 TYR A CE2 
1860 C CZ  . TYR A 239 ? 0.5369 0.8406 0.7070 0.1302  -0.0523 0.2188  236 TYR A CZ  
1861 O OH  . TYR A 239 ? 0.6289 0.9206 0.8167 0.1652  -0.0478 0.2465  236 TYR A OH  
1862 N N   . GLN A 240 ? 0.6121 0.8591 0.6368 0.0127  -0.0658 0.1420  237 GLN A N   
1863 C CA  . GLN A 240 ? 0.6414 0.8663 0.6253 0.0143  -0.0656 0.1519  237 GLN A CA  
1864 C C   . GLN A 240 ? 0.6062 0.7811 0.5791 0.0114  -0.0434 0.1436  237 GLN A C   
1865 O O   . GLN A 240 ? 0.6200 0.7696 0.5838 0.0210  -0.0328 0.1593  237 GLN A O   
1866 C CB  . GLN A 240 ? 0.7429 0.9858 0.6898 -0.0053 -0.0813 0.1400  237 GLN A CB  
1867 C CG  . GLN A 240 ? 0.8204 1.1178 0.7613 -0.0057 -0.1100 0.1504  237 GLN A CG  
1868 C CD  . GLN A 240 ? 0.9567 1.2805 0.9185 0.0231  -0.1186 0.1851  237 GLN A CD  
1869 O OE1 . GLN A 240 ? 1.0579 1.3574 0.9949 0.0398  -0.1111 0.2084  237 GLN A OE1 
1870 N NE2 . GLN A 240 ? 0.8223 1.1976 0.8317 0.0296  -0.1332 0.1910  237 GLN A NE2 
1871 N N   . PHE A 241 ? 0.5183 0.6809 0.4947 -0.0026 -0.0365 0.1210  238 PHE A N   
1872 C CA  . PHE A 241 ? 0.5981 0.7261 0.5720 -0.0058 -0.0196 0.1120  238 PHE A CA  
1873 C C   . PHE A 241 ? 0.6178 0.7268 0.6165 0.0057  -0.0092 0.1173  238 PHE A C   
1874 O O   . PHE A 241 ? 0.5860 0.6699 0.5833 0.0059  0.0022  0.1221  238 PHE A O   
1875 C CB  . PHE A 241 ? 0.5555 0.6800 0.5318 -0.0182 -0.0178 0.0913  238 PHE A CB  
1876 C CG  . PHE A 241 ? 0.5616 0.6633 0.5433 -0.0189 -0.0052 0.0833  238 PHE A CG  
1877 C CD1 . PHE A 241 ? 0.5928 0.6821 0.5611 -0.0213 0.0045  0.0830  238 PHE A CD1 
1878 C CD2 . PHE A 241 ? 0.5053 0.6043 0.5058 -0.0169 -0.0030 0.0762  238 PHE A CD2 
1879 C CE1 . PHE A 241 ? 0.5370 0.6170 0.5207 -0.0222 0.0140  0.0763  238 PHE A CE1 
1880 C CE2 . PHE A 241 ? 0.5167 0.6042 0.5238 -0.0180 0.0032  0.0687  238 PHE A CE2 
1881 C CZ  . PHE A 241 ? 0.5355 0.6164 0.5392 -0.0209 0.0106  0.0692  238 PHE A CZ  
1882 N N   . LEU A 242 ? 0.5355 0.6556 0.5578 0.0135  -0.0110 0.1143  239 LEU A N   
1883 C CA  . LEU A 242 ? 0.5519 0.6493 0.5931 0.0243  0.0000  0.1120  239 LEU A CA  
1884 C C   . LEU A 242 ? 0.6085 0.6837 0.6527 0.0374  0.0055  0.1322  239 LEU A C   
1885 O O   . LEU A 242 ? 0.6197 0.6586 0.6709 0.0368  0.0177  0.1287  239 LEU A O   
1886 C CB  . LEU A 242 ? 0.5572 0.6753 0.6190 0.0343  0.0005  0.1066  239 LEU A CB  
1887 C CG  . LEU A 242 ? 0.6454 0.7789 0.7034 0.0214  -0.0005 0.0909  239 LEU A CG  
1888 C CD1 . LEU A 242 ? 0.5084 0.6679 0.5867 0.0306  0.0048  0.0891  239 LEU A CD1 
1889 C CD2 . LEU A 242 ? 0.5602 0.6674 0.6054 0.0123  0.0049  0.0752  239 LEU A CD2 
1890 N N   . GLU A 243 ? 0.6285 0.7250 0.6684 0.0487  -0.0041 0.1547  240 GLU A N   
1891 C CA  . GLU A 243 ? 0.6495 0.7231 0.6910 0.0660  0.0014  0.1817  240 GLU A CA  
1892 C C   . GLU A 243 ? 0.7023 0.7461 0.7197 0.0545  0.0115  0.1915  240 GLU A C   
1893 O O   . GLU A 243 ? 0.7326 0.7431 0.7526 0.0646  0.0227  0.2142  240 GLU A O   
1894 C CB  . GLU A 243 ? 0.6165 0.7309 0.6576 0.0833  -0.0158 0.2072  240 GLU A CB  
1895 C CG  . GLU A 243 ? 0.5916 0.7369 0.6709 0.1023  -0.0204 0.2073  240 GLU A CG  
1896 C CD  . GLU A 243 ? 0.6369 0.7426 0.7422 0.1280  -0.0029 0.2171  240 GLU A CD  
1897 O OE1 . GLU A 243 ? 0.6950 0.7731 0.7942 0.1436  0.0007  0.2461  240 GLU A OE1 
1898 O OE2 . GLU A 243 ? 0.6280 0.7262 0.7565 0.1330  0.0090  0.1959  240 GLU A OE2 
1899 N N   . SER A 244 ? 0.6972 0.7510 0.6939 0.0347  0.0107  0.1768  241 SER A N   
1900 C CA  . SER A 244 ? 0.6826 0.7182 0.6589 0.0240  0.0238  0.1855  241 SER A CA  
1901 C C   . SER A 244 ? 0.7070 0.7144 0.7067 0.0101  0.0401  0.1700  241 SER A C   
1902 O O   . SER A 244 ? 0.7771 0.7729 0.7712 -0.0002 0.0548  0.1780  241 SER A O   
1903 C CB  . SER A 244 ? 0.6107 0.6728 0.5534 0.0129  0.0175  0.1760  241 SER A CB  
1904 O OG  . SER A 244 ? 0.6535 0.7199 0.6087 0.0007  0.0180  0.1470  241 SER A OG  
1905 N N   . LEU A 245 ? 0.6886 0.6906 0.7138 0.0085  0.0376  0.1477  242 LEU A N   
1906 C CA  . LEU A 245 ? 0.7186 0.7015 0.7664 -0.0065 0.0469  0.1295  242 LEU A CA  
1907 C C   . LEU A 245 ? 0.8388 0.7770 0.9051 -0.0055 0.0606  0.1400  242 LEU A C   
1908 O O   . LEU A 245 ? 0.8018 0.7217 0.8632 0.0112  0.0640  0.1645  242 LEU A O   
1909 C CB  . LEU A 245 ? 0.6378 0.6345 0.6948 -0.0082 0.0369  0.1015  242 LEU A CB  
1910 C CG  . LEU A 245 ? 0.6700 0.7010 0.7105 -0.0087 0.0258  0.0951  242 LEU A CG  
1911 C CD1 . LEU A 245 ? 0.5660 0.6088 0.6108 -0.0075 0.0181  0.0756  242 LEU A CD1 
1912 C CD2 . LEU A 245 ? 0.5716 0.6127 0.6063 -0.0199 0.0304  0.0938  242 LEU A CD2 
1913 N N   . ASP A 246 ? 0.9251 0.8445 1.0154 -0.0238 0.0679  0.1221  243 ASP A N   
1914 C CA  . ASP A 246 ? 0.9621 0.8304 1.0732 -0.0296 0.0833  0.1282  243 ASP A CA  
1915 C C   . ASP A 246 ? 0.9697 0.8128 1.0952 -0.0288 0.0799  0.0973  243 ASP A C   
1916 O O   . ASP A 246 ? 0.9902 0.8169 1.1355 -0.0501 0.0816  0.0715  243 ASP A O   
1917 C CB  . ASP A 246 ? 1.0199 0.8830 1.1498 -0.0561 0.0985  0.1350  243 ASP A CB  
1918 C CG  . ASP A 246 ? 1.1343 1.0145 1.2942 -0.0817 0.0927  0.1009  243 ASP A CG  
1919 O OD1 . ASP A 246 ? 1.1520 1.0354 1.3388 -0.1048 0.1051  0.1048  243 ASP A OD1 
1920 O OD2 . ASP A 246 ? 1.1034 1.0035 1.2600 -0.0788 0.0753  0.0726  243 ASP A OD2 
1921 N N   . TRP A 247 ? 0.9219 0.7651 1.0368 -0.0031 0.0753  0.0993  244 TRP A N   
1922 C CA  . TRP A 247 ? 0.9246 0.7368 1.0478 0.0049  0.0789  0.0736  244 TRP A CA  
1923 C C   . TRP A 247 ? 1.0190 0.7610 1.1620 -0.0006 0.0974  0.0754  244 TRP A C   
1924 O O   . TRP A 247 ? 1.0159 0.7303 1.1636 0.0065  0.1092  0.1109  244 TRP A O   
1925 C CB  . TRP A 247 ? 0.8935 0.7229 1.0096 0.0372  0.0762  0.0825  244 TRP A CB  
1926 C CG  . TRP A 247 ? 0.8028 0.6954 0.9032 0.0383  0.0601  0.0831  244 TRP A CG  
1927 C CD1 . TRP A 247 ? 0.7289 0.6569 0.8190 0.0442  0.0511  0.1097  244 TRP A CD1 
1928 C CD2 . TRP A 247 ? 0.7375 0.6608 0.8281 0.0314  0.0515  0.0558  244 TRP A CD2 
1929 N NE1 . TRP A 247 ? 0.7485 0.7220 0.8280 0.0394  0.0388  0.0983  244 TRP A NE1 
1930 C CE2 . TRP A 247 ? 0.7046 0.6755 0.7844 0.0327  0.0399  0.0689  244 TRP A CE2 
1931 C CE3 . TRP A 247 ? 0.7137 0.6275 0.7992 0.0235  0.0523  0.0220  244 TRP A CE3 
1932 C CZ2 . TRP A 247 ? 0.6704 0.6742 0.7392 0.0273  0.0321  0.0538  244 TRP A CZ2 
1933 C CZ3 . TRP A 247 ? 0.6791 0.6329 0.7476 0.0204  0.0426  0.0088  244 TRP A CZ3 
1934 C CH2 . TRP A 247 ? 0.6459 0.6413 0.7085 0.0229  0.0342  0.0271  244 TRP A CH2 
1935 N N   . SER A 248 ? 1.0600 0.7705 1.2117 -0.0143 0.1002  0.0366  245 SER A N   
1936 C CA  . SER A 248 ? 1.1128 0.7455 1.2843 -0.0210 0.1192  0.0313  245 SER A CA  
1937 C C   . SER A 248 ? 1.2137 0.8027 1.3862 0.0180  0.1341  0.0490  245 SER A C   
1938 O O   . SER A 248 ? 1.2200 0.7383 1.4095 0.0216  0.1536  0.0639  245 SER A O   
1939 C CB  . SER A 248 ? 1.1045 0.7184 1.2802 -0.0484 0.1149  -0.0222 245 SER A CB  
1940 O OG  . SER A 248 ? 1.2193 0.7858 1.3870 -0.0287 0.1254  -0.0488 245 SER A OG  
1941 N N   . GLU A 249 ? 1.4141 1.0454 1.5735 0.0481  0.1265  0.0512  246 GLU A N   
1942 C CA  . GLU A 249 ? 1.4501 1.0555 1.6185 0.0897  0.1395  0.0675  246 GLU A CA  
1943 C C   . GLU A 249 ? 1.3959 1.0781 1.5571 0.1152  0.1256  0.0839  246 GLU A C   
1944 O O   . GLU A 249 ? 1.3569 1.0965 1.5023 0.1006  0.1102  0.0670  246 GLU A O   
1945 C CB  . GLU A 249 ? 1.4947 1.0445 1.6665 0.0960  0.1555  0.0236  246 GLU A CB  
1946 C CG  . GLU A 249 ? 1.6206 1.0740 1.8136 0.1079  0.1807  0.0316  246 GLU A CG  
1947 C CD  . GLU A 249 ? 1.7968 1.2010 1.9904 0.1300  0.1997  -0.0090 246 GLU A CD  
1948 O OE1 . GLU A 249 ? 1.8912 1.2443 2.1047 0.1687  0.2206  0.0111  246 GLU A OE1 
1949 O OE2 . GLU A 249 ? 1.8016 1.2207 1.9733 0.1115  0.1942  -0.0600 246 GLU A OE2 
1950 O OXT . GLU A 249 ? 1.4237 1.1126 1.5981 0.1500  0.1291  0.1156  246 GLU A OXT 
# 
