data_11028 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11028 _Entry.Title ; Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-01-25 _Entry.Accession_date 2008-01-27 _Entry.Last_release_date 2009-03-31 _Entry.Original_release_date 2009-03-31 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.120 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solid-state _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Ansgar Siemer . . . 11028 2 Christian Wasmer . . . 11028 3 Adam Lange . . . 11028 4 Helene 'Van Melckebeke' . . . 11028 5 Matthias Ernst . . . 11028 6 Christiane Ritter . H. . 11028 7 Michel Steinmetz . O. . 11028 8 Roland Riek . . . 11028 9 Beat Meier . H. . 11028 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'amyloid fibril' . 11028 'asparagine ladders' . 11028 beta-helix . 11028 beta-solenoid . 11028 HET-s(218-289) . 11028 'hydrophobic core' . 11028 'parallel beta-sheets' . 11028 prion . 11028 'salt bridges' . 11028 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 11028 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 217 11028 '15N chemical shifts' 56 11028 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2009-03-31 2008-01-25 original author . 11028 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 11064 'A more extended version of 11028' 11028 PDB 2RNM 'Structure of the HET-s(218-289) amyloid fibrils.' 11028 PDB . 'A better resolved version of 2RNM' 11028 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 11028 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18339938 _Citation.Full_citation . _Citation.Title ; Amyloid fibrils of the HET-s(218-289) prion form a beta-solenoid with a triangular hydrophobic core. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Science _Citation.Journal_name_full . _Citation.Journal_volume 319 _Citation.Journal_issue 5869 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1523 _Citation.Page_last 1526 _Citation.Year 2008 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Christian Wasmer . . . 11028 1 2 Adam Lange . . . 11028 1 3 Helene 'Van Melckebeke' . . . 11028 1 4 Ansgar Siemer . . . 11028 1 5 Roland Riek . . . 11028 1 6 Beat Meier . H. . 11028 1 stop_ save_ save_reference_citation _Citation.Sf_category citations _Citation.Sf_framecode reference_citation _Citation.Entry_ID 11028 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16518695 _Citation.Full_citation . _Citation.Title ; 13C, 15N Resonance assignment of parts of the HET-s prion protein in its amyloid form. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 34 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 75 _Citation.Page_last 87 _Citation.Year 2006 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ansgar Siemer . . . 11028 2 2 Christiane Ritter . . . 11028 2 3 Michel Steinmetz . O. . 11028 2 4 Matthias Ernst . . . 11028 2 5 Roland Riek . . . 11028 2 6 Beat Meier . H. . 11028 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11028 _Assembly.ID 1 _Assembly.Name HET-s(218-289) _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 HET-s(218-289) 1 $entity_1 A . yes native no no . . . 11028 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'amyloid fibrils' 11028 1 'heterokaryon incompatibility' 11028 1 'prion protein' 11028 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 11028 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name HET-s(218-289) _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A,B,C,D,E _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MKIDAIVGRNSAKDIRTEER ARVQLGNVVTAAALHGGIRI SDQTTNSVETVVGKGESRVL IGNEYGGKGFWDNHHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq ; The sequence of the molecule is numbered from 217 to 296. The residues 218-289 correspond to HET-s(218-289). ; _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 79 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'HET-s(218-289): C-terminal prion forming domain of the HET-s protein.' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8667.732 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11064 . HET-s(218-289) . . . . . 100.00 79 100.00 100.00 4.32e-48 . . . . 11028 1 2 no PDB 2KJ3 . "High-Resolution Structure Of The Het-S(218-289) Prion In Its Amyloid Form Obtained By Solid-State Nmr" . . . . . 100.00 79 100.00 100.00 4.32e-48 . . . . 11028 1 3 no PDB 2LBU . "Haddock Calculated Model Of Congo Red Bound To The Het-S Amyloid" . . . . . 100.00 79 100.00 100.00 4.32e-48 . . . . 11028 1 4 no PDB 2RNM . "Structure Of The Het-s(218-289) Prion In Its Amyloid Form Obtained By Solid-state Nmr" . . . . . 100.00 79 100.00 100.00 4.32e-48 . . . . 11028 1 5 no GB AAB19707 . "s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]" . . . . . 91.14 289 100.00 100.00 6.31e-40 . . . . 11028 1 6 no GB AAB94631 . "small s protein [Podospora anserina]" . . . . . 91.14 289 100.00 100.00 3.91e-40 . . . . 11028 1 7 no PRF 1718317A . "vegetative incompatibility gene s" . . . . . 91.14 289 100.00 100.00 3.16e-40 . . . . 11028 1 8 no SP Q03689 . "RecName: Full=Heterokaryon incompatibility protein s; AltName: Full=Small s protein; AltName: Full=Vegetative incompatibility p" . . . . . 91.14 289 100.00 100.00 3.91e-40 . . . . 11028 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'heterokaryon incompatibility' 11028 1 'prion protein' 11028 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 217 MET . 11028 1 2 218 LYS . 11028 1 3 219 ILE . 11028 1 4 220 ASP . 11028 1 5 221 ALA . 11028 1 6 222 ILE . 11028 1 7 223 VAL . 11028 1 8 224 GLY . 11028 1 9 225 ARG . 11028 1 10 226 ASN . 11028 1 11 227 SER . 11028 1 12 228 ALA . 11028 1 13 229 LYS . 11028 1 14 230 ASP . 11028 1 15 231 ILE . 11028 1 16 232 ARG . 11028 1 17 233 THR . 11028 1 18 234 GLU . 11028 1 19 235 GLU . 11028 1 20 236 ARG . 11028 1 21 237 ALA . 11028 1 22 238 ARG . 11028 1 23 239 VAL . 11028 1 24 240 GLN . 11028 1 25 241 LEU . 11028 1 26 242 GLY . 11028 1 27 243 ASN . 11028 1 28 244 VAL . 11028 1 29 245 VAL . 11028 1 30 246 THR . 11028 1 31 247 ALA . 11028 1 32 248 ALA . 11028 1 33 249 ALA . 11028 1 34 250 LEU . 11028 1 35 251 HIS . 11028 1 36 252 GLY . 11028 1 37 253 GLY . 11028 1 38 254 ILE . 11028 1 39 255 ARG . 11028 1 40 256 ILE . 11028 1 41 257 SER . 11028 1 42 258 ASP . 11028 1 43 259 GLN . 11028 1 44 260 THR . 11028 1 45 261 THR . 11028 1 46 262 ASN . 11028 1 47 263 SER . 11028 1 48 264 VAL . 11028 1 49 265 GLU . 11028 1 50 266 THR . 11028 1 51 267 VAL . 11028 1 52 268 VAL . 11028 1 53 269 GLY . 11028 1 54 270 LYS . 11028 1 55 271 GLY . 11028 1 56 272 GLU . 11028 1 57 273 SER . 11028 1 58 274 ARG . 11028 1 59 275 VAL . 11028 1 60 276 LEU . 11028 1 61 277 ILE . 11028 1 62 278 GLY . 11028 1 63 279 ASN . 11028 1 64 280 GLU . 11028 1 65 281 TYR . 11028 1 66 282 GLY . 11028 1 67 283 GLY . 11028 1 68 284 LYS . 11028 1 69 285 GLY . 11028 1 70 286 PHE . 11028 1 71 287 TRP . 11028 1 72 288 ASP . 11028 1 73 289 ASN . 11028 1 74 290 HIS . 11028 1 75 291 HIS . 11028 1 76 292 HIS . 11028 1 77 293 HIS . 11028 1 78 294 HIS . 11028 1 79 295 HIS . 11028 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 11028 1 . LYS 2 2 11028 1 . ILE 3 3 11028 1 . ASP 4 4 11028 1 . ALA 5 5 11028 1 . ILE 6 6 11028 1 . VAL 7 7 11028 1 . GLY 8 8 11028 1 . ARG 9 9 11028 1 . ASN 10 10 11028 1 . SER 11 11 11028 1 . ALA 12 12 11028 1 . LYS 13 13 11028 1 . ASP 14 14 11028 1 . ILE 15 15 11028 1 . ARG 16 16 11028 1 . THR 17 17 11028 1 . GLU 18 18 11028 1 . GLU 19 19 11028 1 . ARG 20 20 11028 1 . ALA 21 21 11028 1 . ARG 22 22 11028 1 . VAL 23 23 11028 1 . GLN 24 24 11028 1 . LEU 25 25 11028 1 . GLY 26 26 11028 1 . ASN 27 27 11028 1 . VAL 28 28 11028 1 . VAL 29 29 11028 1 . THR 30 30 11028 1 . ALA 31 31 11028 1 . ALA 32 32 11028 1 . ALA 33 33 11028 1 . LEU 34 34 11028 1 . HIS 35 35 11028 1 . GLY 36 36 11028 1 . GLY 37 37 11028 1 . ILE 38 38 11028 1 . ARG 39 39 11028 1 . ILE 40 40 11028 1 . SER 41 41 11028 1 . ASP 42 42 11028 1 . GLN 43 43 11028 1 . THR 44 44 11028 1 . THR 45 45 11028 1 . ASN 46 46 11028 1 . SER 47 47 11028 1 . VAL 48 48 11028 1 . GLU 49 49 11028 1 . THR 50 50 11028 1 . VAL 51 51 11028 1 . VAL 52 52 11028 1 . GLY 53 53 11028 1 . LYS 54 54 11028 1 . GLY 55 55 11028 1 . GLU 56 56 11028 1 . SER 57 57 11028 1 . ARG 58 58 11028 1 . VAL 59 59 11028 1 . LEU 60 60 11028 1 . ILE 61 61 11028 1 . GLY 62 62 11028 1 . ASN 63 63 11028 1 . GLU 64 64 11028 1 . TYR 65 65 11028 1 . GLY 66 66 11028 1 . GLY 67 67 11028 1 . LYS 68 68 11028 1 . GLY 69 69 11028 1 . PHE 70 70 11028 1 . TRP 71 71 11028 1 . ASP 72 72 11028 1 . ASN 73 73 11028 1 . HIS 74 74 11028 1 . HIS 75 75 11028 1 . HIS 76 76 11028 1 . HIS 77 77 11028 1 . HIS 78 78 11028 1 . HIS 79 79 11028 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 11028 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity_1 . 5145 fungus . 'Podospora anserina' 'Podospora anserina' . . Eukaryota Fungi Podospora anserina . . . . . . . . . . . . . . . . . . . . . 11028 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 11028 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity_1 . 'recombinant technology' 'Escherichia coli' . . 469008 Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . . . . . . . . 11028 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11028 _Sample.ID 1 _Sample.Type 'fibrous protein' _Sample.Sub_type . _Sample.Details ; "Wet" fibrils sample: the total amount of water in the sample is at least 60% (weight). Below, the concentration is given with respect to the total protein concentration. ; _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 HET-s(218-289) '[U-100% 13C; U-100% 15N]' . . 1 $entity_1 . protein . 5 40 mg . . . . 11028 1 2 H2O 'natural abundance' . . . . . . . 7.5 . % . . . . 11028 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 11028 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0 . M 11028 1 pH 7.5 . pH 11028 1 pressure 1 . atm 11028 1 temperature 278 2 K 11028 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 11028 _Software.ID 1 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 11028 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11028 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 11028 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 11028 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 11028 2 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 11028 _Software.ID 3 _Software.Name CARA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Rochus Keller' . . 11028 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 11028 3 stop_ save_ save_xwinnmr _Software.Sf_category software _Software.Sf_framecode xwinnmr _Software.Entry_ID 11028 _Software.ID 4 _Software.Name xwinnmr _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 11028 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11028 4 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 11028 _Software.ID 5 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 11028 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11028 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 11028 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 11028 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 850 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 11028 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 600 . . . 11028 1 2 spectrometer_2 Bruker Avance . 850 . . . 11028 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 11028 _Experiment_list.ID 1 _Experiment_list.Details 'All experiments were recorded with a rotation at the magic angle.' loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 DREAM no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 30000 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 2 TOBSY no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 24242 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 3 PDSD no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 19000 54.7 . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 11028 1 4 NCA no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 40000 54.7 . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 11028 1 5 NCO no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 40000 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 6 N(CO)CA no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 40000 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 7 N(CO)CB no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 25000 54.7 . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 11028 1 8 N(CA)CO no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 40000 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 9 CA-CA no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 20000 54.7 . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11028 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 11028 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 adamantan 'methine carbon' . . . . ppm 31.47 external direct 1.0 . . . . . . . . . 11028 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.10132912 . . . . . . . . . 11028 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 11028 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 DREAM 1 $sample_1 solid 11028 1 2 TOBSY 1 $sample_1 solid 11028 1 3 PDSD 1 $sample_1 solid 11028 1 4 NCA 1 $sample_1 solid 11028 1 5 NCO 1 $sample_1 solid 11028 1 6 N(CO)CA 1 $sample_1 solid 11028 1 7 N(CO)CB 1 $sample_1 solid 11028 1 8 N(CA)CO 1 $sample_1 solid 11028 1 9 CA-CA 1 $sample_1 solid 11028 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 10 10 ASN C C 13 174.7 0.2 . 1 . . . . 226 ASN C . 11028 1 2 . 1 1 10 10 ASN CA C 13 52.1 0.2 . 1 . . . . 226 ASN CA . 11028 1 3 . 1 1 10 10 ASN CB C 13 39.9 0.2 . 1 . . . . 226 ASN CB . 11028 1 4 . 1 1 10 10 ASN CG C 13 177.4 0.2 . 1 . . . . 226 ASN CG . 11028 1 5 . 1 1 10 10 ASN N N 15 125.9 0.2 . 1 . . . . 226 ASN N . 11028 1 6 . 1 1 10 10 ASN ND2 N 15 115.4 0.2 . 1 . . . . 226 ASN ND2 . 11028 1 7 . 1 1 11 11 SER C C 13 171.9 0.2 . 1 . . . . 227 SER C . 11028 1 8 . 1 1 11 11 SER CA C 13 56.8 0.2 . 1 . . . . 227 SER CA . 11028 1 9 . 1 1 11 11 SER CB C 13 67.2 0.2 . 1 . . . . 227 SER CB . 11028 1 10 . 1 1 11 11 SER N N 15 119.3 0.2 . 1 . . . . 227 SER N . 11028 1 11 . 1 1 12 12 ALA C C 13 176.9 0.2 . 1 . . . . 228 ALA C . 11028 1 12 . 1 1 12 12 ALA CA C 13 49.5 0.2 . 1 . . . . 228 ALA CA . 11028 1 13 . 1 1 12 12 ALA CB C 13 23.9 0.2 . 1 . . . . 228 ALA CB . 11028 1 14 . 1 1 12 12 ALA N N 15 122.9 0.2 . 1 . . . . 228 ALA N . 11028 1 15 . 1 1 13 13 LYS C C 13 175.2 0.2 . 1 . . . . 229 LYS C . 11028 1 16 . 1 1 13 13 LYS CA C 13 59.9 0.2 . 1 . . . . 229 LYS CA . 11028 1 17 . 1 1 13 13 LYS CB C 13 32.7 0.2 . 1 . . . . 229 LYS CB . 11028 1 18 . 1 1 13 13 LYS CG C 13 25.5 0.2 . 1 . . . . 229 LYS CG . 11028 1 19 . 1 1 13 13 LYS CD C 13 29.7 0.2 . 1 . . . . 229 LYS CD . 11028 1 20 . 1 1 13 13 LYS CE C 13 42.2 0.2 . 1 . . . . 229 LYS CE . 11028 1 21 . 1 1 13 13 LYS N N 15 123.4 0.2 . 1 . . . . 229 LYS N . 11028 1 22 . 1 1 14 14 ASP C C 13 174.4 0.2 . 1 . . . . 230 ASP C . 11028 1 23 . 1 1 14 14 ASP CA C 13 53.2 0.2 . 1 . . . . 230 ASP CA . 11028 1 24 . 1 1 14 14 ASP CB C 13 45.1 0.2 . 1 . . . . 230 ASP CB . 11028 1 25 . 1 1 14 14 ASP CG C 13 179.7 0.2 . 1 . . . . 230 ASP CG . 11028 1 26 . 1 1 14 14 ASP N N 15 118 0.2 . 1 . . . . 230 ASP N . 11028 1 27 . 1 1 15 15 ILE C C 13 174.6 0.2 . 1 . . . . 231 ILE C . 11028 1 28 . 1 1 15 15 ILE CA C 13 60.9 0.2 . 1 . . . . 231 ILE CA . 11028 1 29 . 1 1 15 15 ILE CB C 13 41.8 0.2 . 1 . . . . 231 ILE CB . 11028 1 30 . 1 1 15 15 ILE CG1 C 13 27.6 0.2 . 1 . . . . 231 ILE CG1 . 11028 1 31 . 1 1 15 15 ILE CG2 C 13 17.7 0.2 . 1 . . . . 231 ILE CG2 . 11028 1 32 . 1 1 15 15 ILE CD1 C 13 14.2 0.2 . 1 . . . . 231 ILE CD1 . 11028 1 33 . 1 1 15 15 ILE N N 15 122.9 0.2 . 1 . . . . 231 ILE N . 11028 1 34 . 1 1 16 16 ARG C C 13 175.5 0.2 . 1 . . . . 232 ARG C . 11028 1 35 . 1 1 16 16 ARG CA C 13 54.3 0.2 . 1 . . . . 232 ARG CA . 11028 1 36 . 1 1 16 16 ARG CB C 13 33.1 0.2 . 1 . . . . 232 ARG CB . 11028 1 37 . 1 1 16 16 ARG N N 15 130.1 0.2 . 1 . . . . 232 ARG N . 11028 1 38 . 1 1 17 17 THR C C 13 174.5 0.2 . 1 . . . . 233 THR C . 11028 1 39 . 1 1 17 17 THR CA C 13 59.6 0.2 . 1 . . . . 233 THR CA . 11028 1 40 . 1 1 17 17 THR CB C 13 71.8 0.2 . 1 . . . . 233 THR CB . 11028 1 41 . 1 1 17 17 THR CG2 C 13 23.8 0.2 . 1 . . . . 233 THR CG2 . 11028 1 42 . 1 1 17 17 THR N N 15 113.6 0.2 . 1 . . . . 233 THR N . 11028 1 43 . 1 1 18 18 GLU C C 13 173.8 0.2 . 1 . . . . 234 GLU C . 11028 1 44 . 1 1 18 18 GLU CA C 13 53.8 0.2 . 1 . . . . 234 GLU CA . 11028 1 45 . 1 1 18 18 GLU CB C 13 33.9 0.2 . 1 . . . . 234 GLU CB . 11028 1 46 . 1 1 18 18 GLU CG C 13 35.9 0.2 . 1 . . . . 234 GLU CG . 11028 1 47 . 1 1 18 18 GLU CD C 13 182.9 0.2 . 1 . . . . 234 GLU CD . 11028 1 48 . 1 1 18 18 GLU N N 15 120.3 0.2 . 1 . . . . 234 GLU N . 11028 1 49 . 1 1 19 19 GLU C C 13 174.2 0.2 . 1 . . . . 235 GLU C . 11028 1 50 . 1 1 19 19 GLU CA C 13 58.7 0.2 . 1 . . . . 235 GLU CA . 11028 1 51 . 1 1 19 19 GLU CB C 13 27.5 0.2 . 1 . . . . 235 GLU CB . 11028 1 52 . 1 1 19 19 GLU CG C 13 38.5 0.2 . 1 . . . . 235 GLU CG . 11028 1 53 . 1 1 19 19 GLU CD C 13 184.8 0.2 . 1 . . . . 235 GLU CD . 11028 1 54 . 1 1 19 19 GLU N N 15 117.5 0.2 . 1 . . . . 235 GLU N . 11028 1 55 . 1 1 20 20 ARG C C 13 176.3 0.2 . 1 . . . . 236 ARG C . 11028 1 56 . 1 1 20 20 ARG CA C 13 54.8 0.2 . 1 . . . . 236 ARG CA . 11028 1 57 . 1 1 20 20 ARG CB C 13 30.7 0.2 . 1 . . . . 236 ARG CB . 11028 1 58 . 1 1 20 20 ARG CG C 13 28.4 0.2 . 1 . . . . 236 ARG CG . 11028 1 59 . 1 1 20 20 ARG CD C 13 43.9 0.2 . 1 . . . . 236 ARG CD . 11028 1 60 . 1 1 20 20 ARG N N 15 123 0.2 . 1 . . . . 236 ARG N . 11028 1 61 . 1 1 20 20 ARG NE N 15 85.2 0.2 . 1 . . . . 236 ARG NE . 11028 1 62 . 1 1 21 21 ALA C C 13 176.1 0.2 . 1 . . . . 237 ALA C . 11028 1 63 . 1 1 21 21 ALA CA C 13 53.2 0.2 . 1 . . . . 237 ALA CA . 11028 1 64 . 1 1 21 21 ALA CB C 13 19.9 0.2 . 1 . . . . 237 ALA CB . 11028 1 65 . 1 1 21 21 ALA N N 15 126 0.2 . 1 . . . . 237 ALA N . 11028 1 66 . 1 1 22 22 ARG C C 13 174.7 0.2 . 1 . . . . 238 ARG C . 11028 1 67 . 1 1 22 22 ARG CA C 13 54.7 0.2 . 1 . . . . 238 ARG CA . 11028 1 68 . 1 1 22 22 ARG CB C 13 35.4 0.2 . 1 . . . . 238 ARG CB . 11028 1 69 . 1 1 22 22 ARG CG C 13 26.1 0.2 . 1 . . . . 238 ARG CG . 11028 1 70 . 1 1 22 22 ARG CD C 13 41.2 0.2 . 1 . . . . 238 ARG CD . 11028 1 71 . 1 1 22 22 ARG N N 15 118.4 0.2 . 1 . . . . 238 ARG N . 11028 1 72 . 1 1 23 23 VAL C C 13 173.2 0.2 . 1 . . . . 239 VAL C . 11028 1 73 . 1 1 23 23 VAL CA C 13 60 0.2 . 1 . . . . 239 VAL CA . 11028 1 74 . 1 1 23 23 VAL CB C 13 37 0.2 . 1 . . . . 239 VAL CB . 11028 1 75 . 1 1 23 23 VAL CG1 C 13 20.9 0.2 . 2 . . . . 239 VAL CG1 . 11028 1 76 . 1 1 23 23 VAL CG2 C 13 22.4 0.2 . 2 . . . . 239 VAL CG2 . 11028 1 77 . 1 1 23 23 VAL N N 15 123 0.2 . 1 . . . . 239 VAL N . 11028 1 78 . 1 1 24 24 GLN C C 13 173.2 0.2 . 1 . . . . 240 GLN C . 11028 1 79 . 1 1 24 24 GLN CA C 13 52.8 0.2 . 1 . . . . 240 GLN CA . 11028 1 80 . 1 1 24 24 GLN CB C 13 33 0.2 . 1 . . . . 240 GLN CB . 11028 1 81 . 1 1 24 24 GLN CG C 13 31.6 0.2 . 1 . . . . 240 GLN CG . 11028 1 82 . 1 1 24 24 GLN CD C 13 175.7 0.2 . 1 . . . . 240 GLN CD . 11028 1 83 . 1 1 24 24 GLN N N 15 126.9 0.2 . 1 . . . . 240 GLN N . 11028 1 84 . 1 1 24 24 GLN NE2 N 15 104.6 0.2 . 1 . . . . 240 GLN NE2 . 11028 1 85 . 1 1 25 25 LEU C C 13 172.7 0.2 . 1 . . . . 241 LEU C . 11028 1 86 . 1 1 25 25 LEU CA C 13 52.8 0.2 . 1 . . . . 241 LEU CA . 11028 1 87 . 1 1 25 25 LEU CB C 13 44.8 0.2 . 1 . . . . 241 LEU CB . 11028 1 88 . 1 1 25 25 LEU CG C 13 27.7 0.2 . 1 . . . . 241 LEU CG . 11028 1 89 . 1 1 25 25 LEU CD1 C 13 27.1 0.2 . 2 . . . . 241 LEU CD1 . 11028 1 90 . 1 1 25 25 LEU CD2 C 13 28.1 0.2 . 2 . . . . 241 LEU CD2 . 11028 1 91 . 1 1 25 25 LEU N N 15 131.6 0.2 . 1 . . . . 241 LEU N . 11028 1 92 . 1 1 26 26 GLY C C 13 170.8 0.2 . 1 . . . . 242 GLY C . 11028 1 93 . 1 1 26 26 GLY CA C 13 43.8 0.2 . 1 . . . . 242 GLY CA . 11028 1 94 . 1 1 26 26 GLY N N 15 113.9 0.2 . 1 . . . . 242 GLY N . 11028 1 95 . 1 1 27 27 ASN C C 13 176.1 0.2 . 1 . . . . 243 ASN C . 11028 1 96 . 1 1 27 27 ASN CA C 13 51.3 0.2 . 1 . . . . 243 ASN CA . 11028 1 97 . 1 1 27 27 ASN CB C 13 40.1 0.2 . 1 . . . . 243 ASN CB . 11028 1 98 . 1 1 27 27 ASN CG C 13 176.1 0.2 . 1 . . . . 243 ASN CG . 11028 1 99 . 1 1 27 27 ASN N N 15 110.2 0.2 . 1 . . . . 243 ASN N . 11028 1 100 . 1 1 28 28 VAL C C 13 174.5 0.2 . 1 . . . . 244 VAL C . 11028 1 101 . 1 1 28 28 VAL CA C 13 62.1 0.2 . 1 . . . . 244 VAL CA . 11028 1 102 . 1 1 28 28 VAL CB C 13 34.4 0.2 . 1 . . . . 244 VAL CB . 11028 1 103 . 1 1 28 28 VAL CG1 C 13 22.1 0.2 . 2 . . . . 244 VAL CG1 . 11028 1 104 . 1 1 28 28 VAL CG2 C 13 24.7 0.2 . 2 . . . . 244 VAL CG2 . 11028 1 105 . 1 1 28 28 VAL N N 15 123.1 0.2 . 1 . . . . 244 VAL N . 11028 1 106 . 1 1 29 29 VAL C C 13 175.2 0.2 . 1 . . . . 245 VAL C . 11028 1 107 . 1 1 29 29 VAL CA C 13 61.1 0.2 . 1 . . . . 245 VAL CA . 11028 1 108 . 1 1 29 29 VAL CB C 13 32.2 0.2 . 1 . . . . 245 VAL CB . 11028 1 109 . 1 1 29 29 VAL CG1 C 13 22.5 0.2 . 2 . . . . 245 VAL CG1 . 11028 1 110 . 1 1 29 29 VAL CG2 C 13 20.3 0.2 . 2 . . . . 245 VAL CG2 . 11028 1 111 . 1 1 29 29 VAL N N 15 129.2 0.2 . 1 . . . . 245 VAL N . 11028 1 112 . 1 1 30 30 THR C C 13 175.3 0.2 . 1 . . . . 246 THR C . 11028 1 113 . 1 1 30 30 THR CA C 13 62.4 0.2 . 1 . . . . 246 THR CA . 11028 1 114 . 1 1 30 30 THR CB C 13 70.9 0.2 . 1 . . . . 246 THR CB . 11028 1 115 . 1 1 30 30 THR CG2 C 13 20.8 0.2 . 1 . . . . 246 THR CG2 . 11028 1 116 . 1 1 30 30 THR N N 15 116.7 0.2 . 1 . . . . 246 THR N . 11028 1 117 . 1 1 31 31 ALA C C 13 179.2 0.2 . 1 . . . . 247 ALA C . 11028 1 118 . 1 1 31 31 ALA CA C 13 56.2 0.2 . 1 . . . . 247 ALA CA . 11028 1 119 . 1 1 31 31 ALA CB C 13 17.1 0.2 . 1 . . . . 247 ALA CB . 11028 1 120 . 1 1 31 31 ALA N N 15 121.4 0.2 . 1 . . . . 247 ALA N . 11028 1 121 . 1 1 32 32 ALA C C 13 179.3 0.2 . 1 . . . . 248 ALA C . 11028 1 122 . 1 1 32 32 ALA CA C 13 55.1 0.2 . 1 . . . . 248 ALA CA . 11028 1 123 . 1 1 32 32 ALA CB C 13 18.4 0.2 . 1 . . . . 248 ALA CB . 11028 1 124 . 1 1 32 32 ALA N N 15 119.5 0.2 . 1 . . . . 248 ALA N . 11028 1 125 . 1 1 44 44 THR C C 13 175.2 0.2 . 1 . . . . 260 THR C . 11028 1 126 . 1 1 44 44 THR CA C 13 66.2 0.2 . 1 . . . . 260 THR CA . 11028 1 127 . 1 1 44 44 THR CB C 13 69.9 0.2 . 1 . . . . 260 THR CB . 11028 1 128 . 1 1 44 44 THR CG2 C 13 22.1 0.2 . 1 . . . . 260 THR CG2 . 11028 1 129 . 1 1 44 44 THR N N 15 122.8 0.2 . 1 . . . . 260 THR N . 11028 1 130 . 1 1 45 45 THR C C 13 172.4 0.2 . 1 . . . . 261 THR C . 11028 1 131 . 1 1 45 45 THR CA C 13 61.2 0.2 . 1 . . . . 261 THR CA . 11028 1 132 . 1 1 45 45 THR CB C 13 70.8 0.2 . 1 . . . . 261 THR CB . 11028 1 133 . 1 1 45 45 THR CG2 C 13 21.2 0.2 . 1 . . . . 261 THR CG2 . 11028 1 134 . 1 1 45 45 THR N N 15 124.1 0.2 . 1 . . . . 261 THR N . 11028 1 135 . 1 1 46 46 ASN C C 13 174.7 0.2 . 1 . . . . 262 ASN C . 11028 1 136 . 1 1 46 46 ASN CA C 13 52.4 0.2 . 1 . . . . 262 ASN CA . 11028 1 137 . 1 1 46 46 ASN CB C 13 41 0.2 . 1 . . . . 262 ASN CB . 11028 1 138 . 1 1 46 46 ASN CG C 13 176.5 0.2 . 1 . . . . 262 ASN CG . 11028 1 139 . 1 1 46 46 ASN N N 15 128.1 0.2 . 1 . . . . 262 ASN N . 11028 1 140 . 1 1 46 46 ASN ND2 N 15 113.5 0.2 . 1 . . . . 262 ASN ND2 . 11028 1 141 . 1 1 47 47 SER C C 13 171.6 0.2 . 1 . . . . 263 SER C . 11028 1 142 . 1 1 47 47 SER CA C 13 56.5 0.2 . 1 . . . . 263 SER CA . 11028 1 143 . 1 1 47 47 SER CB C 13 66.1 0.2 . 1 . . . . 263 SER CB . 11028 1 144 . 1 1 47 47 SER N N 15 117.7 0.2 . 1 . . . . 263 SER N . 11028 1 145 . 1 1 48 48 VAL C C 13 174.5 0.2 . 1 . . . . 264 VAL C . 11028 1 146 . 1 1 48 48 VAL CA C 13 57.1 0.2 . 1 . . . . 264 VAL CA . 11028 1 147 . 1 1 48 48 VAL CB C 13 35.6 0.2 . 1 . . . . 264 VAL CB . 11028 1 148 . 1 1 48 48 VAL CG1 C 13 20.7 0.2 . 2 . . . . 264 VAL CG1 . 11028 1 149 . 1 1 48 48 VAL CG2 C 13 23.1 0.2 . 2 . . . . 264 VAL CG2 . 11028 1 150 . 1 1 48 48 VAL N N 15 125.5 0.2 . 1 . . . . 264 VAL N . 11028 1 151 . 1 1 49 49 GLU C C 13 175.9 0.2 . 1 . . . . 265 GLU C . 11028 1 152 . 1 1 49 49 GLU CA C 13 59.5 0.2 . 1 . . . . 265 GLU CA . 11028 1 153 . 1 1 49 49 GLU CB C 13 29.5 0.2 . 1 . . . . 265 GLU CB . 11028 1 154 . 1 1 49 49 GLU CG C 13 37.2 0.2 . 1 . . . . 265 GLU CG . 11028 1 155 . 1 1 49 49 GLU CD C 13 183.6 0.2 . 1 . . . . 265 GLU CD . 11028 1 156 . 1 1 49 49 GLU N N 15 127.4 0.2 . 1 . . . . 265 GLU N . 11028 1 157 . 1 1 50 50 THR C C 13 172.9 0.2 . 1 . . . . 266 THR C . 11028 1 158 . 1 1 50 50 THR CA C 13 60.9 0.2 . 1 . . . . 266 THR CA . 11028 1 159 . 1 1 50 50 THR CB C 13 71.6 0.2 . 1 . . . . 266 THR CB . 11028 1 160 . 1 1 50 50 THR CG2 C 13 22.3 0.2 . 1 . . . . 266 THR CG2 . 11028 1 161 . 1 1 50 50 THR N N 15 113.1 0.2 . 1 . . . . 266 THR N . 11028 1 162 . 1 1 51 51 VAL C C 13 175.3 0.2 . 1 . . . . 267 VAL C . 11028 1 163 . 1 1 51 51 VAL CA C 13 60.7 0.2 . 1 . . . . 267 VAL CA . 11028 1 164 . 1 1 51 51 VAL CB C 13 35.6 0.2 . 1 . . . . 267 VAL CB . 11028 1 165 . 1 1 51 51 VAL CG1 C 13 21.4 0.2 . 2 . . . . 267 VAL CG1 . 11028 1 166 . 1 1 51 51 VAL CG2 C 13 22.8 0.2 . 2 . . . . 267 VAL CG2 . 11028 1 167 . 1 1 51 51 VAL N N 15 124.3 0.2 . 1 . . . . 267 VAL N . 11028 1 168 . 1 1 52 52 VAL C C 13 175.1 0.2 . 1 . . . . 268 VAL C . 11028 1 169 . 1 1 52 52 VAL CA C 13 61.2 0.2 . 1 . . . . 268 VAL CA . 11028 1 170 . 1 1 52 52 VAL CB C 13 34.2 0.2 . 1 . . . . 268 VAL CB . 11028 1 171 . 1 1 52 52 VAL CG1 C 13 20.9 0.2 . 2 . . . . 268 VAL CG1 . 11028 1 172 . 1 1 52 52 VAL CG2 C 13 20.9 0.2 . 2 . . . . 268 VAL CG2 . 11028 1 173 . 1 1 52 52 VAL N N 15 128.7 0.2 . 1 . . . . 268 VAL N . 11028 1 174 . 1 1 53 53 GLY C C 13 172.1 0.2 . 1 . . . . 269 GLY C . 11028 1 175 . 1 1 53 53 GLY CA C 13 44.6 0.2 . 1 . . . . 269 GLY CA . 11028 1 176 . 1 1 53 53 GLY N N 15 113.6 0.2 . 1 . . . . 269 GLY N . 11028 1 177 . 1 1 54 54 LYS C C 13 176.7 0.2 . 1 . . . . 270 LYS C . 11028 1 178 . 1 1 54 54 LYS CA C 13 54.3 0.2 . 1 . . . . 270 LYS CA . 11028 1 179 . 1 1 54 54 LYS CB C 13 35.3 0.2 . 1 . . . . 270 LYS CB . 11028 1 180 . 1 1 54 54 LYS CG C 13 24.3 0.2 . 1 . . . . 270 LYS CG . 11028 1 181 . 1 1 54 54 LYS CD C 13 29.7 0.2 . 1 . . . . 270 LYS CD . 11028 1 182 . 1 1 54 54 LYS CE C 13 41.7 0.2 . 1 . . . . 270 LYS CE . 11028 1 183 . 1 1 54 54 LYS N N 15 121.8 0.2 . 1 . . . . 270 LYS N . 11028 1 184 . 1 1 54 54 LYS NZ N 15 33.9 0.2 . 1 . . . . 270 LYS NZ . 11028 1 185 . 1 1 55 55 GLY C C 13 172.1 0.2 . 1 . . . . 271 GLY C . 11028 1 186 . 1 1 55 55 GLY CA C 13 48.5 0.2 . 1 . . . . 271 GLY CA . 11028 1 187 . 1 1 55 55 GLY N N 15 115.8 0.2 . 1 . . . . 271 GLY N . 11028 1 188 . 1 1 56 56 GLU C C 13 176.4 0.2 . 1 . . . . 272 GLU C . 11028 1 189 . 1 1 56 56 GLU CA C 13 54.2 0.2 . 1 . . . . 272 GLU CA . 11028 1 190 . 1 1 56 56 GLU CB C 13 30 0.2 . 1 . . . . 272 GLU CB . 11028 1 191 . 1 1 56 56 GLU CG C 13 37.3 0.2 . 1 . . . . 272 GLU CG . 11028 1 192 . 1 1 56 56 GLU CD C 13 184.9 0.2 . 1 . . . . 272 GLU CD . 11028 1 193 . 1 1 56 56 GLU N N 15 128.8 0.2 . 1 . . . . 272 GLU N . 11028 1 194 . 1 1 57 57 SER C C 13 173.5 0.2 . 1 . . . . 273 SER C . 11028 1 195 . 1 1 57 57 SER CA C 13 59.3 0.2 . 1 . . . . 273 SER CA . 11028 1 196 . 1 1 57 57 SER CB C 13 66.8 0.2 . 1 . . . . 273 SER CB . 11028 1 197 . 1 1 57 57 SER N N 15 116.6 0.2 . 1 . . . . 273 SER N . 11028 1 198 . 1 1 58 58 ARG C C 13 175.6 0.2 . 1 . . . . 274 ARG C . 11028 1 199 . 1 1 58 58 ARG CA C 13 54.9 0.2 . 1 . . . . 274 ARG CA . 11028 1 200 . 1 1 58 58 ARG CB C 13 32.9 0.2 . 1 . . . . 274 ARG CB . 11028 1 201 . 1 1 58 58 ARG CG C 13 27.9 0.2 . 1 . . . . 274 ARG CG . 11028 1 202 . 1 1 58 58 ARG CD C 13 43.8 0.2 . 1 . . . . 274 ARG CD . 11028 1 203 . 1 1 58 58 ARG N N 15 118.1 0.2 . 1 . . . . 274 ARG N . 11028 1 204 . 1 1 58 58 ARG NE N 15 86.8 0.2 . 1 . . . . 274 ARG NE . 11028 1 205 . 1 1 59 59 VAL C C 13 172.9 0.2 . 1 . . . . 275 VAL C . 11028 1 206 . 1 1 59 59 VAL CA C 13 60.3 0.2 . 1 . . . . 275 VAL CA . 11028 1 207 . 1 1 59 59 VAL CB C 13 36.1 0.2 . 1 . . . . 275 VAL CB . 11028 1 208 . 1 1 59 59 VAL CG1 C 13 21.8 0.2 . 2 . . . . 275 VAL CG1 . 11028 1 209 . 1 1 59 59 VAL CG2 C 13 22.8 0.2 . 2 . . . . 275 VAL CG2 . 11028 1 210 . 1 1 59 59 VAL N N 15 123 0.2 . 1 . . . . 275 VAL N . 11028 1 211 . 1 1 60 60 LEU C C 13 173.8 0.2 . 1 . . . . 276 LEU C . 11028 1 212 . 1 1 60 60 LEU CA C 13 52.7 0.2 . 1 . . . . 276 LEU CA . 11028 1 213 . 1 1 60 60 LEU CB C 13 43.6 0.2 . 1 . . . . 276 LEU CB . 11028 1 214 . 1 1 60 60 LEU CG C 13 26.9 0.2 . 1 . . . . 276 LEU CG . 11028 1 215 . 1 1 60 60 LEU CD1 C 13 24.2 0.2 . 2 . . . . 276 LEU CD1 . 11028 1 216 . 1 1 60 60 LEU CD2 C 13 26.3 0.2 . 2 . . . . 276 LEU CD2 . 11028 1 217 . 1 1 60 60 LEU N N 15 130.6 0.2 . 1 . . . . 276 LEU N . 11028 1 218 . 1 1 61 61 ILE C C 13 173.3 0.2 . 1 . . . . 277 ILE C . 11028 1 219 . 1 1 61 61 ILE CA C 13 58.7 0.2 . 1 . . . . 277 ILE CA . 11028 1 220 . 1 1 61 61 ILE CB C 13 35.7 0.2 . 1 . . . . 277 ILE CB . 11028 1 221 . 1 1 61 61 ILE CG1 C 13 26.3 0.2 . 1 . . . . 277 ILE CG1 . 11028 1 222 . 1 1 61 61 ILE CG2 C 13 18.8 0.2 . 1 . . . . 277 ILE CG2 . 11028 1 223 . 1 1 61 61 ILE CD1 C 13 14.6 0.2 . 1 . . . . 277 ILE CD1 . 11028 1 224 . 1 1 61 61 ILE N N 15 130.4 0.2 . 1 . . . . 277 ILE N . 11028 1 225 . 1 1 62 62 GLY C C 13 172.1 0.2 . 1 . . . . 278 GLY C . 11028 1 226 . 1 1 62 62 GLY CA C 13 44 0.2 . 1 . . . . 278 GLY CA . 11028 1 227 . 1 1 62 62 GLY N N 15 111.6 0.2 . 1 . . . . 278 GLY N . 11028 1 228 . 1 1 63 63 ASN C C 13 173 0.2 . 1 . . . . 279 ASN C . 11028 1 229 . 1 1 63 63 ASN CA C 13 51.9 0.2 . 1 . . . . 279 ASN CA . 11028 1 230 . 1 1 63 63 ASN CB C 13 40.5 0.2 . 1 . . . . 279 ASN CB . 11028 1 231 . 1 1 63 63 ASN CG C 13 176.3 0.2 . 1 . . . . 279 ASN CG . 11028 1 232 . 1 1 63 63 ASN N N 15 114.8 0.2 . 1 . . . . 279 ASN N . 11028 1 233 . 1 1 63 63 ASN ND2 N 15 115.4 0.2 . 1 . . . . 279 ASN ND2 . 11028 1 234 . 1 1 64 64 GLU C C 13 174.9 0.2 . 1 . . . . 280 GLU C . 11028 1 235 . 1 1 64 64 GLU CA C 13 54.6 0.2 . 1 . . . . 280 GLU CA . 11028 1 236 . 1 1 64 64 GLU CB C 13 33.4 0.2 . 1 . . . . 280 GLU CB . 11028 1 237 . 1 1 64 64 GLU CG C 13 37.8 0.2 . 1 . . . . 280 GLU CG . 11028 1 238 . 1 1 64 64 GLU CD C 13 181.8 0.2 . 1 . . . . 280 GLU CD . 11028 1 239 . 1 1 64 64 GLU N N 15 120.6 0.2 . 1 . . . . 280 GLU N . 11028 1 240 . 1 1 65 65 TYR C C 13 176.4 0.2 . 1 . . . . 281 TYR C . 11028 1 241 . 1 1 65 65 TYR CA C 13 56.1 0.2 . 1 . . . . 281 TYR CA . 11028 1 242 . 1 1 65 65 TYR CB C 13 40.4 0.2 . 1 . . . . 281 TYR CB . 11028 1 243 . 1 1 65 65 TYR CG C 13 127.6 0.2 . 1 . . . . 281 TYR CG . 11028 1 244 . 1 1 65 65 TYR CD1 C 13 132.8 0.2 . 3 . . . . 281 TYR CD1 . 11028 1 245 . 1 1 65 65 TYR CD2 C 13 132.8 0.2 . 3 . . . . 281 TYR CD2 . 11028 1 246 . 1 1 65 65 TYR CE1 C 13 117.6 0.2 . 3 . . . . 281 TYR CE1 . 11028 1 247 . 1 1 65 65 TYR CE2 C 13 117.6 0.2 . 3 . . . . 281 TYR CE2 . 11028 1 248 . 1 1 65 65 TYR N N 15 129.1 0.2 . 1 . . . . 281 TYR N . 11028 1 249 . 1 1 66 66 GLY C C 13 174.3 0.2 . 1 . . . . 282 GLY C . 11028 1 250 . 1 1 66 66 GLY CA C 13 46.1 0.2 . 1 . . . . 282 GLY CA . 11028 1 251 . 1 1 66 66 GLY N N 15 110.3 0.2 . 1 . . . . 282 GLY N . 11028 1 252 . 1 1 70 70 PHE C C 13 175.1 0.2 . 1 . . . . 286 PHE C . 11028 1 253 . 1 1 70 70 PHE CA C 13 59.7 0.2 . 1 . . . . 286 PHE CA . 11028 1 254 . 1 1 70 70 PHE CB C 13 41.3 0.2 . 1 . . . . 286 PHE CB . 11028 1 255 . 1 1 70 70 PHE CG C 13 136.5 0.2 . 1 . . . . 286 PHE CG . 11028 1 256 . 1 1 70 70 PHE CD1 C 13 130.9 0.2 . 3 . . . . 286 PHE CD1 . 11028 1 257 . 1 1 70 70 PHE CD2 C 13 130.9 0.2 . 3 . . . . 286 PHE CD2 . 11028 1 258 . 1 1 70 70 PHE CE1 C 13 129.3 0.2 . 3 . . . . 286 PHE CE1 . 11028 1 259 . 1 1 70 70 PHE CE2 C 13 129.3 0.2 . 3 . . . . 286 PHE CE2 . 11028 1 260 . 1 1 70 70 PHE CZ C 13 132.1 0.2 . 1 . . . . 286 PHE CZ . 11028 1 261 . 1 1 70 70 PHE N N 15 127.6 0.2 . 1 . . . . 286 PHE N . 11028 1 262 . 1 1 71 71 TRP C C 13 175.5 0.2 . 1 . . . . 287 TRP C . 11028 1 263 . 1 1 71 71 TRP CA C 13 57.4 0.2 . 1 . . . . 287 TRP CA . 11028 1 264 . 1 1 71 71 TRP CB C 13 29.5 0.2 . 1 . . . . 287 TRP CB . 11028 1 265 . 1 1 71 71 TRP CG C 13 112.1 0.2 . 1 . . . . 287 TRP CG . 11028 1 266 . 1 1 71 71 TRP CD1 C 13 128.4 0.2 . 1 . . . . 287 TRP CD1 . 11028 1 267 . 1 1 71 71 TRP CD2 C 13 129.3 0.2 . 1 . . . . 287 TRP CD2 . 11028 1 268 . 1 1 71 71 TRP CE3 C 13 121 0.2 . 1 . . . . 287 TRP CE3 . 11028 1 269 . 1 1 71 71 TRP CZ2 C 13 117.7 0.2 . 1 . . . . 287 TRP CZ2 . 11028 1 270 . 1 1 71 71 TRP CZ3 C 13 119.8 0.2 . 1 . . . . 287 TRP CZ3 . 11028 1 271 . 1 1 71 71 TRP CH2 C 13 124.1 0.2 . 1 . . . . 287 TRP CH2 . 11028 1 272 . 1 1 71 71 TRP N N 15 118.2 0.2 . 1 . . . . 287 TRP N . 11028 1 273 . 1 1 71 71 TRP NE1 N 15 133.4 0.2 . 1 . . . . 287 TRP NE1 . 11028 1 stop_ save_