data_15053 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15053 _Entry.Title ; HPRP-173-195 SOLUTION STRUCTURE ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-11-27 _Entry.Accession_date 2006-11-27 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Gabriella Saviano G. . . 15053 2 Teodorico Tancredi T. . . 15053 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'HUMAN PRION PROTEIN' 'HUMAN PRION PROTEIN' 15053 NMR NMR 15053 PEPTIDE PEPTIDE 15053 'SOLUTION STRUCTURE' 'SOLUTION STRUCTURE' 15053 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15053 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 133 15053 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 2 . . 2008-10-07 2006-11-27 update BMRB 'Complete Entry Citation' 15053 1 . . 2007-02-01 2006-11-27 original author 'Original Release' 15053 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 15052 'prion protein fragment 173-195' 15053 BMRB 15054 'prion protein fragment 180-195' 15053 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 15053 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18563793 _Citation.Full_citation . _Citation.Title 'Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein alpha2-helical 180-195 segment, and comparison with full-length alpha2-helix-derived peptides' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Pept. Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 14 _Citation.Journal_issue 10 _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 1096 _Citation.Page_last 1102 _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 Luisa Ronga L. . . 15053 1 2 Pasquale Palladino P. . . 15053 1 3 Gabriella Saviano G. . . 15053 1 4 Teodorico Tancredi T. . . 15053 1 5 Ettore Benedetti E. . . 15053 1 6 Raffaele Ragone R. . . 15053 1 7 Filomena Rossi F. . . 15053 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15053 _Assembly.ID 1 _Assembly.Name 'prion protein fragment' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _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 'prion protein fragment, alpha-2 helix' 1 $HPRP173195 A . yes native no no . . . 15053 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HPRP173195 _Entity.Sf_category entity _Entity.Sf_framecode HPRP173195 _Entity.Entry_ID 15053 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name HPRP173195 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; NNFVHDCVNITIKQHTVTTT TKG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _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 23 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method syn _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _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 15824 . Prion_Protein . . . . . 100.00 113 100.00 100.00 3.55e-06 . . . . 15053 1 2 no BMRB 15845 . Prion_Protein . . . . . 100.00 114 100.00 100.00 1.44e-05 . . . . 15053 1 3 no BMRB 16071 . mPrP90 . . . . . 100.00 144 100.00 100.00 8.00e-06 . . . . 15053 1 4 no BMRB 16075 . mPrP90_M129V . . . . . 100.00 141 100.00 100.00 1.35e-05 . . . . 15053 1 5 no BMRB 16076 . mPrP90_P102L . . . . . 100.00 141 100.00 100.00 1.28e-05 . . . . 15053 1 6 no BMRB 16077 . mPrP90_P105L . . . . . 100.00 141 100.00 100.00 1.28e-05 . . . . 15053 1 7 no BMRB 16078 . mPrP90_A117V . . . . . 100.00 142 100.00 100.00 1.21e-05 . . . . 15053 1 8 no BMRB 16079 . mPrP90_3AV . . . . . 100.00 142 100.00 100.00 4.40e-06 . . . . 15053 1 9 no BMRB 16080 . mPrP90_2II . . . . . 100.00 142 100.00 100.00 6.79e-06 . . . . 15053 1 10 no BMRB 16184 . mpp_121-231 . . . . . 100.00 114 100.00 100.00 1.07e-05 . . . . 15053 1 11 no BMRB 16185 . mpp_121-231 . . . . . 100.00 114 100.00 100.00 7.03e-06 . . . . 15053 1 12 no BMRB 16722 . "mouse prion protein double mutant D167S, N173K" . . . . . 100.00 113 100.00 100.00 1.22e-05 . . . . 15053 1 13 no BMRB 16723 . "mouse prion protein double mutant D167S, N173K" . . . . . 95.65 113 100.00 100.00 4.74e-05 . . . . 15053 1 14 no BMRB 16743 . "HuPrP(90-231 M129 Q212P)" . . . . . 100.00 148 100.00 100.00 3.57e-05 . . . . 15053 1 15 no BMRB 17034 . shPrP . . . . . 100.00 162 100.00 100.00 5.55e-05 . . . . 15053 1 16 no BMRB 17081 . "Prion with Y169G mutation" . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 17 no BMRB 17084 . prion . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 18 no BMRB 17087 . "Prion with Y169A, Y225A, Y226A mutation" . . . . . 100.00 114 100.00 100.00 1.10e-05 . . . . 15053 1 19 no BMRB 17174 . Mouse_prion . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 20 no BMRB 17213 . entity . . . . . 100.00 114 100.00 100.00 9.67e-06 . . . . 15053 1 21 no BMRB 17714 . HuPrP . . . . . 100.00 147 100.00 100.00 2.71e-06 . . . . 15053 1 22 no BMRB 17756 . hPrP(121-230) . . . . . 100.00 113 100.00 100.00 1.30e-05 . . . . 15053 1 23 no BMRB 17758 . mPrP(121-232) . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 24 no BMRB 17780 . Hpp_E219K . . . . . 100.00 142 100.00 100.00 7.27e-06 . . . . 15053 1 25 no BMRB 17834 . shPrP . . . . . 100.00 104 100.00 100.00 4.17e-06 . . . . 15053 1 26 no BMRB 18426 . entity . . . . . 100.00 142 100.00 100.00 5.86e-06 . . . . 15053 1 27 no BMRB 18550 . V210I . . . . . 100.00 147 100.00 100.00 2.71e-06 . . . . 15053 1 28 no BMRB 19268 . MAJOR_PRION_PROTEIN . . . . . 100.00 146 100.00 100.00 3.04e-06 . . . . 15053 1 29 no BMRB 4307 . "recombinant Syrian hamster prion protein" . . . . . 100.00 142 100.00 100.00 4.03e-06 . . . . 15053 1 30 no BMRB 4379 . "human prion protein" . . . . . 100.00 112 100.00 100.00 9.57e-06 . . . . 15053 1 31 no BMRB 4402 . "human prion protein" . . . . . 100.00 210 100.00 100.00 1.22e-07 . . . . 15053 1 32 no BMRB 4434 . "human prion protein" . . . . . 100.00 143 100.00 100.00 5.17e-06 . . . . 15053 1 33 no BMRB 4620 . "prion protein" . . . . . 100.00 112 100.00 100.00 1.22e-05 . . . . 15053 1 34 no BMRB 4641 . "PRION PROTEIN" . . . . . 100.00 146 100.00 100.00 4.42e-06 . . . . 15053 1 35 no BMRB 4736 . "human prion protein" . . . . . 100.00 112 100.00 100.00 1.29e-05 . . . . 15053 1 36 no PDB 1AG2 . "Prion Protein Domain Prp(121-231) From Mouse, Nmr, 2 Minimized Average Structure" . . . . . 100.00 103 100.00 100.00 3.42e-06 . . . . 15053 1 37 no PDB 1B10 . "Solution Nmr Structure Of Recombinant Syrian Hamster Prion Protein Rprp(90-231) , 25 Structures" . . . . . 100.00 142 100.00 100.00 4.03e-06 . . . . 15053 1 38 no PDB 1E1G . "Human Prion Protein Variant M166v" . . . . . 100.00 104 100.00 100.00 2.76e-06 . . . . 15053 1 39 no PDB 1E1J . "Human Prion Protein Variant M166v" . . . . . 100.00 104 100.00 100.00 2.76e-06 . . . . 15053 1 40 no PDB 1E1P . "Human Prion Protein Variant S170n" . . . . . 100.00 104 100.00 100.00 2.87e-06 . . . . 15053 1 41 no PDB 1E1S . "Human Prion Protein Variant S170n" . . . . . 100.00 104 100.00 100.00 2.87e-06 . . . . 15053 1 42 no PDB 1E1U . "Human Prion Protein Variant R220k" . . . . . 100.00 104 100.00 100.00 2.62e-06 . . . . 15053 1 43 no PDB 1E1W . "Human Prion Protein Variant R220k" . . . . . 100.00 104 100.00 100.00 2.62e-06 . . . . 15053 1 44 no PDB 1FKC . "Human Prion Protein (Mutant E200k) Fragment 90-231" . . . . . 100.00 142 100.00 100.00 7.27e-06 . . . . 15053 1 45 no PDB 1FO7 . "Human Prion Protein Mutant E200k Fragment 90-231" . . . . . 100.00 142 100.00 100.00 7.27e-06 . . . . 15053 1 46 no PDB 1H0L . "Human Prion Protein 121-230 M166c/e221c" . . . . . 100.00 112 100.00 100.00 4.40e-06 . . . . 15053 1 47 no PDB 1HJM . "Human Prion Protein At Ph 7.0" . . . . . 100.00 104 100.00 100.00 2.41e-05 . . . . 15053 1 48 no PDB 1HJN . "Human Prion Protein At Ph 7.0" . . . . . 100.00 104 100.00 100.00 2.41e-05 . . . . 15053 1 49 no PDB 1I4M . "Crystal Structure Of The Human Prion Protein Reveals A Mechanism For Oligomerization" . . . . . 100.00 108 100.00 100.00 1.26e-05 . . . . 15053 1 50 no PDB 1QLX . "Human Prion Protein" . . . . . 100.00 210 100.00 100.00 1.22e-07 . . . . 15053 1 51 no PDB 1QLZ . "Human Prion Protein" . . . . . 100.00 210 100.00 100.00 1.22e-07 . . . . 15053 1 52 no PDB 1QM0 . "Human Prion Protein Fragment 90-230" . . . . . 100.00 143 100.00 100.00 5.17e-06 . . . . 15053 1 53 no PDB 1QM1 . "Human Prion Protein Fragment 90-230" . . . . . 100.00 143 100.00 100.00 5.17e-06 . . . . 15053 1 54 no PDB 1QM2 . "Human Prion Protein Fragment 121-230" . . . . . 100.00 112 100.00 100.00 9.57e-06 . . . . 15053 1 55 no PDB 1QM3 . "Human Prion Protein Fragment 121-230" . . . . . 100.00 112 100.00 100.00 9.57e-06 . . . . 15053 1 56 no PDB 1XYX . "Mouse Prion Protein Fragment 121-231" . . . . . 100.00 112 100.00 100.00 1.17e-05 . . . . 15053 1 57 no PDB 2IV5 . "Hprp-173-195 Solution Structure" . . . . . 95.65 23 100.00 100.00 7.65e-05 . . . . 15053 1 58 no PDB 2K56 . "Bank Vole Prion Protein (121-231)" . . . . . 100.00 113 100.00 100.00 3.55e-06 . . . . 15053 1 59 no PDB 2K5O . "Mouse Prion Protein (121-231) With Mutation S170n" . . . . . 100.00 114 100.00 100.00 1.44e-05 . . . . 15053 1 60 no PDB 2KFM . "Mouse Prion Protein (121-231) With Mutations Y225a And Y226a" . . . . . 100.00 114 100.00 100.00 1.07e-05 . . . . 15053 1 61 no PDB 2KFO . "Mouse Prion Protein (121-231) With Mutation V166a" . . . . . 100.00 114 100.00 100.00 7.03e-06 . . . . 15053 1 62 no PDB 2KU5 . "Mouse Prion Protein (121-231) With Mutation D167s" . . . . . 100.00 113 100.00 100.00 1.22e-05 . . . . 15053 1 63 no PDB 2KU6 . "Mouse Prion Protein (121-231) With Mutations D167s And N173k" . . . . . 95.65 113 100.00 100.00 4.74e-05 . . . . 15053 1 64 no PDB 2KUN . "Three Dimensional Structure Of Huprp(90-231 M129 Q212p)" . . . . . 100.00 148 100.00 100.00 3.57e-05 . . . . 15053 1 65 no PDB 2L1D . "Mouse Prion Protein (121-231) Containing The Substitution Y169g" . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 66 no PDB 2L1H . "Mouse Prion Protein Fragment 121-231 At 20 C" . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 67 no PDB 2L1K . "Mouse Prion Protein (121-231) Containing The Substitutions Y169a, Y225a, And Y226a" . . . . . 100.00 114 100.00 100.00 1.10e-05 . . . . 15053 1 68 no PDB 2L39 . "Mouse Prion Protein Fragment 121-231 At 37 C" . . . . . 100.00 114 100.00 100.00 9.29e-06 . . . . 15053 1 69 no PDB 2L40 . "Mouse Prion Protein (121-231) Containing The Substitution Y169a" . . . . . 100.00 114 100.00 100.00 9.67e-06 . . . . 15053 1 70 no PDB 2LEJ . "Human Prion Protein Mutant Huprp(90-231, M129, V210i)" . . . . . 100.00 147 100.00 100.00 2.71e-06 . . . . 15053 1 71 no PDB 2LFT . "Human Prion Protein With E219k Protective Polymorphism" . . . . . 100.00 142 100.00 100.00 7.27e-06 . . . . 15053 1 72 no PDB 2LH8 . "Syrian Hamster Prion Protein With Thiamine" . . . . . 100.00 104 100.00 100.00 4.17e-06 . . . . 15053 1 73 no PDB 2LSB . "Solution-State Nmr Structure Of The Human Prion Protein" . . . . . 100.00 142 100.00 100.00 5.86e-06 . . . . 15053 1 74 no PDB 2LV1 . "Solution-state Nmr Structure Of Prion Protein Mutant V210i At Neutral Ph" . . . . . 100.00 147 100.00 100.00 2.71e-06 . . . . 15053 1 75 no PDB 2M8T . "Solution Nmr Structure Of The V209m Variant Of The Human Prion Protein (residues 90-231)" . . . . . 100.00 146 100.00 100.00 3.04e-06 . . . . 15053 1 76 no PDB 2W9E . "Structure Of Icsm 18 (Anti-Prp Therapeutic Antibody) Fab Fragment Complexed With Human Prp Fragment 119-231" . . . . . 100.00 113 100.00 100.00 8.54e-06 . . . . 15053 1 77 no PDB 3HAF . "Human Prion Protein Variant V129 Domain Swapped Dimer" . . . . . 100.00 142 100.00 100.00 7.56e-06 . . . . 15053 1 78 no PDB 3HAK . "Human Prion Protein Variant V129" . . . . . 100.00 103 100.00 100.00 2.76e-06 . . . . 15053 1 79 no PDB 3HER . "Human Prion Protein Variant F198s With V129" . . . . . 100.00 142 100.00 100.00 8.43e-06 . . . . 15053 1 80 no PDB 3HES . "Human Prion Protein Variant F198s With M129" . . . . . 100.00 142 100.00 100.00 7.27e-06 . . . . 15053 1 81 no PDB 3HJ5 . "Human Prion Protein Variant V129 Domain Swapped Dimer" . . . . . 100.00 142 100.00 100.00 7.56e-06 . . . . 15053 1 82 no PDB 4DGI . "Structure Of Pom1 Fab Fragment Complexed With Human Prpc Fragment 120- 230" . . . . . 100.00 111 100.00 100.00 9.62e-06 . . . . 15053 1 83 no PDB 4KML . "Probing The N-terminal Beta-sheet Conversion In The Crystal Structure Of The Full-length Human Prion Protein Bound To A Nanobod" . . . . . 100.00 241 100.00 100.00 2.46e-07 . . . . 15053 1 84 no PDB 4MA7 . "Crystal Structure Of Mouse Prion Protein Complexed With Promazine" . . . . . 100.00 114 100.00 100.00 5.27e-06 . . . . 15053 1 85 no PDB 4MA8 . "Crystal Structure Of Mouse Prion Protein Complexed With Chlorpromazine" . . . . . 100.00 114 100.00 100.00 5.27e-06 . . . . 15053 1 86 no PDB 4N9O . "Probing The N-terminal Beta-sheet Conversion In The Crystal Structure Of The Human Prion Protein Bound To A Nanobody" . . . . . 100.00 142 100.00 100.00 5.86e-06 . . . . 15053 1 87 no PDB 4YXL . "Crystal Structure Of Syrian Hamster Prion Protein Complexed With Pom1 Fab" . . . . . 100.00 166 100.00 100.00 5.46e-05 . . . . 15053 1 88 no DBJ BAA00011 . "prion protein [Homo sapiens]" . . . . . 100.00 245 100.00 100.00 1.98e-07 . . . . 15053 1 89 no DBJ BAA08790 . "prion protein [Rattus norvegicus]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 90 no DBJ BAD51981 . "prion protein [Macaca fascicularis]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 91 no DBJ BAE28320 . "unnamed protein product [Mus musculus]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 92 no DBJ BAE28693 . "unnamed protein product [Mus musculus]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 93 no EMBL CAA58442 . "prion protein [Homo sapiens]" . . . . . 100.00 245 100.00 100.00 1.98e-07 . . . . 15053 1 94 no EMBL CAG46836 . "PRNP [Homo sapiens]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 95 no EMBL CAG46869 . "PRNP [Homo sapiens]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 96 no EMBL CAH92912 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 97 no EMBL CAJ18553 . "Prnp [Mus musculus]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 98 no GB AAA19664 . "prion protein [Homo sapiens]" . . . . . 100.00 245 100.00 100.00 1.98e-07 . . . . 15053 1 99 no GB AAA37013 . "prion protein [Cricetulus sp.]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 100 no GB AAA37014 . "prion protein, partial [Cricetulus migratorius]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 101 no GB AAA37090 . "scrapie prion, partial [Mesocricetus auratus]" . . . . . 100.00 243 100.00 100.00 1.93e-07 . . . . 15053 1 102 no GB AAA37091 . "PrP 33-35-C protein precursor, partial [Mesocricetus auratus]" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 103 no PIR B34759 . "prion protein - golden hamster" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 104 no REF NP_000302 . "major prion protein preproprotein [Homo sapiens]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 105 no REF NP_001009093 . "major prion protein preproprotein [Pan troglodytes]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 106 no REF NP_001040617 . "major prion protein precursor [Macaca mulatta]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 107 no REF NP_001073590 . "major prion protein preproprotein [Homo sapiens]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 108 no REF NP_001073591 . "major prion protein preproprotein [Homo sapiens]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 109 no SP P04156 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=ASCR; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 1 110 no SP P04273 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 111 no SP P04925 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 112 no SP P13852 . "RecName: Full=Major prion protein; Short=PrP; AltName: CD_antigen=CD230; Flags: Precursor" . . . . . 100.00 254 100.00 100.00 2.22e-07 . . . . 15053 1 113 no SP P40245 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" . . . . . 100.00 239 100.00 100.00 1.83e-07 . . . . 15053 1 114 no TPE CAJ43808 . "TPA: prion protein PrP [Pongo abelii]" . . . . . 100.00 253 100.00 100.00 2.19e-07 . . . . 15053 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 . ASN . 15053 1 2 . ASN . 15053 1 3 . PHE . 15053 1 4 . VAL . 15053 1 5 . HIS . 15053 1 6 . ASP . 15053 1 7 . CYS . 15053 1 8 . VAL . 15053 1 9 . ASN . 15053 1 10 . ILE . 15053 1 11 . THR . 15053 1 12 . ILE . 15053 1 13 . LYS . 15053 1 14 . GLN . 15053 1 15 . HIS . 15053 1 16 . THR . 15053 1 17 . VAL . 15053 1 18 . THR . 15053 1 19 . THR . 15053 1 20 . THR . 15053 1 21 . THR . 15053 1 22 . LYS . 15053 1 23 . GLY . 15053 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 . ASN 1 1 15053 1 . ASN 2 2 15053 1 . PHE 3 3 15053 1 . VAL 4 4 15053 1 . HIS 5 5 15053 1 . ASP 6 6 15053 1 . CYS 7 7 15053 1 . VAL 8 8 15053 1 . ASN 9 9 15053 1 . ILE 10 10 15053 1 . THR 11 11 15053 1 . ILE 12 12 15053 1 . LYS 13 13 15053 1 . GLN 14 14 15053 1 . HIS 15 15 15053 1 . THR 16 16 15053 1 . VAL 17 17 15053 1 . THR 18 18 15053 1 . THR 19 19 15053 1 . THR 20 20 15053 1 . THR 21 21 15053 1 . LYS 22 22 15053 1 . GLY 23 23 15053 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 15053 _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 $HPRP173195 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 15053 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 15053 _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 $HPRP173195 . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15053 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Sample.Sf_category sample _Sample.Sf_framecode sample _Sample.Entry_ID 15053 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details TRIFLUOROETHANOL-D2 _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 HPRP173195 'natural abundance' . . 1 $HPRP173195 . . . 1 2 mM . . . . 15053 1 2 TRIFLUOROETHANOL-D2 [U-2H] . . . . . . 100 . . % . . . . 15053 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 15053 _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 pH 5.0 . pH 15053 1 pressure 1.0 . atm 15053 1 temperature 300.0 . K 15053 1 stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 15053 _Software.ID 1 _Software.Name DYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID P.GUNTERT . . 15053 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 15053 1 stop_ save_ save_NMRVIEW _Software.Sf_category software _Software.Sf_framecode NMRVIEW _Software.Entry_ID 15053 _Software.ID 2 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'B Johnson, One Moon Scientific' . . 15053 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 15053 2 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 15053 _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_600 _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode 600 _NMR_spectrometer_list.Entry_ID 15053 _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 . . . 15053 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 15053 _Experiment_list.ID 1 _Experiment_list.Details . 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 NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15053 1 2 COSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15053 1 3 TOCSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15053 1 4 15N-HSQC no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15053 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 15053 _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 H 1 water protons . . . . ppm 5.0 internal direct 1.0 . . . 1 $citations . . 1 $citations 15053 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 15053 _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 NOESY . . . 15053 1 2 COSY . . . 15053 1 3 TOCSY . . . 15053 1 4 15N-HSQC . . . 15053 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 1 1 ASN H H 1 7.05 0.01 . . . . . . 1 ASN HN . 15053 1 2 . 1 1 1 1 ASN HA H 1 4.51 0.01 . . . . . . 1 ASN HA . 15053 1 3 . 1 1 1 1 ASN HB2 H 1 2.70 0.01 . 2 . . . . 1 ASN HB2 . 15053 1 4 . 1 1 1 1 ASN HB3 H 1 2.60 0.01 . 2 . . . . 1 ASN HB3 . 15053 1 5 . 1 1 1 1 ASN HD21 H 1 6.68 0.01 . 2 . . . . 1 ASN HD21 . 15053 1 6 . 1 1 1 1 ASN HD22 H 1 6.07 0.01 . 2 . . . . 1 ASN HD22 . 15053 1 7 . 1 1 2 2 ASN H H 1 7.74 0.01 . . . . . . 2 ASN HN . 15053 1 8 . 1 1 2 2 ASN HA H 1 4.31 0.01 . . . . . . 2 ASN HA . 15053 1 9 . 1 1 2 2 ASN HB3 H 1 2.56 0.01 . . . . . . 2 ASN HB3 . 15053 1 10 . 1 1 2 2 ASN HD21 H 1 6.65 0.01 . 2 . . . . 2 ASN HD21 . 15053 1 11 . 1 1 2 2 ASN HD22 H 1 5.76 0.01 . 2 . . . . 2 ASN HD22 . 15053 1 12 . 1 1 3 3 PHE H H 1 7.45 0.01 . . . . . . 3 PHE HN . 15053 1 13 . 1 1 3 3 PHE HA H 1 4.24 0.01 . . . . . . 3 PHE HA . 15053 1 14 . 1 1 3 3 PHE HB3 H 1 2.98 0.01 . 1 . . . . 3 PHE HB3 . 15053 1 15 . 1 1 4 4 VAL H H 1 7.44 0.01 . . . . . . 4 VAL HN . 15053 1 16 . 1 1 4 4 VAL HA H 1 3.38 0.01 . . . . . . 4 VAL HA . 15053 1 17 . 1 1 4 4 VAL HB H 1 1.91 0.01 . . . . . . 4 VAL HB . 15053 1 18 . 1 1 4 4 VAL HG11 H 1 0.75 0.01 . 1 . . . . 4 VAL HG1 . 15053 1 19 . 1 1 4 4 VAL HG12 H 1 0.75 0.01 . 1 . . . . 4 VAL HG1 . 15053 1 20 . 1 1 4 4 VAL HG13 H 1 0.75 0.01 . 1 . . . . 4 VAL HG1 . 15053 1 21 . 1 1 4 4 VAL HG21 H 1 0.90 0.01 . 1 . . . . 4 VAL HG2 . 15053 1 22 . 1 1 4 4 VAL HG22 H 1 0.90 0.01 . 1 . . . . 4 VAL HG2 . 15053 1 23 . 1 1 4 4 VAL HG23 H 1 0.90 0.01 . 1 . . . . 4 VAL HG2 . 15053 1 24 . 1 1 5 5 HIS H H 1 7.88 0.01 . . . . . . 5 HIS HN . 15053 1 25 . 1 1 5 5 HIS HA H 1 4.00 0.01 . . . . . . 5 HIS HA . 15053 1 26 . 1 1 5 5 HIS HB2 H 1 3.07 0.01 . 2 . . . . 5 HIS HB2 . 15053 1 27 . 1 1 5 5 HIS HB3 H 1 3.13 0.01 . 2 . . . . 5 HIS HB3 . 15053 1 28 . 1 1 5 5 HIS HD2 H 1 7.08 0.01 . . . . . . 5 HIS HD2 . 15053 1 29 . 1 1 5 5 HIS HE1 H 1 8.14 0.01 . . . . . . 5 HIS HE1 . 15053 1 30 . 1 1 6 6 ASP H H 1 8.21 0.01 . . . . . . 6 ASP HN . 15053 1 31 . 1 1 6 6 ASP HA H 1 4.23 0.01 . . . . . . 6 ASP HA . 15053 1 32 . 1 1 6 6 ASP HB2 H 1 2.66 0.01 . 2 . . . . 6 ASP HB2 . 15053 1 33 . 1 1 6 6 ASP HB3 H 1 3.09 0.01 . 2 . . . . 6 ASP HB3 . 15053 1 34 . 1 1 7 7 CYS H H 1 8.00 0.01 . . . . . . 7 CYS HN . 15053 1 35 . 1 1 7 7 CYS HA H 1 3.86 0.01 . . . . . . 7 CYS HA . 15053 1 36 . 1 1 7 7 CYS HB2 H 1 2.89 0.01 . 2 . . . . 7 CYS HB2 . 15053 1 37 . 1 1 7 7 CYS HB3 H 1 2.52 0.01 . 2 . . . . 7 CYS HB3 . 15053 1 38 . 1 1 8 8 VAL H H 1 8.29 0.01 . . . . . . 8 VAL HN . 15053 1 39 . 1 1 8 8 VAL HA H 1 3.36 0.01 . . . . . . 8 VAL HA . 15053 1 40 . 1 1 8 8 VAL HB H 1 1.98 0.01 . . . . . . 8 VAL HB . 15053 1 41 . 1 1 8 8 VAL HG11 H 1 0.77 0.01 . 1 . . . . 8 VAL HG1 . 15053 1 42 . 1 1 8 8 VAL HG12 H 1 0.77 0.01 . 1 . . . . 8 VAL HG1 . 15053 1 43 . 1 1 8 8 VAL HG13 H 1 0.77 0.01 . 1 . . . . 8 VAL HG1 . 15053 1 44 . 1 1 8 8 VAL HG21 H 1 0.87 0.01 . 1 . . . . 8 VAL HG2 . 15053 1 45 . 1 1 8 8 VAL HG22 H 1 0.87 0.01 . 1 . . . . 8 VAL HG2 . 15053 1 46 . 1 1 8 8 VAL HG23 H 1 0.87 0.01 . 1 . . . . 8 VAL HG2 . 15053 1 47 . 1 1 9 9 ASN H H 1 7.91 0.01 . . . . . . 9 ASN HN . 15053 1 48 . 1 1 9 9 ASN HA H 1 4.20 0.01 . . . . . . 9 ASN HA . 15053 1 49 . 1 1 9 9 ASN HB2 H 1 2.58 0.01 . 2 . . . . 9 ASN HB2 . 15053 1 50 . 1 1 9 9 ASN HB3 H 1 2.81 0.01 . 2 . . . . 9 ASN HB3 . 15053 1 51 . 1 1 9 9 ASN HD21 H 1 6.80 0.01 . 2 . . . . 9 ASN HD21 . 15053 1 52 . 1 1 9 9 ASN HD22 H 1 5.66 0.01 . 2 . . . . 9 ASN HD22 . 15053 1 53 . 1 1 10 10 ILE H H 1 8.34 0.01 . . . . . . 10 ILE HN . 15053 1 54 . 1 1 10 10 ILE HA H 1 3.54 0.01 . . . . . . 10 ILE HA . 15053 1 55 . 1 1 10 10 ILE HB H 1 1.76 0.01 . . . . . . 10 ILE HB . 15053 1 56 . 1 1 11 11 THR H H 1 7.96 0.01 . . . . . . 11 THR HN . 15053 1 57 . 1 1 11 11 THR HA H 1 3.88 0.01 . . . . . . 11 THR HA . 15053 1 58 . 1 1 11 11 THR HB H 1 4.31 0.01 . . . . . . 11 THR HB . 15053 1 59 . 1 1 11 11 THR HG21 H 1 1.10 0.01 . 1 . . . . 11 THR HG2 . 15053 1 60 . 1 1 11 11 THR HG22 H 1 1.10 0.01 . 1 . . . . 11 THR HG2 . 15053 1 61 . 1 1 11 11 THR HG23 H 1 1.10 0.01 . 1 . . . . 11 THR HG2 . 15053 1 62 . 1 1 12 12 ILE H H 1 8.55 0.01 . . . . . . 12 ILE HN . 15053 1 63 . 1 1 12 12 ILE HA H 1 3.56 0.01 . . . . . . 12 ILE HA . 15053 1 64 . 1 1 12 12 ILE HB H 1 1.86 0.01 . . . . . . 12 ILE HB . 15053 1 65 . 1 1 13 13 LYS H H 1 8.46 0.01 . . . . . . 13 LYS HN . 15053 1 66 . 1 1 13 13 LYS HA H 1 3.80 0.01 . . . . . . 13 LYS HA . 15053 1 67 . 1 1 13 13 LYS HB3 H 1 1.88 0.01 . 1 . . . . 13 LYS HB3 . 15053 1 68 . 1 1 13 13 LYS HG3 H 1 1.26 0.01 . 1 . . . . 13 LYS HG3 . 15053 1 69 . 1 1 13 13 LYS HD3 H 1 1.49 0.01 . 1 . . . . 13 LYS HD3 . 15053 1 70 . 1 1 13 13 LYS HE3 H 1 2.77 0.01 . 1 . . . . 13 LYS HE3 . 15053 1 71 . 1 1 14 14 GLN H H 1 9.04 0.01 . . . . . . 14 GLN HN . 15053 1 72 . 1 1 14 14 GLN HA H 1 3.86 0.01 . . . . . . 14 GLN HA . 15053 1 73 . 1 1 14 14 GLN HB2 H 1 1.98 0.01 . 2 . . . . 14 GLN HB2 . 15053 1 74 . 1 1 14 14 GLN HB3 H 1 2.16 0.01 . 2 . . . . 14 GLN HB3 . 15053 1 75 . 1 1 14 14 GLN HG2 H 1 1.98 0.01 . 2 . . . . 14 GLN HG2 . 15053 1 76 . 1 1 14 14 GLN HG3 H 1 2.46 0.01 . 2 . . . . 14 GLN HG3 . 15053 1 77 . 1 1 14 14 GLN HE21 H 1 6.37 0.01 . 2 . . . . 14 GLN HE21 . 15053 1 78 . 1 1 14 14 GLN HE22 H 1 5.65 0.01 . 2 . . . . 14 GLN HE22 . 15053 1 79 . 1 1 15 15 HIS H H 1 8.56 0.01 . . . . . . 15 HIS HN . 15053 1 80 . 1 1 15 15 HIS HA H 1 4.04 0.01 . . . . . . 15 HIS HA . 15053 1 81 . 1 1 15 15 HIS HB3 H 1 3.23 0.01 . 1 . . . . 15 HIS HB3 . 15053 1 82 . 1 1 15 15 HIS HD2 H 1 7.08 0.01 . . . . . . 15 HIS HD2 . 15053 1 83 . 1 1 15 15 HIS HE1 H 1 8.20 0.01 . . . . . . 15 HIS HE1 . 15053 1 84 . 1 1 16 16 THR H H 1 8.52 0.01 . . . . . . 16 THR HN . 15053 1 85 . 1 1 16 16 THR HA H 1 3.82 0.01 . . . . . . 16 THR HA . 15053 1 86 . 1 1 16 16 THR HB H 1 4.31 0.01 . . . . . . 16 THR HB . 15053 1 87 . 1 1 16 16 THR HG21 H 1 1.11 0.01 . 1 . . . . 16 THR HG2 . 15053 1 88 . 1 1 16 16 THR HG22 H 1 1.11 0.01 . 1 . . . . 16 THR HG2 . 15053 1 89 . 1 1 16 16 THR HG23 H 1 1.11 0.01 . 1 . . . . 16 THR HG2 . 15053 1 90 . 1 1 17 17 VAL H H 1 8.74 0.01 . . . . . . 17 VAL HN . 15053 1 91 . 1 1 17 17 VAL HA H 1 3.52 0.01 . . . . . . 17 VAL HA . 15053 1 92 . 1 1 17 17 VAL HB H 1 1.98 0.01 . . . . . . 17 VAL HB . 15053 1 93 . 1 1 17 17 VAL HG11 H 1 0.79 0.01 . 1 . . . . 17 VAL HG1 . 15053 1 94 . 1 1 17 17 VAL HG12 H 1 0.79 0.01 . 1 . . . . 17 VAL HG1 . 15053 1 95 . 1 1 17 17 VAL HG13 H 1 0.79 0.01 . 1 . . . . 17 VAL HG1 . 15053 1 96 . 1 1 17 17 VAL HG21 H 1 0.93 0.01 . 1 . . . . 17 VAL HG2 . 15053 1 97 . 1 1 17 17 VAL HG22 H 1 0.93 0.01 . 1 . . . . 17 VAL HG2 . 15053 1 98 . 1 1 17 17 VAL HG23 H 1 0.93 0.01 . 1 . . . . 17 VAL HG2 . 15053 1 99 . 1 1 18 18 THR H H 1 7.91 0.01 . . . . . . 18 THR HN . 15053 1 100 . 1 1 18 18 THR HA H 1 3.68 0.01 . . . . . . 18 THR HA . 15053 1 101 . 1 1 18 18 THR HB H 1 3.99 0.01 . . . . . . 18 THR HB . 15053 1 102 . 1 1 18 18 THR HG21 H 1 1.08 0.01 . 1 . . . . 18 THR HG2 . 15053 1 103 . 1 1 18 18 THR HG22 H 1 1.08 0.01 . 1 . . . . 18 THR HG2 . 15053 1 104 . 1 1 18 18 THR HG23 H 1 1.08 0.01 . 1 . . . . 18 THR HG2 . 15053 1 105 . 1 1 19 19 THR H H 1 7.65 0.01 . . . . . . 19 THR HN . 15053 1 106 . 1 1 19 19 THR HA H 1 3.78 0.01 . . . . . . 19 THR HA . 15053 1 107 . 1 1 19 19 THR HG21 H 1 1.06 0.01 . 1 . . . . 19 THR HG2 . 15053 1 108 . 1 1 19 19 THR HG22 H 1 1.06 0.01 . 1 . . . . 19 THR HG2 . 15053 1 109 . 1 1 19 19 THR HG23 H 1 1.06 0.01 . 1 . . . . 19 THR HG2 . 15053 1 110 . 1 1 20 20 THR H H 1 7.82 0.01 . . . . . . 20 THR HN . 15053 1 111 . 1 1 20 20 THR HA H 1 3.90 0.01 . . . . . . 20 THR HA . 15053 1 112 . 1 1 20 20 THR HB H 1 4.14 0.01 . . . . . . 20 THR HB . 15053 1 113 . 1 1 20 20 THR HG21 H 1 1.15 0.01 . 1 . . . . 20 THR HG2 . 15053 1 114 . 1 1 20 20 THR HG22 H 1 1.15 0.01 . 1 . . . . 20 THR HG2 . 15053 1 115 . 1 1 20 20 THR HG23 H 1 1.15 0.01 . 1 . . . . 20 THR HG2 . 15053 1 116 . 1 1 21 21 THR H H 1 7.62 0.01 . . . . . . 21 THR HN . 15053 1 117 . 1 1 21 21 THR HA H 1 4.16 0.01 . . . . . . 21 THR HA . 15053 1 118 . 1 1 21 21 THR HB H 1 4.56 0.01 . . . . . . 21 THR HB . 15053 1 119 . 1 1 21 21 THR HG21 H 1 1.17 0.01 . 1 . . . . 21 THR HG2 . 15053 1 120 . 1 1 21 21 THR HG22 H 1 1.17 0.01 . 1 . . . . 21 THR HG2 . 15053 1 121 . 1 1 21 21 THR HG23 H 1 1.17 0.01 . 1 . . . . 21 THR HG2 . 15053 1 122 . 1 1 22 22 LYS H H 1 7.62 0.01 . . . . . . 22 LYS HN . 15053 1 123 . 1 1 22 22 LYS HA H 1 4.09 0.01 . . . . . . 22 LYS HA . 15053 1 124 . 1 1 22 22 LYS HB3 H 1 1.85 0.01 . 1 . . . . 22 LYS HB3 . 15053 1 125 . 1 1 22 22 LYS HG3 H 1 1.29 0.01 . 1 . . . . 22 LYS HG3 . 15053 1 126 . 1 1 22 22 LYS HD3 H 1 1.52 0.01 . 1 . . . . 22 LYS HD3 . 15053 1 127 . 1 1 22 22 LYS HE3 H 1 2.85 0.01 . 1 . . . . 22 LYS HE3 . 15053 1 128 . 1 1 22 22 LYS HZ1 H 1 6.93 0.01 . 1 . . . . 22 LYS HZ . 15053 1 129 . 1 1 22 22 LYS HZ2 H 1 6.93 0.01 . 1 . . . . 22 LYS HZ . 15053 1 130 . 1 1 22 22 LYS HZ3 H 1 6.93 0.01 . 1 . . . . 22 LYS HZ . 15053 1 131 . 1 1 23 23 GLY H H 1 7.69 0.01 . . . . . . 23 GLY HN . 15053 1 132 . 1 1 23 23 GLY HA2 H 1 3.87 0.01 . 2 . . . . 23 GLY HA1 . 15053 1 133 . 1 1 23 23 GLY HA3 H 1 3.58 0.01 . 2 . . . . 23 GLY HA2 . 15053 1 stop_ save_