data_15054 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HPRP180-195 STRUCTURE ; _BMRB_accession_number 15054 _BMRB_flat_file_name bmr15054.str _Entry_type original _Submission_date 2006-11-27 _Accession_date 2006-11-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saviano G. . . 2 Tancredi T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 80 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-10-07 update BMRB 'Complete Entry Citation' 2007-02-01 original author 'Original Release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15052 'prion protein fragment 173-195' 15053 'prion protein fragment 173-195, mutant' stop_ save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18563793 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ronga Luisa . . 2 Palladino Pasquale . . 3 Saviano Gabriella . . 4 Tancredi Teodorico . . 5 Benedetti Ettore . . 6 Ragone Raffaele . . 7 Rossi Filomena . . stop_ _Journal_abbreviation 'J. Pept. Sci.' _Journal_volume 14 _Journal_issue 10 _Journal_CSD 9999 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1096 _Page_last 1102 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HPRP-180-195 PEPTIDE' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HPRP-180-195 PEPTIDE' $HPRP-180-195_PEPTIDE stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HPRP-180-195_PEPTIDE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HPRP-180-195_PEPTIDE _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 16 _Mol_residue_sequence VNITIKQHTVTTTTKG loop_ _Residue_seq_code _Residue_label 1 VAL 2 ASN 3 ILE 4 THR 5 ILE 6 LYS 7 GLN 8 HIS 9 THR 10 VAL 11 THR 12 THR 13 THR 14 THR 15 LYS 16 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15053 HPRP173195 100.00 23 100.00 100.00 9.64e+00 BMRB 15845 Prion_Protein 100.00 114 100.00 100.00 8.34e+00 BMRB 16071 mPrP90 100.00 144 100.00 100.00 7.20e+00 BMRB 16075 mPrP90_M129V 100.00 141 100.00 100.00 7.14e+00 BMRB 16076 mPrP90_P102L 100.00 141 100.00 100.00 6.92e+00 BMRB 16077 mPrP90_P105L 100.00 141 100.00 100.00 6.92e+00 BMRB 16078 mPrP90_A117V 100.00 142 100.00 100.00 7.39e+00 BMRB 16079 mPrP90_3AV 100.00 142 100.00 100.00 8.03e+00 BMRB 16080 mPrP90_2II 100.00 142 100.00 100.00 7.16e+00 BMRB 16185 mpp_121-231 100.00 114 100.00 100.00 6.52e+00 BMRB 17081 "Prion with Y169G mutation" 100.00 114 100.00 100.00 9.68e+00 BMRB 17084 prion 100.00 114 100.00 100.00 8.07e+00 BMRB 17174 Mouse_prion 100.00 114 100.00 100.00 8.07e+00 BMRB 17213 entity 100.00 114 100.00 100.00 9.68e+00 BMRB 17714 HuPrP 100.00 147 100.00 100.00 9.80e+00 BMRB 17756 hPrP(121-230) 100.00 113 100.00 100.00 9.50e+00 BMRB 17757 hPrP(121-230) 100.00 113 100.00 100.00 3.21e+00 BMRB 17758 mPrP(121-232) 100.00 114 100.00 100.00 8.07e+00 BMRB 17780 Hpp_E219K 100.00 142 100.00 100.00 6.94e+00 BMRB 17834 shPrP 100.00 104 100.00 100.00 3.34e+00 BMRB 18550 V210I 100.00 147 100.00 100.00 9.80e+00 BMRB 19268 MAJOR_PRION_PROTEIN 100.00 146 100.00 100.00 9.78e+00 BMRB 4307 "recombinant Syrian hamster prion protein" 100.00 142 100.00 100.00 7.62e+00 BMRB 4379 "human prion protein" 100.00 112 100.00 100.00 9.33e+00 BMRB 4402 "human prion protein" 100.00 210 100.00 100.00 1.03e+00 PDB 1B10 "Solution Nmr Structure Of Recombinant Syrian Hamster Prion Protein Rprp(90-231) , 25 Structures" 100.00 142 100.00 100.00 7.62e+00 PDB 1FKC "Human Prion Protein (Mutant E200k) Fragment 90-231" 100.00 142 100.00 100.00 6.94e+00 PDB 1FO7 "Human Prion Protein Mutant E200k Fragment 90-231" 100.00 142 100.00 100.00 6.94e+00 PDB 1H0L "Human Prion Protein 121-230 M166c/e221c" 100.00 112 100.00 100.00 7.54e+00 PDB 1I4M "Crystal Structure Of The Human Prion Protein Reveals A Mechanism For Oligomerization" 100.00 108 100.00 100.00 8.58e+00 PDB 1QLX "Human Prion Protein" 100.00 210 100.00 100.00 1.03e+00 PDB 1QLZ "Human Prion Protein" 100.00 210 100.00 100.00 1.03e+00 PDB 1QM2 "Human Prion Protein Fragment 121-230" 100.00 112 100.00 100.00 9.33e+00 PDB 1QM3 "Human Prion Protein Fragment 121-230" 100.00 112 100.00 100.00 9.33e+00 PDB 1XYX "Mouse Prion Protein Fragment 121-231" 100.00 112 100.00 100.00 8.39e+00 PDB 2K5O "Mouse Prion Protein (121-231) With Mutation S170n" 100.00 114 100.00 100.00 8.34e+00 PDB 2KFO "Mouse Prion Protein (121-231) With Mutation V166a" 100.00 114 100.00 100.00 6.52e+00 PDB 2L1D "Mouse Prion Protein (121-231) Containing The Substitution Y169g" 100.00 114 100.00 100.00 9.68e+00 PDB 2L1H "Mouse Prion Protein Fragment 121-231 At 20 C" 100.00 114 100.00 100.00 8.07e+00 PDB 2L39 "Mouse Prion Protein Fragment 121-231 At 37 C" 100.00 114 100.00 100.00 8.07e+00 PDB 2L40 "Mouse Prion Protein (121-231) Containing The Substitution Y169a" 100.00 114 100.00 100.00 9.68e+00 PDB 2LEJ "Human Prion Protein Mutant Huprp(90-231, M129, V210i)" 100.00 147 100.00 100.00 9.80e+00 PDB 2LFT "Human Prion Protein With E219k Protective Polymorphism" 100.00 142 100.00 100.00 6.94e+00 PDB 2LH8 "Syrian Hamster Prion Protein With Thiamine" 100.00 104 100.00 100.00 3.34e+00 PDB 2LV1 "Solution-state Nmr Structure Of Prion Protein Mutant V210i At Neutral Ph" 100.00 147 100.00 100.00 9.80e+00 PDB 2M8T "Solution Nmr Structure Of The V209m Variant Of The Human Prion Protein (residues 90-231)" 100.00 146 100.00 100.00 9.78e+00 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 8.36e+00 PDB 4DGI "Structure Of Pom1 Fab Fragment Complexed With Human Prpc Fragment 120- 230" 100.00 111 100.00 100.00 8.97e+00 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 2.05e+00 PDB 4MA7 "Crystal Structure Of Mouse Prion Protein Complexed With Promazine" 100.00 114 100.00 100.00 5.05e+00 PDB 4MA8 "Crystal Structure Of Mouse Prion Protein Complexed With Chlorpromazine" 100.00 114 100.00 100.00 5.05e+00 DBJ BAA00011 "prion protein [Homo sapiens]" 100.00 245 100.00 100.00 6.30e-01 DBJ BAA08790 "prion protein [Rattus norvegicus]" 100.00 254 100.00 100.00 1.23e+00 DBJ BAD51981 "prion protein [Macaca fascicularis]" 100.00 253 100.00 100.00 5.82e-01 DBJ BAE28320 "unnamed protein product [Mus musculus]" 100.00 254 100.00 100.00 1.36e+00 DBJ BAE28693 "unnamed protein product [Mus musculus]" 100.00 254 100.00 100.00 1.47e+00 EMBL CAA58442 "prion protein [Homo sapiens]" 100.00 245 100.00 100.00 5.65e-01 EMBL CAG46836 "PRNP [Homo sapiens]" 100.00 253 100.00 100.00 5.82e-01 EMBL CAG46869 "PRNP [Homo sapiens]" 100.00 253 100.00 100.00 5.82e-01 EMBL CAH92912 "hypothetical protein [Pongo abelii]" 100.00 253 100.00 100.00 5.82e-01 EMBL CAJ18553 "Prnp [Mus musculus]" 100.00 254 100.00 100.00 1.36e+00 GB AAA19664 "prion protein [Homo sapiens]" 100.00 245 100.00 100.00 6.30e-01 GB AAA37013 "prion protein [Cricetulus sp.]" 100.00 254 100.00 100.00 9.35e-01 GB AAA37014 "prion protein, partial [Cricetulus migratorius]" 100.00 254 100.00 100.00 8.15e-01 GB AAA37090 "scrapie prion, partial [Mesocricetus auratus]" 100.00 243 100.00 100.00 1.19e+00 GB AAA37091 "PrP 33-35-C protein precursor, partial [Mesocricetus auratus]" 100.00 254 100.00 100.00 7.84e-01 PIR B34759 "prion protein - golden hamster" 100.00 254 100.00 100.00 8.15e-01 REF NP_000302 "major prion protein preproprotein [Homo sapiens]" 100.00 253 100.00 100.00 5.82e-01 REF NP_001009093 "major prion protein preproprotein [Pan troglodytes]" 100.00 253 100.00 100.00 5.82e-01 REF NP_001040617 "major prion protein precursor [Macaca mulatta]" 100.00 253 100.00 100.00 5.82e-01 REF NP_001073590 "major prion protein preproprotein [Homo sapiens]" 100.00 253 100.00 100.00 5.82e-01 REF NP_001073591 "major prion protein preproprotein [Homo sapiens]" 100.00 253 100.00 100.00 5.82e-01 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 5.82e-01 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 7.84e-01 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 1.36e+00 SP P13852 "RecName: Full=Major prion protein; Short=PrP; AltName: CD_antigen=CD230; Flags: Precursor" 100.00 254 100.00 100.00 1.23e+00 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 7.41e-01 TPE CAJ43807 "TPA: prion protein PrP [Cavia porcellus]" 100.00 244 100.00 100.00 1.28e+00 TPE CAJ43808 "TPA: prion protein PrP [Pongo abelii]" 100.00 253 100.00 100.00 5.82e-01 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HPRP-180-195_PEPTIDE Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $HPRP-180-195_PEPTIDE 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details TRIFLUOROETHANOL-D2 loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HPRP-180-195_PEPTIDE . mM 1 2 'natural abundance' TRIFLUOROETHANOL-D2 100 % . . [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version . loop_ _Vendor _Address _Electronic_address P.GUNTERTH . . stop_ loop_ _Task refinement stop_ _Details . save_ save_NMRVIEW _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'B Johnson, One Moon Scientific' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_15N-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . pH pressure 1.0 . atm temperature 300.0 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label water H 1 protons ppm 5.0 internal direct . . . 1.0 $citations $citations 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label NOESY TOCSY COSY 15N-HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HPRP-180-195 PEPTIDE' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 VAL H H 7.40 0.01 . 2 1 1 VAL HA H 3.58 0.01 . 3 1 1 VAL HB H 1.93 0.01 . 4 1 1 VAL HG2 H 0.84 0.01 1 5 2 2 ASN H H 7.80 0.01 . 6 2 2 ASN HA H 4.19 0.01 . 7 2 2 ASN HB3 H 2.60 0.01 1 8 2 2 ASN HD21 H 6.91 0.01 2 9 2 2 ASN HD22 H 5.97 0.01 2 10 3 3 ILE H H 7.14 0.01 . 11 3 3 ILE HA H 3.65 0.01 . 12 3 3 ILE HB H 1.80 0.01 . 13 3 3 ILE HG13 H 1.39 0.01 . 14 3 3 ILE HG2 H 1.06 0.01 1 15 3 3 ILE HD1 H 0.77 0.01 1 16 4 4 THR H H 7.69 0.01 . 17 4 4 THR HA H 3.99 0.01 . 18 4 4 THR HB H 4.12 0.01 . 19 4 4 THR HG2 H 1.08 0.01 1 20 5 5 ILE H H 7.96 0.01 . 21 5 5 ILE HA H 3.60 0.01 . 22 5 5 ILE HB H 1.78 0.01 . 23 5 5 ILE HG13 H 1.57 0.01 . 24 5 5 ILE HG2 H 0.93 0.01 1 25 5 5 ILE HD1 H 0.66 0.01 1 26 6 6 LYS H H 7.98 0.01 . 27 6 6 LYS HA H 3.84 0.01 . 28 6 6 LYS HB3 H 1.86 0.01 1 29 6 6 LYS HG3 H 1.27 0.01 1 30 6 6 LYS HD3 H 1.50 0.01 1 31 6 6 LYS HE3 H 2.75 0.01 1 32 7 7 GLN H H 8.74 0.01 . 33 7 7 GLN HA H 3.84 0.01 . 34 7 7 GLN HB2 H 2.14 0.01 2 35 7 7 GLN HB3 H 1.94 0.01 2 36 7 7 GLN HG2 H 2.14 0.01 2 37 7 7 GLN HG3 H 2.39 0.01 2 38 7 7 GLN HE21 H 6.44 0.01 2 39 7 7 GLN HE22 H 5.66 0.01 2 40 8 8 HIS H H 8.62 0.01 . 41 8 8 HIS HA H 4.04 0.01 . 42 8 8 HIS HB3 H 3.21 0.01 1 43 8 8 HIS HD2 H 7.03 0.01 . 44 8 8 HIS HE1 H 8.03 0.01 . 45 9 9 THR H H 8.42 0.01 . 46 9 9 THR HA H 3.82 0.01 . 47 9 9 THR HB H 4.28 0.01 . 48 9 9 THR HG2 H 1.11 0.01 1 49 10 10 VAL H H 8.66 0.01 . 50 10 10 VAL HA H 3.50 0.01 . 51 10 10 VAL HB H 1.97 0.01 . 52 10 10 VAL HG1 H 0.77 0.01 1 53 10 10 VAL HG2 H 0.91 0.01 1 54 11 11 THR H H 7.96 0.01 . 55 11 11 THR HA H 3.66 0.01 . 56 11 11 THR HB H 3.99 0.01 . 57 11 11 THR HG2 H 1.05 0.01 1 58 12 12 THR H H 7.67 0.01 . 59 12 12 THR HA H 3.78 0.01 . 60 12 12 THR HB H 4.04 0.01 . 61 12 12 THR HG2 H 1.03 0.01 1 62 13 13 THR H H 7.79 0.01 . 63 13 13 THR HA H 3.89 0.01 . 64 13 13 THR HB H 4.14 0.01 . 65 13 13 THR HG1 H 4.79 0.01 . 66 13 13 THR HG2 H 1.16 0.01 1 67 14 14 THR H H 7.60 0.01 . 68 14 14 THR HA H 4.10 0.01 . 69 14 14 THR HB H 4.16 0.01 . 70 14 14 THR HG1 H 4.59 0.01 . 71 14 14 THR HG2 H 1.16 0.01 1 72 15 15 LYS H H 7.61 0.01 . 73 15 15 LYS HA H 4.05 0.01 . 74 15 15 LYS HB3 H 1.84 0.01 1 75 15 15 LYS HG3 H 1.28 0.01 1 76 15 15 LYS HD3 H 1.51 0.01 1 77 15 15 LYS HE3 H 2.84 0.01 1 78 16 16 GLY H H 7.69 0.01 . 79 16 16 GLY HA2 H 3.85 0.01 2 80 16 16 GLY HA3 H 3.57 0.01 2 stop_ save_