data_16757 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16757 _Entry.Title ; Location and properties of metal-binding sites on the human prion protein ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-03-03 _Entry.Accession_date 2010-03-03 _Entry.Last_release_date 2010-03-24 _Entry.Original_release_date 2010-03-24 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _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 Graham Jacksn . S. . 16757 2 Ian Murray . . . 16757 3 Laszlo Hosszu . L.P. . 16757 4 Nicholas Gibbs . . . 16757 5 Johnathan Waltho . P. . 16757 6 Anthony Clarke . R. . 16757 7 John Collinge . . . 16757 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID binding_constants 1 16757 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID 'binding constants' 1 16757 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 . . 2010-03-24 2010-03-03 original author . 16757 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 16757 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11438695 _Citation.Full_citation . _Citation.Title 'Location and properties of metal-binding sites on the human prion protein' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full . _Citation.Journal_volume 98 _Citation.Journal_issue 15 _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 8531 _Citation.Page_last 8535 _Citation.Year 2001 _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 Graham Jacksn . S. . 16757 1 2 Ian Murray . . . 16757 1 3 Laszlo Hosszu . L.P. . 16757 1 4 Nicholas Gibbs . . . 16757 1 5 Johnathan Waltho . P. . 16757 1 6 Anthony Clarke . R. . 16757 1 7 John Collinge . . . 16757 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16757 _Assembly.ID 1 _Assembly.Name 'PrP/copper complex' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _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 PrP^(91-231) 1 $PrP_(91-231) A . yes native no no . . . 16757 1 2 Cu 2 $CU B . no native no no . . . 16757 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PrP_(91-231) _Entity.Sf_category entity _Entity.Sf_framecode PrP_(91-231) _Entity.Entry_ID 16757 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name PrP^(91-231) _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SDPGQGGGTHSQWNKPSKPK TNMKHMAGAAAAGAVVGGLG GYVLGSAMSRPIIHFGSDYE DRYYRENMHRYPNQVYYRPM DEYSNQNDFVHNCVNITIKQ HTVTTTTKGENFTETDVKMM ERVVEQMCITQYERESQAYY QRGSS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 91,S _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 145 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _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 'alpha configuration' _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 15676 . V129/D178N_prion_protein . . . . . 100.00 146 99.31 100.00 1.57e-103 . . . . 16757 1 2 no BMRB 16743 . "HuPrP(90-231 M129 Q212P)" . . . . . 97.93 148 97.18 99.30 2.34e-98 . . . . 16757 1 3 no BMRB 17714 . HuPrP . . . . . 99.31 147 97.22 100.00 1.73e-101 . . . . 16757 1 4 no BMRB 17756 . hPrP(121-230) . . . . . 75.86 113 97.27 100.00 2.58e-73 . . . . 16757 1 5 no BMRB 17780 . Hpp_E219K . . . . . 97.93 142 97.18 100.00 3.16e-99 . . . . 16757 1 6 no BMRB 18426 . entity . . . . . 97.93 142 97.89 100.00 8.90e-100 . . . . 16757 1 7 no BMRB 18550 . V210I . . . . . 99.31 147 97.22 100.00 1.73e-101 . . . . 16757 1 8 no BMRB 19268 . MAJOR_PRION_PROTEIN . . . . . 100.00 146 97.24 100.00 8.88e-102 . . . . 16757 1 9 no BMRB 4402 . "human prion protein" . . . . . 97.24 210 97.87 100.00 1.27e-97 . . . . 16757 1 10 no BMRB 4434 . "human prion protein" . . . . . 97.24 143 97.87 100.00 4.64e-99 . . . . 16757 1 11 no BMRB 4641 . "PRION PROTEIN" . . . . . 100.00 146 97.24 100.00 1.23e-101 . . . . 16757 1 12 no PDB 1FKC . "Human Prion Protein (Mutant E200k) Fragment 90-231" . . . . . 97.93 142 97.18 100.00 3.16e-99 . . . . 16757 1 13 no PDB 1FO7 . "Human Prion Protein Mutant E200k Fragment 90-231" . . . . . 97.93 142 97.18 100.00 3.16e-99 . . . . 16757 1 14 no PDB 1HJM . "Human Prion Protein At Ph 7.0" . . . . . 71.03 104 97.09 100.00 3.07e-68 . . . . 16757 1 15 no PDB 1HJN . "Human Prion Protein At Ph 7.0" . . . . . 71.03 104 97.09 100.00 3.07e-68 . . . . 16757 1 16 no PDB 1I4M . "Crystal Structure Of The Human Prion Protein Reveals A Mechanism For Oligomerization" . . . . . 74.48 108 97.22 100.00 5.08e-72 . . . . 16757 1 17 no PDB 1QLX . "Human Prion Protein" . . . . . 97.24 210 97.87 100.00 1.27e-97 . . . . 16757 1 18 no PDB 1QLZ . "Human Prion Protein" . . . . . 97.24 210 97.87 100.00 1.27e-97 . . . . 16757 1 19 no PDB 1QM0 . "Human Prion Protein Fragment 90-230" . . . . . 97.24 143 97.87 100.00 4.64e-99 . . . . 16757 1 20 no PDB 1QM1 . "Human Prion Protein Fragment 90-230" . . . . . 97.24 143 97.87 100.00 4.64e-99 . . . . 16757 1 21 no PDB 2K1D . "Nmr Studies Of A Pathogenic Mutant (d178n) Of The Human Prion Protein" . . . . . 100.00 146 99.31 100.00 1.57e-103 . . . . 16757 1 22 no PDB 2KUN . "Three Dimensional Structure Of Huprp(90-231 M129 Q212p)" . . . . . 97.93 148 97.18 99.30 2.34e-98 . . . . 16757 1 23 no PDB 2LEJ . "Human Prion Protein Mutant Huprp(90-231, M129, V210i)" . . . . . 99.31 147 97.22 100.00 1.73e-101 . . . . 16757 1 24 no PDB 2LFT . "Human Prion Protein With E219k Protective Polymorphism" . . . . . 97.93 142 97.18 100.00 3.16e-99 . . . . 16757 1 25 no PDB 2LSB . "Solution-State Nmr Structure Of The Human Prion Protein" . . . . . 97.93 142 97.89 100.00 8.90e-100 . . . . 16757 1 26 no PDB 2LV1 . "Solution-state Nmr Structure Of Prion Protein Mutant V210i At Neutral Ph" . . . . . 99.31 147 97.22 100.00 1.73e-101 . . . . 16757 1 27 no PDB 2M8T . "Solution Nmr Structure Of The V209m Variant Of The Human Prion Protein (residues 90-231)" . . . . . 100.00 146 97.24 100.00 8.88e-102 . . . . 16757 1 28 no PDB 2W9E . "Structure Of Icsm 18 (Anti-Prp Therapeutic Antibody) Fab Fragment Complexed With Human Prp Fragment 119-231" . . . . . 77.93 113 97.35 100.00 1.06e-75 . . . . 16757 1 29 no PDB 3HAF . "Human Prion Protein Variant V129 Domain Swapped Dimer" . . . . . 97.93 142 98.59 100.00 3.02e-100 . . . . 16757 1 30 no PDB 3HAK . "Human Prion Protein Variant V129" . . . . . 71.03 103 98.06 100.00 7.45e-69 . . . . 16757 1 31 no PDB 3HEQ . "Human Prion Protein Variant D178n With M129" . . . . . 97.93 142 98.59 100.00 1.77e-100 . . . . 16757 1 32 no PDB 3HER . "Human Prion Protein Variant F198s With V129" . . . . . 97.93 142 97.89 99.30 5.00e-99 . . . . 16757 1 33 no PDB 3HES . "Human Prion Protein Variant F198s With M129" . . . . . 97.93 142 97.18 99.30 1.98e-98 . . . . 16757 1 34 no PDB 3HJ5 . "Human Prion Protein Variant V129 Domain Swapped Dimer" . . . . . 97.93 142 98.59 100.00 3.02e-100 . . . . 16757 1 35 no PDB 3HJX . "Human Prion Protein Variant D178n With V129" . . . . . 73.10 106 99.06 100.00 1.21e-71 . . . . 16757 1 36 no PDB 4DGI . "Structure Of Pom1 Fab Fragment Complexed With Human Prpc Fragment 120- 230" . . . . . 76.55 111 97.30 100.00 2.42e-74 . . . . 16757 1 37 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" . . . . . 97.93 241 97.89 100.00 4.51e-98 . . . . 16757 1 38 no PDB 4N9O . "Probing The N-terminal Beta-sheet Conversion In The Crystal Structure Of The Human Prion Protein Bound To A Nanobody" . . . . . 97.93 142 97.89 100.00 8.90e-100 . . . . 16757 1 39 no DBJ BAA00011 . "prion protein [Homo sapiens]" . . . . . 97.93 245 97.18 99.30 3.84e-95 . . . . 16757 1 40 no DBJ BAG32276 . "prion [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 41 no DBJ BAG32277 . "prion [Homo sapiens]" . . . . . 97.93 253 98.59 100.00 4.38e-98 . . . . 16757 1 42 no DBJ BAG32278 . "alternatively spliced variant form of prion [Homo sapiens]" . . . . . 88.28 230 97.66 100.00 4.38e-87 . . . . 16757 1 43 no DBJ BAG32279 . "alternatively spliced variant form of prion [Homo sapiens]" . . . . . 88.28 230 98.44 100.00 1.38e-87 . . . . 16757 1 44 no EMBL CAA58442 . "prion protein [Homo sapiens]" . . . . . 97.93 245 97.89 100.00 1.51e-97 . . . . 16757 1 45 no EMBL CAG46836 . "PRNP [Homo sapiens]" . . . . . 97.93 253 97.89 99.30 1.02e-95 . . . . 16757 1 46 no EMBL CAG46869 . "PRNP [Homo sapiens]" . . . . . 97.93 253 98.59 100.00 4.38e-98 . . . . 16757 1 47 no GB AAA19664 . "prion protein [Homo sapiens]" . . . . . 97.93 245 97.18 99.30 3.84e-95 . . . . 16757 1 48 no GB AAA60182 . "prion protein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 49 no GB AAA68633 . "major prion protein precursor [Gorilla gorilla]" . . . . . 97.93 253 97.18 100.00 4.14e-97 . . . . 16757 1 50 no GB AAB59442 . "prion protein, partial [Homo sapiens]" . . . . . 97.93 224 97.89 100.00 7.96e-98 . . . . 16757 1 51 no GB AAB59443 . "prion protein, partial [Homo sapiens]" . . . . . 97.93 233 97.89 100.00 8.82e-98 . . . . 16757 1 52 no REF NP_000302 . "major prion protein preproprotein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 53 no REF NP_001073590 . "major prion protein preproprotein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 54 no REF NP_001073591 . "major prion protein preproprotein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 55 no REF NP_001073592 . "major prion protein preproprotein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 56 no REF NP_898902 . "major prion protein preproprotein [Homo sapiens]" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 57 no SP P04156 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=ASCR; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_" . . . . . 97.93 253 97.89 100.00 1.45e-97 . . . . 16757 1 58 no SP P40252 . "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" . . . . . 97.93 253 97.18 100.00 4.51e-97 . . . . 16757 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 . SER . 16757 1 2 . ASP . 16757 1 3 . PRO . 16757 1 4 . GLY . 16757 1 5 . GLN . 16757 1 6 . GLY . 16757 1 7 . GLY . 16757 1 8 . GLY . 16757 1 9 . THR . 16757 1 10 . HIS . 16757 1 11 . SER . 16757 1 12 . GLN . 16757 1 13 . TRP . 16757 1 14 . ASN . 16757 1 15 . LYS . 16757 1 16 . PRO . 16757 1 17 . SER . 16757 1 18 . LYS . 16757 1 19 . PRO . 16757 1 20 . LYS . 16757 1 21 . THR . 16757 1 22 . ASN . 16757 1 23 . MET . 16757 1 24 . LYS . 16757 1 25 . HIS . 16757 1 26 . MET . 16757 1 27 . ALA . 16757 1 28 . GLY . 16757 1 29 . ALA . 16757 1 30 . ALA . 16757 1 31 . ALA . 16757 1 32 . ALA . 16757 1 33 . GLY . 16757 1 34 . ALA . 16757 1 35 . VAL . 16757 1 36 . VAL . 16757 1 37 . GLY . 16757 1 38 . GLY . 16757 1 39 . LEU . 16757 1 40 . GLY . 16757 1 41 . GLY . 16757 1 42 . TYR . 16757 1 43 . VAL . 16757 1 44 . LEU . 16757 1 45 . GLY . 16757 1 46 . SER . 16757 1 47 . ALA . 16757 1 48 . MET . 16757 1 49 . SER . 16757 1 50 . ARG . 16757 1 51 . PRO . 16757 1 52 . ILE . 16757 1 53 . ILE . 16757 1 54 . HIS . 16757 1 55 . PHE . 16757 1 56 . GLY . 16757 1 57 . SER . 16757 1 58 . ASP . 16757 1 59 . TYR . 16757 1 60 . GLU . 16757 1 61 . ASP . 16757 1 62 . ARG . 16757 1 63 . TYR . 16757 1 64 . TYR . 16757 1 65 . ARG . 16757 1 66 . GLU . 16757 1 67 . ASN . 16757 1 68 . MET . 16757 1 69 . HIS . 16757 1 70 . ARG . 16757 1 71 . TYR . 16757 1 72 . PRO . 16757 1 73 . ASN . 16757 1 74 . GLN . 16757 1 75 . VAL . 16757 1 76 . TYR . 16757 1 77 . TYR . 16757 1 78 . ARG . 16757 1 79 . PRO . 16757 1 80 . MET . 16757 1 81 . ASP . 16757 1 82 . GLU . 16757 1 83 . TYR . 16757 1 84 . SER . 16757 1 85 . ASN . 16757 1 86 . GLN . 16757 1 87 . ASN . 16757 1 88 . ASP . 16757 1 89 . PHE . 16757 1 90 . VAL . 16757 1 91 . HIS . 16757 1 92 . ASN . 16757 1 93 . CYS . 16757 1 94 . VAL . 16757 1 95 . ASN . 16757 1 96 . ILE . 16757 1 97 . THR . 16757 1 98 . ILE . 16757 1 99 . LYS . 16757 1 100 . GLN . 16757 1 101 . HIS . 16757 1 102 . THR . 16757 1 103 . VAL . 16757 1 104 . THR . 16757 1 105 . THR . 16757 1 106 . THR . 16757 1 107 . THR . 16757 1 108 . LYS . 16757 1 109 . GLY . 16757 1 110 . GLU . 16757 1 111 . ASN . 16757 1 112 . PHE . 16757 1 113 . THR . 16757 1 114 . GLU . 16757 1 115 . THR . 16757 1 116 . ASP . 16757 1 117 . VAL . 16757 1 118 . LYS . 16757 1 119 . MET . 16757 1 120 . MET . 16757 1 121 . GLU . 16757 1 122 . ARG . 16757 1 123 . VAL . 16757 1 124 . VAL . 16757 1 125 . GLU . 16757 1 126 . GLN . 16757 1 127 . MET . 16757 1 128 . CYS . 16757 1 129 . ILE . 16757 1 130 . THR . 16757 1 131 . GLN . 16757 1 132 . TYR . 16757 1 133 . GLU . 16757 1 134 . ARG . 16757 1 135 . GLU . 16757 1 136 . SER . 16757 1 137 . GLN . 16757 1 138 . ALA . 16757 1 139 . TYR . 16757 1 140 . TYR . 16757 1 141 . GLN . 16757 1 142 . ARG . 16757 1 143 . GLY . 16757 1 144 . SER . 16757 1 145 . SER . 16757 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 . SER 1 1 16757 1 . ASP 2 2 16757 1 . PRO 3 3 16757 1 . GLY 4 4 16757 1 . GLN 5 5 16757 1 . GLY 6 6 16757 1 . GLY 7 7 16757 1 . GLY 8 8 16757 1 . THR 9 9 16757 1 . HIS 10 10 16757 1 . SER 11 11 16757 1 . GLN 12 12 16757 1 . TRP 13 13 16757 1 . ASN 14 14 16757 1 . LYS 15 15 16757 1 . PRO 16 16 16757 1 . SER 17 17 16757 1 . LYS 18 18 16757 1 . PRO 19 19 16757 1 . LYS 20 20 16757 1 . THR 21 21 16757 1 . ASN 22 22 16757 1 . MET 23 23 16757 1 . LYS 24 24 16757 1 . HIS 25 25 16757 1 . MET 26 26 16757 1 . ALA 27 27 16757 1 . GLY 28 28 16757 1 . ALA 29 29 16757 1 . ALA 30 30 16757 1 . ALA 31 31 16757 1 . ALA 32 32 16757 1 . GLY 33 33 16757 1 . ALA 34 34 16757 1 . VAL 35 35 16757 1 . VAL 36 36 16757 1 . GLY 37 37 16757 1 . GLY 38 38 16757 1 . LEU 39 39 16757 1 . GLY 40 40 16757 1 . GLY 41 41 16757 1 . TYR 42 42 16757 1 . VAL 43 43 16757 1 . LEU 44 44 16757 1 . GLY 45 45 16757 1 . SER 46 46 16757 1 . ALA 47 47 16757 1 . MET 48 48 16757 1 . SER 49 49 16757 1 . ARG 50 50 16757 1 . PRO 51 51 16757 1 . ILE 52 52 16757 1 . ILE 53 53 16757 1 . HIS 54 54 16757 1 . PHE 55 55 16757 1 . GLY 56 56 16757 1 . SER 57 57 16757 1 . ASP 58 58 16757 1 . TYR 59 59 16757 1 . GLU 60 60 16757 1 . ASP 61 61 16757 1 . ARG 62 62 16757 1 . TYR 63 63 16757 1 . TYR 64 64 16757 1 . ARG 65 65 16757 1 . GLU 66 66 16757 1 . ASN 67 67 16757 1 . MET 68 68 16757 1 . HIS 69 69 16757 1 . ARG 70 70 16757 1 . TYR 71 71 16757 1 . PRO 72 72 16757 1 . ASN 73 73 16757 1 . GLN 74 74 16757 1 . VAL 75 75 16757 1 . TYR 76 76 16757 1 . TYR 77 77 16757 1 . ARG 78 78 16757 1 . PRO 79 79 16757 1 . MET 80 80 16757 1 . ASP 81 81 16757 1 . GLU 82 82 16757 1 . TYR 83 83 16757 1 . SER 84 84 16757 1 . ASN 85 85 16757 1 . GLN 86 86 16757 1 . ASN 87 87 16757 1 . ASP 88 88 16757 1 . PHE 89 89 16757 1 . VAL 90 90 16757 1 . HIS 91 91 16757 1 . ASN 92 92 16757 1 . CYS 93 93 16757 1 . VAL 94 94 16757 1 . ASN 95 95 16757 1 . ILE 96 96 16757 1 . THR 97 97 16757 1 . ILE 98 98 16757 1 . LYS 99 99 16757 1 . GLN 100 100 16757 1 . HIS 101 101 16757 1 . THR 102 102 16757 1 . VAL 103 103 16757 1 . THR 104 104 16757 1 . THR 105 105 16757 1 . THR 106 106 16757 1 . THR 107 107 16757 1 . LYS 108 108 16757 1 . GLY 109 109 16757 1 . GLU 110 110 16757 1 . ASN 111 111 16757 1 . PHE 112 112 16757 1 . THR 113 113 16757 1 . GLU 114 114 16757 1 . THR 115 115 16757 1 . ASP 116 116 16757 1 . VAL 117 117 16757 1 . LYS 118 118 16757 1 . MET 119 119 16757 1 . MET 120 120 16757 1 . GLU 121 121 16757 1 . ARG 122 122 16757 1 . VAL 123 123 16757 1 . VAL 124 124 16757 1 . GLU 125 125 16757 1 . GLN 126 126 16757 1 . MET 127 127 16757 1 . CYS 128 128 16757 1 . ILE 129 129 16757 1 . THR 130 130 16757 1 . GLN 131 131 16757 1 . TYR 132 132 16757 1 . GLU 133 133 16757 1 . ARG 134 134 16757 1 . GLU 135 135 16757 1 . SER 136 136 16757 1 . GLN 137 137 16757 1 . ALA 138 138 16757 1 . TYR 139 139 16757 1 . TYR 140 140 16757 1 . GLN 141 141 16757 1 . ARG 142 142 16757 1 . GLY 143 143 16757 1 . SER 144 144 16757 1 . SER 145 145 16757 1 stop_ save_ save_CU _Entity.Sf_category entity _Entity.Sf_framecode CU _Entity.Entry_ID 16757 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CU _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _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 . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CU _Entity.Nonpolymer_comp_label $chem_comp_CU _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _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 . 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 . CU . 16757 2 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 16757 _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 $PrP_(91-231) . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 16757 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 16757 _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 $PrP_(91-231) . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 16757 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CU _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CU _Chem_comp.Entry_ID 16757 _Chem_comp.ID CU _Chem_comp.Provenance . _Chem_comp.Name 'COPPER (II) ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CU _Chem_comp.Ambiguous_flag . _Chem_comp.Initial_date . _Chem_comp.Modified_date . _Chem_comp.Release_status . _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CU _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic no _Chem_comp.Aromatic no _Chem_comp.Formula Cu _Chem_comp.Formula_weight 63.546 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 13:36:24 2009 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Cu++] SMILES CACTVS 3.341 16757 CU [Cu++] SMILES_CANONICAL CACTVS 3.341 16757 CU [Cu+2] SMILES ACDLabs 10.04 16757 CU [Cu+2] SMILES 'OpenEye OEToolkits' 1.5.0 16757 CU [Cu+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 16757 CU InChI=1/Cu/q+2 InChI InChI 1.02b 16757 CU JPVYNHNXODAKFH-UHFFFAOYAL InChIKey InChI 1.02b 16757 CU stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID copper(2+) 'SYSTEMATIC NAME' ACDLabs 10.04 16757 CU 'copper(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 16757 CU stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CU . CU . . CU . . N 2 . . . . . . . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 . . 16757 CU stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 16757 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'titrated with 125 uM increments of CuSO4 to a final concentration of 1000 uM' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _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 PrP^(91-231) [U-15N] . . 1 $PrP_(91-231) . . 500 . . uM . . . . 16757 1 2 Mops 'natural abundance' . . . . . . 5 . . mM . . . . 16757 1 3 CuSO4 'natural abundance' . . 2 $CU . . 1000 . . uM . . . . 16757 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 16757 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 16757 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 16757 _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 6.0 . pH 16757 1 pressure 1 . atm 16757 1 temperature 298 . K 16757 1 stop_ save_ ############################ # Computer software used # ############################ save_Felix _Software.Sf_category software _Software.Sf_framecode Felix _Software.Entry_ID 16757 _Software.ID 1 _Software.Name FELIX _Software.Version 97 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Accelrys Software Inc.' . . 16757 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 16757 1 processing 16757 1 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 16757 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 16757 _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 DRX . 600 . . . 16757 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 16757 _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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16757 1 stop_ save_ save_binding_data _Binding_value_list.Sf_category binding_data _Binding_value_list.Sf_framecode binding_data _Binding_value_list.Entry_ID 16757 _Binding_value_list.ID 1 _Binding_value_list.Sample_condition_list_ID 1 _Binding_value_list.Sample_condition_list_label $sample_conditions_1 _Binding_value_list.Details . _Binding_value_list.Text_data_format . _Binding_value_list.Text_data . loop_ _Binding_experiment.Experiment_ID _Binding_experiment.Experiment_name _Binding_experiment.Sample_ID _Binding_experiment.Sample_label _Binding_experiment.Sample_state _Binding_experiment.Entry_ID _Binding_experiment.Binding_value_list_ID 1 '2D 1H-15N HSQC' 1 $sample_1 isotropic 16757 1 stop_ loop_ _Binding_software.Software_ID _Binding_software.Software_label _Binding_software.Method_ID _Binding_software.Method_label _Binding_software.Entry_ID _Binding_software.Binding_value_list_ID 1 $Felix . . 16757 1 stop_ loop_ _Binding_result.ID _Binding_result.Experiment_ID _Binding_result.Assembly_ID _Binding_result.Atm_obs_assembly_atom_ID _Binding_result.Atm_obs_entity_assembly_ID _Binding_result.Atm_obs_entity_ID _Binding_result.Atm_obs_comp_index_ID _Binding_result.Atm_obs_seq_ID _Binding_result.Atm_obs_comp_ID _Binding_result.Atm_obs_atom_ID _Binding_result.Atm_obs_atom_type _Binding_result.Atm_obs_atom_isotope_number _Binding_result.Resonance_ID _Binding_result.Atm_obs_auth_entity_assembly_ID _Binding_result.Atm_obs_auth_seq_ID _Binding_result.Atm_obs_auth_comp_ID _Binding_result.Atm_obs_auth_atom_ID _Binding_result.Expt_observed_param _Binding_result.Val_type _Binding_result.Val _Binding_result.Val_err _Binding_result.Val_units _Binding_result.Entry_ID _Binding_result.Binding_value_list_ID 1 1 1 . 1 1 . . . . . . . . . . . 'chemical shifts' Kd 41 . fM 16757 1 stop_ loop_ _Binding_partners.Binding_result_ID _Binding_partners.Assembly_ID _Binding_partners.Entity_assembly_ID _Binding_partners.Entity_assembly_name _Binding_partners.Entity_ID _Binding_partners.Entity_label _Binding_partners.Entry_ID _Binding_partners.Binding_value_list_ID 1 1 1 PrP^(91-231) 1 $PrP_(91-231) 16757 1 1 1 2 Cu 2 $CU 16757 1 stop_ save_