data_5358 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5358 _Entry.Title ; 1H, 15N, 13C Backbone Chemical Shift Assignments for Trypsin-Bound Bovine Pancreatic Trypsin Inhibitor (BPTI) at pH 5.8 and 36 Degrees ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-04-30 _Entry.Accession_date 2001-04-30 _Entry.Last_release_date 2002-04-30 _Entry.Original_release_date 2002-04-30 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 Clelia Biamonti . . . . 5358 2 Michael Baran . C . . 5358 3 Gaetano Montelione . T . . 5358 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5358 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 109 5358 '15N chemical shifts' 53 5358 '1H chemical shifts' 93 5358 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 . . 2002-05-08 . original BMRB . 5358 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5359 'Free form of BPTI.' 5358 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5358 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Structural and Dynamic Investigations of Macromolecular Recognition Processes by Nuclear Magnetic Resonance Spectroscopy ; _Citation.Status published _Citation.Type thesis _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 'Rutgers University' _Citation.Thesis_institution_city 'Piscataway, NJ' _Citation.Thesis_institution_country 'U. S. A.' _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year 1996 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Clelia Biamonti . . . . 5358 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_BPTI _Assembly.Sf_category assembly _Assembly.Sf_framecode system_BPTI _Assembly.Entry_ID 5358 _Assembly.ID 1 _Assembly.Name 'Trypsin-Bound Bovine Pancreatic Trypsin Inhibitor' _Assembly.BMRB_code . _Assembly.Number_of_components . _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 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5358 1 stop_ 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 BPTI 1 $BPTI . . . native . . . . . 5358 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 5 5 SG . 1 . 1 CYS 55 55 SG . . . . . . . . . . . . 5358 1 2 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 38 38 SG . . . . . . . . . . . . 5358 1 3 disulfide single . 1 . 1 CYS 30 30 SG . 1 . 1 CYS 51 51 SG . . . . . . . . . . . . 5358 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 2PTC . . . . . . 5358 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID BPTI abbreviation 5358 1 'Trypsin-Bound Bovine Pancreatic Trypsin Inhibitor' system 5358 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_BPTI _Entity.Sf_category entity _Entity.Sf_framecode BPTI _Entity.Entry_ID 5358 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'bovine pancreatic trypsin inhibitor' _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 ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCMRTCGGA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 58 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . no BMRB 1039 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 1156 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 1179 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 236 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 237 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 262 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 263 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 264 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 338 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 411 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 412 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 413 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 414 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 415 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 416 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 419 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 45 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 46 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 48 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 485 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 4868 . BPTI-R52 . . . . . 100.00 58 98.28 98.28 2.63e-25 . . . . 5358 1 . no BMRB 49 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 4968 . BPTI . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 5171 . BPTI . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 5358 1 . no BMRB 5307 . 'Basic Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no BMRB 5359 . 'bovine pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1B0C . 'Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallized From Thiocyanate, Chloride Or Sulfate' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1BHC . 'Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1BPI . 'The Structure Of Bovine Pancreatic Trypsin Inhibitor At 125k: Definition Of Carboxyl-Terminal Residues Glycine-57 And Alanine-58' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1BPT . 'Crevice-Forming Mutants Of Bpti: Crystal Structures Of F22a, Y23a, N43g, And F45a' . . . . . 100.00 58 98.28 98.28 2.13e-25 . . . . 5358 1 . no PDB 1BTH . 'Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1BTI . ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; . . . . . 100.00 58 98.28 98.28 2.15e-25 . . . . 5358 1 . no PDB 1BZ5 . 'Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallize From Thiocyanate, Chloride Or Sulfate' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1BZX . 'The Crystal Structure Of Anionic Salmon Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1CBW . 'Bovine Chymotrypsin Complexed To Bpti' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1CO7 . 'R117h Mutant Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 99 100.00 100.00 3.82e-27 . . . . 5358 1 . no PDB 1D0D . 'Crystal Structure Of Tick Anticoagulant Protein Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1EAW . 'Crystal Structure Of The Mtsp1 (Matriptase)-Bpti (Aprotinin) Complex' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1F5R . 'Rat Trypsinogen Mutant Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 5358 1 . no PDB 1F7Z . 'Rat Trypsinogen K15a Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 5358 1 . no PDB 1FAN . ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; . . . . . 100.00 58 98.28 98.28 2.15e-25 . . . . 5358 1 . no PDB 1FY8 . 'Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1JV8 . 'Nmr Structure Of Bpti Mutant G37a' . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 5358 1 . no PDB 1JV9 . 'Nmr Structure Of Bpti Mutant G37a' . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 5358 1 . no PDB 1MTN . 'Bovine Alpha-Chymotrypsin:bpti Crystallization' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1NAG . ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; . . . . . 100.00 58 98.28 98.28 1.77e-25 . . . . 5358 1 . no PDB 1OA5 . 'The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1OA6 . 'The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1PIT . ; Determination Of A High-Quality Nuclear Magnetic Resonance Solution Structure Of The Bovine Pancreatic Trypsin Inhibitor And Comparison With Three Crystal Structures ; . . . . . 98.28 58 100.00 100.00 1.20e-25 . . . . 5358 1 . no PDB 1TPA . 'The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 1UUA . 'Solution Structure Of A Truncated Bovine Pancreatic Trypsin Inhibitor, 3-58 Bpti' . . . . . 96.55 56 100.00 100.00 6.00e-25 . . . . 5358 1 . no PDB 1YKT . 'TrypsinBPTI COMPLEX MUTANT' . . . . . 96.55 56 100.00 100.00 4.09e-25 . . . . 5358 1 . no PDB 2FI4 . 'Crystal Structure Of A Bpti Variant (Cys14->ser) In Complex With Trypsin' . . . . . 100.00 58 98.28 98.28 1.65e-25 . . . . 5358 1 . no PDB 2FI5 . 'Crystal Structure Of A Bpti Variant (Cys38->ser) In Complex With Trypsin' . . . . . 100.00 58 98.28 98.28 1.65e-25 . . . . 5358 1 . no PDB 2FTL . 'Crystal Structure Of Trypsin Complexed With Bpti At 100k' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2FTM . 'Crystal Structure Of Trypsin Complexed With The Bpti Variant (Tyr35->gly)' . . . . . 100.00 58 98.28 98.28 3.52e-25 . . . . 5358 1 . no PDB 2HEX . 'Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2IJO . 'Crystal Structure Of The West Nile Virus Ns2b-Ns3 Protease Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2KAI . ; Refined 2.5 Angstroms X-Ray Crystal Structure Of The Complex Formed By Porcine Kallikrein A And The Bovine Pancreatic Trypsin Inhibitor. Crystallization, Patterson Search, Structure Determination, Refinement, Structure And Comparison With Its Components And With The Bovine Trypsin- Pancreatic Trypsin Inhibitor Complex ; . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2PTC . 'The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2R9P . 'Human Mesotrypsin Complexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2RA3 . 'Human Cationic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2TGP . 'The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 2TPI . 'On The Disordered Activation Domain In Trypsinogen. Chemical Labelling And Low-Temperature Crystallography' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 3BTK . 'The Crystal Structures Of The Complexes Between Bovine Beta- Trypsin And Ten P1 Variants Of Bpti' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 3TGI . 'Wild-Type Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 5358 1 . no PDB 3TGJ . 'S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 5358 1 . no PDB 3TGK . 'Trypsinogen Mutant D194n And Deletion Of Ile 16-Val 17 Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 5358 1 . no PDB 3TPI . 'The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 4PTI . 'The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 4TPI . ; The Refined 2.2-Angstroms (0.22-Nm) X-Ray Crystal Structure Of The Ternary Complex Formed By Bovine Trypsinogen, Valine-Valine And The Arg15 Analogue Of Bovine Pancreatic Trypsin Inhibitor ; . . . . . 100.00 58 98.28 100.00 8.10e-26 . . . . 5358 1 . no PDB 5PTI . 'Structure Of Bovine Pancreatic Trypsin Inhibitor. Results Of Joint Neutron And X-Ray Refinement Of Crystal Form Ii' . . . . . 98.28 58 100.00 100.00 1.20e-25 . . . . 5358 1 . no PDB 6PTI . 'Structure Of Form Iii Crystals Of Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no PDB 8PTI . 'Crystal Structure Of A Y35g Mutant Of Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 98.28 98.28 3.52e-25 . . . . 5358 1 . no PDB 9PTI . 'Basic Pancreatic Trypsin Inhibitor (Met 52 Oxidized)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no EMBL CAA27062 . 'unnamed protein product [Bos taurus]' . . . . . 100.00 89 100.00 100.00 2.03e-26 . . . . 5358 1 . no EMBL CAA27063 . 'unnamed protein product [Bos taurus]' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no EMBL CAA28371 . 'unnamed protein product [synthetic construct]' . . . . . 100.00 59 100.00 100.00 2.97e-26 . . . . 5358 1 . no EMBL CAA28886 . 'trypsin ihibitor precursor [Bos taurus]' . . . . . 100.00 92 100.00 100.00 4.78e-27 . . . . 5358 1 . no EMBL CAA37967 . 'aprotinin [synthetic construct]' . . . . . 100.00 59 100.00 100.00 3.60e-26 . . . . 5358 1 . no GenBank AAA72535 . 'alkaline phosphatase/pancreatic trypsin inhibitor precursor' . . . . . 100.00 79 98.28 100.00 1.24e-26 . . . . 5358 1 . no GenBank AAB25189 . 'major cationic kallikrein inhibitor [cattle, posterior pituitary gland, Peptide, 58 aa]' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no GenBank AAD13685 . 'trypsin inhibitor [Bos taurus]' . . . . . 100.00 100 100.00 100.00 3.43e-27 . . . . 5358 1 . no PRF 1405218A . 'aprotinin analog' . . . . . 98.28 57 100.00 100.00 1.07e-25 . . . . 5358 1 . no PRF 1405218D . 'aprotinin analog' . . . . . 100.00 59 100.00 100.00 3.05e-26 . . . . 5358 1 . no PRF 1510193A . BPTI . . . . . 100.00 100 98.28 100.00 1.02e-26 . . . . 5358 1 . no PRF 681071A . 'inhibitor,basic pancreatic trypsin' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 5358 1 . no SWISS-PROT P00974 . 'Pancreatic trypsin inhibitor precursor (Basic protease inhibitor) (BPTI) (BPI) (Aprotinin)' . . . . . 100.00 100 100.00 100.00 3.43e-27 . . . . 5358 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID BPTI abbreviation 5358 1 'bovine pancreatic trypsin inhibitor' common 5358 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 . ARG . 5358 1 2 . PRO . 5358 1 3 . ASP . 5358 1 4 . PHE . 5358 1 5 . CYS . 5358 1 6 . LEU . 5358 1 7 . GLU . 5358 1 8 . PRO . 5358 1 9 . PRO . 5358 1 10 . TYR . 5358 1 11 . THR . 5358 1 12 . GLY . 5358 1 13 . PRO . 5358 1 14 . CYS . 5358 1 15 . LYS . 5358 1 16 . ALA . 5358 1 17 . ARG . 5358 1 18 . ILE . 5358 1 19 . ILE . 5358 1 20 . ARG . 5358 1 21 . TYR . 5358 1 22 . PHE . 5358 1 23 . TYR . 5358 1 24 . ASN . 5358 1 25 . ALA . 5358 1 26 . LYS . 5358 1 27 . ALA . 5358 1 28 . GLY . 5358 1 29 . LEU . 5358 1 30 . CYS . 5358 1 31 . GLN . 5358 1 32 . THR . 5358 1 33 . PHE . 5358 1 34 . VAL . 5358 1 35 . TYR . 5358 1 36 . GLY . 5358 1 37 . GLY . 5358 1 38 . CYS . 5358 1 39 . ARG . 5358 1 40 . ALA . 5358 1 41 . LYS . 5358 1 42 . ARG . 5358 1 43 . ASN . 5358 1 44 . ASN . 5358 1 45 . PHE . 5358 1 46 . LYS . 5358 1 47 . SER . 5358 1 48 . ALA . 5358 1 49 . GLU . 5358 1 50 . ASP . 5358 1 51 . CYS . 5358 1 52 . MET . 5358 1 53 . ARG . 5358 1 54 . THR . 5358 1 55 . CYS . 5358 1 56 . GLY . 5358 1 57 . GLY . 5358 1 58 . ALA . 5358 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 . ARG 1 1 5358 1 . PRO 2 2 5358 1 . ASP 3 3 5358 1 . PHE 4 4 5358 1 . CYS 5 5 5358 1 . LEU 6 6 5358 1 . GLU 7 7 5358 1 . PRO 8 8 5358 1 . PRO 9 9 5358 1 . TYR 10 10 5358 1 . THR 11 11 5358 1 . GLY 12 12 5358 1 . PRO 13 13 5358 1 . CYS 14 14 5358 1 . LYS 15 15 5358 1 . ALA 16 16 5358 1 . ARG 17 17 5358 1 . ILE 18 18 5358 1 . ILE 19 19 5358 1 . ARG 20 20 5358 1 . TYR 21 21 5358 1 . PHE 22 22 5358 1 . TYR 23 23 5358 1 . ASN 24 24 5358 1 . ALA 25 25 5358 1 . LYS 26 26 5358 1 . ALA 27 27 5358 1 . GLY 28 28 5358 1 . LEU 29 29 5358 1 . CYS 30 30 5358 1 . GLN 31 31 5358 1 . THR 32 32 5358 1 . PHE 33 33 5358 1 . VAL 34 34 5358 1 . TYR 35 35 5358 1 . GLY 36 36 5358 1 . GLY 37 37 5358 1 . CYS 38 38 5358 1 . ARG 39 39 5358 1 . ALA 40 40 5358 1 . LYS 41 41 5358 1 . ARG 42 42 5358 1 . ASN 43 43 5358 1 . ASN 44 44 5358 1 . PHE 45 45 5358 1 . LYS 46 46 5358 1 . SER 47 47 5358 1 . ALA 48 48 5358 1 . GLU 49 49 5358 1 . ASP 50 50 5358 1 . CYS 51 51 5358 1 . MET 52 52 5358 1 . ARG 53 53 5358 1 . THR 54 54 5358 1 . CYS 55 55 5358 1 . GLY 56 56 5358 1 . GLY 57 57 5358 1 . ALA 58 58 5358 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 5358 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $BPTI . 9913 . . 'Bos taurus' Cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . 5358 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 5358 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $BPTI . 'recombinant technology' 'Escherichia coli' E.coli . . Escherichia coli . . . . . . . . . . 5358 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 5358 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 'bovine pancreatic trypsin inhibitor' . . . 1 $BPTI . . 0.75 . . mM . . . . 5358 1 2 CaCl2 . . . . . . . 25 . . mM . . . . 5358 1 3 NaAzide . . . . . . . 3 . . mM . . . . 5358 1 4 H2O . . . . . . . 90 . . % . . . . 5358 1 5 D2O . . . . . . . 10 . . % . . . . 5358 1 stop_ save_ ####################### # Sample conditions # ####################### save_BPTI_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode BPTI_cond_1 _Sample_condition_list.Entry_ID 5358 _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 5.8 . n/a 5358 1 temperature 309 . K 5358 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5358 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer VARIAN _NMR_spectrometer.Model Unity _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5358 _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 NMR_spectrometer VARIAN Unity . 500 . . . 5358 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 5358 _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 HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 2 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 3 (HA)CANH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 4 (HA)CA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 5 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 6 HCACO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5358 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5358 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS . . . . . ppm . . indirect 0.251449537 . . . . . 5358 1 H 1 DSS . . . . . ppm 0.00 external direct 1.0 external cylindrical . . . 5358 1 N 15 DSS . . . . . ppm . . indirect 0.101329118 . . . . . 5358 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_BPTI_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode BPTI_shifts_1 _Assigned_chem_shift_list.Entry_ID 5358 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $BPTI_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 HSQC 1 $Sample_1 . 5358 1 2 HNCA 1 $Sample_1 . 5358 1 3 (HA)CANH 1 $Sample_1 . 5358 1 4 (HA)CA(CO)NH 1 $Sample_1 . 5358 1 5 HNCO 1 $Sample_1 . 5358 1 6 HCACO 1 $Sample_1 . 5358 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.Ambiguity_set_ID _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 2 2 PRO C C 13 177.7 . . 1 . . . . . . . . . 5358 1 2 . 1 1 2 2 PRO CA C 13 63.1 . . 1 . . . . . . . . . 5358 1 3 . 1 1 2 2 PRO HA H 1 4.42 . . 1 . . . . . . . . . 5358 1 4 . 1 1 3 3 ASP N N 15 124.0 . . 1 . . . . . . . . . 5358 1 5 . 1 1 3 3 ASP H H 1 8.74 . . 1 . . . . . . . . . 5358 1 6 . 1 1 3 3 ASP C C 13 180.1 . . 1 . . . . . . . . . 5358 1 7 . 1 1 3 3 ASP CA C 13 57.4 . . 1 . . . . . . . . . 5358 1 8 . 1 1 3 3 ASP HA H 1 4.38 . . 1 . . . . . . . . . 5358 1 9 . 1 1 4 4 PHE N N 15 117.0 . . 1 . . . . . . . . . 5358 1 10 . 1 1 4 4 PHE H H 1 7.89 . . 1 . . . . . . . . . 5358 1 11 . 1 1 4 4 PHE C C 13 177.6 . . 1 . . . . . . . . . 5358 1 12 . 1 1 4 4 PHE CA C 13 59.2 . . 1 . . . . . . . . . 5358 1 13 . 1 1 4 4 PHE HA H 1 4.70 . . 1 . . . . . . . . . 5358 1 14 . 1 1 5 5 CYS N N 15 121.7 . . 1 . . . . . . . . . 5358 1 15 . 1 1 5 5 CYS H H 1 7.51 . . 1 . . . . . . . . . 5358 1 16 . 1 1 5 5 CYS C C 13 173.4 . . 1 . . . . . . . . . 5358 1 17 . 1 1 5 5 CYS CA C 13 57.9 . . 1 . . . . . . . . . 5358 1 18 . 1 1 5 5 CYS HA H 1 4.46 . . 1 . . . . . . . . . 5358 1 19 . 1 1 6 6 LEU N N 15 114.4 . . 1 . . . . . . . . . 5358 1 20 . 1 1 6 6 LEU H H 1 7.66 . . 1 . . . . . . . . . 5358 1 21 . 1 1 6 6 LEU C C 13 178.6 . . 1 . . . . . . . . . 5358 1 22 . 1 1 6 6 LEU CA C 13 54.8 . . 1 . . . . . . . . . 5358 1 23 . 1 1 6 6 LEU HA H 1 4.61 . . 1 . . . . . . . . . 5358 1 24 . 1 1 7 7 GLU N N 15 121.0 . . 1 . . . . . . . . . 5358 1 25 . 1 1 7 7 GLU H H 1 7.59 . . 1 . . . . . . . . . 5358 1 26 . 1 1 7 7 GLU C C 13 175.0 . . 1 . . . . . . . . . 5358 1 27 . 1 1 7 7 GLU CA C 13 55.0 . . 1 . . . . . . . . . 5358 1 28 . 1 1 7 7 GLU HA H 1 4.68 . . 1 . . . . . . . . . 5358 1 29 . 1 1 8 8 PRO C C 13 174.7 . . 1 . . . . . . . . . 5358 1 30 . 1 1 8 8 PRO CA C 13 61.9 . . 1 . . . . . . . . . 5358 1 31 . 1 1 8 8 PRO HA H 1 4.74 . . 1 . . . . . . . . . 5358 1 32 . 1 1 9 9 PRO C C 13 176.1 . . 1 . . . . . . . . . 5358 1 33 . 1 1 9 9 PRO CA C 13 62.7 . . 1 . . . . . . . . . 5358 1 34 . 1 1 9 9 PRO HA H 1 3.84 . . 1 . . . . . . . . . 5358 1 35 . 1 1 10 10 TYR N N 15 123.9 . . 1 . . . . . . . . . 5358 1 36 . 1 1 10 10 TYR H H 1 7.88 . . 1 . . . . . . . . . 5358 1 37 . 1 1 10 10 TYR C C 13 175.3 . . 1 . . . . . . . . . 5358 1 38 . 1 1 10 10 TYR CA C 13 56.6 . . 1 . . . . . . . . . 5358 1 39 . 1 1 10 10 TYR HA H 1 5.03 . . 1 . . . . . . . . . 5358 1 40 . 1 1 11 11 THR N N 15 129.2 . . 1 . . . . . . . . . 5358 1 41 . 1 1 11 11 THR H H 1 9.05 . . 1 . . . . . . . . . 5358 1 42 . 1 1 11 11 THR C C 13 177.0 . . 1 . . . . . . . . . 5358 1 43 . 1 1 11 11 THR CA C 13 67.4 . . 1 . . . . . . . . . 5358 1 44 . 1 1 11 11 THR HA H 1 4.72 . . 1 . . . . . . . . . 5358 1 45 . 1 1 12 12 GLY N N 15 107.5 . . 1 . . . . . . . . . 5358 1 46 . 1 1 12 12 GLY H H 1 7.34 . . 1 . . . . . . . . . 5358 1 47 . 1 1 12 12 GLY CA C 13 46.1 . . 1 . . . . . . . . . 5358 1 48 . 1 1 13 13 PRO C C 13 179.6 . . 1 . . . . . . . . . 5358 1 49 . 1 1 13 13 PRO CA C 13 64.3 . . 1 . . . . . . . . . 5358 1 50 . 1 1 13 13 PRO HA H 1 5.10 . . 1 . . . . . . . . . 5358 1 51 . 1 1 14 14 CYS N N 15 119.1 . . 1 . . . . . . . . . 5358 1 52 . 1 1 14 14 CYS H H 1 8.56 . . 1 . . . . . . . . . 5358 1 53 . 1 1 14 14 CYS C C 13 175.4 . . 1 . . . . . . . . . 5358 1 54 . 1 1 14 14 CYS CA C 13 61.1 . . 1 . . . . . . . . . 5358 1 55 . 1 1 15 15 LYS N N 15 118.6 . . 1 . . . . . . . . . 5358 1 56 . 1 1 15 15 LYS H H 1 6.76 . . 1 . . . . . . . . . 5358 1 57 . 1 1 15 15 LYS C C 13 178.3 . . 1 . . . . . . . . . 5358 1 58 . 1 1 15 15 LYS CA C 13 58.4 . . 1 . . . . . . . . . 5358 1 59 . 1 1 15 15 LYS HA H 1 4.67 . . 1 . . . . . . . . . 5358 1 60 . 1 1 16 16 ALA N N 15 126.1 . . 1 . . . . . . . . . 5358 1 61 . 1 1 16 16 ALA H H 1 9.35 . . 1 . . . . . . . . . 5358 1 62 . 1 1 16 16 ALA C C 13 175.1 . . 1 . . . . . . . . . 5358 1 63 . 1 1 16 16 ALA CA C 13 52.8 . . 1 . . . . . . . . . 5358 1 64 . 1 1 17 17 ARG N N 15 118.9 . . 1 . . . . . . . . . 5358 1 65 . 1 1 17 17 ARG H H 1 8.55 . . 1 . . . . . . . . . 5358 1 66 . 1 1 17 17 ARG C C 13 173.3 . . 1 . . . . . . . . . 5358 1 67 . 1 1 17 17 ARG CA C 13 55.2 . . 1 . . . . . . . . . 5358 1 68 . 1 1 18 18 ILE N N 15 123.8 . . 1 . . . . . . . . . 5358 1 69 . 1 1 18 18 ILE H H 1 8.13 . . 1 . . . . . . . . . 5358 1 70 . 1 1 18 18 ILE C C 13 176.2 . . 1 . . . . . . . . . 5358 1 71 . 1 1 18 18 ILE CA C 13 60.4 . . 1 . . . . . . . . . 5358 1 72 . 1 1 18 18 ILE HA H 1 4.69 . . 1 . . . . . . . . . 5358 1 73 . 1 1 19 19 ILE N N 15 127.9 . . 1 . . . . . . . . . 5358 1 74 . 1 1 19 19 ILE H H 1 8.28 . . 1 . . . . . . . . . 5358 1 75 . 1 1 19 19 ILE C C 13 176.4 . . 1 . . . . . . . . . 5358 1 76 . 1 1 19 19 ILE CA C 13 61.7 . . 1 . . . . . . . . . 5358 1 77 . 1 1 19 19 ILE HA H 1 4.22 . . 1 . . . . . . . . . 5358 1 78 . 1 1 20 20 ARG N N 15 130.8 . . 1 . . . . . . . . . 5358 1 79 . 1 1 20 20 ARG H H 1 8.36 . . 1 . . . . . . . . . 5358 1 80 . 1 1 20 20 ARG C C 13 173.5 . . 1 . . . . . . . . . 5358 1 81 . 1 1 20 20 ARG CA C 13 52.0 . . 1 . . . . . . . . . 5358 1 82 . 1 1 20 20 ARG HA H 1 4.26 . . 1 . . . . . . . . . 5358 1 83 . 1 1 21 21 TYR N N 15 115.8 . . 1 . . . . . . . . . 5358 1 84 . 1 1 21 21 TYR H H 1 9.23 . . 1 . . . . . . . . . 5358 1 85 . 1 1 21 21 TYR C C 13 175.8 . . 1 . . . . . . . . . 5358 1 86 . 1 1 21 21 TYR CA C 13 57.5 . . 1 . . . . . . . . . 5358 1 87 . 1 1 21 21 TYR HA H 1 5.78 . . 1 . . . . . . . . . 5358 1 88 . 1 1 22 22 PHE N N 15 120.5 . . 1 . . . . . . . . . 5358 1 89 . 1 1 22 22 PHE H H 1 9.86 . . 1 . . . . . . . . . 5358 1 90 . 1 1 22 22 PHE C C 13 173.1 . . 1 . . . . . . . . . 5358 1 91 . 1 1 22 22 PHE CA C 13 55.2 . . 1 . . . . . . . . . 5358 1 92 . 1 1 22 22 PHE HA H 1 5.35 . . 1 . . . . . . . . . 5358 1 93 . 1 1 23 23 TYR N N 15 125.7 . . 1 . . . . . . . . . 5358 1 94 . 1 1 23 23 TYR H H 1 10.61 . . 1 . . . . . . . . . 5358 1 95 . 1 1 23 23 TYR C C 13 173.9 . . 1 . . . . . . . . . 5358 1 96 . 1 1 23 23 TYR CA C 13 59.9 . . 1 . . . . . . . . . 5358 1 97 . 1 1 23 23 TYR HA H 1 4.42 . . 1 . . . . . . . . . 5358 1 98 . 1 1 24 24 ASN N N 15 126.0 . . 1 . . . . . . . . . 5358 1 99 . 1 1 24 24 ASN H H 1 7.81 . . 1 . . . . . . . . . 5358 1 100 . 1 1 24 24 ASN C C 13 175.5 . . 1 . . . . . . . . . 5358 1 101 . 1 1 24 24 ASN CA C 13 50.8 . . 1 . . . . . . . . . 5358 1 102 . 1 1 24 24 ASN HA H 1 4.69 . . 1 . . . . . . . . . 5358 1 103 . 1 1 25 25 ALA N N 15 127.0 . . 1 . . . . . . . . . 5358 1 104 . 1 1 25 25 ALA H H 1 8.85 . . 1 . . . . . . . . . 5358 1 105 . 1 1 25 25 ALA C C 13 179.6 . . 1 . . . . . . . . . 5358 1 106 . 1 1 25 25 ALA CA C 13 55.0 . . 1 . . . . . . . . . 5358 1 107 . 1 1 25 25 ALA HA H 1 3.87 . . 1 . . . . . . . . . 5358 1 108 . 1 1 26 26 LYS N N 15 117.5 . . 1 . . . . . . . . . 5358 1 109 . 1 1 26 26 LYS H H 1 7.98 . . 1 . . . . . . . . . 5358 1 110 . 1 1 26 26 LYS C C 13 177.8 . . 1 . . . . . . . . . 5358 1 111 . 1 1 26 26 LYS CA C 13 58.8 . . 1 . . . . . . . . . 5358 1 112 . 1 1 26 26 LYS HA H 1 4.14 . . 1 . . . . . . . . . 5358 1 113 . 1 1 27 27 ALA N N 15 119.0 . . 1 . . . . . . . . . 5358 1 114 . 1 1 27 27 ALA H H 1 6.88 . . 1 . . . . . . . . . 5358 1 115 . 1 1 27 27 ALA C C 13 178.2 . . 1 . . . . . . . . . 5358 1 116 . 1 1 27 27 ALA CA C 13 52.0 . . 1 . . . . . . . . . 5358 1 117 . 1 1 27 27 ALA HA H 1 4.38 . . 1 . . . . . . . . . 5358 1 118 . 1 1 28 28 GLY N N 15 107.1 . . 1 . . . . . . . . . 5358 1 119 . 1 1 28 28 GLY H H 1 8.21 . . 1 . . . . . . . . . 5358 1 120 . 1 1 28 28 GLY C C 13 173.8 . . 1 . . . . . . . . . 5358 1 121 . 1 1 28 28 GLY CA C 13 46.0 . . 1 . . . . . . . . . 5358 1 122 . 1 1 29 29 LEU N N 15 115.0 . . 1 . . . . . . . . . 5358 1 123 . 1 1 29 29 LEU H H 1 6.88 . . 1 . . . . . . . . . 5358 1 124 . 1 1 29 29 LEU C C 13 175.8 . . 1 . . . . . . . . . 5358 1 125 . 1 1 29 29 LEU CA C 13 53.9 . . 1 . . . . . . . . . 5358 1 126 . 1 1 29 29 LEU HA H 1 4.85 . . 1 . . . . . . . . . 5358 1 127 . 1 1 30 30 CYS N N 15 118.2 . . 1 . . . . . . . . . 5358 1 128 . 1 1 30 30 CYS H H 1 8.44 . . 1 . . . . . . . . . 5358 1 129 . 1 1 30 30 CYS C C 13 174.0 . . 1 . . . . . . . . . 5358 1 130 . 1 1 30 30 CYS CA C 13 58.0 . . 1 . . . . . . . . . 5358 1 131 . 1 1 31 31 GLN N N 15 123.5 . . 1 . . . . . . . . . 5358 1 132 . 1 1 31 31 GLN H H 1 8.83 . . 1 . . . . . . . . . 5358 1 133 . 1 1 31 31 GLN C C 13 174.4 . . 1 . . . . . . . . . 5358 1 134 . 1 1 31 31 GLN CA C 13 54.1 . . 1 . . . . . . . . . 5358 1 135 . 1 1 32 32 THR N N 15 109.0 . . 1 . . . . . . . . . 5358 1 136 . 1 1 32 32 THR H H 1 8.13 . . 1 . . . . . . . . . 5358 1 137 . 1 1 32 32 THR C C 13 175.5 . . 1 . . . . . . . . . 5358 1 138 . 1 1 32 32 THR CA C 13 60.7 . . 1 . . . . . . . . . 5358 1 139 . 1 1 32 32 THR HA H 1 5.36 . . 1 . . . . . . . . . 5358 1 140 . 1 1 33 33 PHE N N 15 119.3 . . 1 . . . . . . . . . 5358 1 141 . 1 1 33 33 PHE H H 1 9.38 . . 1 . . . . . . . . . 5358 1 142 . 1 1 33 33 PHE C C 13 172.0 . . 1 . . . . . . . . . 5358 1 143 . 1 1 33 33 PHE CA C 13 55.7 . . 1 . . . . . . . . . 5358 1 144 . 1 1 33 33 PHE HA H 1 4.96 . . 1 . . . . . . . . . 5358 1 145 . 1 1 34 34 VAL N N 15 118.0 . . 1 . . . . . . . . . 5358 1 146 . 1 1 34 34 VAL H H 1 8.45 . . 1 . . . . . . . . . 5358 1 147 . 1 1 34 34 VAL C C 13 173.1 . . 1 . . . . . . . . . 5358 1 148 . 1 1 34 34 VAL CA C 13 63.1 . . 1 . . . . . . . . . 5358 1 149 . 1 1 34 34 VAL HA H 1 3.94 . . 1 . . . . . . . . . 5358 1 150 . 1 1 35 35 TYR N N 15 130.7 . . 1 . . . . . . . . . 5358 1 151 . 1 1 35 35 TYR H H 1 9.55 . . 1 . . . . . . . . . 5358 1 152 . 1 1 35 35 TYR C C 13 174.8 . . 1 . . . . . . . . . 5358 1 153 . 1 1 35 35 TYR CA C 13 54.7 . . 1 . . . . . . . . . 5358 1 154 . 1 1 36 36 GLY N N 15 115.7 . . 1 . . . . . . . . . 5358 1 155 . 1 1 36 36 GLY H H 1 9.02 . . 1 . . . . . . . . . 5358 1 156 . 1 1 37 37 GLY N N 15 98.3 . . 1 . . . . . . . . . 5358 1 157 . 1 1 37 37 GLY H H 1 4.40 . . 1 . . . . . . . . . 5358 1 158 . 1 1 37 37 GLY C C 13 173.3 . . 1 . . . . . . . . . 5358 1 159 . 1 1 38 38 CYS N N 15 116.0 . . 1 . . . . . . . . . 5358 1 160 . 1 1 38 38 CYS H H 1 8.05 . . 1 . . . . . . . . . 5358 1 161 . 1 1 38 38 CYS C C 13 173.8 . . 1 . . . . . . . . . 5358 1 162 . 1 1 38 38 CYS CA C 13 55.6 . . 1 . . . . . . . . . 5358 1 163 . 1 1 38 38 CYS HA H 1 4.90 . . 1 . . . . . . . . . 5358 1 164 . 1 1 39 39 ARG N N 15 113.7 . . 1 . . . . . . . . . 5358 1 165 . 1 1 39 39 ARG H H 1 9.35 . . 1 . . . . . . . . . 5358 1 166 . 1 1 39 39 ARG C C 13 174.7 . . 1 . . . . . . . . . 5358 1 167 . 1 1 39 39 ARG CA C 13 57.1 . . 1 . . . . . . . . . 5358 1 168 . 1 1 39 39 ARG HA H 1 4.03 . . 1 . . . . . . . . . 5358 1 169 . 1 1 40 40 ALA N N 15 117.9 . . 1 . . . . . . . . . 5358 1 170 . 1 1 40 40 ALA H H 1 7.40 . . 1 . . . . . . . . . 5358 1 171 . 1 1 40 40 ALA C C 13 180.4 . . 1 . . . . . . . . . 5358 1 172 . 1 1 40 40 ALA CA C 13 53.9 . . 1 . . . . . . . . . 5358 1 173 . 1 1 41 41 LYS N N 15 121.4 . . 1 . . . . . . . . . 5358 1 174 . 1 1 41 41 LYS H H 1 8.34 . . 1 . . . . . . . . . 5358 1 175 . 1 1 41 41 LYS C C 13 176.9 . . 1 . . . . . . . . . 5358 1 176 . 1 1 41 41 LYS CA C 13 55.5 . . 1 . . . . . . . . . 5358 1 177 . 1 1 41 41 LYS HA H 1 4.54 . . 1 . . . . . . . . . 5358 1 178 . 1 1 42 42 ARG N N 15 116.2 . . 1 . . . . . . . . . 5358 1 179 . 1 1 42 42 ARG H H 1 8.41 . . 1 . . . . . . . . . 5358 1 180 . 1 1 42 42 ARG C C 13 178.0 . . 1 . . . . . . . . . 5358 1 181 . 1 1 42 42 ARG CA C 13 59.0 . . 1 . . . . . . . . . 5358 1 182 . 1 1 42 42 ARG HA H 1 3.75 . . 1 . . . . . . . . . 5358 1 183 . 1 1 43 43 ASN N N 15 116.8 . . 1 . . . . . . . . . 5358 1 184 . 1 1 43 43 ASN H H 1 7.31 . . 1 . . . . . . . . . 5358 1 185 . 1 1 43 43 ASN C C 13 174.9 . . 1 . . . . . . . . . 5358 1 186 . 1 1 43 43 ASN CA C 13 51.1 . . 1 . . . . . . . . . 5358 1 187 . 1 1 44 44 ASN N N 15 121.3 . . 1 . . . . . . . . . 5358 1 188 . 1 1 44 44 ASN H H 1 6.87 . . 1 . . . . . . . . . 5358 1 189 . 1 1 44 44 ASN C C 13 174.4 . . 1 . . . . . . . . . 5358 1 190 . 1 1 44 44 ASN CA C 13 54.1 . . 1 . . . . . . . . . 5358 1 191 . 1 1 45 45 PHE N N 15 123.0 . . 1 . . . . . . . . . 5358 1 192 . 1 1 45 45 PHE H H 1 10.02 . . 1 . . . . . . . . . 5358 1 193 . 1 1 45 45 PHE C C 13 176.7 . . 1 . . . . . . . . . 5358 1 194 . 1 1 45 45 PHE CA C 13 56.3 . . 1 . . . . . . . . . 5358 1 195 . 1 1 45 45 PHE HA H 1 5.24 . . 1 . . . . . . . . . 5358 1 196 . 1 1 46 46 LYS N N 15 120.9 . . 1 . . . . . . . . . 5358 1 197 . 1 1 46 46 LYS H H 1 10.01 . . 1 . . . . . . . . . 5358 1 198 . 1 1 46 46 LYS C C 13 176.2 . . 1 . . . . . . . . . 5358 1 199 . 1 1 46 46 LYS CA C 13 58.5 . . 1 . . . . . . . . . 5358 1 200 . 1 1 46 46 LYS HA H 1 4.49 . . 1 . . . . . . . . . 5358 1 201 . 1 1 47 47 SER N N 15 109.2 . . 1 . . . . . . . . . 5358 1 202 . 1 1 47 47 SER H H 1 7.54 . . 1 . . . . . . . . . 5358 1 203 . 1 1 47 47 SER C C 13 173.6 . . 1 . . . . . . . . . 5358 1 204 . 1 1 47 47 SER CA C 13 56.4 . . 1 . . . . . . . . . 5358 1 205 . 1 1 47 47 SER HA H 1 4.61 . . 1 . . . . . . . . . 5358 1 206 . 1 1 48 48 ALA N N 15 126.0 . . 1 . . . . . . . . . 5358 1 207 . 1 1 48 48 ALA H H 1 8.23 . . 1 . . . . . . . . . 5358 1 208 . 1 1 48 48 ALA C C 13 179.7 . . 1 . . . . . . . . . 5358 1 209 . 1 1 48 48 ALA CA C 13 55.4 . . 1 . . . . . . . . . 5358 1 210 . 1 1 48 48 ALA HA H 1 3.22 . . 1 . . . . . . . . . 5358 1 211 . 1 1 49 49 GLU N N 15 118.2 . . 1 . . . . . . . . . 5358 1 212 . 1 1 49 49 GLU H H 1 8.68 . . 1 . . . . . . . . . 5358 1 213 . 1 1 49 49 GLU C C 13 179.6 . . 1 . . . . . . . . . 5358 1 214 . 1 1 49 49 GLU CA C 13 60.5 . . 1 . . . . . . . . . 5358 1 215 . 1 1 49 49 GLU HA H 1 3.94 . . 1 . . . . . . . . . 5358 1 216 . 1 1 50 50 ASP N N 15 120.7 . . 1 . . . . . . . . . 5358 1 217 . 1 1 50 50 ASP H H 1 7.92 . . 1 . . . . . . . . . 5358 1 218 . 1 1 50 50 ASP C C 13 178.0 . . 1 . . . . . . . . . 5358 1 219 . 1 1 50 50 ASP CA C 13 57.6 . . 1 . . . . . . . . . 5358 1 220 . 1 1 50 50 ASP HA H 1 4.37 . . 1 . . . . . . . . . 5358 1 221 . 1 1 51 51 CYS N N 15 120.1 . . 1 . . . . . . . . . 5358 1 222 . 1 1 51 51 CYS H H 1 7.04 . . 1 . . . . . . . . . 5358 1 223 . 1 1 51 51 CYS C C 13 175.6 . . 1 . . . . . . . . . 5358 1 224 . 1 1 51 51 CYS CA C 13 58.9 . . 1 . . . . . . . . . 5358 1 225 . 1 1 51 51 CYS HA H 1 1.79 . . 1 . . . . . . . . . 5358 1 226 . 1 1 52 52 MET N N 15 121.5 . . 1 . . . . . . . . . 5358 1 227 . 1 1 52 52 MET C C 13 180.4 . . 1 . . . . . . . . . 5358 1 228 . 1 1 52 52 MET CA C 13 56.7 . . 1 . . . . . . . . . 5358 1 229 . 1 1 52 52 MET HA H 1 4.26 . . 1 . . . . . . . . . 5358 1 230 . 1 1 53 53 ARG N N 15 121.7 . . 1 . . . . . . . . . 5358 1 231 . 1 1 53 53 ARG H H 1 8.35 . . 1 . . . . . . . . . 5358 1 232 . 1 1 53 53 ARG C C 13 178.5 . . 1 . . . . . . . . . 5358 1 233 . 1 1 53 53 ARG CA C 13 59.5 . . 1 . . . . . . . . . 5358 1 234 . 1 1 53 53 ARG HA H 1 4.06 . . 1 . . . . . . . . . 5358 1 235 . 1 1 54 54 THR N N 15 113.7 . . 1 . . . . . . . . . 5358 1 236 . 1 1 54 54 THR H H 1 7.48 . . 1 . . . . . . . . . 5358 1 237 . 1 1 54 54 THR C C 13 176.5 . . 1 . . . . . . . . . 5358 1 238 . 1 1 54 54 THR CA C 13 66.3 . . 1 . . . . . . . . . 5358 1 239 . 1 1 54 54 THR HA H 1 4.18 . . 1 . . . . . . . . . 5358 1 240 . 1 1 55 55 CYS N N 15 115.2 . . 1 . . . . . . . . . 5358 1 241 . 1 1 55 55 CYS H H 1 8.30 . . 1 . . . . . . . . . 5358 1 242 . 1 1 55 55 CYS C C 13 174.1 . . 1 . . . . . . . . . 5358 1 243 . 1 1 55 55 CYS CA C 13 54.5 . . 1 . . . . . . . . . 5358 1 244 . 1 1 55 55 CYS HA H 1 4.73 . . 1 . . . . . . . . . 5358 1 245 . 1 1 56 56 GLY N N 15 107.9 . . 1 . . . . . . . . . 5358 1 246 . 1 1 56 56 GLY H H 1 8.01 . . 1 . . . . . . . . . 5358 1 247 . 1 1 56 56 GLY C C 13 174.8 . . 1 . . . . . . . . . 5358 1 248 . 1 1 56 56 GLY CA C 13 46.7 . . 1 . . . . . . . . . 5358 1 249 . 1 1 57 57 GLY N N 15 109.5 . . 1 . . . . . . . . . 5358 1 250 . 1 1 57 57 GLY H H 1 8.26 . . 1 . . . . . . . . . 5358 1 251 . 1 1 57 57 GLY C C 13 172.6 . . 1 . . . . . . . . . 5358 1 252 . 1 1 57 57 GLY CA C 13 45.2 . . 1 . . . . . . . . . 5358 1 253 . 1 1 58 58 ALA N N 15 129.9 . . 1 . . . . . . . . . 5358 1 254 . 1 1 58 58 ALA H H 1 8.01 . . 1 . . . . . . . . . 5358 1 255 . 1 1 58 58 ALA CA C 13 54.4 . . 1 . . . . . . . . . 5358 1 stop_ save_