data_4968 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4968 _Entry.Title ; Bovine Pancreatic Trypsin Inhibitor pH 5.8 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-03-07 _Entry.Accession_date 2001-03-07 _Entry.Last_release_date 2001-03-07 _Entry.Original_release_date 2001-03-07 _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 Daniel Monleon . . . . 4968 2 Michael Baran . C. . . 4968 3 Gaetano Montelione . T. . . 4968 4 Parag Sahasrabudhe . . . . 4968 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4968 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 119 4968 '15N chemical shifts' 52 4968 '1H chemical shifts' 358 4968 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2002-02-26 . original author 'Original release.' 4968 1 . . 2002-04-30 . update author 'Update of chemical shift table.' 4968 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5307 'Time domain data of BPTI at pH 5.8' 4968 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4968 _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 ; Rapid Data Collection and Analysis of Protein Resonance Assignments Using AutoProc, AutoPeak, and AutoAssign Software ; _Citation.Status submitted _Citation.Type journal _Citation.Journal_abbrev 'J. Struct. Funct. Genomics' _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 . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _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 Daniel Monleon . . . . 4968 1 2 Hunter Moseley . N.B. . . 4968 1 3 Kimberly Colson . . . . 4968 1 4 Clemens Anklin . . . . 4968 1 5 Robert Oswald . . . . 4968 1 6 Thomas Szyperski . A. . . 4968 1 7 Gaetano Montelione . T. . . 4968 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_BPTI _Assembly.Sf_category assembly _Assembly.Sf_framecode system_BPTI _Assembly.Entry_ID 4968 _Assembly.ID 1 _Assembly.Name 'Bovine Pancreatic Trypsin Inhibitor monomer' _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 4968 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_monomer . . . native . . . . . 4968 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 . . . . . . . . . . . . 4968 1 2 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 38 38 SG . . . . . . . . . . . . 4968 1 3 disulfide single . 1 . 1 CYS 30 30 SG . 1 . 1 CYS 51 51 SG . . . . . . . . . . . . 4968 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID BPTI abbreviation 4968 1 'Bovine Pancreatic Trypsin Inhibitor monomer' system 4968 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_BPTI_monomer _Entity.Sf_category entity _Entity.Sf_framecode BPTI_monomer _Entity.Entry_ID 4968 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name BPTI _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 . . . . 4968 1 . no BMRB 1156 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 1179 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 236 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 237 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 262 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 263 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 264 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 338 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 411 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 412 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 413 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 414 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 415 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 416 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 419 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 45 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 46 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 48 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 485 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 4868 . BPTI-R52 . . . . . 100.00 58 98.28 98.28 2.63e-25 . . . . 4968 1 . no BMRB 49 . 'basic pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 5171 . BPTI . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 4968 1 . no BMRB 5307 . 'Basic Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 5358 . 'bovine pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no BMRB 5359 . 'bovine pancreatic trypsin inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 1 . no PDB 1BHC . 'Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 1BTH . 'Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 1CBW . 'Bovine Chymotrypsin Complexed To Bpti' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 1EAW . 'Crystal Structure Of The Mtsp1 (Matriptase)-Bpti (Aprotinin) Complex' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no PDB 1F5R . 'Rat Trypsinogen Mutant Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 4968 1 . no PDB 1F7Z . 'Rat Trypsinogen K15a Complexed With Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 4968 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 . . . . 4968 1 . no PDB 1FY8 . 'Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no PDB 1JV8 . 'Nmr Structure Of Bpti Mutant G37a' . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 4968 1 . no PDB 1JV9 . 'Nmr Structure Of Bpti Mutant G37a' . . . . . 100.00 58 98.28 98.28 1.04e-25 . . . . 4968 1 . no PDB 1MTN . 'Bovine Alpha-Chymotrypsin:bpti Crystallization' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 1YKT . 'TrypsinBPTI COMPLEX MUTANT' . . . . . 96.55 56 100.00 100.00 4.09e-25 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 2FTL . 'Crystal Structure Of Trypsin Complexed With Bpti At 100k' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 1 . no PDB 2HEX . 'Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 2R9P . 'Human Mesotrypsin Complexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no PDB 2RA3 . 'Human Cationic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 3TGJ . 'S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' . . . . . 100.00 65 100.00 100.00 3.02e-26 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 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 . . . . 4968 1 . no PDB 6PTI . 'Structure Of Form Iii Crystals Of Bovine Pancreatic Trypsin Inhibitor' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 1 . no PDB 9PTI . 'Basic Pancreatic Trypsin Inhibitor (Met 52 Oxidized)' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no EMBL CAA27062 . 'unnamed protein product [Bos taurus]' . . . . . 100.00 89 100.00 100.00 2.03e-26 . . . . 4968 1 . no EMBL CAA27063 . 'unnamed protein product [Bos taurus]' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 1 . no EMBL CAA28371 . 'unnamed protein product [synthetic construct]' . . . . . 100.00 59 100.00 100.00 2.97e-26 . . . . 4968 1 . no EMBL CAA28886 . 'trypsin ihibitor precursor [Bos taurus]' . . . . . 100.00 92 100.00 100.00 4.78e-27 . . . . 4968 1 . no EMBL CAA37967 . 'aprotinin [synthetic construct]' . . . . . 100.00 59 100.00 100.00 3.60e-26 . . . . 4968 1 . no GenBank AAA72535 . 'alkaline phosphatase/pancreatic trypsin inhibitor precursor' . . . . . 100.00 79 98.28 100.00 1.24e-26 . . . . 4968 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 . . . . 4968 1 . no GenBank AAD13685 . 'trypsin inhibitor [Bos taurus]' . . . . . 100.00 100 100.00 100.00 3.43e-27 . . . . 4968 1 . no PRF 1405218A . 'aprotinin analog' . . . . . 98.28 57 100.00 100.00 1.07e-25 . . . . 4968 1 . no PRF 1405218D . 'aprotinin analog' . . . . . 100.00 59 100.00 100.00 3.05e-26 . . . . 4968 1 . no PRF 1510193A . BPTI . . . . . 100.00 100 98.28 100.00 1.02e-26 . . . . 4968 1 . no PRF 681071A . 'inhibitor,basic pancreatic trypsin' . . . . . 100.00 58 100.00 100.00 3.54e-26 . . . . 4968 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 . . . . 4968 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID BPTI abbreviation 4968 1 BPTI common 4968 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 . 4968 1 2 . PRO . 4968 1 3 . ASP . 4968 1 4 . PHE . 4968 1 5 . CYS . 4968 1 6 . LEU . 4968 1 7 . GLU . 4968 1 8 . PRO . 4968 1 9 . PRO . 4968 1 10 . TYR . 4968 1 11 . THR . 4968 1 12 . GLY . 4968 1 13 . PRO . 4968 1 14 . CYS . 4968 1 15 . LYS . 4968 1 16 . ALA . 4968 1 17 . ARG . 4968 1 18 . ILE . 4968 1 19 . ILE . 4968 1 20 . ARG . 4968 1 21 . TYR . 4968 1 22 . PHE . 4968 1 23 . TYR . 4968 1 24 . ASN . 4968 1 25 . ALA . 4968 1 26 . LYS . 4968 1 27 . ALA . 4968 1 28 . GLY . 4968 1 29 . LEU . 4968 1 30 . CYS . 4968 1 31 . GLN . 4968 1 32 . THR . 4968 1 33 . PHE . 4968 1 34 . VAL . 4968 1 35 . TYR . 4968 1 36 . GLY . 4968 1 37 . GLY . 4968 1 38 . CYS . 4968 1 39 . ARG . 4968 1 40 . ALA . 4968 1 41 . LYS . 4968 1 42 . ARG . 4968 1 43 . ASN . 4968 1 44 . ASN . 4968 1 45 . PHE . 4968 1 46 . LYS . 4968 1 47 . SER . 4968 1 48 . ALA . 4968 1 49 . GLU . 4968 1 50 . ASP . 4968 1 51 . CYS . 4968 1 52 . MET . 4968 1 53 . ARG . 4968 1 54 . THR . 4968 1 55 . CYS . 4968 1 56 . GLY . 4968 1 57 . GLY . 4968 1 58 . ALA . 4968 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 4968 1 . PRO 2 2 4968 1 . ASP 3 3 4968 1 . PHE 4 4 4968 1 . CYS 5 5 4968 1 . LEU 6 6 4968 1 . GLU 7 7 4968 1 . PRO 8 8 4968 1 . PRO 9 9 4968 1 . TYR 10 10 4968 1 . THR 11 11 4968 1 . GLY 12 12 4968 1 . PRO 13 13 4968 1 . CYS 14 14 4968 1 . LYS 15 15 4968 1 . ALA 16 16 4968 1 . ARG 17 17 4968 1 . ILE 18 18 4968 1 . ILE 19 19 4968 1 . ARG 20 20 4968 1 . TYR 21 21 4968 1 . PHE 22 22 4968 1 . TYR 23 23 4968 1 . ASN 24 24 4968 1 . ALA 25 25 4968 1 . LYS 26 26 4968 1 . ALA 27 27 4968 1 . GLY 28 28 4968 1 . LEU 29 29 4968 1 . CYS 30 30 4968 1 . GLN 31 31 4968 1 . THR 32 32 4968 1 . PHE 33 33 4968 1 . VAL 34 34 4968 1 . TYR 35 35 4968 1 . GLY 36 36 4968 1 . GLY 37 37 4968 1 . CYS 38 38 4968 1 . ARG 39 39 4968 1 . ALA 40 40 4968 1 . LYS 41 41 4968 1 . ARG 42 42 4968 1 . ASN 43 43 4968 1 . ASN 44 44 4968 1 . PHE 45 45 4968 1 . LYS 46 46 4968 1 . SER 47 47 4968 1 . ALA 48 48 4968 1 . GLU 49 49 4968 1 . ASP 50 50 4968 1 . CYS 51 51 4968 1 . MET 52 52 4968 1 . ARG 53 53 4968 1 . THR 54 54 4968 1 . CYS 55 55 4968 1 . GLY 56 56 4968 1 . GLY 57 57 4968 1 . ALA 58 58 4968 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 4968 _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_monomer . 9913 . . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . 4968 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 4968 _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_monomer . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli n/a . . . . . n/a . . . 4968 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 4968 _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 BPTI '[U-100% 13C; U-100% 15N]' . . 1 $BPTI_monomer . . 0.9 . . mM . . . . 4968 1 2 D2O . . . . . . . 5 . . % . . . . 4968 1 3 NaOAc . . . . . . . 20 . . mM . . . . 4968 1 4 CaCl2 . . . . . . . 25 . . mM . . . . 4968 1 5 NaN3 . . . . . . . 0.02 . . % . . . . 4968 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 4968 _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 0.1 n/a 4968 1 temperature 303 0.2 K 4968 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4968 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer VARIAN _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4968 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer VARIAN _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4968 _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_1 VARIAN INOVA . 500 . . . 4968 1 2 NMR_spectrometer_2 VARIAN INOVA . 600 . . . 4968 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 4968 _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 'N15 HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 2 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 3 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 4 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 5 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 6 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 7 HN(CA)CO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 8 'HCCH TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 1 9 'HC(CO)CH TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4968 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 4968 _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 . . . . . 4968 1 H 1 DSS . . . . . ppm 0.00 external direct 1.0 external cylindrical . . . 4968 1 N 15 DSS . . . . . ppm . . indirect 0.101329118 . . . . . 4968 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 4968 _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 'N15 HSQC' 1 $Sample_1 . 4968 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 1 1 ARG HA H 1 4.538 . . 1 . . . . . . . . . 4968 1 2 . 1 1 1 1 ARG HB2 H 1 2.058 . . 2 . . . . . . . . . 4968 1 3 . 1 1 1 1 ARG CA C 13 53.720 . . 1 . . . . . . . . . 4968 1 4 . 1 1 1 1 ARG HB3 H 1 1.978 . . 2 . . . . . . . . . 4968 1 5 . 1 1 2 2 PRO HG3 H 1 1.778 . . 2 . . . . . . . . . 4968 1 6 . 1 1 2 2 PRO CA C 13 63.720 . . 1 . . . . . . . . . 4968 1 7 . 1 1 2 2 PRO CD C 13 51.720 . . 1 . . . . . . . . . 4968 1 8 . 1 1 2 2 PRO HA H 1 4.508 . . 1 . . . . . . . . . 4968 1 9 . 1 1 2 2 PRO HD2 H 1 3.908 . . 2 . . . . . . . . . 4968 1 10 . 1 1 2 2 PRO HD3 H 1 3.778 . . 2 . . . . . . . . . 4968 1 11 . 1 1 3 3 ASP H H 1 8.644 . . 1 . . . . . . . . . 4968 1 12 . 1 1 3 3 ASP HA H 1 4.428 . . 1 . . . . . . . . . 4968 1 13 . 1 1 3 3 ASP HB2 H 1 2.948 . . 1 . . . . . . . . . 4968 1 14 . 1 1 3 3 ASP CA C 13 57.720 . . 1 . . . . . . . . . 4968 1 15 . 1 1 3 3 ASP HB3 H 1 2.948 . . 1 . . . . . . . . . 4968 1 16 . 1 1 3 3 ASP N N 15 123.360 . . 1 . . . . . . . . . 4968 1 17 . 1 1 4 4 PHE HZ H 1 7.488 . . 1 . . . . . . . . . 4968 1 18 . 1 1 4 4 PHE H H 1 7.804 . . 1 . . . . . . . . . 4968 1 19 . 1 1 4 4 PHE CD1 C 13 133.220 . . 1 . . . . . . . . . 4968 1 20 . 1 1 4 4 PHE CE1 C 13 132.720 . . 1 . . . . . . . . . 4968 1 21 . 1 1 4 4 PHE CD2 C 13 133.220 . . 1 . . . . . . . . . 4968 1 22 . 1 1 4 4 PHE HA H 1 4.768 . . 1 . . . . . . . . . 4968 1 23 . 1 1 4 4 PHE CE2 C 13 132.720 . . 1 . . . . . . . . . 4968 1 24 . 1 1 4 4 PHE HB2 H 1 3.528 . . 2 . . . . . . . . . 4968 1 25 . 1 1 4 4 PHE HD1 H 1 7.178 . . 1 . . . . . . . . . 4968 1 26 . 1 1 4 4 PHE HB3 H 1 3.118 . . 2 . . . . . . . . . 4968 1 27 . 1 1 4 4 PHE CZ C 13 130.720 . . 1 . . . . . . . . . 4968 1 28 . 1 1 4 4 PHE HE1 H 1 7.548 . . 1 . . . . . . . . . 4968 1 29 . 1 1 4 4 PHE HD2 H 1 7.178 . . 1 . . . . . . . . . 4968 1 30 . 1 1 4 4 PHE N N 15 115.660 . . 1 . . . . . . . . . 4968 1 31 . 1 1 4 4 PHE HE2 H 1 7.548 . . 1 . . . . . . . . . 4968 1 32 . 1 1 5 5 CYS H H 1 7.434 . . 1 . . . . . . . . . 4968 1 33 . 1 1 5 5 CYS HA H 1 4.528 . . 1 . . . . . . . . . 4968 1 34 . 1 1 5 5 CYS HB2 H 1 2.918 . . 2 . . . . . . . . . 4968 1 35 . 1 1 5 5 CYS CA C 13 58.220 . . 1 . . . . . . . . . 4968 1 36 . 1 1 5 5 CYS HB3 H 1 3.038 . . 2 . . . . . . . . . 4968 1 37 . 1 1 5 5 CYS N N 15 120.660 . . 1 . . . . . . . . . 4968 1 38 . 1 1 6 6 LEU CA C 13 54.720 . . 1 . . . . . . . . . 4968 1 39 . 1 1 6 6 LEU H H 1 7.544 . . 1 . . . . . . . . . 4968 1 40 . 1 1 6 6 LEU CD1 C 13 23.720 . . 2 . . . . . . . . . 4968 1 41 . 1 1 6 6 LEU CD2 C 13 25.220 . . 2 . . . . . . . . . 4968 1 42 . 1 1 6 6 LEU HA H 1 4.668 . . 1 . . . . . . . . . 4968 1 43 . 1 1 6 6 LEU CG C 13 28.220 . . 1 . . . . . . . . . 4968 1 44 . 1 1 6 6 LEU HB2 H 1 2.028 . . 1 . . . . . . . . . 4968 1 45 . 1 1 6 6 LEU HB3 H 1 2.028 . . 1 . . . . . . . . . 4968 1 46 . 1 1 6 6 LEU HD11 H 1 1.028 . . 2 . . . . . . . . . 4968 1 47 . 1 1 6 6 LEU HD12 H 1 1.028 . . 2 . . . . . . . . . 4968 1 48 . 1 1 6 6 LEU HD13 H 1 1.028 . . 2 . . . . . . . . . 4968 1 49 . 1 1 6 6 LEU HD21 H 1 1.118 . . 2 . . . . . . . . . 4968 1 50 . 1 1 6 6 LEU HD22 H 1 1.118 . . 2 . . . . . . . . . 4968 1 51 . 1 1 6 6 LEU HD23 H 1 1.118 . . 2 . . . . . . . . . 4968 1 52 . 1 1 6 6 LEU N N 15 113.960 . . 1 . . . . . . . . . 4968 1 53 . 1 1 6 6 LEU HG H 1 1.878 . . 1 . . . . . . . . . 4968 1 54 . 1 1 7 7 GLU H H 1 7.484 . . 1 . . . . . . . . . 4968 1 55 . 1 1 7 7 GLU HA H 1 4.758 . . 1 . . . . . . . . . 4968 1 56 . 1 1 7 7 GLU HG2 H 1 2.728 . . 2 . . . . . . . . . 4968 1 57 . 1 1 7 7 GLU HG3 H 1 2.828 . . 2 . . . . . . . . . 4968 1 58 . 1 1 7 7 GLU HB2 H 1 2.338 . . 2 . . . . . . . . . 4968 1 59 . 1 1 7 7 GLU HB3 H 1 2.428 . . 2 . . . . . . . . . 4968 1 60 . 1 1 7 7 GLU N N 15 120.560 . . 1 . . . . . . . . . 4968 1 61 . 1 1 8 8 PRO HG2 H 1 2.298 . . 1 . . . . . . . . . 4968 1 62 . 1 1 8 8 PRO HG3 H 1 2.298 . . 1 . . . . . . . . . 4968 1 63 . 1 1 8 8 PRO CA C 13 62.220 . . 1 . . . . . . . . . 4968 1 64 . 1 1 8 8 PRO CD C 13 50.720 . . 1 . . . . . . . . . 4968 1 65 . 1 1 8 8 PRO HA H 1 4.808 . . 1 . . . . . . . . . 4968 1 66 . 1 1 8 8 PRO HB2 H 1 2.008 . . 2 . . . . . . . . . 4968 1 67 . 1 1 8 8 PRO HB3 H 1 2.618 . . 2 . . . . . . . . . 4968 1 68 . 1 1 8 8 PRO HD2 H 1 3.898 . . 2 . . . . . . . . . 4968 1 69 . 1 1 8 8 PRO HD3 H 1 4.168 . . 2 . . . . . . . . . 4968 1 70 . 1 1 9 9 PRO HG3 H 1 1.438 . . 2 . . . . . . . . . 4968 1 71 . 1 1 9 9 PRO CA C 13 63.220 . . 1 . . . . . . . . . 4968 1 72 . 1 1 9 9 PRO CB C 13 30.220 . . 1 . . . . . . . . . 4968 1 73 . 1 1 9 9 PRO HA H 1 3.888 . . 1 . . . . . . . . . 4968 1 74 . 1 1 9 9 PRO CG C 13 26.220 . . 1 . . . . . . . . . 4968 1 75 . 1 1 9 9 PRO HD2 H 1 3.108 . . 2 . . . . . . . . . 4968 1 76 . 1 1 9 9 PRO HD3 H 1 3.518 . . 2 . . . . . . . . . 4968 1 77 . 1 1 10 10 TYR CA C 13 56.720 . . 1 . . . . . . . . . 4968 1 78 . 1 1 10 10 TYR H H 1 7.764 . . 1 . . . . . . . . . 4968 1 79 . 1 1 10 10 TYR CD1 C 13 135.220 . . 1 . . . . . . . . . 4968 1 80 . 1 1 10 10 TYR CE1 C 13 120.220 . . 1 . . . . . . . . . 4968 1 81 . 1 1 10 10 TYR CD2 C 13 135.220 . . 1 . . . . . . . . . 4968 1 82 . 1 1 10 10 TYR HA H 1 5.108 . . 1 . . . . . . . . . 4968 1 83 . 1 1 10 10 TYR CE2 C 13 120.220 . . 1 . . . . . . . . . 4968 1 84 . 1 1 10 10 TYR HB2 H 1 3.138 . . 1 . . . . . . . . . 4968 1 85 . 1 1 10 10 TYR HD1 H 1 7.498 . . 1 . . . . . . . . . 4968 1 86 . 1 1 10 10 TYR HB3 H 1 3.138 . . 1 . . . . . . . . . 4968 1 87 . 1 1 10 10 TYR HE1 H 1 7.268 . . 1 . . . . . . . . . 4968 1 88 . 1 1 10 10 TYR HD2 H 1 7.498 . . 1 . . . . . . . . . 4968 1 89 . 1 1 10 10 TYR N N 15 122.860 . . 1 . . . . . . . . . 4968 1 90 . 1 1 10 10 TYR HE2 H 1 7.268 . . 1 . . . . . . . . . 4968 1 91 . 1 1 11 11 THR HG21 H 1 1.558 . . 1 . . . . . . . . . 4968 1 92 . 1 1 11 11 THR HG22 H 1 1.558 . . 1 . . . . . . . . . 4968 1 93 . 1 1 11 11 THR HG23 H 1 1.558 . . 1 . . . . . . . . . 4968 1 94 . 1 1 11 11 THR CA C 13 67.220 . . 1 . . . . . . . . . 4968 1 95 . 1 1 11 11 THR CB C 13 70.720 . . 1 . . . . . . . . . 4968 1 96 . 1 1 11 11 THR H H 1 8.914 . . 1 . . . . . . . . . 4968 1 97 . 1 1 11 11 THR HA H 1 4.698 . . 1 . . . . . . . . . 4968 1 98 . 1 1 11 11 THR HB H 1 4.228 . . 1 . . . . . . . . . 4968 1 99 . 1 1 11 11 THR CG2 C 13 21.720 . . 1 . . . . . . . . . 4968 1 100 . 1 1 11 11 THR N N 15 127.060 . . 1 . . . . . . . . . 4968 1 101 . 1 1 12 12 GLY H H 1 7.134 . . 1 . . . . . . . . . 4968 1 102 . 1 1 12 12 GLY HA2 H 1 3.428 . . 2 . . . . . . . . . 4968 1 103 . 1 1 12 12 GLY HA3 H 1 4.068 . . 2 . . . . . . . . . 4968 1 104 . 1 1 12 12 GLY CA C 13 46.720 . . 1 . . . . . . . . . 4968 1 105 . 1 1 12 12 GLY N N 15 106.860 . . 1 . . . . . . . . . 4968 1 106 . 1 1 13 13 PRO HG2 H 1 2.168 . . 1 . . . . . . . . . 4968 1 107 . 1 1 13 13 PRO HG3 H 1 2.168 . . 1 . . . . . . . . . 4968 1 108 . 1 1 13 13 PRO CA C 13 64.720 . . 1 . . . . . . . . . 4968 1 109 . 1 1 13 13 PRO HA H 1 4.728 . . 1 . . . . . . . . . 4968 1 110 . 1 1 13 13 PRO HB2 H 1 2.278 . . 2 . . . . . . . . . 4968 1 111 . 1 1 13 13 PRO HB3 H 1 2.358 . . 2 . . . . . . . . . 4968 1 112 . 1 1 13 13 PRO HD2 H 1 3.768 . . 2 . . . . . . . . . 4968 1 113 . 1 1 13 13 PRO HD3 H 1 3.808 . . 2 . . . . . . . . . 4968 1 114 . 1 1 14 14 CYS H H 1 8.594 . . 1 . . . . . . . . . 4968 1 115 . 1 1 14 14 CYS HA H 1 4.748 . . 1 . . . . . . . . . 4968 1 116 . 1 1 14 14 CYS HB2 H 1 2.958 . . 2 . . . . . . . . . 4968 1 117 . 1 1 14 14 CYS CA C 13 60.220 . . 1 . . . . . . . . . 4968 1 118 . 1 1 14 14 CYS HB3 H 1 3.658 . . 2 . . . . . . . . . 4968 1 119 . 1 1 14 14 CYS N N 15 117.660 . . 1 . . . . . . . . . 4968 1 120 . 1 1 15 15 LYS HG2 H 1 1.568 . . 1 . . . . . . . . . 4968 1 121 . 1 1 15 15 LYS HG3 H 1 1.568 . . 1 . . . . . . . . . 4968 1 122 . 1 1 15 15 LYS CA C 13 56.220 . . 1 . . . . . . . . . 4968 1 123 . 1 1 15 15 LYS H H 1 7.964 . . 1 . . . . . . . . . 4968 1 124 . 1 1 15 15 LYS HA H 1 4.578 . . 1 . . . . . . . . . 4968 1 125 . 1 1 15 15 LYS HB2 H 1 1.768 . . 2 . . . . . . . . . 4968 1 126 . 1 1 15 15 LYS HB3 H 1 2.268 . . 2 . . . . . . . . . 4968 1 127 . 1 1 15 15 LYS N N 15 115.260 . . 1 . . . . . . . . . 4968 1 128 . 1 1 16 16 ALA H H 1 8.194 . . 1 . . . . . . . . . 4968 1 129 . 1 1 16 16 ALA HA H 1 4.478 . . 1 . . . . . . . . . 4968 1 130 . 1 1 16 16 ALA HB1 H 1 1.348 . . 1 . . . . . . . . . 4968 1 131 . 1 1 16 16 ALA HB2 H 1 1.348 . . 1 . . . . . . . . . 4968 1 132 . 1 1 16 16 ALA HB3 H 1 1.348 . . 1 . . . . . . . . . 4968 1 133 . 1 1 16 16 ALA CA C 13 52.220 . . 1 . . . . . . . . . 4968 1 134 . 1 1 16 16 ALA CB C 13 20.220 . . 1 . . . . . . . . . 4968 1 135 . 1 1 16 16 ALA N N 15 123.460 . . 1 . . . . . . . . . 4968 1 136 . 1 1 17 17 ARG HG2 H 1 1.458 . . 2 . . . . . . . . . 4968 1 137 . 1 1 17 17 ARG HG3 H 1 1.478 . . 2 . . . . . . . . . 4968 1 138 . 1 1 17 17 ARG CA C 13 55.220 . . 1 . . . . . . . . . 4968 1 139 . 1 1 17 17 ARG H H 1 8.184 . . 1 . . . . . . . . . 4968 1 140 . 1 1 17 17 ARG HA H 1 4.488 . . 1 . . . . . . . . . 4968 1 141 . 1 1 17 17 ARG HB2 H 1 1.788 . . 1 . . . . . . . . . 4968 1 142 . 1 1 17 17 ARG HB3 H 1 1.788 . . 1 . . . . . . . . . 4968 1 143 . 1 1 17 17 ARG HD2 H 1 3.278 . . 1 . . . . . . . . . 4968 1 144 . 1 1 17 17 ARG N N 15 118.060 . . 1 . . . . . . . . . 4968 1 145 . 1 1 17 17 ARG HD3 H 1 3.278 . . 1 . . . . . . . . . 4968 1 146 . 1 1 18 18 ILE HG21 H 1 1.138 . . 1 . . . . . . . . . 4968 1 147 . 1 1 18 18 ILE HG22 H 1 1.138 . . 1 . . . . . . . . . 4968 1 148 . 1 1 18 18 ILE HG23 H 1 1.138 . . 1 . . . . . . . . . 4968 1 149 . 1 1 18 18 ILE HG12 H 1 1.148 . . 2 . . . . . . . . . 4968 1 150 . 1 1 18 18 ILE HG13 H 1 1.548 . . 2 . . . . . . . . . 4968 1 151 . 1 1 18 18 ILE CA C 13 60.220 . . 1 . . . . . . . . . 4968 1 152 . 1 1 18 18 ILE CD1 C 13 14.220 . . 1 . . . . . . . . . 4968 1 153 . 1 1 18 18 ILE H H 1 8.084 . . 1 . . . . . . . . . 4968 1 154 . 1 1 18 18 ILE HA H 1 4.368 . . 1 . . . . . . . . . 4968 1 155 . 1 1 18 18 ILE HB H 1 2.038 . . 1 . . . . . . . . . 4968 1 156 . 1 1 18 18 ILE HD11 H 1 0.878 . . 1 . . . . . . . . . 4968 1 157 . 1 1 18 18 ILE HD12 H 1 0.878 . . 1 . . . . . . . . . 4968 1 158 . 1 1 18 18 ILE HD13 H 1 0.878 . . 1 . . . . . . . . . 4968 1 159 . 1 1 18 18 ILE CG2 C 13 18.720 . . 1 . . . . . . . . . 4968 1 160 . 1 1 18 18 ILE N N 15 125.060 . . 1 . . . . . . . . . 4968 1 161 . 1 1 19 19 ILE HG21 H 1 0.888 . . 1 . . . . . . . . . 4968 1 162 . 1 1 19 19 ILE HG22 H 1 0.888 . . 1 . . . . . . . . . 4968 1 163 . 1 1 19 19 ILE HG23 H 1 0.888 . . 1 . . . . . . . . . 4968 1 164 . 1 1 19 19 ILE HG12 H 1 1.568 . . 2 . . . . . . . . . 4968 1 165 . 1 1 19 19 ILE HG13 H 1 1.648 . . 2 . . . . . . . . . 4968 1 166 . 1 1 19 19 ILE CA C 13 61.220 . . 1 . . . . . . . . . 4968 1 167 . 1 1 19 19 ILE CD1 C 13 10.720 . . 1 . . . . . . . . . 4968 1 168 . 1 1 19 19 ILE H H 1 8.654 . . 1 . . . . . . . . . 4968 1 169 . 1 1 19 19 ILE HA H 1 4.478 . . 1 . . . . . . . . . 4968 1 170 . 1 1 19 19 ILE HB H 1 2.128 . . 1 . . . . . . . . . 4968 1 171 . 1 1 19 19 ILE HD11 H 1 0.858 . . 1 . . . . . . . . . 4968 1 172 . 1 1 19 19 ILE HD12 H 1 0.858 . . 1 . . . . . . . . . 4968 1 173 . 1 1 19 19 ILE HD13 H 1 0.858 . . 1 . . . . . . . . . 4968 1 174 . 1 1 19 19 ILE CG2 C 13 17.720 . . 1 . . . . . . . . . 4968 1 175 . 1 1 19 19 ILE N N 15 128.160 . . 1 . . . . . . . . . 4968 1 176 . 1 1 20 20 ARG HG2 H 1 1.528 . . 2 . . . . . . . . . 4968 1 177 . 1 1 20 20 ARG HG3 H 1 1.928 . . 2 . . . . . . . . . 4968 1 178 . 1 1 20 20 ARG CA C 13 52.220 . . 1 . . . . . . . . . 4968 1 179 . 1 1 20 20 ARG H H 1 8.364 . . 1 . . . . . . . . . 4968 1 180 . 1 1 20 20 ARG HA H 1 4.898 . . 1 . . . . . . . . . 4968 1 181 . 1 1 20 20 ARG HB2 H 1 1.008 . . 2 . . . . . . . . . 4968 1 182 . 1 1 20 20 ARG HB3 H 1 1.978 . . 2 . . . . . . . . . 4968 1 183 . 1 1 20 20 ARG HE H 1 7.628 . . 1 . . . . . . . . . 4968 1 184 . 1 1 20 20 ARG HD2 H 1 3.198 . . 2 . . . . . . . . . 4968 1 185 . 1 1 20 20 ARG N N 15 129.560 . . 1 . . . . . . . . . 4968 1 186 . 1 1 20 20 ARG HD3 H 1 3.658 . . 2 . . . . . . . . . 4968 1 187 . 1 1 21 21 TYR CA C 13 57.720 . . 1 . . . . . . . . . 4968 1 188 . 1 1 21 21 TYR H H 1 9.154 . . 1 . . . . . . . . . 4968 1 189 . 1 1 21 21 TYR CD1 C 13 133.220 . . 1 . . . . . . . . . 4968 1 190 . 1 1 21 21 TYR CE1 C 13 119.720 . . 1 . . . . . . . . . 4968 1 191 . 1 1 21 21 TYR CD2 C 13 133.220 . . 1 . . . . . . . . . 4968 1 192 . 1 1 21 21 TYR HA H 1 5.858 . . 1 . . . . . . . . . 4968 1 193 . 1 1 21 21 TYR CE2 C 13 119.720 . . 1 . . . . . . . . . 4968 1 194 . 1 1 21 21 TYR HB2 H 1 2.868 . . 1 . . . . . . . . . 4968 1 195 . 1 1 21 21 TYR HD1 H 1 6.888 . . 1 . . . . . . . . . 4968 1 196 . 1 1 21 21 TYR HB3 H 1 2.868 . . 1 . . . . . . . . . 4968 1 197 . 1 1 21 21 TYR HE1 H 1 6.968 . . 1 . . . . . . . . . 4968 1 198 . 1 1 21 21 TYR HD2 H 1 6.888 . . 1 . . . . . . . . . 4968 1 199 . 1 1 21 21 TYR N N 15 115.660 . . 1 . . . . . . . . . 4968 1 200 . 1 1 21 21 TYR HE2 H 1 6.968 . . 1 . . . . . . . . . 4968 1 201 . 1 1 22 22 PHE HZ H 1 7.498 . . 1 . . . . . . . . . 4968 1 202 . 1 1 22 22 PHE CA C 13 55.220 . . 1 . . . . . . . . . 4968 1 203 . 1 1 22 22 PHE H H 1 9.754 . . 1 . . . . . . . . . 4968 1 204 . 1 1 22 22 PHE HA H 1 5.438 . . 1 . . . . . . . . . 4968 1 205 . 1 1 22 22 PHE N N 15 119.960 . . 1 . . . . . . . . . 4968 1 206 . 1 1 22 22 PHE CD1 C 13 133.720 . . 1 . . . . . . . . . 4968 1 207 . 1 1 22 22 PHE CD2 C 13 133.720 . . 1 . . . . . . . . . 4968 1 208 . 1 1 22 22 PHE CE1 C 13 131.720 . . 1 . . . . . . . . . 4968 1 209 . 1 1 22 22 PHE CE2 C 13 131.720 . . 1 . . . . . . . . . 4968 1 210 . 1 1 22 22 PHE HB2 H 1 2.978 . . 2 . . . . . . . . . 4968 1 211 . 1 1 22 22 PHE CZ C 13 130.720 . . 1 . . . . . . . . . 4968 1 212 . 1 1 22 22 PHE HB3 H 1 3.078 . . 2 . . . . . . . . . 4968 1 213 . 1 1 22 22 PHE HD1 H 1 7.328 . . 1 . . . . . . . . . 4968 1 214 . 1 1 22 22 PHE HD2 H 1 7.328 . . 1 . . . . . . . . . 4968 1 215 . 1 1 22 22 PHE HE1 H 1 7.408 . . 1 . . . . . . . . . 4968 1 216 . 1 1 22 22 PHE HE2 H 1 7.408 . . 1 . . . . . . . . . 4968 1 217 . 1 1 23 23 TYR CA C 13 59.720 . . 1 . . . . . . . . . 4968 1 218 . 1 1 23 23 TYR H H 1 10.524 . . 1 . . . . . . . . . 4968 1 219 . 1 1 23 23 TYR CD1 C 13 133.720 . . 1 . . . . . . . . . 4968 1 220 . 1 1 23 23 TYR CE1 C 13 118.220 . . 1 . . . . . . . . . 4968 1 221 . 1 1 23 23 TYR CD2 C 13 133.720 . . 1 . . . . . . . . . 4968 1 222 . 1 1 23 23 TYR HA H 1 4.468 . . 1 . . . . . . . . . 4968 1 223 . 1 1 23 23 TYR CE2 C 13 118.220 . . 1 . . . . . . . . . 4968 1 224 . 1 1 23 23 TYR HB2 H 1 3.638 . . 2 . . . . . . . . . 4968 1 225 . 1 1 23 23 TYR HD1 H 1 7.378 . . 1 . . . . . . . . . 4968 1 226 . 1 1 23 23 TYR HB3 H 1 2.898 . . 2 . . . . . . . . . 4968 1 227 . 1 1 23 23 TYR HE1 H 1 6.508 . . 1 . . . . . . . . . 4968 1 228 . 1 1 23 23 TYR HD2 H 1 7.378 . . 1 . . . . . . . . . 4968 1 229 . 1 1 23 23 TYR N N 15 124.860 . . 1 . . . . . . . . . 4968 1 230 . 1 1 23 23 TYR HE2 H 1 6.508 . . 1 . . . . . . . . . 4968 1 231 . 1 1 24 24 ASN HD22 H 1 8.078 . . 2 . . . . . . . . . 4968 1 232 . 1 1 24 24 ASN CA C 13 50.720 . . 1 . . . . . . . . . 4968 1 233 . 1 1 24 24 ASN H H 1 7.734 . . 1 . . . . . . . . . 4968 1 234 . 1 1 24 24 ASN HA H 1 4.778 . . 1 . . . . . . . . . 4968 1 235 . 1 1 24 24 ASN HB2 H 1 2.348 . . 2 . . . . . . . . . 4968 1 236 . 1 1 24 24 ASN HB3 H 1 3.038 . . 2 . . . . . . . . . 4968 1 237 . 1 1 24 24 ASN N N 15 125.560 . . 1 . . . . . . . . . 4968 1 238 . 1 1 24 24 ASN HD21 H 1 7.288 . . 2 . . . . . . . . . 4968 1 239 . 1 1 25 25 ALA H H 1 8.754 . . 1 . . . . . . . . . 4968 1 240 . 1 1 25 25 ALA HA H 1 3.938 . . 1 . . . . . . . . . 4968 1 241 . 1 1 25 25 ALA HB1 H 1 1.728 . . 1 . . . . . . . . . 4968 1 242 . 1 1 25 25 ALA HB2 H 1 1.728 . . 1 . . . . . . . . . 4968 1 243 . 1 1 25 25 ALA HB3 H 1 1.728 . . 1 . . . . . . . . . 4968 1 244 . 1 1 25 25 ALA CA C 13 54.720 . . 1 . . . . . . . . . 4968 1 245 . 1 1 25 25 ALA CB C 13 19.220 . . 1 . . . . . . . . . 4968 1 246 . 1 1 25 25 ALA N N 15 126.560 . . 1 . . . . . . . . . 4968 1 247 . 1 1 26 26 LYS HE3 H 1 3.228 . . 1 . . . . . . . . . 4968 1 248 . 1 1 26 26 LYS HG2 H 1 1.678 . . 2 . . . . . . . . . 4968 1 249 . 1 1 26 26 LYS HG3 H 1 1.878 . . 2 . . . . . . . . . 4968 1 250 . 1 1 26 26 LYS CA C 13 58.720 . . 1 . . . . . . . . . 4968 1 251 . 1 1 26 26 LYS H H 1 7.884 . . 1 . . . . . . . . . 4968 1 252 . 1 1 26 26 LYS HA H 1 4.238 . . 1 . . . . . . . . . 4968 1 253 . 1 1 26 26 LYS HB2 H 1 2.058 . . 1 . . . . . . . . . 4968 1 254 . 1 1 26 26 LYS HB3 H 1 2.058 . . 1 . . . . . . . . . 4968 1 255 . 1 1 26 26 LYS N N 15 116.460 . . 1 . . . . . . . . . 4968 1 256 . 1 1 26 26 LYS HE2 H 1 3.228 . . 1 . . . . . . . . . 4968 1 257 . 1 1 27 27 ALA H H 1 6.794 . . 1 . . . . . . . . . 4968 1 258 . 1 1 27 27 ALA HA H 1 4.468 . . 1 . . . . . . . . . 4968 1 259 . 1 1 27 27 ALA HB1 H 1 1.358 . . 1 . . . . . . . . . 4968 1 260 . 1 1 27 27 ALA HB2 H 1 1.358 . . 1 . . . . . . . . . 4968 1 261 . 1 1 27 27 ALA HB3 H 1 1.358 . . 1 . . . . . . . . . 4968 1 262 . 1 1 27 27 ALA CA C 13 52.220 . . 1 . . . . . . . . . 4968 1 263 . 1 1 27 27 ALA CB C 13 20.720 . . 1 . . . . . . . . . 4968 1 264 . 1 1 27 27 ALA N N 15 118.260 . . 1 . . . . . . . . . 4968 1 265 . 1 1 28 28 GLY H H 1 8.104 . . 1 . . . . . . . . . 4968 1 266 . 1 1 28 28 GLY HA2 H 1 4.088 . . 1 . . . . . . . . . 4968 1 267 . 1 1 28 28 GLY HA3 H 1 4.088 . . 1 . . . . . . . . . 4968 1 268 . 1 1 28 28 GLY CA C 13 46.220 . . 1 . . . . . . . . . 4968 1 269 . 1 1 28 28 GLY N N 15 106.660 . . 1 . . . . . . . . . 4968 1 270 . 1 1 29 29 LEU CA C 13 53.720 . . 1 . . . . . . . . . 4968 1 271 . 1 1 29 29 LEU H H 1 6.794 . . 1 . . . . . . . . . 4968 1 272 . 1 1 29 29 LEU CD1 C 13 25.220 . . 1 . . . . . . . . . 4968 1 273 . 1 1 29 29 LEU CD2 C 13 25.220 . . 1 . . . . . . . . . 4968 1 274 . 1 1 29 29 LEU HA H 1 4.918 . . 1 . . . . . . . . . 4968 1 275 . 1 1 29 29 LEU CG C 13 26.220 . . 1 . . . . . . . . . 4968 1 276 . 1 1 29 29 LEU HB2 H 1 1.618 . . 2 . . . . . . . . . 4968 1 277 . 1 1 29 29 LEU HB3 H 1 1.888 . . 2 . . . . . . . . . 4968 1 278 . 1 1 29 29 LEU HD11 H 1 0.928 . . 2 . . . . . . . . . 4968 1 279 . 1 1 29 29 LEU HD12 H 1 0.928 . . 2 . . . . . . . . . 4968 1 280 . 1 1 29 29 LEU HD13 H 1 0.928 . . 2 . . . . . . . . . 4968 1 281 . 1 1 29 29 LEU HD21 H 1 1.018 . . 2 . . . . . . . . . 4968 1 282 . 1 1 29 29 LEU HD22 H 1 1.018 . . 2 . . . . . . . . . 4968 1 283 . 1 1 29 29 LEU HD23 H 1 1.018 . . 2 . . . . . . . . . 4968 1 284 . 1 1 29 29 LEU N N 15 114.360 . . 1 . . . . . . . . . 4968 1 285 . 1 1 29 29 LEU HG H 1 1.598 . . 1 . . . . . . . . . 4968 1 286 . 1 1 30 30 CYS H H 1 8.354 . . 1 . . . . . . . . . 4968 1 287 . 1 1 30 30 CYS HA H 1 5.798 . . 1 . . . . . . . . . 4968 1 288 . 1 1 30 30 CYS HB2 H 1 2.828 . . 2 . . . . . . . . . 4968 1 289 . 1 1 30 30 CYS CA C 13 58.220 . . 1 . . . . . . . . . 4968 1 290 . 1 1 30 30 CYS HB3 H 1 3.858 . . 2 . . . . . . . . . 4968 1 291 . 1 1 30 30 CYS CB C 13 49.720 . . 1 . . . . . . . . . 4968 1 292 . 1 1 30 30 CYS N N 15 118.560 . . 1 . . . . . . . . . 4968 1 293 . 1 1 31 31 GLN HE21 H 1 7.338 . . 2 . . . . . . . . . 4968 1 294 . 1 1 31 31 GLN HG2 H 1 2.078 . . 2 . . . . . . . . . 4968 1 295 . 1 1 31 31 GLN HE22 H 1 7.508 . . 2 . . . . . . . . . 4968 1 296 . 1 1 31 31 GLN HG3 H 1 2.428 . . 2 . . . . . . . . . 4968 1 297 . 1 1 31 31 GLN CA C 13 54.220 . . 1 . . . . . . . . . 4968 1 298 . 1 1 31 31 GLN H H 1 8.744 . . 1 . . . . . . . . . 4968 1 299 . 1 1 31 31 GLN HA H 1 5.008 . . 1 . . . . . . . . . 4968 1 300 . 1 1 31 31 GLN HB2 H 1 1.908 . . 2 . . . . . . . . . 4968 1 301 . 1 1 31 31 GLN HB3 H 1 2.338 . . 2 . . . . . . . . . 4968 1 302 . 1 1 31 31 GLN N N 15 122.960 . . 1 . . . . . . . . . 4968 1 303 . 1 1 32 32 THR HG21 H 1 0.768 . . 1 . . . . . . . . . 4968 1 304 . 1 1 32 32 THR HG22 H 1 0.768 . . 1 . . . . . . . . . 4968 1 305 . 1 1 32 32 THR HG23 H 1 0.768 . . 1 . . . . . . . . . 4968 1 306 . 1 1 32 32 THR CA C 13 61.220 . . 1 . . . . . . . . . 4968 1 307 . 1 1 32 32 THR CB C 13 72.720 . . 1 . . . . . . . . . 4968 1 308 . 1 1 32 32 THR H H 1 8.024 . . 1 . . . . . . . . . 4968 1 309 . 1 1 32 32 THR HA H 1 5.458 . . 1 . . . . . . . . . 4968 1 310 . 1 1 32 32 THR HB H 1 4.208 . . 1 . . . . . . . . . 4968 1 311 . 1 1 32 32 THR CG2 C 13 22.720 . . 1 . . . . . . . . . 4968 1 312 . 1 1 32 32 THR N N 15 108.660 . . 1 . . . . . . . . . 4968 1 313 . 1 1 33 33 PHE HZ H 1 7.168 . . 1 . . . . . . . . . 4968 1 314 . 1 1 33 33 PHE H H 1 9.334 . . 1 . . . . . . . . . 4968 1 315 . 1 1 33 33 PHE CE1 C 13 131.720 . . 1 . . . . . . . . . 4968 1 316 . 1 1 33 33 PHE CD2 C 13 134.220 . . 1 . . . . . . . . . 4968 1 317 . 1 1 33 33 PHE HA H 1 5.038 . . 1 . . . . . . . . . 4968 1 318 . 1 1 33 33 PHE CE2 C 13 131.720 . . 1 . . . . . . . . . 4968 1 319 . 1 1 33 33 PHE HB2 H 1 3.128 . . 2 . . . . . . . . . 4968 1 320 . 1 1 33 33 PHE HD1 H 1 7.248 . . 1 . . . . . . . . . 4968 1 321 . 1 1 33 33 PHE HB3 H 1 3.248 . . 2 . . . . . . . . . 4968 1 322 . 1 1 33 33 PHE CZ C 13 129.720 . . 1 . . . . . . . . . 4968 1 323 . 1 1 33 33 PHE HE1 H 1 7.308 . . 1 . . . . . . . . . 4968 1 324 . 1 1 33 33 PHE HD2 H 1 7.248 . . 1 . . . . . . . . . 4968 1 325 . 1 1 33 33 PHE N N 15 119.160 . . 1 . . . . . . . . . 4968 1 326 . 1 1 33 33 PHE HE2 H 1 7.308 . . 1 . . . . . . . . . 4968 1 327 . 1 1 34 34 VAL HG11 H 1 0.878 . . 2 . . . . . . . . . 4968 1 328 . 1 1 34 34 VAL HG12 H 1 0.878 . . 2 . . . . . . . . . 4968 1 329 . 1 1 34 34 VAL HG13 H 1 0.878 . . 2 . . . . . . . . . 4968 1 330 . 1 1 34 34 VAL HG21 H 1 0.978 . . 2 . . . . . . . . . 4968 1 331 . 1 1 34 34 VAL HG22 H 1 0.978 . . 2 . . . . . . . . . 4968 1 332 . 1 1 34 34 VAL HG23 H 1 0.978 . . 2 . . . . . . . . . 4968 1 333 . 1 1 34 34 VAL CA C 13 62.720 . . 1 . . . . . . . . . 4968 1 334 . 1 1 34 34 VAL CB C 13 32.220 . . 1 . . . . . . . . . 4968 1 335 . 1 1 34 34 VAL H H 1 8.334 . . 1 . . . . . . . . . 4968 1 336 . 1 1 34 34 VAL HA H 1 4.088 . . 1 . . . . . . . . . 4968 1 337 . 1 1 34 34 VAL HB H 1 2.118 . . 1 . . . . . . . . . 4968 1 338 . 1 1 34 34 VAL CG1 C 13 21.720 . . 2 . . . . . . . . . 4968 1 339 . 1 1 34 34 VAL CG2 C 13 22.720 . . 2 . . . . . . . . . 4968 1 340 . 1 1 34 34 VAL N N 15 118.660 . . 1 . . . . . . . . . 4968 1 341 . 1 1 35 35 TYR H H 1 9.354 . . 1 . . . . . . . . . 4968 1 342 . 1 1 35 35 TYR CD1 C 13 134.220 . . 1 . . . . . . . . . 4968 1 343 . 1 1 35 35 TYR CE1 C 13 118.720 . . 1 . . . . . . . . . 4968 1 344 . 1 1 35 35 TYR CD2 C 13 134.220 . . 1 . . . . . . . . . 4968 1 345 . 1 1 35 35 TYR HA H 1 5.058 . . 1 . . . . . . . . . 4968 1 346 . 1 1 35 35 TYR CE2 C 13 121.220 . . 1 . . . . . . . . . 4968 1 347 . 1 1 35 35 TYR HB2 H 1 2.678 . . 2 . . . . . . . . . 4968 1 348 . 1 1 35 35 TYR HD1 H 1 6.868 . . 2 . . . . . . . . . 4968 1 349 . 1 1 35 35 TYR HB3 H 1 2.828 . . 2 . . . . . . . . . 4968 1 350 . 1 1 35 35 TYR HE1 H 1 6.958 . . 2 . . . . . . . . . 4968 1 351 . 1 1 35 35 TYR HD2 H 1 7.948 . . 2 . . . . . . . . . 4968 1 352 . 1 1 35 35 TYR N N 15 129.660 . . 1 . . . . . . . . . 4968 1 353 . 1 1 35 35 TYR HE2 H 1 7.058 . . 2 . . . . . . . . . 4968 1 354 . 1 1 36 36 GLY H H 1 8.574 . . 1 . . . . . . . . . 4968 1 355 . 1 1 36 36 GLY HA2 H 1 3.408 . . 2 . . . . . . . . . 4968 1 356 . 1 1 36 36 GLY HA3 H 1 4.478 . . 2 . . . . . . . . . 4968 1 357 . 1 1 36 36 GLY CA C 13 45.720 . . 1 . . . . . . . . . 4968 1 358 . 1 1 36 36 GLY N N 15 113.860 . . 1 . . . . . . . . . 4968 1 359 . 1 1 37 37 GLY HA2 H 1 3.088 . . 2 . . . . . . . . . 4968 1 360 . 1 1 37 37 GLY HA3 H 1 4.408 . . 2 . . . . . . . . . 4968 1 361 . 1 1 37 37 GLY CA C 13 45.720 . . 1 . . . . . . . . . 4968 1 362 . 1 1 38 38 CYS H H 1 7.774 . . 1 . . . . . . . . . 4968 1 363 . 1 1 38 38 CYS HA H 1 5.128 . . 1 . . . . . . . . . 4968 1 364 . 1 1 38 38 CYS HB2 H 1 3.208 . . 2 . . . . . . . . . 4968 1 365 . 1 1 38 38 CYS CA C 13 55.720 . . 1 . . . . . . . . . 4968 1 366 . 1 1 38 38 CYS HB3 H 1 4.118 . . 2 . . . . . . . . . 4968 1 367 . 1 1 38 38 CYS N N 15 114.960 . . 1 . . . . . . . . . 4968 1 368 . 1 1 39 39 ARG HG2 H 1 1.768 . . 1 . . . . . . . . . 4968 1 369 . 1 1 39 39 ARG HG3 H 1 1.768 . . 1 . . . . . . . . . 4968 1 370 . 1 1 39 39 ARG CA C 13 56.720 . . 1 . . . . . . . . . 4968 1 371 . 1 1 39 39 ARG H H 1 9.044 . . 1 . . . . . . . . . 4968 1 372 . 1 1 39 39 ARG HA H 1 4.108 . . 1 . . . . . . . . . 4968 1 373 . 1 1 39 39 ARG HB2 H 1 2.458 . . 1 . . . . . . . . . 4968 1 374 . 1 1 39 39 ARG HB3 H 1 2.458 . . 1 . . . . . . . . . 4968 1 375 . 1 1 39 39 ARG HE H 1 7.478 . . 1 . . . . . . . . . 4968 1 376 . 1 1 39 39 ARG HD2 H 1 3.428 . . 1 . . . . . . . . . 4968 1 377 . 1 1 39 39 ARG N N 15 113.260 . . 1 . . . . . . . . . 4968 1 378 . 1 1 39 39 ARG HD3 H 1 3.428 . . 1 . . . . . . . . . 4968 1 379 . 1 1 40 40 ALA H H 1 7.354 . . 1 . . . . . . . . . 4968 1 380 . 1 1 40 40 ALA HA H 1 4.258 . . 1 . . . . . . . . . 4968 1 381 . 1 1 40 40 ALA HB1 H 1 1.368 . . 1 . . . . . . . . . 4968 1 382 . 1 1 40 40 ALA HB2 H 1 1.368 . . 1 . . . . . . . . . 4968 1 383 . 1 1 40 40 ALA HB3 H 1 1.368 . . 1 . . . . . . . . . 4968 1 384 . 1 1 40 40 ALA CA C 13 54.220 . . 1 . . . . . . . . . 4968 1 385 . 1 1 40 40 ALA CB C 13 20.220 . . 1 . . . . . . . . . 4968 1 386 . 1 1 40 40 ALA N N 15 118.060 . . 1 . . . . . . . . . 4968 1 387 . 1 1 41 41 LYS CA C 13 55.720 . . 1 . . . . . . . . . 4968 1 388 . 1 1 41 41 LYS H H 1 8.284 . . 1 . . . . . . . . . 4968 1 389 . 1 1 41 41 LYS HA H 1 4.618 . . 1 . . . . . . . . . 4968 1 390 . 1 1 41 41 LYS HB2 H 1 1.828 . . 2 . . . . . . . . . 4968 1 391 . 1 1 41 41 LYS HB3 H 1 2.418 . . 2 . . . . . . . . . 4968 1 392 . 1 1 41 41 LYS N N 15 120.960 . . 1 . . . . . . . . . 4968 1 393 . 1 1 42 42 ARG HG2 H 1 1.398 . . 2 . . . . . . . . . 4968 1 394 . 1 1 42 42 ARG HG3 H 1 1.648 . . 2 . . . . . . . . . 4968 1 395 . 1 1 42 42 ARG CA C 13 59.220 . . 1 . . . . . . . . . 4968 1 396 . 1 1 42 42 ARG CB C 13 29.720 . . 1 . . . . . . . . . 4968 1 397 . 1 1 42 42 ARG H H 1 8.294 . . 1 . . . . . . . . . 4968 1 398 . 1 1 42 42 ARG HA H 1 3.828 . . 1 . . . . . . . . . 4968 1 399 . 1 1 42 42 ARG HB2 H 1 0.538 . . 2 . . . . . . . . . 4968 1 400 . 1 1 42 42 ARG HE H 1 7.298 . . 1 . . . . . . . . . 4968 1 401 . 1 1 42 42 ARG HB3 H 1 1.208 . . 2 . . . . . . . . . 4968 1 402 . 1 1 42 42 ARG N N 15 115.560 . . 1 . . . . . . . . . 4968 1 403 . 1 1 42 42 ARG HD2 H 1 2.868 . . 2 . . . . . . . . . 4968 1 404 . 1 1 42 42 ARG HD3 H 1 3.038 . . 2 . . . . . . . . . 4968 1 405 . 1 1 43 43 ASN HD22 H 1 8.138 . . 2 . . . . . . . . . 4968 1 406 . 1 1 43 43 ASN CA C 13 51.220 . . 1 . . . . . . . . . 4968 1 407 . 1 1 43 43 ASN CB C 13 35.220 . . 1 . . . . . . . . . 4968 1 408 . 1 1 43 43 ASN H H 1 7.184 . . 1 . . . . . . . . . 4968 1 409 . 1 1 43 43 ASN HA H 1 5.218 . . 1 . . . . . . . . . 4968 1 410 . 1 1 43 43 ASN HB2 H 1 3.448 . . 2 . . . . . . . . . 4968 1 411 . 1 1 43 43 ASN HB3 H 1 3.558 . . 2 . . . . . . . . . 4968 1 412 . 1 1 43 43 ASN N N 15 116.160 . . 1 . . . . . . . . . 4968 1 413 . 1 1 43 43 ASN HD21 H 1 7.948 . . 2 . . . . . . . . . 4968 1 414 . 1 1 44 44 ASN H H 1 6.744 . . 1 . . . . . . . . . 4968 1 415 . 1 1 44 44 ASN HA H 1 5.068 . . 1 . . . . . . . . . 4968 1 416 . 1 1 44 44 ASN HB2 H 1 2.668 . . 2 . . . . . . . . . 4968 1 417 . 1 1 44 44 ASN CA C 13 54.220 . . 1 . . . . . . . . . 4968 1 418 . 1 1 44 44 ASN HB3 H 1 2.948 . . 2 . . . . . . . . . 4968 1 419 . 1 1 44 44 ASN N N 15 121.060 . . 1 . . . . . . . . . 4968 1 420 . 1 1 45 45 PHE H H 1 9.904 . . 1 . . . . . . . . . 4968 1 421 . 1 1 45 45 PHE HA H 1 5.308 . . 1 . . . . . . . . . 4968 1 422 . 1 1 45 45 PHE HZ H 1 7.808 . . 1 . . . . . . . . . 4968 1 423 . 1 1 45 45 PHE HB2 H 1 2.958 . . 2 . . . . . . . . . 4968 1 424 . 1 1 45 45 PHE CA C 13 56.220 . . 1 . . . . . . . . . 4968 1 425 . 1 1 45 45 PHE HB3 H 1 3.578 . . 2 . . . . . . . . . 4968 1 426 . 1 1 45 45 PHE CZ C 13 130.720 . . 1 . . . . . . . . . 4968 1 427 . 1 1 45 45 PHE N N 15 122.360 . . 1 . . . . . . . . . 4968 1 428 . 1 1 46 46 LYS HE3 H 1 3.238 . . 1 . . . . . . . . . 4968 1 429 . 1 1 46 46 LYS HG2 H 1 1.658 . . 2 . . . . . . . . . 4968 1 430 . 1 1 46 46 LYS HG3 H 1 1.788 . . 2 . . . . . . . . . 4968 1 431 . 1 1 46 46 LYS CA C 13 58.220 . . 1 . . . . . . . . . 4968 1 432 . 1 1 46 46 LYS H H 1 9.884 . . 1 . . . . . . . . . 4968 1 433 . 1 1 46 46 LYS HA H 1 4.558 . . 1 . . . . . . . . . 4968 1 434 . 1 1 46 46 LYS HB2 H 1 2.168 . . 2 . . . . . . . . . 4968 1 435 . 1 1 46 46 LYS HB3 H 1 2.278 . . 2 . . . . . . . . . 4968 1 436 . 1 1 46 46 LYS N N 15 120.260 . . 1 . . . . . . . . . 4968 1 437 . 1 1 46 46 LYS HE2 H 1 3.238 . . 1 . . . . . . . . . 4968 1 438 . 1 1 47 47 SER H H 1 7.444 . . 1 . . . . . . . . . 4968 1 439 . 1 1 47 47 SER HA H 1 4.708 . . 1 . . . . . . . . . 4968 1 440 . 1 1 47 47 SER HB2 H 1 4.028 . . 2 . . . . . . . . . 4968 1 441 . 1 1 47 47 SER CA C 13 56.220 . . 1 . . . . . . . . . 4968 1 442 . 1 1 47 47 SER HB3 H 1 4.288 . . 2 . . . . . . . . . 4968 1 443 . 1 1 47 47 SER CB C 13 67.220 . . 1 . . . . . . . . . 4968 1 444 . 1 1 47 47 SER N N 15 108.560 . . 1 . . . . . . . . . 4968 1 445 . 1 1 48 48 ALA H H 1 8.114 . . 1 . . . . . . . . . 4968 1 446 . 1 1 48 48 ALA HA H 1 3.318 . . 1 . . . . . . . . . 4968 1 447 . 1 1 48 48 ALA HB1 H 1 1.208 . . 1 . . . . . . . . . 4968 1 448 . 1 1 48 48 ALA HB2 H 1 1.208 . . 1 . . . . . . . . . 4968 1 449 . 1 1 48 48 ALA HB3 H 1 1.208 . . 1 . . . . . . . . . 4968 1 450 . 1 1 48 48 ALA CA C 13 55.220 . . 1 . . . . . . . . . 4968 1 451 . 1 1 48 48 ALA CB C 13 17.720 . . 1 . . . . . . . . . 4968 1 452 . 1 1 48 48 ALA N N 15 125.360 . . 1 . . . . . . . . . 4968 1 453 . 1 1 49 49 GLU HG2 H 1 2.378 . . 2 . . . . . . . . . 4968 1 454 . 1 1 49 49 GLU HG3 H 1 2.528 . . 2 . . . . . . . . . 4968 1 455 . 1 1 49 49 GLU CA C 13 60.720 . . 1 . . . . . . . . . 4968 1 456 . 1 1 49 49 GLU H H 1 8.554 . . 1 . . . . . . . . . 4968 1 457 . 1 1 49 49 GLU HA H 1 4.038 . . 1 . . . . . . . . . 4968 1 458 . 1 1 49 49 GLU HB2 H 1 2.018 . . 2 . . . . . . . . . 4968 1 459 . 1 1 49 49 GLU HB3 H 1 2.188 . . 2 . . . . . . . . . 4968 1 460 . 1 1 49 49 GLU N N 15 119.560 . . 1 . . . . . . . . . 4968 1 461 . 1 1 50 50 ASP H H 1 7.814 . . 1 . . . . . . . . . 4968 1 462 . 1 1 50 50 ASP HA H 1 4.458 . . 1 . . . . . . . . . 4968 1 463 . 1 1 50 50 ASP HB2 H 1 2.898 . . 2 . . . . . . . . . 4968 1 464 . 1 1 50 50 ASP CA C 13 57.720 . . 1 . . . . . . . . . 4968 1 465 . 1 1 50 50 ASP HB3 H 1 3.058 . . 2 . . . . . . . . . 4968 1 466 . 1 1 50 50 ASP N N 15 119.760 . . 1 . . . . . . . . . 4968 1 467 . 1 1 51 51 CYS H H 1 6.964 . . 1 . . . . . . . . . 4968 1 468 . 1 1 51 51 CYS HA H 1 1.878 . . 1 . . . . . . . . . 4968 1 469 . 1 1 51 51 CYS HB2 H 1 3.128 . . 2 . . . . . . . . . 4968 1 470 . 1 1 51 51 CYS CA C 13 59.220 . . 1 . . . . . . . . . 4968 1 471 . 1 1 51 51 CYS HB3 H 1 3.348 . . 2 . . . . . . . . . 4968 1 472 . 1 1 51 51 CYS N N 15 119.560 . . 1 . . . . . . . . . 4968 1 473 . 1 1 52 52 MET HG2 H 1 2.868 . . 1 . . . . . . . . . 4968 1 474 . 1 1 52 52 MET HG3 H 1 2.868 . . 1 . . . . . . . . . 4968 1 475 . 1 1 52 52 MET CA C 13 57.220 . . 1 . . . . . . . . . 4968 1 476 . 1 1 52 52 MET H H 1 8.544 . . 1 . . . . . . . . . 4968 1 477 . 1 1 52 52 MET CE C 13 16.720 . . 1 . . . . . . . . . 4968 1 478 . 1 1 52 52 MET HA H 1 4.328 . . 1 . . . . . . . . . 4968 1 479 . 1 1 52 52 MET HB2 H 1 2.128 . . 2 . . . . . . . . . 4968 1 480 . 1 1 52 52 MET HB3 H 1 2.228 . . 2 . . . . . . . . . 4968 1 481 . 1 1 52 52 MET HE1 H 1 2.338 . . 1 . . . . . . . . . 4968 1 482 . 1 1 52 52 MET HE2 H 1 2.338 . . 1 . . . . . . . . . 4968 1 483 . 1 1 52 52 MET HE3 H 1 2.338 . . 1 . . . . . . . . . 4968 1 484 . 1 1 52 52 MET N N 15 121.060 . . 1 . . . . . . . . . 4968 1 485 . 1 1 53 53 ARG HG2 H 1 1.808 . . 2 . . . . . . . . . 4968 1 486 . 1 1 53 53 ARG HG3 H 1 1.928 . . 2 . . . . . . . . . 4968 1 487 . 1 1 53 53 ARG CA C 13 59.720 . . 1 . . . . . . . . . 4968 1 488 . 1 1 53 53 ARG H H 1 8.254 . . 1 . . . . . . . . . 4968 1 489 . 1 1 53 53 ARG HA H 1 4.148 . . 1 . . . . . . . . . 4968 1 490 . 1 1 53 53 ARG HB2 H 1 2.018 . . 2 . . . . . . . . . 4968 1 491 . 1 1 53 53 ARG HB3 H 1 2.098 . . 2 . . . . . . . . . 4968 1 492 . 1 1 53 53 ARG HE H 1 7.468 . . 1 . . . . . . . . . 4968 1 493 . 1 1 53 53 ARG HD2 H 1 3.378 . . 1 . . . . . . . . . 4968 1 494 . 1 1 53 53 ARG N N 15 120.260 . . 1 . . . . . . . . . 4968 1 495 . 1 1 53 53 ARG HD3 H 1 3.378 . . 1 . . . . . . . . . 4968 1 496 . 1 1 54 54 THR HG21 H 1 1.778 . . 1 . . . . . . . . . 4968 1 497 . 1 1 54 54 THR HG22 H 1 1.778 . . 1 . . . . . . . . . 4968 1 498 . 1 1 54 54 THR HG23 H 1 1.778 . . 1 . . . . . . . . . 4968 1 499 . 1 1 54 54 THR CA C 13 66.720 . . 1 . . . . . . . . . 4968 1 500 . 1 1 54 54 THR CB C 13 69.720 . . 1 . . . . . . . . . 4968 1 501 . 1 1 54 54 THR H H 1 7.374 . . 1 . . . . . . . . . 4968 1 502 . 1 1 54 54 THR HA H 1 4.238 . . 1 . . . . . . . . . 4968 1 503 . 1 1 54 54 THR HB H 1 4.168 . . 1 . . . . . . . . . 4968 1 504 . 1 1 54 54 THR CG2 C 13 22.720 . . 1 . . . . . . . . . 4968 1 505 . 1 1 54 54 THR N N 15 113.260 . . 1 . . . . . . . . . 4968 1 506 . 1 1 55 55 CYS H H 1 8.214 . . 1 . . . . . . . . . 4968 1 507 . 1 1 55 55 CYS HA H 1 4.608 . . 1 . . . . . . . . . 4968 1 508 . 1 1 55 55 CYS HB2 H 1 2.188 . . 2 . . . . . . . . . 4968 1 509 . 1 1 55 55 CYS CA C 13 54.720 . . 1 . . . . . . . . . 4968 1 510 . 1 1 55 55 CYS HB3 H 1 2.408 . . 2 . . . . . . . . . 4968 1 511 . 1 1 55 55 CYS N N 15 114.560 . . 1 . . . . . . . . . 4968 1 512 . 1 1 56 56 GLY H H 1 7.924 . . 1 . . . . . . . . . 4968 1 513 . 1 1 56 56 GLY HA2 H 1 4.008 . . 1 . . . . . . . . . 4968 1 514 . 1 1 56 56 GLY HA3 H 1 4.008 . . 1 . . . . . . . . . 4968 1 515 . 1 1 56 56 GLY CA C 13 46.720 . . 1 . . . . . . . . . 4968 1 516 . 1 1 56 56 GLY N N 15 107.560 . . 1 . . . . . . . . . 4968 1 517 . 1 1 57 57 GLY H H 1 8.154 . . 1 . . . . . . . . . 4968 1 518 . 1 1 57 57 GLY HA2 H 1 4.158 . . 2 . . . . . . . . . 4968 1 519 . 1 1 57 57 GLY HA3 H 1 3.968 . . 2 . . . . . . . . . 4968 1 520 . 1 1 57 57 GLY CA C 13 45.220 . . 1 . . . . . . . . . 4968 1 521 . 1 1 57 57 GLY N N 15 108.560 . . 1 . . . . . . . . . 4968 1 522 . 1 1 58 58 ALA H H 1 7.904 . . 1 . . . . . . . . . 4968 1 523 . 1 1 58 58 ALA HA H 1 4.188 . . 1 . . . . . . . . . 4968 1 524 . 1 1 58 58 ALA HB1 H 1 1.478 . . 1 . . . . . . . . . 4968 1 525 . 1 1 58 58 ALA HB2 H 1 1.478 . . 1 . . . . . . . . . 4968 1 526 . 1 1 58 58 ALA HB3 H 1 1.478 . . 1 . . . . . . . . . 4968 1 527 . 1 1 58 58 ALA CA C 13 54.720 . . 1 . . . . . . . . . 4968 1 528 . 1 1 58 58 ALA CB C 13 20.220 . . 1 . . . . . . . . . 4968 1 529 . 1 1 58 58 ALA N N 15 129.260 . . 1 . . . . . . . . . 4968 1 stop_ save_