data_45 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 45 _Entry.Title ; Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor) ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Gerhard Wagner . . . 45 2 Kurt Wuthrich . . . 45 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 45 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 329 45 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 5 . . 2010-06-10 . revision BMRB 'Complete natural source information' 45 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 45 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 45 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 45 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 45 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 45 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wagner, Gerhard, Wuthrich, Kurt, "Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor)," J. Mol. Biol. 155, 347-366 (1982). ; _Citation.Title ; Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 155 _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 347 _Citation.Page_last 366 _Citation.Year 1982 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Gerhard Wagner . . . 45 1 2 Kurt Wuthrich . . . 45 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_basic_pancreatic_trypsin_inhibitor _Assembly.Sf_category assembly _Assembly.Sf_framecode system_basic_pancreatic_trypsin_inhibitor _Assembly.Entry_ID 45 _Assembly.ID 1 _Assembly.Name 'basic 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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'basic pancreatic trypsin inhibitor' 1 $basic_pancreatic_trypsin_inhibitor . . . . . . . . . 45 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'basic pancreatic trypsin inhibitor' system 45 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_basic_pancreatic_trypsin_inhibitor _Entity.Sf_category entity _Entity.Sf_framecode basic_pancreatic_trypsin_inhibitor _Entity.Entry_ID 45 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'basic 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 ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCMRTCGGA ; _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 . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1039 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 2 no BMRB 1156 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 3 no BMRB 1179 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 4 no BMRB 236 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 5 no BMRB 237 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 6 no BMRB 262 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 7 no BMRB 263 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 8 no BMRB 264 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 9 no BMRB 338 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 10 no BMRB 411 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 11 no BMRB 412 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 12 no BMRB 413 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 13 no BMRB 414 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 14 no BMRB 415 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 15 no BMRB 416 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 16 no BMRB 419 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 17 no BMRB 46 . "basic pancreatic trypsin inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 18 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 1.39e-33 . . . . 45 1 19 no PDB 1BHC . "Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 20 no PDB 1BPI . "The Structure Of Bovine Pancreatic Trypsin Inhibitor At 125k: Definition Of Carboxyl-Terminal Residues Glycine-57 And Alanine-5" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 21 no PDB 1BPT . "Crevice-Forming Mutants Of Bpti: Crystal Structures Of F22a, Y23a, N43g, And F45a" . . . . . 100.00 58 98.28 98.28 1.43e-32 . . . . 45 1 22 no PDB 1BTH . "Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 23 no PDB 1BTI . "Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" . . . . . 100.00 58 98.28 98.28 1.45e-32 . . . . 45 1 24 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 1.39e-33 . . . . 45 1 25 no PDB 1BZX . "The Crystal Structure Of Anionic Salmon Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 26 no PDB 1CBW . "Bovine Chymotrypsin Complexed To Bpti" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 27 no PDB 1CO7 . "R117h Mutant Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" . . . . . 100.00 99 100.00 100.00 2.25e-34 . . . . 45 1 28 no PDB 1D0D . "Crystal Structure Of Tick Anticoagulant Protein Complexed With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 29 no PDB 1EAW . "Crystal Structure Of The Mtsp1 (matriptase)-bpti (aprotinin) Complex" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 30 no PDB 1F5R . "Rat Trypsinogen Mutant Complexed With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 65 100.00 100.00 1.34e-33 . . . . 45 1 31 no PDB 1F7Z . "Rat Trypsinogen K15a Complexed With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 65 100.00 100.00 1.34e-33 . . . . 45 1 32 no PDB 1FAN . "Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" . . . . . 100.00 58 98.28 98.28 1.45e-32 . . . . 45 1 33 no PDB 1FY8 . "Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 34 no PDB 1JV8 . "Nmr Structure Of Bpti Mutant G37a" . . . . . 100.00 58 98.28 98.28 5.64e-33 . . . . 45 1 35 no PDB 1JV9 . "Nmr Structure Of Bpti Mutant G37a" . . . . . 100.00 58 98.28 98.28 5.64e-33 . . . . 45 1 36 no PDB 1MTN . "Bovine Alpha-Chymotrypsin:bpti Crystallization" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 37 no PDB 1NAG . "Crevice-forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" . . . . . 100.00 58 98.28 98.28 1.13e-32 . . . . 45 1 38 no PDB 1OA5 . "The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 39 no PDB 1OA6 . "The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 40 no PDB 1PIT . "Determination Of A High-Quality Nuclear Magnetic Resonance Solution Structure Of The Bovine Pancreatic Trypsin Inhibitor And Co" . . . . . 98.28 58 100.00 100.00 6.78e-33 . . . . 45 1 41 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 1.39e-33 . . . . 45 1 42 no PDB 1UUA . "Solution Structure Of A Truncated Bovine Pancreatic Trypsin Inhibitor, 3-58 Bpti" . . . . . 96.55 56 100.00 100.00 5.26e-32 . . . . 45 1 43 no PDB 1YKT . "TrypsinBPTI COMPLEX MUTANT" . . . . . 96.55 56 100.00 100.00 3.19e-32 . . . . 45 1 44 no PDB 2FI4 . "Crystal Structure Of A Bpti Variant (Cys14->ser) In Complex With Trypsin" . . . . . 100.00 58 98.28 98.28 1.02e-32 . . . . 45 1 45 no PDB 2FI5 . "Crystal Structure Of A Bpti Variant (Cys38->ser) In Complex With Trypsin" . . . . . 100.00 58 98.28 98.28 1.02e-32 . . . . 45 1 46 no PDB 2FTL . "Crystal Structure Of Trypsin Complexed With Bpti At 100k" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 47 no PDB 2FTM . "Crystal Structure Of Trypsin Complexed With The Bpti Variant (Tyr35- >gly)" . . . . . 100.00 58 98.28 98.28 2.75e-32 . . . . 45 1 48 no PDB 2HEX . "Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 49 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 1.39e-33 . . . . 45 1 50 no PDB 2KAI . "Refined 2.5 Angstroms X-Ray Crystal Structure Of The Complex Formed By Porcine Kallikrein A And The Bovine Pancreatic Trypsin I" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 51 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 1.39e-33 . . . . 45 1 52 no PDB 2R9P . "Human Mesotrypsin Complexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 53 no PDB 2RA3 . "Human Cationic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (bpti)" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 54 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 1.39e-33 . . . . 45 1 55 no PDB 2TPI . "On The Disordered Activation Domain In Trypsinogen. Chemical Labelling And Low-Temperature Crystallography" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 56 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 1.39e-33 . . . . 45 1 57 no PDB 3FP6 . "Anionic Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined To The 1.49 A Resolution Limit" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 58 no PDB 3FP7 . "Anionic Trypsin Variant S195a In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Cleaved At The Scissile Bond (Lys15-Al" . . . . . 74.14 43 100.00 100.00 2.59e-21 . . . . 45 1 59 no PDB 3FP8 . "Anionic Trypsin Variant S195a In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined To The 1.46 A Resolution Li" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 60 no PDB 3GYM . "Structure Of Prostasin In Complex With Aprotinin" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 61 no PDB 3LDI . "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 62 no PDB 3LDJ . "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 63 no PDB 3LDM . "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 64 no PDB 3OTJ . "A Crystal Structure Of Trypsin Complexed With Bpti (Bovine Pancreatic Trypsin Inhibitor) By X-RayNEUTRON JOINT REFINEMENT" . . . . . 98.28 58 100.00 100.00 6.78e-33 . . . . 45 1 65 no PDB 3TGI . "Wild-Type Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" . . . . . 100.00 65 100.00 100.00 1.34e-33 . . . . 45 1 66 no PDB 3TGJ . "S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" . . . . . 100.00 65 100.00 100.00 1.34e-33 . . . . 45 1 67 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 1.34e-33 . . . . 45 1 68 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 1.39e-33 . . . . 45 1 69 no PDB 3U1J . "Aprotinin Bound To Dengue Virus Protease" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 70 no PDB 4BNR . "Extremely Stable Complex Of Crayfish Trypsin With Bovine Trypsin Inhibitor" . . . . . 100.00 100 100.00 100.00 2.00e-34 . . . . 45 1 71 no PDB 4DG4 . "Human Mesotrypsin-s39y Complexed With Bovine Pancreatic Trypsin Inhibitor (bpti)" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 72 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 1.39e-33 . . . . 45 1 73 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 " . . . . . 100.00 58 98.28 100.00 4.07e-33 . . . . 45 1 74 no PDB 4WWY . "Human Cationic Trypsin G193r Mutant In Complex With Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 75 no PDB 4WXV . "Human Cationic Trypsin K97d Mutant In Complex With Bovine Pancreatic Trypsin Inhibitor (bpti)" . . . . . 94.83 55 100.00 100.00 1.85e-31 . . . . 45 1 76 no PDB 4Y0Z . "Trypsin In Complex With With Bpti Mutant Aminobutyric Acid" . . . . . 100.00 58 98.28 98.28 8.16e-33 . . . . 45 1 77 no PDB 4Y10 . "Trypsin In Complex With With Bpti Mutant (2s)-2-amino-4,4- Difluorobutanoic Acid" . . . . . 100.00 58 98.28 98.28 8.16e-33 . . . . 45 1 78 no PDB 4Y11 . "Trypsin In Complex With With Bpti Mutant (2s)-2-amino-4,4,4- Trifluorobutanoic Acid" . . . . . 100.00 58 98.28 98.28 8.16e-33 . . . . 45 1 79 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 6.78e-33 . . . . 45 1 80 no PDB 6PTI . "Structure Of Form Iii Crystals Of Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 81 no PDB 8PTI . "Crystal Structure Of A Y35g Mutant Of Bovine Pancreatic Trypsin Inhibitor" . . . . . 100.00 58 98.28 98.28 2.75e-32 . . . . 45 1 82 no PDB 9PTI . "Basic Pancreatic Trypsin Inhibitor (met 52 Oxidized)" . . . . . 100.00 58 98.28 98.28 1.55e-32 . . . . 45 1 83 no EMBL CAA27062 . "unnamed protein product [Bos taurus]" . . . . . 100.00 89 100.00 100.00 1.49e-33 . . . . 45 1 84 no EMBL CAA27063 . "unnamed protein product [Bos taurus]" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 85 no EMBL CAA28371 . "unnamed protein product [synthetic construct]" . . . . . 100.00 59 100.00 100.00 1.13e-33 . . . . 45 1 86 no EMBL CAA28886 . "trypsin ihibitor precursor [Bos taurus]" . . . . . 100.00 92 100.00 100.00 2.48e-34 . . . . 45 1 87 no EMBL CAA37967 . "aprotinin [synthetic construct]" . . . . . 100.00 59 100.00 100.00 1.45e-33 . . . . 45 1 88 no GB AAA72535 . "alkaline phosphatase/pancreatic trypsin inhibitor precursor [synthetic construct]" . . . . . 100.00 79 98.28 100.00 6.02e-34 . . . . 45 1 89 no GB AAB25189 . "major cationic kallikrein inhibitor [cattle, posterior pituitary gland, Peptide, 58 aa]" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 90 no GB AAD13685 . "trypsin inhibitor [Bos taurus]" . . . . . 100.00 100 100.00 100.00 2.00e-34 . . . . 45 1 91 no GB ABX57797 . "aprotinin precursor [Plastid transformation vector pAPR20]" . . . . . 100.00 104 100.00 100.00 6.80e-35 . . . . 45 1 92 no GB ABX57799 . "aprotinin precursor [Plastid transformation vector pAPR21]" . . . . . 100.00 100 100.00 100.00 9.39e-35 . . . . 45 1 93 no PRF 1405218A . "aprotinin analog" . . . . . 98.28 57 100.00 100.00 5.69e-33 . . . . 45 1 94 no PRF 1405218D . "aprotinin analog" . . . . . 100.00 59 100.00 100.00 1.17e-33 . . . . 45 1 95 no PRF 1510193A . BPTI . . . . . 100.00 100 98.28 100.00 8.30e-34 . . . . 45 1 96 no PRF 681071A . "inhibitor,basic pancreatic trypsin" . . . . . 100.00 58 100.00 100.00 1.39e-33 . . . . 45 1 97 no SP P00974 . "RecName: Full=Pancreatic trypsin inhibitor; AltName: Full=Aprotinin; AltName: Full=Basic protease inhibitor; Short=BPI; Short=B" . . . . . 100.00 100 100.00 100.00 2.00e-34 . . . . 45 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'basic pancreatic trypsin inhibitor' common 45 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 . 45 1 2 . PRO . 45 1 3 . ASP . 45 1 4 . PHE . 45 1 5 . CYS . 45 1 6 . LEU . 45 1 7 . GLU . 45 1 8 . PRO . 45 1 9 . PRO . 45 1 10 . TYR . 45 1 11 . THR . 45 1 12 . GLY . 45 1 13 . PRO . 45 1 14 . CYS . 45 1 15 . LYS . 45 1 16 . ALA . 45 1 17 . ARG . 45 1 18 . ILE . 45 1 19 . ILE . 45 1 20 . ARG . 45 1 21 . TYR . 45 1 22 . PHE . 45 1 23 . TYR . 45 1 24 . ASN . 45 1 25 . ALA . 45 1 26 . LYS . 45 1 27 . ALA . 45 1 28 . GLY . 45 1 29 . LEU . 45 1 30 . CYS . 45 1 31 . GLN . 45 1 32 . THR . 45 1 33 . PHE . 45 1 34 . VAL . 45 1 35 . TYR . 45 1 36 . GLY . 45 1 37 . GLY . 45 1 38 . CYS . 45 1 39 . ARG . 45 1 40 . ALA . 45 1 41 . LYS . 45 1 42 . ARG . 45 1 43 . ASN . 45 1 44 . ASN . 45 1 45 . PHE . 45 1 46 . LYS . 45 1 47 . SER . 45 1 48 . ALA . 45 1 49 . GLU . 45 1 50 . ASP . 45 1 51 . CYS . 45 1 52 . MET . 45 1 53 . ARG . 45 1 54 . THR . 45 1 55 . CYS . 45 1 56 . GLY . 45 1 57 . GLY . 45 1 58 . ALA . 45 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 45 1 . PRO 2 2 45 1 . ASP 3 3 45 1 . PHE 4 4 45 1 . CYS 5 5 45 1 . LEU 6 6 45 1 . GLU 7 7 45 1 . PRO 8 8 45 1 . PRO 9 9 45 1 . TYR 10 10 45 1 . THR 11 11 45 1 . GLY 12 12 45 1 . PRO 13 13 45 1 . CYS 14 14 45 1 . LYS 15 15 45 1 . ALA 16 16 45 1 . ARG 17 17 45 1 . ILE 18 18 45 1 . ILE 19 19 45 1 . ARG 20 20 45 1 . TYR 21 21 45 1 . PHE 22 22 45 1 . TYR 23 23 45 1 . ASN 24 24 45 1 . ALA 25 25 45 1 . LYS 26 26 45 1 . ALA 27 27 45 1 . GLY 28 28 45 1 . LEU 29 29 45 1 . CYS 30 30 45 1 . GLN 31 31 45 1 . THR 32 32 45 1 . PHE 33 33 45 1 . VAL 34 34 45 1 . TYR 35 35 45 1 . GLY 36 36 45 1 . GLY 37 37 45 1 . CYS 38 38 45 1 . ARG 39 39 45 1 . ALA 40 40 45 1 . LYS 41 41 45 1 . ARG 42 42 45 1 . ASN 43 43 45 1 . ASN 44 44 45 1 . PHE 45 45 45 1 . LYS 46 46 45 1 . SER 47 47 45 1 . ALA 48 48 45 1 . GLU 49 49 45 1 . ASP 50 50 45 1 . CYS 51 51 45 1 . MET 52 52 45 1 . ARG 53 53 45 1 . THR 54 54 45 1 . CYS 55 55 45 1 . GLY 56 56 45 1 . GLY 57 57 45 1 . ALA 58 58 45 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 45 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $basic_pancreatic_trypsin_inhibitor . 9909 organism . 'Bos primigenius' cow . . Eukaryota Metazoa Bos primigenius generic . . . pancreas . . . . . . . . . . . . . . . . 45 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 45 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $basic_pancreatic_trypsin_inhibitor . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 45 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 45 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 45 _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 4.6 . na 45 1 temperature 341 . K 45 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 45 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 45 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 45 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 45 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 45 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 45 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . TSP . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 45 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 45 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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 $sample_one . 45 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 3 3 ASP H H 1 8.49 . . 1 . . . . . . . . 45 1 2 . 1 1 3 3 ASP HA H 1 4.23 . . 1 . . . . . . . . 45 1 3 . 1 1 3 3 ASP HB2 H 1 2.79 . . 1 . . . . . . . . 45 1 4 . 1 1 3 3 ASP HB3 H 1 2.79 . . 1 . . . . . . . . 45 1 5 . 1 1 4 4 PHE H H 1 7.57 . . 1 . . . . . . . . 45 1 6 . 1 1 4 4 PHE HA H 1 4.63 . . 1 . . . . . . . . 45 1 7 . 1 1 4 4 PHE HB2 H 1 2.99 . . 2 . . . . . . . . 45 1 8 . 1 1 4 4 PHE HB3 H 1 3.34 . . 2 . . . . . . . . 45 1 9 . 1 1 4 4 PHE HD1 H 1 7.01 . . 1 . . . . . . . . 45 1 10 . 1 1 4 4 PHE HD2 H 1 7.01 . . 1 . . . . . . . . 45 1 11 . 1 1 4 4 PHE HE1 H 1 7.4 . . 1 . . . . . . . . 45 1 12 . 1 1 4 4 PHE HE2 H 1 7.4 . . 1 . . . . . . . . 45 1 13 . 1 1 4 4 PHE HZ H 1 7.06 . . 1 . . . . . . . . 45 1 14 . 1 1 5 5 CYS H H 1 7.37 . . 1 . . . . . . . . 45 1 15 . 1 1 5 5 CYS HA H 1 4.39 . . 1 . . . . . . . . 45 1 16 . 1 1 5 5 CYS HB2 H 1 2.75 . . 2 . . . . . . . . 45 1 17 . 1 1 5 5 CYS HB3 H 1 2.91 . . 2 . . . . . . . . 45 1 18 . 1 1 6 6 LEU H H 1 7.5 . . 1 . . . . . . . . 45 1 19 . 1 1 6 6 LEU HA H 1 4.52 . . 1 . . . . . . . . 45 1 20 . 1 1 6 6 LEU HB2 H 1 1.88 . . 1 . . . . . . . . 45 1 21 . 1 1 6 6 LEU HB3 H 1 1.88 . . 1 . . . . . . . . 45 1 22 . 1 1 6 6 LEU HG H 1 1.71 . . 1 . . . . . . . . 45 1 23 . 1 1 6 6 LEU HD11 H 1 .88 . . 2 . . . . . . . . 45 1 24 . 1 1 6 6 LEU HD12 H 1 .88 . . 2 . . . . . . . . 45 1 25 . 1 1 6 6 LEU HD13 H 1 .88 . . 2 . . . . . . . . 45 1 26 . 1 1 6 6 LEU HD21 H 1 .98 . . 2 . . . . . . . . 45 1 27 . 1 1 6 6 LEU HD22 H 1 .98 . . 2 . . . . . . . . 45 1 28 . 1 1 6 6 LEU HD23 H 1 .98 . . 2 . . . . . . . . 45 1 29 . 1 1 7 7 GLU H H 1 7.5 . . 1 . . . . . . . . 45 1 30 . 1 1 7 7 GLU HA H 1 4.61 . . 1 . . . . . . . . 45 1 31 . 1 1 7 7 GLU HB2 H 1 2.18 . . 2 . . . . . . . . 45 1 32 . 1 1 7 7 GLU HB3 H 1 2.27 . . 2 . . . . . . . . 45 1 33 . 1 1 7 7 GLU HG2 H 1 2.58 . . 1 . . . . . . . . 45 1 34 . 1 1 7 7 GLU HG3 H 1 2.58 . . 1 . . . . . . . . 45 1 35 . 1 1 8 8 PRO HA H 1 4.67 . . 1 . . . . . . . . 45 1 36 . 1 1 8 8 PRO HB2 H 1 1.88 . . 2 . . . . . . . . 45 1 37 . 1 1 8 8 PRO HB3 H 1 2.45 . . 2 . . . . . . . . 45 1 38 . 1 1 8 8 PRO HG2 H 1 2.12 . . 1 . . . . . . . . 45 1 39 . 1 1 8 8 PRO HG3 H 1 2.12 . . 1 . . . . . . . . 45 1 40 . 1 1 8 8 PRO HD2 H 1 3.98 . . 2 . . . . . . . . 45 1 41 . 1 1 8 8 PRO HD3 H 1 3.7 . . 2 . . . . . . . . 45 1 42 . 1 1 9 9 PRO HA H 1 3.77 . . 1 . . . . . . . . 45 1 43 . 1 1 9 9 PRO HB2 H 1 .27 . . 2 . . . . . . . . 45 1 44 . 1 1 9 9 PRO HB3 H 1 .14 . . 2 . . . . . . . . 45 1 45 . 1 1 9 9 PRO HG2 H 1 1.3 . . 2 . . . . . . . . 45 1 46 . 1 1 9 9 PRO HG3 H 1 .19 . . 2 . . . . . . . . 45 1 47 . 1 1 9 9 PRO HD2 H 1 2.97 . . 2 . . . . . . . . 45 1 48 . 1 1 9 9 PRO HD3 H 1 3.18 . . 2 . . . . . . . . 45 1 49 . 1 1 10 10 TYR H H 1 7.64 . . 1 . . . . . . . . 45 1 50 . 1 1 10 10 TYR HA H 1 4.96 . . 1 . . . . . . . . 45 1 51 . 1 1 10 10 TYR HB2 H 1 2.95 . . 1 . . . . . . . . 45 1 52 . 1 1 10 10 TYR HB3 H 1 2.95 . . 1 . . . . . . . . 45 1 53 . 1 1 10 10 TYR HD1 H 1 7.34 . . 1 . . . . . . . . 45 1 54 . 1 1 10 10 TYR HD2 H 1 7.34 . . 1 . . . . . . . . 45 1 55 . 1 1 10 10 TYR HE1 H 1 7.1 . . 1 . . . . . . . . 45 1 56 . 1 1 10 10 TYR HE2 H 1 7.1 . . 1 . . . . . . . . 45 1 57 . 1 1 11 11 THR H H 1 8.74 . . 1 . . . . . . . . 45 1 58 . 1 1 11 11 THR HA H 1 4.55 . . 1 . . . . . . . . 45 1 59 . 1 1 11 11 THR HB H 1 4.07 . . 1 . . . . . . . . 45 1 60 . 1 1 11 11 THR HG21 H 1 1.4 . . 1 . . . . . . . . 45 1 61 . 1 1 11 11 THR HG22 H 1 1.4 . . 1 . . . . . . . . 45 1 62 . 1 1 11 11 THR HG23 H 1 1.4 . . 1 . . . . . . . . 45 1 63 . 1 1 12 12 GLY H H 1 7 . . 1 . . . . . . . . 45 1 64 . 1 1 12 12 GLY HA2 H 1 3.32 . . 2 . . . . . . . . 45 1 65 . 1 1 12 12 GLY HA3 H 1 3.97 . . 2 . . . . . . . . 45 1 66 . 1 1 14 14 CYS H H 1 8.54 . . 1 . . . . . . . . 45 1 67 . 1 1 14 14 CYS HA H 1 4.56 . . 1 . . . . . . . . 45 1 68 . 1 1 14 14 CYS HB2 H 1 2.81 . . 2 . . . . . . . . 45 1 69 . 1 1 14 14 CYS HB3 H 1 3.48 . . 2 . . . . . . . . 45 1 70 . 1 1 15 15 LYS H H 1 7.83 . . 1 . . . . . . . . 45 1 71 . 1 1 15 15 LYS HA H 1 4.45 . . 1 . . . . . . . . 45 1 72 . 1 1 15 15 LYS HB2 H 1 1.59 . . 2 . . . . . . . . 45 1 73 . 1 1 15 15 LYS HB3 H 1 2.08 . . 2 . . . . . . . . 45 1 74 . 1 1 15 15 LYS HG2 H 1 1.31 . . 2 . . . . . . . . 45 1 75 . 1 1 15 15 LYS HG3 H 1 1.41 . . 2 . . . . . . . . 45 1 76 . 1 1 16 16 ALA H H 1 8.17 . . 1 . . . . . . . . 45 1 77 . 1 1 16 16 ALA HA H 1 4.33 . . 1 . . . . . . . . 45 1 78 . 1 1 16 16 ALA HB1 H 1 1.18 . . 1 . . . . . . . . 45 1 79 . 1 1 16 16 ALA HB2 H 1 1.18 . . 1 . . . . . . . . 45 1 80 . 1 1 16 16 ALA HB3 H 1 1.18 . . 1 . . . . . . . . 45 1 81 . 1 1 17 17 ARG H H 1 7.95 . . 1 . . . . . . . . 45 1 82 . 1 1 17 17 ARG HA H 1 4.33 . . 1 . . . . . . . . 45 1 83 . 1 1 17 17 ARG HB2 H 1 1.63 . . 1 . . . . . . . . 45 1 84 . 1 1 17 17 ARG HB3 H 1 1.63 . . 1 . . . . . . . . 45 1 85 . 1 1 18 18 ILE H H 1 8.04 . . 1 . . . . . . . . 45 1 86 . 1 1 18 18 ILE HA H 1 4.24 . . 1 . . . . . . . . 45 1 87 . 1 1 18 18 ILE HB H 1 1.9 . . 1 . . . . . . . . 45 1 88 . 1 1 18 18 ILE HG12 H 1 1.07 . . 1 . . . . . . . . 45 1 89 . 1 1 18 18 ILE HG13 H 1 1.07 . . 1 . . . . . . . . 45 1 90 . 1 1 18 18 ILE HG21 H 1 .97 . . 1 . . . . . . . . 45 1 91 . 1 1 18 18 ILE HG22 H 1 .97 . . 1 . . . . . . . . 45 1 92 . 1 1 18 18 ILE HG23 H 1 .97 . . 1 . . . . . . . . 45 1 93 . 1 1 18 18 ILE HD11 H 1 .73 . . 1 . . . . . . . . 45 1 94 . 1 1 18 18 ILE HD12 H 1 .73 . . 1 . . . . . . . . 45 1 95 . 1 1 18 18 ILE HD13 H 1 .73 . . 1 . . . . . . . . 45 1 96 . 1 1 19 19 ILE H H 1 8.46 . . 1 . . . . . . . . 45 1 97 . 1 1 19 19 ILE HA H 1 4.35 . . 1 . . . . . . . . 45 1 98 . 1 1 19 19 ILE HB H 1 1.96 . . 1 . . . . . . . . 45 1 99 . 1 1 19 19 ILE HG12 H 1 1.46 . . 1 . . . . . . . . 45 1 100 . 1 1 19 19 ILE HG13 H 1 1.46 . . 1 . . . . . . . . 45 1 101 . 1 1 19 19 ILE HG21 H 1 .74 . . 1 . . . . . . . . 45 1 102 . 1 1 19 19 ILE HG22 H 1 .74 . . 1 . . . . . . . . 45 1 103 . 1 1 19 19 ILE HG23 H 1 .74 . . 1 . . . . . . . . 45 1 104 . 1 1 19 19 ILE HD11 H 1 .73 . . 1 . . . . . . . . 45 1 105 . 1 1 19 19 ILE HD12 H 1 .73 . . 1 . . . . . . . . 45 1 106 . 1 1 19 19 ILE HD13 H 1 .73 . . 1 . . . . . . . . 45 1 107 . 1 1 20 20 ARG H H 1 8.33 . . 1 . . . . . . . . 45 1 108 . 1 1 20 20 ARG HA H 1 4.72 . . 1 . . . . . . . . 45 1 109 . 1 1 20 20 ARG HB2 H 1 .86 . . 2 . . . . . . . . 45 1 110 . 1 1 20 20 ARG HB3 H 1 1.83 . . 2 . . . . . . . . 45 1 111 . 1 1 20 20 ARG HG2 H 1 1.37 . . 2 . . . . . . . . 45 1 112 . 1 1 20 20 ARG HG3 H 1 1.72 . . 2 . . . . . . . . 45 1 113 . 1 1 20 20 ARG HD2 H 1 3.08 . . 2 . . . . . . . . 45 1 114 . 1 1 20 20 ARG HD3 H 1 3.48 . . 2 . . . . . . . . 45 1 115 . 1 1 20 20 ARG HE H 1 7.37 . . 1 . . . . . . . . 45 1 116 . 1 1 21 21 TYR H H 1 9.1 . . 1 . . . . . . . . 45 1 117 . 1 1 21 21 TYR HA H 1 5.71 . . 1 . . . . . . . . 45 1 118 . 1 1 21 21 TYR HB2 H 1 2.72 . . 1 . . . . . . . . 45 1 119 . 1 1 21 21 TYR HB3 H 1 2.72 . . 1 . . . . . . . . 45 1 120 . 1 1 21 21 TYR HD1 H 1 6.74 . . 1 . . . . . . . . 45 1 121 . 1 1 21 21 TYR HD2 H 1 6.74 . . 1 . . . . . . . . 45 1 122 . 1 1 21 21 TYR HE1 H 1 6.79 . . 1 . . . . . . . . 45 1 123 . 1 1 21 21 TYR HE2 H 1 6.79 . . 1 . . . . . . . . 45 1 124 . 1 1 22 22 PHE H H 1 9.74 . . 1 . . . . . . . . 45 1 125 . 1 1 22 22 PHE HA H 1 5.3 . . 1 . . . . . . . . 45 1 126 . 1 1 22 22 PHE HB2 H 1 2.85 . . 2 . . . . . . . . 45 1 127 . 1 1 22 22 PHE HB3 H 1 2.96 . . 2 . . . . . . . . 45 1 128 . 1 1 22 22 PHE HD1 H 1 7.16 . . 3 . . . . . . . . 45 1 129 . 1 1 22 22 PHE HD2 H 1 7.27 . . 3 . . . . . . . . 45 1 130 . 1 1 22 22 PHE HE1 H 1 6.98 . . 3 . . . . . . . . 45 1 131 . 1 1 22 22 PHE HE2 H 1 7.07 . . 3 . . . . . . . . 45 1 132 . 1 1 22 22 PHE HZ H 1 7.31 . . 1 . . . . . . . . 45 1 133 . 1 1 23 23 TYR H H 1 10.46 . . 1 . . . . . . . . 45 1 134 . 1 1 23 23 TYR HA H 1 4.32 . . 1 . . . . . . . . 45 1 135 . 1 1 23 23 TYR HB2 H 1 2.74 . . 2 . . . . . . . . 45 1 136 . 1 1 23 23 TYR HB3 H 1 3.49 . . 2 . . . . . . . . 45 1 137 . 1 1 23 23 TYR HD1 H 1 7.19 . . 1 . . . . . . . . 45 1 138 . 1 1 23 23 TYR HD2 H 1 7.19 . . 1 . . . . . . . . 45 1 139 . 1 1 23 23 TYR HE1 H 1 6.35 . . 1 . . . . . . . . 45 1 140 . 1 1 23 23 TYR HE2 H 1 6.35 . . 1 . . . . . . . . 45 1 141 . 1 1 24 24 ASN H H 1 7.78 . . 1 . . . . . . . . 45 1 142 . 1 1 24 24 ASN HA H 1 4.65 . . 1 . . . . . . . . 45 1 143 . 1 1 24 24 ASN HB2 H 1 2.18 . . 2 . . . . . . . . 45 1 144 . 1 1 24 24 ASN HB3 H 1 2.86 . . 2 . . . . . . . . 45 1 145 . 1 1 24 24 ASN HD21 H 1 6.96 . . 2 . . . . . . . . 45 1 146 . 1 1 24 24 ASN HD22 H 1 7.79 . . 2 . . . . . . . . 45 1 147 . 1 1 25 25 ALA H H 1 8.59 . . 1 . . . . . . . . 45 1 148 . 1 1 25 25 ALA HA H 1 3.81 . . 1 . . . . . . . . 45 1 149 . 1 1 25 25 ALA HB1 H 1 1.58 . . 1 . . . . . . . . 45 1 150 . 1 1 25 25 ALA HB2 H 1 1.58 . . 1 . . . . . . . . 45 1 151 . 1 1 25 25 ALA HB3 H 1 1.58 . . 1 . . . . . . . . 45 1 152 . 1 1 26 26 LYS H H 1 7.82 . . 1 . . . . . . . . 45 1 153 . 1 1 26 26 LYS HA H 1 4.11 . . 1 . . . . . . . . 45 1 154 . 1 1 26 26 LYS HB2 H 1 1.89 . . 1 . . . . . . . . 45 1 155 . 1 1 26 26 LYS HB3 H 1 1.89 . . 1 . . . . . . . . 45 1 156 . 1 1 27 27 ALA H H 1 6.77 . . 1 . . . . . . . . 45 1 157 . 1 1 27 27 ALA HA H 1 4.35 . . 1 . . . . . . . . 45 1 158 . 1 1 27 27 ALA HB1 H 1 1.2 . . 1 . . . . . . . . 45 1 159 . 1 1 27 27 ALA HB2 H 1 1.2 . . 1 . . . . . . . . 45 1 160 . 1 1 27 27 ALA HB3 H 1 1.2 . . 1 . . . . . . . . 45 1 161 . 1 1 28 28 GLY H H 1 8.07 . . 1 . . . . . . . . 45 1 162 . 1 1 28 28 GLY HA2 H 1 3.64 . . 2 . . . . . . . . 45 1 163 . 1 1 28 28 GLY HA3 H 1 3.95 . . 2 . . . . . . . . 45 1 164 . 1 1 29 29 LEU H H 1 6.76 . . 1 . . . . . . . . 45 1 165 . 1 1 29 29 LEU HA H 1 4.73 . . 1 . . . . . . . . 45 1 166 . 1 1 29 29 LEU HB2 H 1 1.45 . . 2 . . . . . . . . 45 1 167 . 1 1 29 29 LEU HB3 H 1 1.69 . . 2 . . . . . . . . 45 1 168 . 1 1 29 29 LEU HG H 1 1.44 . . 1 . . . . . . . . 45 1 169 . 1 1 29 29 LEU HD11 H 1 .78 . . 2 . . . . . . . . 45 1 170 . 1 1 29 29 LEU HD12 H 1 .78 . . 2 . . . . . . . . 45 1 171 . 1 1 29 29 LEU HD13 H 1 .78 . . 2 . . . . . . . . 45 1 172 . 1 1 29 29 LEU HD21 H 1 .87 . . 2 . . . . . . . . 45 1 173 . 1 1 29 29 LEU HD22 H 1 .87 . . 2 . . . . . . . . 45 1 174 . 1 1 29 29 LEU HD23 H 1 .87 . . 2 . . . . . . . . 45 1 175 . 1 1 30 30 CYS H H 1 8.23 . . 1 . . . . . . . . 45 1 176 . 1 1 30 30 CYS HA H 1 5.58 . . 1 . . . . . . . . 45 1 177 . 1 1 30 30 CYS HB2 H 1 2.71 . . 2 . . . . . . . . 45 1 178 . 1 1 30 30 CYS HB3 H 1 3.63 . . 2 . . . . . . . . 45 1 179 . 1 1 31 31 GLN H H 1 8.74 . . 1 . . . . . . . . 45 1 180 . 1 1 31 31 GLN HA H 1 4.87 . . 1 . . . . . . . . 45 1 181 . 1 1 31 31 GLN HB2 H 1 1.77 . . 2 . . . . . . . . 45 1 182 . 1 1 31 31 GLN HB3 H 1 2.16 . . 2 . . . . . . . . 45 1 183 . 1 1 31 31 GLN HG2 H 1 1.83 . . 2 . . . . . . . . 45 1 184 . 1 1 31 31 GLN HG3 H 1 2.02 . . 2 . . . . . . . . 45 1 185 . 1 1 31 31 GLN HE21 H 1 7.22 . . 2 . . . . . . . . 45 1 186 . 1 1 31 31 GLN HE22 H 1 7.3 . . 2 . . . . . . . . 45 1 187 . 1 1 32 32 THR H H 1 7.94 . . 1 . . . . . . . . 45 1 188 . 1 1 32 32 THR HA H 1 5.24 . . 1 . . . . . . . . 45 1 189 . 1 1 32 32 THR HB H 1 4.04 . . 1 . . . . . . . . 45 1 190 . 1 1 32 32 THR HG21 H 1 .62 . . 1 . . . . . . . . 45 1 191 . 1 1 32 32 THR HG22 H 1 .62 . . 1 . . . . . . . . 45 1 192 . 1 1 32 32 THR HG23 H 1 .62 . . 1 . . . . . . . . 45 1 193 . 1 1 33 33 PHE H H 1 9.32 . . 1 . . . . . . . . 45 1 194 . 1 1 33 33 PHE HA H 1 4.91 . . 1 . . . . . . . . 45 1 195 . 1 1 33 33 PHE HB2 H 1 2.98 . . 2 . . . . . . . . 45 1 196 . 1 1 33 33 PHE HB3 H 1 3.13 . . 2 . . . . . . . . 45 1 197 . 1 1 33 33 PHE HD1 H 1 7.13 . . 1 . . . . . . . . 45 1 198 . 1 1 33 33 PHE HD2 H 1 7.13 . . 1 . . . . . . . . 45 1 199 . 1 1 33 33 PHE HE1 H 1 7.2 . . 1 . . . . . . . . 45 1 200 . 1 1 33 33 PHE HE2 H 1 7.2 . . 1 . . . . . . . . 45 1 201 . 1 1 33 33 PHE HZ H 1 7.33 . . 1 . . . . . . . . 45 1 202 . 1 1 34 34 VAL H H 1 8.17 . . 1 . . . . . . . . 45 1 203 . 1 1 34 34 VAL HA H 1 3.98 . . 1 . . . . . . . . 45 1 204 . 1 1 34 34 VAL HB H 1 1.96 . . 1 . . . . . . . . 45 1 205 . 1 1 34 34 VAL HG11 H 1 .73 . . 2 . . . . . . . . 45 1 206 . 1 1 34 34 VAL HG12 H 1 .73 . . 2 . . . . . . . . 45 1 207 . 1 1 34 34 VAL HG13 H 1 .73 . . 2 . . . . . . . . 45 1 208 . 1 1 34 34 VAL HG21 H 1 .83 . . 2 . . . . . . . . 45 1 209 . 1 1 34 34 VAL HG22 H 1 .83 . . 2 . . . . . . . . 45 1 210 . 1 1 34 34 VAL HG23 H 1 .83 . . 2 . . . . . . . . 45 1 211 . 1 1 35 35 TYR H H 1 9.26 . . 1 . . . . . . . . 45 1 212 . 1 1 35 35 TYR HA H 1 4.9 . . 1 . . . . . . . . 45 1 213 . 1 1 35 35 TYR HB2 H 1 2.52 . . 2 . . . . . . . . 45 1 214 . 1 1 35 35 TYR HB3 H 1 2.64 . . 2 . . . . . . . . 45 1 215 . 1 1 35 35 TYR HE1 H 1 6.83 . . 1 . . . . . . . . 45 1 216 . 1 1 35 35 TYR HE2 H 1 6.83 . . 1 . . . . . . . . 45 1 217 . 1 1 36 36 GLY H H 1 8.49 . . 1 . . . . . . . . 45 1 218 . 1 1 36 36 GLY HA2 H 1 3.28 . . 2 . . . . . . . . 45 1 219 . 1 1 36 36 GLY HA3 H 1 4.33 . . 2 . . . . . . . . 45 1 220 . 1 1 37 37 GLY HA2 H 1 2.92 . . 2 . . . . . . . . 45 1 221 . 1 1 37 37 GLY HA3 H 1 4.24 . . 2 . . . . . . . . 45 1 222 . 1 1 38 38 CYS H H 1 7.74 . . 1 . . . . . . . . 45 1 223 . 1 1 38 38 CYS HA H 1 4.97 . . 1 . . . . . . . . 45 1 224 . 1 1 38 38 CYS HB2 H 1 3.15 . . 2 . . . . . . . . 45 1 225 . 1 1 38 38 CYS HB3 H 1 3.8 . . 2 . . . . . . . . 45 1 226 . 1 1 39 39 ARG H H 1 8.92 . . 1 . . . . . . . . 45 1 227 . 1 1 39 39 ARG HA H 1 3.95 . . 1 . . . . . . . . 45 1 228 . 1 1 39 39 ARG HB2 H 1 2.26 . . 1 . . . . . . . . 45 1 229 . 1 1 39 39 ARG HB3 H 1 2.26 . . 1 . . . . . . . . 45 1 230 . 1 1 40 40 ALA H H 1 7.3 . . 1 . . . . . . . . 45 1 231 . 1 1 40 40 ALA HA H 1 4.13 . . 1 . . . . . . . . 45 1 232 . 1 1 40 40 ALA HB1 H 1 1.23 . . 1 . . . . . . . . 45 1 233 . 1 1 40 40 ALA HB2 H 1 1.23 . . 1 . . . . . . . . 45 1 234 . 1 1 40 40 ALA HB3 H 1 1.23 . . 1 . . . . . . . . 45 1 235 . 1 1 41 41 LYS H H 1 8.22 . . 1 . . . . . . . . 45 1 236 . 1 1 41 41 LYS HA H 1 4.49 . . 1 . . . . . . . . 45 1 237 . 1 1 41 41 LYS HB2 H 1 1.67 . . 2 . . . . . . . . 45 1 238 . 1 1 41 41 LYS HB3 H 1 2.26 . . 2 . . . . . . . . 45 1 239 . 1 1 41 41 LYS HG2 H 1 1.32 . . 2 . . . . . . . . 45 1 240 . 1 1 41 41 LYS HG3 H 1 1.49 . . 2 . . . . . . . . 45 1 241 . 1 1 42 42 ARG H H 1 8.15 . . 1 . . . . . . . . 45 1 242 . 1 1 42 42 ARG HA H 1 3.73 . . 1 . . . . . . . . 45 1 243 . 1 1 42 42 ARG HB2 H 1 .53 . . 2 . . . . . . . . 45 1 244 . 1 1 42 42 ARG HB3 H 1 1.18 . . 2 . . . . . . . . 45 1 245 . 1 1 42 42 ARG HG2 H 1 1.22 . . 2 . . . . . . . . 45 1 246 . 1 1 42 42 ARG HG3 H 1 1.48 . . 2 . . . . . . . . 45 1 247 . 1 1 42 42 ARG HD2 H 1 2.76 . . 2 . . . . . . . . 45 1 248 . 1 1 42 42 ARG HD3 H 1 2.86 . . 2 . . . . . . . . 45 1 249 . 1 1 42 42 ARG HE H 1 6.8 . . 1 . . . . . . . . 45 1 250 . 1 1 43 43 ASN H H 1 7.22 . . 1 . . . . . . . . 45 1 251 . 1 1 43 43 ASN HA H 1 5.03 . . 1 . . . . . . . . 45 1 252 . 1 1 43 43 ASN HB2 H 1 3.28 . . 2 . . . . . . . . 45 1 253 . 1 1 43 43 ASN HB3 H 1 3.34 . . 2 . . . . . . . . 45 1 254 . 1 1 43 43 ASN HD21 H 1 7.77 . . 2 . . . . . . . . 45 1 255 . 1 1 43 43 ASN HD22 H 1 7.97 . . 2 . . . . . . . . 45 1 256 . 1 1 44 44 ASN H H 1 6.73 . . 1 . . . . . . . . 45 1 257 . 1 1 44 44 ASN HA H 1 4.9 . . 1 . . . . . . . . 45 1 258 . 1 1 44 44 ASN HB2 H 1 2.54 . . 2 . . . . . . . . 45 1 259 . 1 1 44 44 ASN HB3 H 1 2.8 . . 2 . . . . . . . . 45 1 260 . 1 1 45 45 PHE H H 1 9.85 . . 1 . . . . . . . . 45 1 261 . 1 1 45 45 PHE HA H 1 5.16 . . 1 . . . . . . . . 45 1 262 . 1 1 45 45 PHE HB2 H 1 2.8 . . 2 . . . . . . . . 45 1 263 . 1 1 45 45 PHE HB3 H 1 3.41 . . 2 . . . . . . . . 45 1 264 . 1 1 45 45 PHE HD1 H 1 7.39 . . 1 . . . . . . . . 45 1 265 . 1 1 45 45 PHE HD2 H 1 7.39 . . 1 . . . . . . . . 45 1 266 . 1 1 45 45 PHE HE1 H 1 7.87 . . 1 . . . . . . . . 45 1 267 . 1 1 45 45 PHE HE2 H 1 7.87 . . 1 . . . . . . . . 45 1 268 . 1 1 45 45 PHE HZ H 1 7.62 . . 1 . . . . . . . . 45 1 269 . 1 1 46 46 LYS H H 1 9.71 . . 1 . . . . . . . . 45 1 270 . 1 1 46 46 LYS HA H 1 4.37 . . 1 . . . . . . . . 45 1 271 . 1 1 46 46 LYS HB2 H 1 .95 . . 2 . . . . . . . . 45 1 272 . 1 1 46 46 LYS HB3 H 1 2.01 . . 2 . . . . . . . . 45 1 273 . 1 1 47 47 SER H H 1 7.46 . . 1 . . . . . . . . 45 1 274 . 1 1 47 47 SER HA H 1 4.6 . . 1 . . . . . . . . 45 1 275 . 1 1 47 47 SER HB2 H 1 3.9 . . 2 . . . . . . . . 45 1 276 . 1 1 47 47 SER HB3 H 1 4.16 . . 2 . . . . . . . . 45 1 277 . 1 1 48 48 ALA H H 1 8.03 . . 1 . . . . . . . . 45 1 278 . 1 1 48 48 ALA HA H 1 3.17 . . 1 . . . . . . . . 45 1 279 . 1 1 48 48 ALA HB1 H 1 1.05 . . 1 . . . . . . . . 45 1 280 . 1 1 48 48 ALA HB2 H 1 1.05 . . 1 . . . . . . . . 45 1 281 . 1 1 48 48 ALA HB3 H 1 1.05 . . 1 . . . . . . . . 45 1 282 . 1 1 49 49 GLU H H 1 8.48 . . 1 . . . . . . . . 45 1 283 . 1 1 49 49 GLU HA H 1 3.89 . . 1 . . . . . . . . 45 1 284 . 1 1 49 49 GLU HB2 H 1 1.77 . . 2 . . . . . . . . 45 1 285 . 1 1 49 49 GLU HB3 H 1 2.02 . . 2 . . . . . . . . 45 1 286 . 1 1 49 49 GLU HG2 H 1 2.23 . . 2 . . . . . . . . 45 1 287 . 1 1 49 49 GLU HG3 H 1 2.36 . . 2 . . . . . . . . 45 1 288 . 1 1 50 50 ASP H H 1 7.72 . . 1 . . . . . . . . 45 1 289 . 1 1 50 50 ASP HA H 1 4.31 . . 1 . . . . . . . . 45 1 290 . 1 1 50 50 ASP HB2 H 1 2.73 . . 1 . . . . . . . . 45 1 291 . 1 1 50 50 ASP HB3 H 1 2.73 . . 1 . . . . . . . . 45 1 292 . 1 1 51 51 CYS H H 1 6.95 . . 1 . . . . . . . . 45 1 293 . 1 1 51 51 CYS HA H 1 1.81 . . 1 . . . . . . . . 45 1 294 . 1 1 51 51 CYS HB2 H 1 2.9 . . 2 . . . . . . . . 45 1 295 . 1 1 51 51 CYS HB3 H 1 3.15 . . 2 . . . . . . . . 45 1 296 . 1 1 52 52 MET H H 1 8.5 . . 1 . . . . . . . . 45 1 297 . 1 1 52 52 MET HA H 1 4.12 . . 1 . . . . . . . . 45 1 298 . 1 1 52 52 MET HB2 H 1 2 . . 2 . . . . . . . . 45 1 299 . 1 1 52 52 MET HB3 H 1 2.06 . . 2 . . . . . . . . 45 1 300 . 1 1 52 52 MET HG2 H 1 2.7 . . 1 . . . . . . . . 45 1 301 . 1 1 52 52 MET HG3 H 1 2.7 . . 1 . . . . . . . . 45 1 302 . 1 1 52 52 MET HE1 H 1 2.16 . . 1 . . . . . . . . 45 1 303 . 1 1 52 52 MET HE2 H 1 2.16 . . 1 . . . . . . . . 45 1 304 . 1 1 52 52 MET HE3 H 1 2.16 . . 1 . . . . . . . . 45 1 305 . 1 1 53 53 ARG H H 1 8.25 . . 1 . . . . . . . . 45 1 306 . 1 1 53 53 ARG HA H 1 4.02 . . 1 . . . . . . . . 45 1 307 . 1 1 53 53 ARG HB2 H 1 1.61 . . 1 . . . . . . . . 45 1 308 . 1 1 53 53 ARG HB3 H 1 1.61 . . 1 . . . . . . . . 45 1 309 . 1 1 54 54 THR H H 1 7.38 . . 1 . . . . . . . . 45 1 310 . 1 1 54 54 THR HA H 1 4.1 . . 1 . . . . . . . . 45 1 311 . 1 1 54 54 THR HB H 1 3.95 . . 1 . . . . . . . . 45 1 312 . 1 1 54 54 THR HG21 H 1 1.59 . . 1 . . . . . . . . 45 1 313 . 1 1 54 54 THR HG22 H 1 1.59 . . 1 . . . . . . . . 45 1 314 . 1 1 54 54 THR HG23 H 1 1.59 . . 1 . . . . . . . . 45 1 315 . 1 1 55 55 CYS H H 1 8.09 . . 1 . . . . . . . . 45 1 316 . 1 1 55 55 CYS HA H 1 4.63 . . 1 . . . . . . . . 45 1 317 . 1 1 55 55 CYS HB2 H 1 1.98 . . 2 . . . . . . . . 45 1 318 . 1 1 55 55 CYS HB3 H 1 2.23 . . 2 . . . . . . . . 45 1 319 . 1 1 56 56 GLY H H 1 7.82 . . 1 . . . . . . . . 45 1 320 . 1 1 56 56 GLY HA2 H 1 3.9 . . 1 . . . . . . . . 45 1 321 . 1 1 56 56 GLY HA3 H 1 3.9 . . 1 . . . . . . . . 45 1 322 . 1 1 57 57 GLY H H 1 7.98 . . 1 . . . . . . . . 45 1 323 . 1 1 57 57 GLY HA2 H 1 3.87 . . 2 . . . . . . . . 45 1 324 . 1 1 57 57 GLY HA3 H 1 4.01 . . 2 . . . . . . . . 45 1 325 . 1 1 58 58 ALA H H 1 7.72 . . 1 . . . . . . . . 45 1 326 . 1 1 58 58 ALA HA H 1 4.09 . . 1 . . . . . . . . 45 1 327 . 1 1 58 58 ALA HB1 H 1 1.32 . . 1 . . . . . . . . 45 1 328 . 1 1 58 58 ALA HB2 H 1 1.32 . . 1 . . . . . . . . 45 1 329 . 1 1 58 58 ALA HB3 H 1 1.32 . . 1 . . . . . . . . 45 1 stop_ save_