data_18491 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18491 _Entry.Title ; 1H chemical shifts of Thermolysin 255-316 fragment ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-05-30 _Entry.Accession_date 2012-05-30 _Entry.Last_release_date 2012-06-18 _Entry.Original_release_date 2012-06-18 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Manuel Rico . . . 18491 2 'M Angeles' Jimenez . . . 18491 3 Carlos Gonzalez . . . 18491 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18491 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 448 18491 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2012-06-18 2012-05-30 original author . 18491 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18495 'Th205-316 dimer' 18491 PDB 1TRL . 18491 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18491 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7993910 _Citation.Full_citation . _Citation.Title 'NMR solution structure of the C-terminal fragment 255-316 of Thermolysin: A dimer formed by subunits having native structure' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 33 _Citation.Journal_issue 49 _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 14834 _Citation.Page_last 14847 _Citation.Year 1994 _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 Manuel Rico . . . 18491 1 2 'M Angeles' Jimenez . . . 18491 1 3 Carlos Gonzalez . . . 18491 1 4 Vincenzo 'de Filippis' . . . 18491 1 5 Angelo Fontana . . . 18491 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'dimer structure' 18491 1 'protein fragment' 18491 1 thermolysin 18491 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18491 _Assembly.ID 1 _Assembly.Name 'Th255-316 dimer' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; Homodimer Symmetric Two identical subunits ; _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 'Th255-316, chain 1' 1 $Th255-316 A . yes native no no . . . 18491 1 2 'Th255-316, chain 2' 1 $Th255-316 A . yes native no no . . . 18491 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1TRL . . 'solution NMR' . . . 18491 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Th255-316 _Entity.Sf_category entity _Entity.Sf_framecode Th255-316 _Entity.Entry_ID 18491 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Th255-316 _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 ; VVGIGRDKLGKIFYRALTQY LTPTSNFSQLRAAAVQSATD LYGSTSQEVASVKQAFDAVG VK ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq ; N-terminal residue is 255. Residues are numbered according to full-length Thermolysin. ; _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 62 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6624.5 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 18495 . Th205-316 . . . . . 100.00 112 100.00 100.00 3.36e-34 . . . . 18491 1 2 no PDB 1FJ3 . "Thermolysin (50% Acetone Soaked)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 3 no PDB 1FJO . "Thermolysin (60% Acetone Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 4 no PDB 1FJQ . "Thermolysin (70% Acetone Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 5 no PDB 1FJT . "Thermolysin (50% Acetonitrile Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 6 no PDB 1FJU . "Thermolysin (80% Acetonitrile Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 7 no PDB 1FJV . "Thermolysin (60% Acetonitrile Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 8 no PDB 1FJW . "Thermolysin (50 Mm Phenol Soaked)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 9 no PDB 1GXW . "The 2.2 A Resolution Structure Of Thermolysin Crystallized In Presence Of Potassium Thiocyanate" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 10 no PDB 1HYT . "Re-Determination And Refinement Of The Complex Of Benzylsuccinic Acid With Thermolysin And Its Relation To The Complex With Car" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 11 no PDB 1KEI . "Thermolysin (substrate-free)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 12 no PDB 1KJO . "Thermolysin Complexed With Z-L-Threonine (Benzyloxycarbonyl-L- Threonine)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 13 no PDB 1KJP . "Thermolysin Complexed With Z-L-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 14 no PDB 1KKK . "Thermolysin Complexed With Z-L-Aspartic Acid (Benzyloxycarbonyl-L- Aspartic Acid)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 15 no PDB 1KL6 . "Thermolysin Complexed With Z-l-alanine (benzyloxycarbonyl-l-alanine)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 16 no PDB 1KR6 . "Thermolysin Complexed With Z-d-glutamic Acid (benzyloxycarbonyl-d- Glutamic Acid)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 17 no PDB 1KRO . "Thermolysin Complexed With Z-D-Threonine (Benzyloxycarbonyl-D- Threonine)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 18 no PDB 1KS7 . "Thermolysin Complexed With Z-D-Aspartic Acid (Benzyloxycarbonyl-D- Aspartic Acid)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 19 no PDB 1KTO . "Thermolysin Complexed With Z-d-alanine (benzyloxycarbonyl-d-alanine)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 20 no PDB 1L3F . "Thermolysin In The Absence Of Substrate Has An Open Conformation" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 21 no PDB 1LNA . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.11e-32 . . . . 18491 1 22 no PDB 1LNB . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 23 no PDB 1LNC . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 24 no PDB 1LND . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 25 no PDB 1LNE . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 26 no PDB 1LNF . "A Structural Analysis Of Metal Substitutions In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 27 no PDB 1OS0 . "Thermolysin With An Alpha-Amino Phosphinic Inhibitor" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 28 no PDB 1PE5 . "Thermolysin With Tricyclic Inhibitor" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 29 no PDB 1PE7 . "Thermolysin With Bicyclic Inhibitor" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 30 no PDB 1PE8 . "Thermolysin With Monocyclic Inhibitor" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 31 no PDB 1QF0 . "Thermolysin (E.C.3.4.24.27) Complexed With (2-Sulphanyl-3- Phenylpropanoyl)-Phe-Tyr. Parameters For Zn-Bidentation Of Mercaptoa" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 32 no PDB 1QF1 . "Thermolysin (E.C.3.4.24.27) Complexed With (2- Sulphanylheptanoyl)-Phe-Ala. Parameters For Zn-Bidentation Of Mercaptoacyldipept" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 33 no PDB 1QF2 . "Thermolysin (E.C.3.4.24.27) Complexed With (2-Sulphanyl-3- Phenylpropanoyl)-Gly-(5-Phenylproline). Parameters For Zn- Monodenta" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 34 no PDB 1THL . "Thermolysin Complexed With A Novel Glutaramide Derivative, N-(1-(2(r, S)-carboxy-4-phenylbutyl) Cyclopentylcarbonyl)-(s)-trypto" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 35 no PDB 1TLI . "Thermolysin (2% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 36 no PDB 1TLP . "Crystallographic Structural Analysis Of Phosphoramidates As Inhibitors And Transition-State Analogs Of Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 37 no PDB 1TLX . "Thermolysin (Native)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 38 no PDB 1TMN . "Binding Of N-Carboxymethyl Dipeptide Inhibitors To Thermolysin Determined By X-Ray Crystallography. A Novel Class Of Transition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 39 no PDB 1TRL . "Nmr Solution Structure Of The C-Terminal Fragment 255-316 Of Thermolysin: A Dimer Formed By Subunits Having The Native Structur" . . . . . 100.00 62 100.00 100.00 1.01e-34 . . . . 18491 1 40 no PDB 1Y3G . "Crystal Structure Of A Silanediol Protease Inhibitor Bound To Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 41 no PDB 1Z9G . "Crystal Structure Analysis Of Thermolysin Complexed With The Inhibitor (R)-Retro-Thiorphan" . . . . . 98.39 316 100.00 100.00 1.72e-31 . . . . 18491 1 42 no PDB 1ZDP . "Crystal Structure Analysis Of Thermolysin Complexed With The Inhibitor (S)-Thiorphan" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 43 no PDB 2A7G . "On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 44 no PDB 2G4Z . "Anomalous Substructure Of Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 45 no PDB 2TLI . "Thermolysin (5% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 46 no PDB 2TLX . "Thermolysin (Native)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 47 no PDB 2TMN . "Crystallographic Structural Analysis Of Phosphoramidates As Inhibitors And Transition-State Analogs Of Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 48 no PDB 2WHZ . "Dipeptide Inhibitors Of Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 49 no PDB 2WI0 . "Dipeptide Inhibitors Of Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 50 no PDB 3DNZ . "Thermolysin By Lb Nanotemplate Method Before High X-Ray Dose On Esrf Id14-2 Beamline" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 51 no PDB 3DO0 . "Thermolysin By Classical Hanging Drop Method After High X- Ray Dose On Esrf Id14-2 Beamline" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 52 no PDB 3DO1 . "Thermolysin By Classical Hanging Drop Method Before High X- Ray Dose On Esrf Id14-2 Beamline" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 53 no PDB 3DO2 . "Thermolysin By Lb Nanotemplate Method After High X-Ray Dose On Esrf Id14-2 Beamline" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 54 no PDB 3EIM . "Metal Exchange In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 55 no PDB 3F28 . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 56 no PDB 3F2P . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 57 no PDB 3FB0 . "Metal Exchange In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 58 no PDB 3FBO . "Metal Exchange In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 59 no PDB 3FCQ . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 60 no PDB 3FGD . "Drugscore Fp: Thermoylsin In Complex With Fragment." . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 61 no PDB 3FLF . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 62 no PDB 3FOR . "Thermolysin Complexed With Bnpa (2-Benzyl-3-Nitro Propanoic Acid Amide)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 63 no PDB 3FV4 . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 64 no PDB 3FVP . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 65 no PDB 3FXP . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 66 no PDB 3FXS . "Metal Exchange In Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 67 no PDB 3LS7 . "Crystal Structure Of Thermolysin In Complex With Xenon" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 68 no PDB 3MS3 . "Crystal Structure Of Thermolysin In Complex With Aniline" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 69 no PDB 3MSA . "Crystal Structure Of Thermolysin In Complex With 3-Bromophenol" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 70 no PDB 3MSF . "Crystal Structure Of Thermolysin In Complex With Urea" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 71 no PDB 3MSN . "Crystal Structure Of Thermolysin In Complex With N-Methylurea" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 72 no PDB 3N21 . "Crystal Structure Of Thermolysin In Complex With S-1,2-Propandiol" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 73 no PDB 3NN7 . "Crystal Structure Of Thermolysin In Complex With 2-Bromoacetate" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 74 no PDB 3P7P . "Radiation Damage Study Of Thermolysin - 100k Structure A (0.1 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 75 no PDB 3P7Q . "Radiation Damage Study Of Thermolysin - 100k Structure B (2.5 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 76 no PDB 3P7R . "Radiation Damage Study Of Thermolysin - 100k Structure C (4.9 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 77 no PDB 3P7S . "Radiation Damage Study Of Thermolysin - 100k Structure D (7.2 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 78 no PDB 3P7T . "Radiation Damage Study Of Thermolysin - 160k Structure A (0.1 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 79 no PDB 3P7U . "Radiation Damage Study Of Thermolysin - 160k Structure B (2.4 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 80 no PDB 3P7V . "Radiation Damage Study Of Thermolysin - 160k Structure C (4.8 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 81 no PDB 3P7W . "Radiation Damage Study Of Thermolysin - 160k Structure D (7.1 Mgy)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 82 no PDB 3QGO . "Structure Of Thermolysin In Complex With L-phenylalanine Methylester" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 83 no PDB 3QH1 . "Structure Of Thermolysin In Complex With N-benzyloxycarbonyl-l- Aspartic Acid" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 84 no PDB 3QH5 . "Structure Of Thermolysin In Complex With N-carbobenzyloxy-l-aspartic Acid And L-phenylalanine Methyl Ester" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 85 no PDB 3SSB . "Structure Of Insect Metalloproteinase Inhibitor In Complex With Thermolysin" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 86 no PDB 3T2H . "Tetragonal Thermolysin In The Presence Of Tmao" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 87 no PDB 3T2I . "Tetragonal Thermolysin In The Presence Of Sarcosine" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 88 no PDB 3T2J . "Tetragonal Thermolysin In The Presence Of Betaine" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 89 no PDB 3T73 . "Thermolysin In Complex With Ubtln22" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 90 no PDB 3T74 . "Thermolysin In Complex With Ubtln27" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 91 no PDB 3T87 . "Thermolysin In Complex With Ubtln28" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 92 no PDB 3T8C . "Thermolysin In Complex With Ubtln30" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 93 no PDB 3T8D . "Thermolysin In Complex With Ubtln31" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 94 no PDB 3T8F . "Thermolysin In Complex With Ubtln34" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 95 no PDB 3T8G . "Thermolysin In Complex With Ubtln26" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 96 no PDB 3T8H . "Thermolysin In Complex With Ubtln29" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 97 no PDB 3TLI . "Thermolysin (10% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 98 no PDB 3TMN . "The Binding Of L-Valyl-L-Tryptophan To Crystalline Thermolysin Illustrates The Mode Of Interaction Of A Product Of Peptide Hydr" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 99 no PDB 3ZI6 . "Structure Of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (ddc) Using The Grob Robot Goniometer" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 100 no PDB 4D91 . "Thermolysin In Complex With Dmso And Acetate" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 101 no PDB 4D9W . "Thermolysin In Complex With Ubtln32" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 102 no PDB 4H57 . "Thermolysin Inhibition" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 103 no PDB 4M65 . "In Situ Thermolysin Crystallized On A Mitegen Micromesh With Asparagine Ligand" . . . . . 100.00 317 100.00 100.00 3.40e-32 . . . . 18491 1 104 no PDB 4MTW . "Thermolysin In Complex With Ubtln36" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 105 no PDB 4MWP . "Thermolysin In Complex With Ubtln46" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 106 no PDB 4MXJ . "Thermolysin In Complex With Ubtln35" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 107 no PDB 4MZN . "Thermolysin In Complex With Ubtln59" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 108 no PDB 4N4E . "Thermolysin In Complex With Ubtln58" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 109 no PDB 4N5P . "Thermolysin In Complex With Ubtln20" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 110 no PDB 4N66 . "Thermolysin In Complex With Ubtln37" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 111 no PDB 4OI5 . "Glycerol-free Structure Of Thermolysin In Complex With Ubtln58" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 112 no PDB 4OW3 . "Thermolysin Structure Determined By Free-electron Laser" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 113 no PDB 4TLI . "Thermolysin (25% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 114 no PDB 4TLN . "Binding Of Hydroxamic Acid Inhibitors To Crystalline Thermolysin Suggests A Pentacoordinate Zinc Intermediate In Catalysis" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 115 no PDB 4TMN . "Slow-And Fast-Binding Inhibitors Of Thermolysin Display Different Modes Of Binding. Crystallographic Analysis Of Extended Phosp" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 116 no PDB 4TNL . "1.8 A Resolution Room Temperature Structure Of Thermolysin Recorded Using An Xfel" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 117 no PDB 5A3Y . "Sad Structure Of Thermolysin Obtained By Multi Crystal Data Collection" . . . . . 100.00 548 100.00 100.00 1.94e-31 . . . . 18491 1 118 no PDB 5TLI . "Thermolysin (60% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 119 no PDB 5TLN . "Binding Of Hydroxamic Acid Inhibitors To Crystalline Thermolysin Suggests A Pentacoordinate Zinc Intermediate In Catalysis" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 120 no PDB 5TMN . "Slow-And Fast-Binding Inhibitors Of Thermolysin Display Different Modes Of Binding. Crystallographic Analysis Of Extended Phosp" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 121 no PDB 6TLI . "Thermolysin (60% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 122 no PDB 6TMN . "Structures Of Two Thermolysin-inhibitor Complexes That Differ By A Single Hydrogen Bond" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 123 no PDB 7TLI . "Thermolysin (90% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 124 no PDB 7TLN . "Structural Analysis Of The Inhibition Of Thermolysin By An Active- Site-directed Irreversible Inhibitor" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 125 no PDB 8TLI . "Thermolysin (100% Isopropanol Soaked Crystals)" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 126 no PDB 8TLN . "Structural Comparison Suggests That Thermolysin And Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis" . . . . . 100.00 316 100.00 100.00 3.08e-32 . . . . 18491 1 127 no EMBL CAA54291 . "thermolysin [Bacillus thermoproteolyticus]" . . . . . 100.00 548 100.00 100.00 1.89e-31 . . . . 18491 1 128 no GB AAA22625 . "neutral protease (nprS) precursor [Geobacillus stearothermophilus]" . . . . . 100.00 551 100.00 100.00 2.17e-31 . . . . 18491 1 129 no GB AAB02774 . "neutral protease nprM precursor [Geobacillus stearothermophilus]" . . . . . 100.00 552 100.00 100.00 2.08e-31 . . . . 18491 1 130 no SP P00800 . "RecName: Full=Thermolysin; AltName: Full=Thermostable neutral proteinase; Flags: Precursor" . . . . . 100.00 548 100.00 100.00 1.94e-31 . . . . 18491 1 131 no SP P43133 . "RecName: Full=Thermolysin; AltName: Full=Neutral protease; Flags: Precursor" . . . . . 100.00 551 100.00 100.00 2.17e-31 . . . . 18491 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 1 255 VAL . 18491 1 2 256 VAL . 18491 1 3 257 GLY . 18491 1 4 258 ILE . 18491 1 5 259 GLY . 18491 1 6 260 ARG . 18491 1 7 261 ASP . 18491 1 8 262 LYS . 18491 1 9 263 LEU . 18491 1 10 264 GLY . 18491 1 11 265 LYS . 18491 1 12 266 ILE . 18491 1 13 267 PHE . 18491 1 14 268 TYR . 18491 1 15 269 ARG . 18491 1 16 270 ALA . 18491 1 17 271 LEU . 18491 1 18 272 THR . 18491 1 19 273 GLN . 18491 1 20 274 TYR . 18491 1 21 275 LEU . 18491 1 22 276 THR . 18491 1 23 277 PRO . 18491 1 24 278 THR . 18491 1 25 279 SER . 18491 1 26 280 ASN . 18491 1 27 281 PHE . 18491 1 28 282 SER . 18491 1 29 283 GLN . 18491 1 30 284 LEU . 18491 1 31 285 ARG . 18491 1 32 286 ALA . 18491 1 33 287 ALA . 18491 1 34 288 ALA . 18491 1 35 289 VAL . 18491 1 36 290 GLN . 18491 1 37 291 SER . 18491 1 38 292 ALA . 18491 1 39 293 THR . 18491 1 40 294 ASP . 18491 1 41 295 LEU . 18491 1 42 296 TYR . 18491 1 43 297 GLY . 18491 1 44 298 SER . 18491 1 45 299 THR . 18491 1 46 300 SER . 18491 1 47 301 GLN . 18491 1 48 302 GLU . 18491 1 49 303 VAL . 18491 1 50 304 ALA . 18491 1 51 305 SER . 18491 1 52 306 VAL . 18491 1 53 307 LYS . 18491 1 54 308 GLN . 18491 1 55 309 ALA . 18491 1 56 310 PHE . 18491 1 57 311 ASP . 18491 1 58 312 ALA . 18491 1 59 313 VAL . 18491 1 60 314 GLY . 18491 1 61 315 VAL . 18491 1 62 316 LYS . 18491 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 . VAL 1 1 18491 1 . VAL 2 2 18491 1 . GLY 3 3 18491 1 . ILE 4 4 18491 1 . GLY 5 5 18491 1 . ARG 6 6 18491 1 . ASP 7 7 18491 1 . LYS 8 8 18491 1 . LEU 9 9 18491 1 . GLY 10 10 18491 1 . LYS 11 11 18491 1 . ILE 12 12 18491 1 . PHE 13 13 18491 1 . TYR 14 14 18491 1 . ARG 15 15 18491 1 . ALA 16 16 18491 1 . LEU 17 17 18491 1 . THR 18 18 18491 1 . GLN 19 19 18491 1 . TYR 20 20 18491 1 . LEU 21 21 18491 1 . THR 22 22 18491 1 . PRO 23 23 18491 1 . THR 24 24 18491 1 . SER 25 25 18491 1 . ASN 26 26 18491 1 . PHE 27 27 18491 1 . SER 28 28 18491 1 . GLN 29 29 18491 1 . LEU 30 30 18491 1 . ARG 31 31 18491 1 . ALA 32 32 18491 1 . ALA 33 33 18491 1 . ALA 34 34 18491 1 . VAL 35 35 18491 1 . GLN 36 36 18491 1 . SER 37 37 18491 1 . ALA 38 38 18491 1 . THR 39 39 18491 1 . ASP 40 40 18491 1 . LEU 41 41 18491 1 . TYR 42 42 18491 1 . GLY 43 43 18491 1 . SER 44 44 18491 1 . THR 45 45 18491 1 . SER 46 46 18491 1 . GLN 47 47 18491 1 . GLU 48 48 18491 1 . VAL 49 49 18491 1 . ALA 50 50 18491 1 . SER 51 51 18491 1 . VAL 52 52 18491 1 . LYS 53 53 18491 1 . GLN 54 54 18491 1 . ALA 55 55 18491 1 . PHE 56 56 18491 1 . ASP 57 57 18491 1 . ALA 58 58 18491 1 . VAL 59 59 18491 1 . GLY 60 60 18491 1 . VAL 61 61 18491 1 . LYS 62 62 18491 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 18491 _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 $Th255-316 . 1427 organism . 'Bacillus thermoproteolyticus' 'Bacillus thermoproteolyticus' . . Bacteria . Bacillus thermoproteolyticus . . . . . . . . . . . . . . . . . . . . . 18491 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 18491 _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 $Th255-316 . 'Subtilisin limited proteolysis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18491 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18491 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Th255-316 'natural abundance' . . 1 $Th255-316 . . 1 . . mM . . . . 18491 1 2 TSP 'natural abundance' . . . . . . 0.1 . . mM . . . . 18491 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18491 1 4 D2P 'natural abundance' . . . . . . 10 . . % . . . . 18491 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 18491 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Th255-316 'natural abundance' . . 1 $Th255-316 . . 1 . . mM . . . . 18491 2 2 TSP 'natural abundance' . . . . . . 0.1 . . mM . . . . 18491 2 3 D2O 'natural abundance' . . . . . . 100 . . % . . . . 18491 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18491 _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 'ionic strength' 0 . M 18491 1 pH 4.8 . pH 18491 1 pressure 1 . atm 18491 1 temperature 298 . K 18491 1 stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Software.Sf_category software _Software.Sf_framecode UXNMR _Software.Entry_ID 18491 _Software.ID 1 _Software.Name UXNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 18491 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18491 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 18491 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18491 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker AMX . 600 . . . 18491 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 18491 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-1H COSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 2 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 3 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 4 '2D 1H-1H COSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 5 '2D 1H-1H TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 6 '2D 1H-1H NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18491 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18491 _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 1 TSP 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . . . . . . . 18491 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18491 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _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 '0.01 ppm' _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 '2D 1H-1H COSY' . . . 18491 1 2 '2D 1H-1H TOCSY' . . . 18491 1 3 '2D 1H-1H NOESY' . . . 18491 1 4 '2D 1H-1H COSY' . . . 18491 1 5 '2D 1H-1H TOCSY' . . . 18491 1 6 '2D 1H-1H NOESY' . . . 18491 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 1 1 VAL HA H 1 3.84 0.01 . 1 . . . . 255 VAL HA . 18491 1 2 . 1 1 1 1 VAL HB H 1 2.18 0.01 . 1 . . . . 255 VAL HB . 18491 1 3 . 1 1 1 1 VAL HG11 H 1 0.97 0.01 . 1 . . . . 255 VAL QG1 . 18491 1 4 . 1 1 1 1 VAL HG12 H 1 0.97 0.01 . 1 . . . . 255 VAL QG1 . 18491 1 5 . 1 1 1 1 VAL HG13 H 1 0.97 0.01 . 1 . . . . 255 VAL QG1 . 18491 1 6 . 1 1 1 1 VAL HG21 H 1 0.97 0.01 . 1 . . . . 255 VAL QG2 . 18491 1 7 . 1 1 1 1 VAL HG22 H 1 0.97 0.01 . 1 . . . . 255 VAL QG2 . 18491 1 8 . 1 1 1 1 VAL HG23 H 1 0.97 0.01 . 1 . . . . 255 VAL QG2 . 18491 1 9 . 1 1 2 2 VAL H H 1 8.62 0.01 . 1 . . . . 256 VAL H . 18491 1 10 . 1 1 2 2 VAL HA H 1 4.14 0.01 . 1 . . . . 256 VAL HA . 18491 1 11 . 1 1 2 2 VAL HB H 1 2.02 0.01 . 1 . . . . 256 VAL HB . 18491 1 12 . 1 1 2 2 VAL HG11 H 1 0.96 0.01 . 1 . . . . 256 VAL QG1 . 18491 1 13 . 1 1 2 2 VAL HG12 H 1 0.96 0.01 . 1 . . . . 256 VAL QG1 . 18491 1 14 . 1 1 2 2 VAL HG13 H 1 0.96 0.01 . 1 . . . . 256 VAL QG1 . 18491 1 15 . 1 1 2 2 VAL HG21 H 1 0.96 0.01 . 1 . . . . 256 VAL QG2 . 18491 1 16 . 1 1 2 2 VAL HG22 H 1 0.96 0.01 . 1 . . . . 256 VAL QG2 . 18491 1 17 . 1 1 2 2 VAL HG23 H 1 0.96 0.01 . 1 . . . . 256 VAL QG2 . 18491 1 18 . 1 1 3 3 GLY H H 1 8.59 0.01 . 1 . . . . 257 GLY H . 18491 1 19 . 1 1 3 3 GLY HA2 H 1 3.85 0.01 . 2 . . . . 257 GLY HA2 . 18491 1 20 . 1 1 3 3 GLY HA3 H 1 4.07 0.01 . 2 . . . . 257 GLY HA3 . 18491 1 21 . 1 1 4 4 ILE H H 1 7.87 0.01 . 1 . . . . 258 ILE H . 18491 1 22 . 1 1 4 4 ILE HA H 1 4.35 0.01 . 1 . . . . 258 ILE HA . 18491 1 23 . 1 1 4 4 ILE HB H 1 1.85 0.01 . 1 . . . . 258 ILE HB . 18491 1 24 . 1 1 4 4 ILE HG12 H 1 1.38 0.01 . 2 . . . . 258 ILE HG12 . 18491 1 25 . 1 1 4 4 ILE HG13 H 1 1.56 0.01 . 2 . . . . 258 ILE HG13 . 18491 1 26 . 1 1 4 4 ILE HG21 H 1 0.86 0.01 . 1 . . . . 258 ILE QG2 . 18491 1 27 . 1 1 4 4 ILE HG22 H 1 0.86 0.01 . 1 . . . . 258 ILE QG2 . 18491 1 28 . 1 1 4 4 ILE HG23 H 1 0.86 0.01 . 1 . . . . 258 ILE QG2 . 18491 1 29 . 1 1 4 4 ILE HD11 H 1 0.75 0.01 . 1 . . . . 258 ILE QD1 . 18491 1 30 . 1 1 4 4 ILE HD12 H 1 0.75 0.01 . 1 . . . . 258 ILE QD1 . 18491 1 31 . 1 1 4 4 ILE HD13 H 1 0.75 0.01 . 1 . . . . 258 ILE QD1 . 18491 1 32 . 1 1 5 5 GLY H H 1 8.61 0.01 . 1 . . . . 259 GLY H . 18491 1 33 . 1 1 5 5 GLY HA2 H 1 3.90 0.01 . 2 . . . . 259 GLY HA2 . 18491 1 34 . 1 1 5 5 GLY HA3 H 1 4.08 0.01 . 2 . . . . 259 GLY HA3 . 18491 1 35 . 1 1 6 6 ARG H H 1 9.15 0.01 . 1 . . . . 260 ARG H . 18491 1 36 . 1 1 6 6 ARG HA H 1 4.00 0.01 . 1 . . . . 260 ARG HA . 18491 1 37 . 1 1 6 6 ARG HB2 H 1 1.85 0.01 . 2 . . . . 260 ARG HB2 . 18491 1 38 . 1 1 6 6 ARG HB3 H 1 2.08 0.01 . 2 . . . . 260 ARG HB3 . 18491 1 39 . 1 1 6 6 ARG HG2 H 1 1.62 0.01 . 1 . . . . 260 ARG HG2 . 18491 1 40 . 1 1 6 6 ARG HG3 H 1 1.62 0.01 . 1 . . . . 260 ARG HG3 . 18491 1 41 . 1 1 6 6 ARG HD2 H 1 2.79 0.01 . 2 . . . . 260 ARG HD2 . 18491 1 42 . 1 1 6 6 ARG HD3 H 1 3.10 0.01 . 2 . . . . 260 ARG HD3 . 18491 1 43 . 1 1 7 7 ASP H H 1 9.15 0.01 . 1 . . . . 261 ASP H . 18491 1 44 . 1 1 7 7 ASP HA H 1 3.95 0.01 . 1 . . . . 261 ASP HA . 18491 1 45 . 1 1 7 7 ASP HB2 H 1 2.61 0.01 . 2 . . . . 261 ASP HB2 . 18491 1 46 . 1 1 7 7 ASP HB3 H 1 2.76 0.01 . 2 . . . . 261 ASP HB3 . 18491 1 47 . 1 1 8 8 LYS H H 1 7.49 0.01 . 1 . . . . 262 LYS H . 18491 1 48 . 1 1 8 8 LYS HA H 1 4.16 0.01 . 1 . . . . 262 LYS HA . 18491 1 49 . 1 1 8 8 LYS HB2 H 1 1.95 0.01 . 1 . . . . 262 LYS HB2 . 18491 1 50 . 1 1 8 8 LYS HB3 H 1 1.95 0.01 . 1 . . . . 262 LYS HB3 . 18491 1 51 . 1 1 8 8 LYS HG2 H 1 1.38 0.01 . 2 . . . . 262 LYS HG2 . 18491 1 52 . 1 1 8 8 LYS HG3 H 1 1.42 0.01 . 2 . . . . 262 LYS HG3 . 18491 1 53 . 1 1 8 8 LYS HD2 H 1 1.58 0.01 . 1 . . . . 262 LYS HD2 . 18491 1 54 . 1 1 8 8 LYS HD3 H 1 1.58 0.01 . 1 . . . . 262 LYS HD3 . 18491 1 55 . 1 1 8 8 LYS HE2 H 1 3.00 0.01 . 1 . . . . 262 LYS HE2 . 18491 1 56 . 1 1 8 8 LYS HE3 H 1 3.00 0.01 . 1 . . . . 262 LYS HE3 . 18491 1 57 . 1 1 9 9 LEU H H 1 8.10 0.01 . 1 . . . . 263 LEU H . 18491 1 58 . 1 1 9 9 LEU HA H 1 4.16 0.01 . 1 . . . . 263 LEU HA . 18491 1 59 . 1 1 9 9 LEU HB2 H 1 1.76 0.01 . 2 . . . . 263 LEU HB2 . 18491 1 60 . 1 1 9 9 LEU HB3 H 1 1.99 0.01 . 2 . . . . 263 LEU HB3 . 18491 1 61 . 1 1 9 9 LEU HG H 1 2.00 0.01 . 1 . . . . 263 LEU HG . 18491 1 62 . 1 1 9 9 LEU HD11 H 1 1.08 0.01 . 2 . . . . 263 LEU QD1 . 18491 1 63 . 1 1 9 9 LEU HD12 H 1 1.08 0.01 . 2 . . . . 263 LEU QD1 . 18491 1 64 . 1 1 9 9 LEU HD13 H 1 1.08 0.01 . 2 . . . . 263 LEU QD1 . 18491 1 65 . 1 1 9 9 LEU HD21 H 1 1.12 0.01 . 2 . . . . 263 LEU QD2 . 18491 1 66 . 1 1 9 9 LEU HD22 H 1 1.12 0.01 . 2 . . . . 263 LEU QD2 . 18491 1 67 . 1 1 9 9 LEU HD23 H 1 1.12 0.01 . 2 . . . . 263 LEU QD2 . 18491 1 68 . 1 1 10 10 GLY H H 1 8.82 0.01 . 1 . . . . 264 GLY H . 18491 1 69 . 1 1 10 10 GLY HA2 H 1 4.00 0.01 . 1 . . . . 264 GLY HA2 . 18491 1 70 . 1 1 10 10 GLY HA3 H 1 4.00 0.01 . 1 . . . . 264 GLY HA3 . 18491 1 71 . 1 1 11 11 LYS H H 1 8.35 0.01 . 1 . . . . 265 LYS H . 18491 1 72 . 1 1 11 11 LYS HA H 1 4.00 0.01 . 1 . . . . 265 LYS HA . 18491 1 73 . 1 1 11 11 LYS HB2 H 1 1.99 0.01 . 2 . . . . 265 LYS HB2 . 18491 1 74 . 1 1 11 11 LYS HB3 H 1 2.23 0.01 . 2 . . . . 265 LYS HB3 . 18491 1 75 . 1 1 11 11 LYS HG2 H 1 1.49 0.01 . 2 . . . . 265 LYS HG2 . 18491 1 76 . 1 1 11 11 LYS HG3 H 1 1.76 0.01 . 2 . . . . 265 LYS HG3 . 18491 1 77 . 1 1 11 11 LYS HD2 H 1 1.76 0.01 . 1 . . . . 265 LYS HD2 . 18491 1 78 . 1 1 11 11 LYS HD3 H 1 1.76 0.01 . 1 . . . . 265 LYS HD3 . 18491 1 79 . 1 1 11 11 LYS HE2 H 1 2.98 0.01 . 1 . . . . 265 LYS HE2 . 18491 1 80 . 1 1 11 11 LYS HE3 H 1 2.98 0.01 . 1 . . . . 265 LYS HE3 . 18491 1 81 . 1 1 12 12 ILE H H 1 8.64 0.01 . 1 . . . . 266 ILE H . 18491 1 82 . 1 1 12 12 ILE HA H 1 3.56 0.01 . 1 . . . . 266 ILE HA . 18491 1 83 . 1 1 12 12 ILE HB H 1 2.18 0.01 . 1 . . . . 266 ILE HB . 18491 1 84 . 1 1 12 12 ILE HG12 H 1 2.29 0.01 . 1 . . . . 266 ILE HG12 . 18491 1 85 . 1 1 12 12 ILE HG13 H 1 2.29 0.01 . 1 . . . . 266 ILE HG13 . 18491 1 86 . 1 1 12 12 ILE HG21 H 1 0.92 0.01 . 1 . . . . 266 ILE QG2 . 18491 1 87 . 1 1 12 12 ILE HG22 H 1 0.92 0.01 . 1 . . . . 266 ILE QG2 . 18491 1 88 . 1 1 12 12 ILE HG23 H 1 0.92 0.01 . 1 . . . . 266 ILE QG2 . 18491 1 89 . 1 1 12 12 ILE HD11 H 1 0.88 0.01 . 1 . . . . 266 ILE QD1 . 18491 1 90 . 1 1 12 12 ILE HD12 H 1 0.88 0.01 . 1 . . . . 266 ILE QD1 . 18491 1 91 . 1 1 12 12 ILE HD13 H 1 0.88 0.01 . 1 . . . . 266 ILE QD1 . 18491 1 92 . 1 1 13 13 PHE H H 1 8.84 0.01 . 1 . . . . 267 PHE H . 18491 1 93 . 1 1 13 13 PHE HA H 1 4.02 0.01 . 1 . . . . 267 PHE HA . 18491 1 94 . 1 1 13 13 PHE HB2 H 1 2.48 0.01 . 2 . . . . 267 PHE HB2 . 18491 1 95 . 1 1 13 13 PHE HB3 H 1 2.66 0.01 . 2 . . . . 267 PHE HB3 . 18491 1 96 . 1 1 13 13 PHE HD1 H 1 6.79 0.01 . 3 . . . . 267 PHE HD1 . 18491 1 97 . 1 1 13 13 PHE HD2 H 1 6.79 0.01 . 3 . . . . 267 PHE HD2 . 18491 1 98 . 1 1 13 13 PHE HE1 H 1 7.04 0.01 . 3 . . . . 267 PHE HE1 . 18491 1 99 . 1 1 13 13 PHE HE2 H 1 7.04 0.01 . 3 . . . . 267 PHE HE2 . 18491 1 100 . 1 1 13 13 PHE HZ H 1 7.21 0.01 . 1 . . . . 267 PHE HZ . 18491 1 101 . 1 1 14 14 TYR H H 1 8.95 0.01 . 1 . . . . 268 TYR H . 18491 1 102 . 1 1 14 14 TYR HA H 1 3.76 0.01 . 1 . . . . 268 TYR HA . 18491 1 103 . 1 1 14 14 TYR HB2 H 1 2.98 0.01 . 2 . . . . 268 TYR HB2 . 18491 1 104 . 1 1 14 14 TYR HB3 H 1 3.01 0.01 . 2 . . . . 268 TYR HB3 . 18491 1 105 . 1 1 14 14 TYR HD1 H 1 6.89 0.01 . 3 . . . . 268 TYR HD1 . 18491 1 106 . 1 1 14 14 TYR HD2 H 1 6.89 0.01 . 3 . . . . 268 TYR HD2 . 18491 1 107 . 1 1 14 14 TYR HE1 H 1 6.74 0.01 . 3 . . . . 268 TYR HE1 . 18491 1 108 . 1 1 14 14 TYR HE2 H 1 6.74 0.01 . 3 . . . . 268 TYR HE2 . 18491 1 109 . 1 1 15 15 ARG H H 1 7.88 0.01 . 1 . . . . 269 ARG H . 18491 1 110 . 1 1 15 15 ARG HA H 1 3.84 0.01 . 1 . . . . 269 ARG HA . 18491 1 111 . 1 1 15 15 ARG HB2 H 1 2.08 0.01 . 1 . . . . 269 ARG HB2 . 18491 1 112 . 1 1 15 15 ARG HB3 H 1 2.08 0.01 . 1 . . . . 269 ARG HB3 . 18491 1 113 . 1 1 15 15 ARG HG2 H 1 1.61 0.01 . 1 . . . . 269 ARG HG2 . 18491 1 114 . 1 1 15 15 ARG HG3 H 1 1.61 0.01 . 1 . . . . 269 ARG HG3 . 18491 1 115 . 1 1 15 15 ARG HD2 H 1 3.20 0.01 . 2 . . . . 269 ARG HD2 . 18491 1 116 . 1 1 15 15 ARG HD3 H 1 3.30 0.01 . 2 . . . . 269 ARG HD3 . 18491 1 117 . 1 1 15 15 ARG HE H 1 9.26 0.01 . 1 . . . . 269 ARG HE . 18491 1 118 . 1 1 15 15 ARG HH11 H 1 6.24 0.01 . 2 . . . . 269 ARG HH11 . 18491 1 119 . 1 1 15 15 ARG HH12 H 1 6.24 0.01 . 2 . . . . 269 ARG HH12 . 18491 1 120 . 1 1 15 15 ARG HH21 H 1 7.10 0.01 . 2 . . . . 269 ARG HH21 . 18491 1 121 . 1 1 15 15 ARG HH22 H 1 7.10 0.01 . 2 . . . . 269 ARG HH22 . 18491 1 122 . 1 1 16 16 ALA H H 1 8.24 0.01 . 1 . . . . 270 ALA H . 18491 1 123 . 1 1 16 16 ALA HA H 1 4.02 0.01 . 1 . . . . 270 ALA HA . 18491 1 124 . 1 1 16 16 ALA HB1 H 1 1.30 0.01 . 1 . . . . 270 ALA QB . 18491 1 125 . 1 1 16 16 ALA HB2 H 1 1.30 0.01 . 1 . . . . 270 ALA QB . 18491 1 126 . 1 1 16 16 ALA HB3 H 1 1.30 0.01 . 1 . . . . 270 ALA QB . 18491 1 127 . 1 1 17 17 LEU H H 1 8.26 0.01 . 1 . . . . 271 LEU H . 18491 1 128 . 1 1 17 17 LEU HA H 1 3.66 0.01 . 1 . . . . 271 LEU HA . 18491 1 129 . 1 1 17 17 LEU HB2 H 1 1.36 0.01 . 1 . . . . 271 LEU HB2 . 18491 1 130 . 1 1 17 17 LEU HB3 H 1 1.36 0.01 . 1 . . . . 271 LEU HB3 . 18491 1 131 . 1 1 17 17 LEU HG H 1 1.15 0.01 . 1 . . . . 271 LEU HG . 18491 1 132 . 1 1 17 17 LEU HD11 H 1 0.06 0.01 . 2 . . . . 271 LEU QD1 . 18491 1 133 . 1 1 17 17 LEU HD12 H 1 0.06 0.01 . 2 . . . . 271 LEU QD1 . 18491 1 134 . 1 1 17 17 LEU HD13 H 1 0.06 0.01 . 2 . . . . 271 LEU QD1 . 18491 1 135 . 1 1 17 17 LEU HD21 H 1 0.24 0.01 . 2 . . . . 271 LEU QD2 . 18491 1 136 . 1 1 17 17 LEU HD22 H 1 0.24 0.01 . 2 . . . . 271 LEU QD2 . 18491 1 137 . 1 1 17 17 LEU HD23 H 1 0.24 0.01 . 2 . . . . 271 LEU QD2 . 18491 1 138 . 1 1 18 18 THR H H 1 7.38 0.01 . 1 . . . . 272 THR H . 18491 1 139 . 1 1 18 18 THR HA H 1 4.01 0.01 . 1 . . . . 272 THR HA . 18491 1 140 . 1 1 18 18 THR HB H 1 3.97 0.01 . 1 . . . . 272 THR HB . 18491 1 141 . 1 1 18 18 THR HG21 H 1 0.72 0.01 . 1 . . . . 272 THR QG2 . 18491 1 142 . 1 1 18 18 THR HG22 H 1 0.72 0.01 . 1 . . . . 272 THR QG2 . 18491 1 143 . 1 1 18 18 THR HG23 H 1 0.72 0.01 . 1 . . . . 272 THR QG2 . 18491 1 144 . 1 1 19 19 GLN H H 1 8.12 0.01 . 1 . . . . 273 GLN H . 18491 1 145 . 1 1 19 19 GLN HA H 1 4.37 0.01 . 1 . . . . 273 GLN HA . 18491 1 146 . 1 1 19 19 GLN HB2 H 1 1.22 0.01 . 1 . . . . 273 GLN HB2 . 18491 1 147 . 1 1 19 19 GLN HB3 H 1 1.32 0.01 . 1 . . . . 273 GLN HB3 . 18491 1 148 . 1 1 19 19 GLN HG2 H 1 1.62 0.01 . 2 . . . . 273 GLN HG2 . 18491 1 149 . 1 1 19 19 GLN HG3 H 1 1.94 0.01 . 2 . . . . 273 GLN HG3 . 18491 1 150 . 1 1 19 19 GLN HE21 H 1 6.63 0.01 . 2 . . . . 273 GLN HE21 . 18491 1 151 . 1 1 19 19 GLN HE22 H 1 7.10 0.01 . 2 . . . . 273 GLN HE22 . 18491 1 152 . 1 1 20 20 TYR H H 1 7.12 0.01 . 1 . . . . 274 TYR H . 18491 1 153 . 1 1 20 20 TYR HA H 1 5.04 0.01 . 1 . . . . 274 TYR HA . 18491 1 154 . 1 1 20 20 TYR HB2 H 1 2.67 0.01 . 2 . . . . 274 TYR HB2 . 18491 1 155 . 1 1 20 20 TYR HB3 H 1 3.33 0.01 . 2 . . . . 274 TYR HB3 . 18491 1 156 . 1 1 20 20 TYR HD1 H 1 7.04 0.01 . 3 . . . . 274 TYR HD1 . 18491 1 157 . 1 1 20 20 TYR HD2 H 1 7.04 0.01 . 3 . . . . 274 TYR HD2 . 18491 1 158 . 1 1 20 20 TYR HE1 H 1 6.62 0.01 . 3 . . . . 274 TYR HE1 . 18491 1 159 . 1 1 20 20 TYR HE2 H 1 6.62 0.01 . 3 . . . . 274 TYR HE2 . 18491 1 160 . 1 1 21 21 LEU H H 1 7.85 0.01 . 1 . . . . 275 LEU H . 18491 1 161 . 1 1 21 21 LEU HA H 1 4.40 0.01 . 1 . . . . 275 LEU HA . 18491 1 162 . 1 1 21 21 LEU HB2 H 1 1.63 0.01 . 2 . . . . 275 LEU HB2 . 18491 1 163 . 1 1 21 21 LEU HB3 H 1 1.82 0.01 . 2 . . . . 275 LEU HB3 . 18491 1 164 . 1 1 21 21 LEU HG H 1 1.82 0.01 . 1 . . . . 275 LEU HG . 18491 1 165 . 1 1 21 21 LEU HD11 H 1 0.95 0.01 . 2 . . . . 275 LEU QD1 . 18491 1 166 . 1 1 21 21 LEU HD12 H 1 0.95 0.01 . 2 . . . . 275 LEU QD1 . 18491 1 167 . 1 1 21 21 LEU HD13 H 1 0.95 0.01 . 2 . . . . 275 LEU QD1 . 18491 1 168 . 1 1 21 21 LEU HD21 H 1 1.05 0.01 . 2 . . . . 275 LEU QD2 . 18491 1 169 . 1 1 21 21 LEU HD22 H 1 1.05 0.01 . 2 . . . . 275 LEU QD2 . 18491 1 170 . 1 1 21 21 LEU HD23 H 1 1.05 0.01 . 2 . . . . 275 LEU QD2 . 18491 1 171 . 1 1 22 22 THR H H 1 8.25 0.01 . 1 . . . . 276 THR H . 18491 1 172 . 1 1 22 22 THR HA H 1 4.68 0.01 . 1 . . . . 276 THR HA . 18491 1 173 . 1 1 22 22 THR HB H 1 4.45 0.01 . 1 . . . . 276 THR HB . 18491 1 174 . 1 1 22 22 THR HG21 H 1 1.12 0.01 . 1 . . . . 276 THR QG2 . 18491 1 175 . 1 1 22 22 THR HG22 H 1 1.12 0.01 . 1 . . . . 276 THR QG2 . 18491 1 176 . 1 1 22 22 THR HG23 H 1 1.12 0.01 . 1 . . . . 276 THR QG2 . 18491 1 177 . 1 1 23 23 PRO HA H 1 3.32 0.01 . 1 . . . . 277 PRO HA . 18491 1 178 . 1 1 23 23 PRO HB2 H 1 1.69 0.01 . 2 . . . . 277 PRO HB2 . 18491 1 179 . 1 1 23 23 PRO HB3 H 1 2.25 0.01 . 2 . . . . 277 PRO HB3 . 18491 1 180 . 1 1 23 23 PRO HG2 H 1 1.78 0.01 . 2 . . . . 277 PRO HG2 . 18491 1 181 . 1 1 23 23 PRO HG3 H 1 2.02 0.01 . 2 . . . . 277 PRO HG3 . 18491 1 182 . 1 1 23 23 PRO HD2 H 1 3.46 0.01 . 2 . . . . 277 PRO HD2 . 18491 1 183 . 1 1 23 23 PRO HD3 H 1 3.68 0.01 . 2 . . . . 277 PRO HD3 . 18491 1 184 . 1 1 24 24 THR H H 1 7.32 0.01 . 1 . . . . 278 THR H . 18491 1 185 . 1 1 24 24 THR HA H 1 4.56 0.01 . 1 . . . . 278 THR HA . 18491 1 186 . 1 1 24 24 THR HB H 1 4.66 0.01 . 1 . . . . 278 THR HB . 18491 1 187 . 1 1 24 24 THR HG21 H 1 1.12 0.01 . 1 . . . . 278 THR QG2 . 18491 1 188 . 1 1 24 24 THR HG22 H 1 1.12 0.01 . 1 . . . . 278 THR QG2 . 18491 1 189 . 1 1 24 24 THR HG23 H 1 1.12 0.01 . 1 . . . . 278 THR QG2 . 18491 1 190 . 1 1 25 25 SER H H 1 7.90 0.01 . 1 . . . . 279 SER H . 18491 1 191 . 1 1 25 25 SER HA H 1 4.58 0.01 . 1 . . . . 279 SER HA . 18491 1 192 . 1 1 25 25 SER HB2 H 1 4.05 0.01 . 1 . . . . 279 SER HB2 . 18491 1 193 . 1 1 25 25 SER HB3 H 1 4.05 0.01 . 1 . . . . 279 SER HB3 . 18491 1 194 . 1 1 25 25 SER HG H 1 5.90 0.01 . 1 . . . . 279 SER HG . 18491 1 195 . 1 1 26 26 ASN H H 1 8.39 0.01 . 1 . . . . 280 ASN H . 18491 1 196 . 1 1 26 26 ASN HA H 1 4.99 0.01 . 1 . . . . 280 ASN HA . 18491 1 197 . 1 1 26 26 ASN HB2 H 1 3.11 0.01 . 2 . . . . 280 ASN HB2 . 18491 1 198 . 1 1 26 26 ASN HB3 H 1 3.57 0.01 . 2 . . . . 280 ASN HB3 . 18491 1 199 . 1 1 26 26 ASN HD21 H 1 7.04 0.01 . 2 . . . . 280 ASN HD21 . 18491 1 200 . 1 1 26 26 ASN HD22 H 1 7.55 0.01 . 2 . . . . 280 ASN HD22 . 18491 1 201 . 1 1 27 27 PHE H H 1 8.78 0.01 . 1 . . . . 281 PHE H . 18491 1 202 . 1 1 27 27 PHE HA H 1 4.18 0.01 . 1 . . . . 281 PHE HA . 18491 1 203 . 1 1 27 27 PHE HB2 H 1 3.03 0.01 . 2 . . . . 281 PHE HB2 . 18491 1 204 . 1 1 27 27 PHE HB3 H 1 3.41 0.01 . 2 . . . . 281 PHE HB3 . 18491 1 205 . 1 1 27 27 PHE HD1 H 1 7.38 0.01 . 3 . . . . 281 PHE HD1 . 18491 1 206 . 1 1 27 27 PHE HD2 H 1 7.38 0.01 . 3 . . . . 281 PHE HD2 . 18491 1 207 . 1 1 27 27 PHE HE1 H 1 7.38 0.01 . 3 . . . . 281 PHE HE1 . 18491 1 208 . 1 1 27 27 PHE HE2 H 1 7.38 0.01 . 3 . . . . 281 PHE HE2 . 18491 1 209 . 1 1 27 27 PHE HZ H 1 7.60 0.01 . 1 . . . . 281 PHE HZ . 18491 1 210 . 1 1 28 28 SER H H 1 8.61 0.01 . 1 . . . . 282 SER H . 18491 1 211 . 1 1 28 28 SER HA H 1 4.08 0.01 . 1 . . . . 282 SER HA . 18491 1 212 . 1 1 28 28 SER HB2 H 1 3.84 0.01 . 1 . . . . 282 SER HB2 . 18491 1 213 . 1 1 28 28 SER HB3 H 1 3.84 0.01 . 1 . . . . 282 SER HB3 . 18491 1 214 . 1 1 29 29 GLN H H 1 8.30 0.01 . 1 . . . . 283 GLN H . 18491 1 215 . 1 1 29 29 GLN HA H 1 4.18 0.01 . 1 . . . . 283 GLN HA . 18491 1 216 . 1 1 29 29 GLN HB2 H 1 2.18 0.01 . 2 . . . . 283 GLN HB2 . 18491 1 217 . 1 1 29 29 GLN HB3 H 1 2.51 0.01 . 2 . . . . 283 GLN HB3 . 18491 1 218 . 1 1 29 29 GLN HG2 H 1 2.64 0.01 . 1 . . . . 283 GLN HG2 . 18491 1 219 . 1 1 29 29 GLN HG3 H 1 2.64 0.01 . 1 . . . . 283 GLN HG3 . 18491 1 220 . 1 1 29 29 GLN HE21 H 1 6.74 0.01 . 2 . . . . 283 GLN HE21 . 18491 1 221 . 1 1 29 29 GLN HE22 H 1 7.57 0.01 . 2 . . . . 283 GLN HE22 . 18491 1 222 . 1 1 30 30 LEU H H 1 8.99 0.01 . 1 . . . . 284 LEU H . 18491 1 223 . 1 1 30 30 LEU HA H 1 4.09 0.01 . 1 . . . . 284 LEU HA . 18491 1 224 . 1 1 30 30 LEU HB2 H 1 1.86 0.01 . 2 . . . . 284 LEU HB2 . 18491 1 225 . 1 1 30 30 LEU HB3 H 1 1.92 0.01 . 2 . . . . 284 LEU HB3 . 18491 1 226 . 1 1 30 30 LEU HG H 1 2.06 0.01 . 1 . . . . 284 LEU HG . 18491 1 227 . 1 1 30 30 LEU HD11 H 1 1.07 0.01 . 2 . . . . 284 LEU QD1 . 18491 1 228 . 1 1 30 30 LEU HD12 H 1 1.07 0.01 . 2 . . . . 284 LEU QD1 . 18491 1 229 . 1 1 30 30 LEU HD13 H 1 1.07 0.01 . 2 . . . . 284 LEU QD1 . 18491 1 230 . 1 1 30 30 LEU HD21 H 1 1.19 0.01 . 2 . . . . 284 LEU QD2 . 18491 1 231 . 1 1 30 30 LEU HD22 H 1 1.19 0.01 . 2 . . . . 284 LEU QD2 . 18491 1 232 . 1 1 30 30 LEU HD23 H 1 1.19 0.01 . 2 . . . . 284 LEU QD2 . 18491 1 233 . 1 1 31 31 ARG H H 1 8.09 0.01 . 1 . . . . 285 ARG H . 18491 1 234 . 1 1 31 31 ARG HA H 1 4.12 0.01 . 1 . . . . 285 ARG HA . 18491 1 235 . 1 1 31 31 ARG HB2 H 1 0.84 0.01 . 2 . . . . 285 ARG HB2 . 18491 1 236 . 1 1 31 31 ARG HB3 H 1 1.58 0.01 . 2 . . . . 285 ARG HB3 . 18491 1 237 . 1 1 31 31 ARG HG2 H 1 0.64 0.01 . 2 . . . . 285 ARG HG2 . 18491 1 238 . 1 1 31 31 ARG HG3 H 1 1.20 0.01 . 2 . . . . 285 ARG HG3 . 18491 1 239 . 1 1 31 31 ARG HD2 H 1 3.07 0.01 . 2 . . . . 285 ARG HD2 . 18491 1 240 . 1 1 31 31 ARG HD3 H 1 3.14 0.01 . 2 . . . . 285 ARG HD3 . 18491 1 241 . 1 1 31 31 ARG HE H 1 7.67 0.01 . 1 . . . . 285 ARG HE . 18491 1 242 . 1 1 32 32 ALA H H 1 7.71 0.01 . 1 . . . . 286 ALA H . 18491 1 243 . 1 1 32 32 ALA HA H 1 3.85 0.01 . 1 . . . . 286 ALA HA . 18491 1 244 . 1 1 32 32 ALA HB1 H 1 1.39 0.01 . 1 . . . . 286 ALA QB . 18491 1 245 . 1 1 32 32 ALA HB2 H 1 1.39 0.01 . 1 . . . . 286 ALA QB . 18491 1 246 . 1 1 32 32 ALA HB3 H 1 1.39 0.01 . 1 . . . . 286 ALA QB . 18491 1 247 . 1 1 33 33 ALA H H 1 8.28 0.01 . 1 . . . . 287 ALA H . 18491 1 248 . 1 1 33 33 ALA HA H 1 3.83 0.01 . 1 . . . . 287 ALA HA . 18491 1 249 . 1 1 33 33 ALA HB1 H 1 1.49 0.01 . 1 . . . . 287 ALA QB . 18491 1 250 . 1 1 33 33 ALA HB2 H 1 1.49 0.01 . 1 . . . . 287 ALA QB . 18491 1 251 . 1 1 33 33 ALA HB3 H 1 1.49 0.01 . 1 . . . . 287 ALA QB . 18491 1 252 . 1 1 34 34 ALA H H 1 8.44 0.01 . 1 . . . . 288 ALA H . 18491 1 253 . 1 1 34 34 ALA HA H 1 3.75 0.01 . 1 . . . . 288 ALA HA . 18491 1 254 . 1 1 34 34 ALA HB1 H 1 1.19 0.01 . 1 . . . . 288 ALA QB . 18491 1 255 . 1 1 34 34 ALA HB2 H 1 1.19 0.01 . 1 . . . . 288 ALA QB . 18491 1 256 . 1 1 34 34 ALA HB3 H 1 1.19 0.01 . 1 . . . . 288 ALA QB . 18491 1 257 . 1 1 35 35 VAL H H 1 8.64 0.01 . 1 . . . . 289 VAL H . 18491 1 258 . 1 1 35 35 VAL HA H 1 3.34 0.01 . 1 . . . . 289 VAL HA . 18491 1 259 . 1 1 35 35 VAL HB H 1 1.98 0.01 . 1 . . . . 289 VAL HB . 18491 1 260 . 1 1 35 35 VAL HG11 H 1 0.82 0.01 . 1 . . . . 289 VAL QG1 . 18491 1 261 . 1 1 35 35 VAL HG12 H 1 0.82 0.01 . 1 . . . . 289 VAL QG1 . 18491 1 262 . 1 1 35 35 VAL HG13 H 1 0.82 0.01 . 1 . . . . 289 VAL QG1 . 18491 1 263 . 1 1 35 35 VAL HG21 H 1 0.82 0.01 . 1 . . . . 289 VAL QG2 . 18491 1 264 . 1 1 35 35 VAL HG22 H 1 0.82 0.01 . 1 . . . . 289 VAL QG2 . 18491 1 265 . 1 1 35 35 VAL HG23 H 1 0.82 0.01 . 1 . . . . 289 VAL QG2 . 18491 1 266 . 1 1 36 36 GLN H H 1 8.67 0.01 . 1 . . . . 290 GLN H . 18491 1 267 . 1 1 36 36 GLN HA H 1 3.72 0.01 . 1 . . . . 290 GLN HA . 18491 1 268 . 1 1 36 36 GLN HB2 H 1 1.33 0.01 . 1 . . . . 290 GLN HB2 . 18491 1 269 . 1 1 36 36 GLN HB3 H 1 1.33 0.01 . 1 . . . . 290 GLN HB3 . 18491 1 270 . 1 1 36 36 GLN HG2 H 1 1.82 0.01 . 2 . . . . 290 GLN HG2 . 18491 1 271 . 1 1 36 36 GLN HG3 H 1 1.88 0.01 . 2 . . . . 290 GLN HG3 . 18491 1 272 . 1 1 36 36 GLN HE21 H 1 7.02 0.01 . 2 . . . . 290 GLN HE21 . 18491 1 273 . 1 1 36 36 GLN HE22 H 1 7.71 0.01 . 2 . . . . 290 GLN HE22 . 18491 1 274 . 1 1 37 37 SER H H 1 8.21 0.01 . 1 . . . . 291 SER H . 18491 1 275 . 1 1 37 37 SER HA H 1 4.27 0.01 . 1 . . . . 291 SER HA . 18491 1 276 . 1 1 37 37 SER HB2 H 1 3.96 0.01 . 2 . . . . 291 SER HB2 . 18491 1 277 . 1 1 37 37 SER HB3 H 1 4.10 0.01 . 2 . . . . 291 SER HB3 . 18491 1 278 . 1 1 37 37 SER HG H 1 4.55 0.01 . 1 . . . . 291 SER HG . 18491 1 279 . 1 1 38 38 ALA H H 1 8.48 0.01 . 1 . . . . 292 ALA H . 18491 1 280 . 1 1 38 38 ALA HA H 1 4.12 0.01 . 1 . . . . 292 ALA HA . 18491 1 281 . 1 1 38 38 ALA HB1 H 1 1.49 0.01 . 1 . . . . 292 ALA QB . 18491 1 282 . 1 1 38 38 ALA HB2 H 1 1.49 0.01 . 1 . . . . 292 ALA QB . 18491 1 283 . 1 1 38 38 ALA HB3 H 1 1.49 0.01 . 1 . . . . 292 ALA QB . 18491 1 284 . 1 1 39 39 THR H H 1 8.27 0.01 . 1 . . . . 293 THR H . 18491 1 285 . 1 1 39 39 THR HA H 1 3.41 0.01 . 1 . . . . 293 THR HA . 18491 1 286 . 1 1 39 39 THR HB H 1 4.54 0.01 . 1 . . . . 293 THR HB . 18491 1 287 . 1 1 39 39 THR HG21 H 1 1.18 0.01 . 1 . . . . 293 THR QG2 . 18491 1 288 . 1 1 39 39 THR HG22 H 1 1.18 0.01 . 1 . . . . 293 THR QG2 . 18491 1 289 . 1 1 39 39 THR HG23 H 1 1.18 0.01 . 1 . . . . 293 THR QG2 . 18491 1 290 . 1 1 40 40 ASP H H 1 8.89 0.01 . 1 . . . . 294 ASP H . 18491 1 291 . 1 1 40 40 ASP HA H 1 4.15 0.01 . 1 . . . . 294 ASP HA . 18491 1 292 . 1 1 40 40 ASP HB2 H 1 2.76 0.01 . 2 . . . . 294 ASP HB2 . 18491 1 293 . 1 1 40 40 ASP HB3 H 1 3.10 0.01 . 2 . . . . 294 ASP HB3 . 18491 1 294 . 1 1 41 41 LEU H H 1 7.44 0.01 . 1 . . . . 295 LEU H . 18491 1 295 . 1 1 41 41 LEU HA H 1 3.89 0.01 . 1 . . . . 295 LEU HA . 18491 1 296 . 1 1 41 41 LEU HB2 H 1 0.32 0.01 . 2 . . . . 295 LEU HB2 . 18491 1 297 . 1 1 41 41 LEU HB3 H 1 1.32 0.01 . 2 . . . . 295 LEU HB3 . 18491 1 298 . 1 1 41 41 LEU HG H 1 1.69 0.01 . 1 . . . . 295 LEU HG . 18491 1 299 . 1 1 41 41 LEU HD11 H 1 0.75 0.01 . 2 . . . . 295 LEU QD1 . 18491 1 300 . 1 1 41 41 LEU HD12 H 1 0.75 0.01 . 2 . . . . 295 LEU QD1 . 18491 1 301 . 1 1 41 41 LEU HD13 H 1 0.75 0.01 . 2 . . . . 295 LEU QD1 . 18491 1 302 . 1 1 41 41 LEU HD21 H 1 0.75 0.01 . 2 . . . . 295 LEU QD2 . 18491 1 303 . 1 1 41 41 LEU HD22 H 1 0.75 0.01 . 2 . . . . 295 LEU QD2 . 18491 1 304 . 1 1 41 41 LEU HD23 H 1 0.75 0.01 . 2 . . . . 295 LEU QD2 . 18491 1 305 . 1 1 42 42 TYR H H 1 8.33 0.01 . 1 . . . . 296 TYR H . 18491 1 306 . 1 1 42 42 TYR HA H 1 3.51 0.01 . 1 . . . . 296 TYR HA . 18491 1 307 . 1 1 42 42 TYR HB2 H 1 2.91 0.01 . 1 . . . . 296 TYR HB2 . 18491 1 308 . 1 1 42 42 TYR HB3 H 1 2.91 0.01 . 1 . . . . 296 TYR HB3 . 18491 1 309 . 1 1 42 42 TYR HD1 H 1 7.16 0.01 . 3 . . . . 296 TYR HD1 . 18491 1 310 . 1 1 42 42 TYR HD2 H 1 7.16 0.01 . 3 . . . . 296 TYR HD2 . 18491 1 311 . 1 1 42 42 TYR HE1 H 1 7.16 0.01 . 3 . . . . 296 TYR HE1 . 18491 1 312 . 1 1 42 42 TYR HE2 H 1 7.16 0.01 . 3 . . . . 296 TYR HE2 . 18491 1 313 . 1 1 43 43 GLY H H 1 8.11 0.01 . 1 . . . . 297 GLY H . 18491 1 314 . 1 1 43 43 GLY HA2 H 1 4.03 0.01 . 2 . . . . 297 GLY HA2 . 18491 1 315 . 1 1 43 43 GLY HA3 H 1 4.85 0.01 . 2 . . . . 297 GLY HA3 . 18491 1 316 . 1 1 44 44 SER H H 1 9.43 0.01 . 1 . . . . 298 SER H . 18491 1 317 . 1 1 44 44 SER HA H 1 4.22 0.01 . 1 . . . . 298 SER HA . 18491 1 318 . 1 1 44 44 SER HB2 H 1 4.02 0.01 . 2 . . . . 298 SER HB2 . 18491 1 319 . 1 1 44 44 SER HB3 H 1 4.75 0.01 . 2 . . . . 298 SER HB3 . 18491 1 320 . 1 1 45 45 THR H H 1 8.15 0.01 . 1 . . . . 299 THR H . 18491 1 321 . 1 1 45 45 THR HA H 1 4.58 0.01 . 1 . . . . 299 THR HA . 18491 1 322 . 1 1 45 45 THR HB H 1 4.65 0.01 . 1 . . . . 299 THR HB . 18491 1 323 . 1 1 45 45 THR HG21 H 1 1.22 0.01 . 1 . . . . 299 THR QG2 . 18491 1 324 . 1 1 45 45 THR HG22 H 1 1.22 0.01 . 1 . . . . 299 THR QG2 . 18491 1 325 . 1 1 45 45 THR HG23 H 1 1.22 0.01 . 1 . . . . 299 THR QG2 . 18491 1 326 . 1 1 46 46 SER H H 1 7.38 0.01 . 1 . . . . 300 SER H . 18491 1 327 . 1 1 46 46 SER HA H 1 4.35 0.01 . 1 . . . . 300 SER HA . 18491 1 328 . 1 1 46 46 SER HB2 H 1 3.91 0.01 . 2 . . . . 300 SER HB2 . 18491 1 329 . 1 1 46 46 SER HB3 H 1 4.05 0.01 . 2 . . . . 300 SER HB3 . 18491 1 330 . 1 1 47 47 GLN H H 1 9.40 0.01 . 1 . . . . 301 GLN H . 18491 1 331 . 1 1 47 47 GLN HA H 1 4.13 0.01 . 1 . . . . 301 GLN HA . 18491 1 332 . 1 1 47 47 GLN HB2 H 1 2.00 0.01 . 2 . . . . 301 GLN HB2 . 18491 1 333 . 1 1 47 47 GLN HB3 H 1 2.08 0.01 . 2 . . . . 301 GLN HB3 . 18491 1 334 . 1 1 47 47 GLN HG2 H 1 2.42 0.01 . 1 . . . . 301 GLN HG2 . 18491 1 335 . 1 1 47 47 GLN HG3 H 1 2.42 0.01 . 1 . . . . 301 GLN HG3 . 18491 1 336 . 1 1 47 47 GLN HE21 H 1 6.95 0.01 . 2 . . . . 301 GLN HE21 . 18491 1 337 . 1 1 47 47 GLN HE22 H 1 7.63 0.01 . 2 . . . . 301 GLN HE22 . 18491 1 338 . 1 1 48 48 GLU H H 1 9.74 0.01 . 1 . . . . 302 GLU H . 18491 1 339 . 1 1 48 48 GLU HA H 1 3.73 0.01 . 1 . . . . 302 GLU HA . 18491 1 340 . 1 1 48 48 GLU HB2 H 1 1.50 0.01 . 2 . . . . 302 GLU HB2 . 18491 1 341 . 1 1 48 48 GLU HB3 H 1 2.15 0.01 . 2 . . . . 302 GLU HB3 . 18491 1 342 . 1 1 48 48 GLU HG2 H 1 1.75 0.01 . 1 . . . . 302 GLU HG2 . 18491 1 343 . 1 1 48 48 GLU HG3 H 1 1.75 0.01 . 1 . . . . 302 GLU HG3 . 18491 1 344 . 1 1 49 49 VAL H H 1 7.70 0.01 . 1 . . . . 303 VAL H . 18491 1 345 . 1 1 49 49 VAL HA H 1 3.35 0.01 . 1 . . . . 303 VAL HA . 18491 1 346 . 1 1 49 49 VAL HB H 1 2.03 0.01 . 1 . . . . 303 VAL HB . 18491 1 347 . 1 1 49 49 VAL HG11 H 1 0.96 0.01 . 2 . . . . 303 VAL QG1 . 18491 1 348 . 1 1 49 49 VAL HG12 H 1 0.96 0.01 . 2 . . . . 303 VAL QG1 . 18491 1 349 . 1 1 49 49 VAL HG13 H 1 0.96 0.01 . 2 . . . . 303 VAL QG1 . 18491 1 350 . 1 1 49 49 VAL HG21 H 1 1.04 0.01 . 2 . . . . 303 VAL QG2 . 18491 1 351 . 1 1 49 49 VAL HG22 H 1 1.04 0.01 . 2 . . . . 303 VAL QG2 . 18491 1 352 . 1 1 49 49 VAL HG23 H 1 1.04 0.01 . 2 . . . . 303 VAL QG2 . 18491 1 353 . 1 1 50 50 ALA H H 1 7.25 0.01 . 1 . . . . 304 ALA H . 18491 1 354 . 1 1 50 50 ALA HA H 1 4.07 0.01 . 1 . . . . 304 ALA HA . 18491 1 355 . 1 1 50 50 ALA HB1 H 1 1.52 0.01 . 1 . . . . 304 ALA QB . 18491 1 356 . 1 1 50 50 ALA HB2 H 1 1.52 0.01 . 1 . . . . 304 ALA QB . 18491 1 357 . 1 1 50 50 ALA HB3 H 1 1.52 0.01 . 1 . . . . 304 ALA QB . 18491 1 358 . 1 1 51 51 SER H H 1 8.84 0.01 . 1 . . . . 305 SER H . 18491 1 359 . 1 1 51 51 SER HA H 1 4.24 0.01 . 1 . . . . 305 SER HA . 18491 1 360 . 1 1 51 51 SER HB2 H 1 3.83 0.01 . 2 . . . . 305 SER HB2 . 18491 1 361 . 1 1 51 51 SER HB3 H 1 3.99 0.01 . 2 . . . . 305 SER HB3 . 18491 1 362 . 1 1 52 52 VAL H H 1 8.16 0.01 . 1 . . . . 306 VAL H . 18491 1 363 . 1 1 52 52 VAL HA H 1 3.67 0.01 . 1 . . . . 306 VAL HA . 18491 1 364 . 1 1 52 52 VAL HB H 1 2.23 0.01 . 1 . . . . 306 VAL HB . 18491 1 365 . 1 1 52 52 VAL HG11 H 1 0.94 0.01 . 2 . . . . 306 VAL QG1 . 18491 1 366 . 1 1 52 52 VAL HG12 H 1 0.94 0.01 . 2 . . . . 306 VAL QG1 . 18491 1 367 . 1 1 52 52 VAL HG13 H 1 0.94 0.01 . 2 . . . . 306 VAL QG1 . 18491 1 368 . 1 1 52 52 VAL HG21 H 1 1.09 0.01 . 2 . . . . 306 VAL QG2 . 18491 1 369 . 1 1 52 52 VAL HG22 H 1 1.09 0.01 . 2 . . . . 306 VAL QG2 . 18491 1 370 . 1 1 52 52 VAL HG23 H 1 1.09 0.01 . 2 . . . . 306 VAL QG2 . 18491 1 371 . 1 1 53 53 LYS H H 1 8.25 0.01 . 1 . . . . 307 LYS H . 18491 1 372 . 1 1 53 53 LYS HA H 1 3.69 0.01 . 1 . . . . 307 LYS HA . 18491 1 373 . 1 1 53 53 LYS HB2 H 1 1.94 0.01 . 1 . . . . 307 LYS HB2 . 18491 1 374 . 1 1 53 53 LYS HB3 H 1 1.94 0.01 . 1 . . . . 307 LYS HB3 . 18491 1 375 . 1 1 53 53 LYS HG2 H 1 1.68 0.01 . 1 . . . . 307 LYS HG2 . 18491 1 376 . 1 1 53 53 LYS HG3 H 1 1.68 0.01 . 1 . . . . 307 LYS HG3 . 18491 1 377 . 1 1 53 53 LYS HD2 H 1 1.68 0.01 . 1 . . . . 307 LYS HD2 . 18491 1 378 . 1 1 53 53 LYS HD3 H 1 1.68 0.01 . 1 . . . . 307 LYS HD3 . 18491 1 379 . 1 1 53 53 LYS HE2 H 1 2.72 0.01 . 2 . . . . 307 LYS HE2 . 18491 1 380 . 1 1 53 53 LYS HE3 H 1 2.94 0.01 . 2 . . . . 307 LYS HE3 . 18491 1 381 . 1 1 53 53 LYS HZ1 H 1 7.67 0.01 . 1 . . . . 307 LYS QZ . 18491 1 382 . 1 1 53 53 LYS HZ2 H 1 7.67 0.01 . 1 . . . . 307 LYS QZ . 18491 1 383 . 1 1 53 53 LYS HZ3 H 1 7.67 0.01 . 1 . . . . 307 LYS QZ . 18491 1 384 . 1 1 54 54 GLN H H 1 7.99 0.01 . 1 . . . . 308 GLN H . 18491 1 385 . 1 1 54 54 GLN HA H 1 4.07 0.01 . 1 . . . . 308 GLN HA . 18491 1 386 . 1 1 54 54 GLN HB2 H 1 2.21 0.01 . 1 . . . . 308 GLN HB2 . 18491 1 387 . 1 1 54 54 GLN HB3 H 1 2.21 0.01 . 1 . . . . 308 GLN HB3 . 18491 1 388 . 1 1 54 54 GLN HG2 H 1 2.44 0.01 . 2 . . . . 308 GLN HG2 . 18491 1 389 . 1 1 54 54 GLN HG3 H 1 2.61 0.01 . 2 . . . . 308 GLN HG3 . 18491 1 390 . 1 1 54 54 GLN HE21 H 1 6.86 0.01 . 2 . . . . 308 GLN HE21 . 18491 1 391 . 1 1 54 54 GLN HE22 H 1 7.48 0.01 . 2 . . . . 308 GLN HE22 . 18491 1 392 . 1 1 55 55 ALA H H 1 8.20 0.01 . 1 . . . . 309 ALA H . 18491 1 393 . 1 1 55 55 ALA HA H 1 4.12 0.01 . 1 . . . . 309 ALA HA . 18491 1 394 . 1 1 55 55 ALA HB1 H 1 1.46 0.01 . 1 . . . . 309 ALA QB . 18491 1 395 . 1 1 55 55 ALA HB2 H 1 1.46 0.01 . 1 . . . . 309 ALA QB . 18491 1 396 . 1 1 55 55 ALA HB3 H 1 1.46 0.01 . 1 . . . . 309 ALA QB . 18491 1 397 . 1 1 56 56 PHE H H 1 8.08 0.01 . 1 . . . . 310 PHE H . 18491 1 398 . 1 1 56 56 PHE HA H 1 4.15 0.01 . 1 . . . . 310 PHE HA . 18491 1 399 . 1 1 56 56 PHE HB2 H 1 3.02 0.01 . 2 . . . . 310 PHE HB2 . 18491 1 400 . 1 1 56 56 PHE HB3 H 1 3.08 0.01 . 2 . . . . 310 PHE HB3 . 18491 1 401 . 1 1 56 56 PHE HD1 H 1 7.42 0.01 . 3 . . . . 310 PHE HD1 . 18491 1 402 . 1 1 56 56 PHE HD2 H 1 7.42 0.01 . 3 . . . . 310 PHE HD2 . 18491 1 403 . 1 1 56 56 PHE HE1 H 1 6.82 0.01 . 3 . . . . 310 PHE HE1 . 18491 1 404 . 1 1 56 56 PHE HE2 H 1 6.82 0.01 . 3 . . . . 310 PHE HE2 . 18491 1 405 . 1 1 56 56 PHE HZ H 1 6.98 0.01 . 1 . . . . 310 PHE HZ . 18491 1 406 . 1 1 57 57 ASP H H 1 8.66 0.01 . 1 . . . . 311 ASP H . 18491 1 407 . 1 1 57 57 ASP HA H 1 4.61 0.01 . 1 . . . . 311 ASP HA . 18491 1 408 . 1 1 57 57 ASP HB2 H 1 2.80 0.01 . 1 . . . . 311 ASP HB2 . 18491 1 409 . 1 1 57 57 ASP HB3 H 1 2.80 0.01 . 1 . . . . 311 ASP HB3 . 18491 1 410 . 1 1 58 58 ALA H H 1 7.53 0.01 . 1 . . . . 312 ALA H . 18491 1 411 . 1 1 58 58 ALA HA H 1 4.33 0.01 . 1 . . . . 312 ALA HA . 18491 1 412 . 1 1 58 58 ALA HB1 H 1 1.48 0.01 . 1 . . . . 312 ALA QB . 18491 1 413 . 1 1 58 58 ALA HB2 H 1 1.48 0.01 . 1 . . . . 312 ALA QB . 18491 1 414 . 1 1 58 58 ALA HB3 H 1 1.48 0.01 . 1 . . . . 312 ALA QB . 18491 1 415 . 1 1 59 59 VAL H H 1 7.27 0.01 . 1 . . . . 313 VAL H . 18491 1 416 . 1 1 59 59 VAL HA H 1 3.78 0.01 . 1 . . . . 313 VAL HA . 18491 1 417 . 1 1 59 59 VAL HB H 1 2.26 0.01 . 1 . . . . 313 VAL HB . 18491 1 418 . 1 1 59 59 VAL HG11 H 1 0.58 0.01 . 2 . . . . 313 VAL QG1 . 18491 1 419 . 1 1 59 59 VAL HG12 H 1 0.58 0.01 . 2 . . . . 313 VAL QG1 . 18491 1 420 . 1 1 59 59 VAL HG13 H 1 0.58 0.01 . 2 . . . . 313 VAL QG1 . 18491 1 421 . 1 1 59 59 VAL HG21 H 1 1.13 0.01 . 2 . . . . 313 VAL QG2 . 18491 1 422 . 1 1 59 59 VAL HG22 H 1 1.13 0.01 . 2 . . . . 313 VAL QG2 . 18491 1 423 . 1 1 59 59 VAL HG23 H 1 1.13 0.01 . 2 . . . . 313 VAL QG2 . 18491 1 424 . 1 1 60 60 GLY H H 1 8.66 0.01 . 1 . . . . 314 GLY H . 18491 1 425 . 1 1 60 60 GLY HA2 H 1 3.94 0.01 . 1 . . . . 314 GLY HA2 . 18491 1 426 . 1 1 60 60 GLY HA3 H 1 3.94 0.01 . 1 . . . . 314 GLY HA3 . 18491 1 427 . 1 1 61 61 VAL H H 1 7.76 0.01 . 1 . . . . 315 VAL H . 18491 1 428 . 1 1 61 61 VAL HA H 1 4.08 0.01 . 1 . . . . 315 VAL HA . 18491 1 429 . 1 1 61 61 VAL HB H 1 2.13 0.01 . 1 . . . . 315 VAL HB . 18491 1 430 . 1 1 61 61 VAL HG11 H 1 0.94 0.01 . 2 . . . . 315 VAL QG1 . 18491 1 431 . 1 1 61 61 VAL HG12 H 1 0.94 0.01 . 2 . . . . 315 VAL QG1 . 18491 1 432 . 1 1 61 61 VAL HG13 H 1 0.94 0.01 . 2 . . . . 315 VAL QG1 . 18491 1 433 . 1 1 61 61 VAL HG21 H 1 0.96 0.01 . 2 . . . . 315 VAL QG2 . 18491 1 434 . 1 1 61 61 VAL HG22 H 1 0.96 0.01 . 2 . . . . 315 VAL QG2 . 18491 1 435 . 1 1 61 61 VAL HG23 H 1 0.96 0.01 . 2 . . . . 315 VAL QG2 . 18491 1 436 . 1 1 62 62 LYS H H 1 8.00 0.01 . 1 . . . . 316 LYS H . 18491 1 437 . 1 1 62 62 LYS HA H 1 4.21 0.01 . 1 . . . . 316 LYS HA . 18491 1 438 . 1 1 62 62 LYS HB2 H 1 1.72 0.01 . 2 . . . . 316 LYS HB2 . 18491 1 439 . 1 1 62 62 LYS HB3 H 1 1.85 0.01 . 2 . . . . 316 LYS HB3 . 18491 1 440 . 1 1 62 62 LYS HG2 H 1 1.39 0.01 . 1 . . . . 316 LYS HG2 . 18491 1 441 . 1 1 62 62 LYS HG3 H 1 1.39 0.01 . 1 . . . . 316 LYS HG3 . 18491 1 442 . 1 1 62 62 LYS HD2 H 1 1.66 0.01 . 1 . . . . 316 LYS HD2 . 18491 1 443 . 1 1 62 62 LYS HD3 H 1 1.66 0.01 . 1 . . . . 316 LYS HD3 . 18491 1 444 . 1 1 62 62 LYS HE2 H 1 2.97 0.01 . 1 . . . . 316 LYS HE2 . 18491 1 445 . 1 1 62 62 LYS HE3 H 1 2.97 0.01 . 1 . . . . 316 LYS HE3 . 18491 1 446 . 1 1 62 62 LYS HZ1 H 1 7.46 0.01 . 1 . . . . 316 LYS QZ . 18491 1 447 . 1 1 62 62 LYS HZ2 H 1 7.46 0.01 . 1 . . . . 316 LYS QZ . 18491 1 448 . 1 1 62 62 LYS HZ3 H 1 7.46 0.01 . 1 . . . . 316 LYS QZ . 18491 1 stop_ save_