data_17096 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17096 _Entry.Title ; Stopped-flow NMR spectroscopy: Real-Time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-08-02 _Entry.Accession_date 2010-08-02 _Entry.Last_release_date 2010-11-10 _Entry.Original_release_date 2010-11-10 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Sydney Hoeltzli . D. . 17096 2 Carl Frieden . . . 17096 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID chemical_rates 4 17096 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID 'kinetic rates' 1 17096 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2010-11-10 2010-08-02 original author . 17096 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17096 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7568125 _Citation.Full_citation . _Citation.Title 'Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full . _Citation.Journal_volume 92 _Citation.Journal_issue 20 _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 9318 _Citation.Page_last 9322 _Citation.Year 1995 _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 Sydney Hoeltzli . D. . 17096 1 2 Carl Frieden . . . 17096 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17096 _Assembly.ID 1 _Assembly.Name 'DHFR unfolding' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 DHFR 1 $DHFR A . yes native no no . . 'rate is with respect to unfolding' 17096 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DHFR _Entity.Sf_category entity _Entity.Sf_framecode DHFR _Entity.Entry_ID 17096 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name DHFR _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 ; MVGSLNCIVAVSQNMGIGKN GDLPWPPLRNEFRYFQRMTT TSSVEGKQNLVIMGKKTWFS IPEKNRPLKGRINLVLSREL KEPPQGAHFLSRSLDDALKL TEQPELANKVDMVWIVGGSS VYKEAMNHPGHLKLFVTRIM QDFESDTFFPEIDLEKYKLL PEYPGVLSDVQEEKGIKYKF EVYEKND ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 187 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _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 19563 . DHFR . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 2 no BMRB 19564 . DHFR . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 3 no BMRB 19565 . DHFR . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 4 no BMRB 19566 . DHFR . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 5 no BMRB 19567 . DHFR . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 6 no PDB 1BOZ . "Structure-Based Design And Synthesis Of Lipophilic 2,4- Diamino-6-Substituted Quinazolines And Their Evaluation As Inhibitors O" . . . . . 99.47 186 99.46 99.46 3.54e-132 . . . . 17096 1 7 no PDB 1DHF . "Crystal Structures Of Recombinant Human Dihydrofolate Reductase Complexed With Folate And 5-Deazofolate" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 8 no PDB 1DLR . "Methotrexate-Resistant Variants Of Human Dihydrofolate Reductase With Substitution Of Leucine 22: Kinetics, Crystallography And" . . . . . 99.47 186 99.46 99.46 6.87e-133 . . . . 17096 1 9 no PDB 1DLS . "Methotrexate-Resistant Variants Of Human Dihydrofolate Reductase With Substitution Of Leucine 22: Kinetics, Crystallography And" . . . . . 99.47 186 99.46 99.46 1.10e-132 . . . . 17096 1 10 no PDB 1DRF . "Crystal Structure Of Human Dihydrofolate Reductase Complexed With Folate" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 11 no PDB 1HFP . "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" . . . . . 99.47 186 99.46 99.46 3.54e-132 . . . . 17096 1 12 no PDB 1HFQ . "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" . . . . . 99.47 186 99.46 99.46 1.90e-132 . . . . 17096 1 13 no PDB 1HFR . "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 14 no PDB 1KMS . "Human Dihydrofolate Reductase Complexed With Nadph And 6- ([5-Quinolylamino]methyl)-2,4-Diamino-5-Methylpyrido[2,3- D]pyrimidin" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 15 no PDB 1KMV . "Human Dihydrofolate Reductase Complexed With Nadph And (Z)- 6-(2-[2,5-Dimethoxyphenyl]ethen-1-Yl)-2,4-Diamino-5- Methylpyrido[2" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 16 no PDB 1MVS . "Analysis Of Two Polymorphic Forms Of A Pyrido[2,3- D]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex With Human Dihy" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 17 no PDB 1MVT . "Analysis Of Two Polymorphic Forms Of A Pyrido[2,3- D]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex With Human Dihy" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 18 no PDB 1OHJ . "Human Dihydrofolate Reductase, Monoclinic (P21) Crystal Form" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 19 no PDB 1OHK . "Human Dihydrofolate Reductase, Orthorhombic (P21 21 21) Crystal Form" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 20 no PDB 1PD8 . "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-n-methylanilino Pyridopyrimidine Antifolate Complex With Hu" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 21 no PDB 1PD9 . "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-N-Methylanilino Pyridopyrimidine Antifolate Complex With Hu" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 22 no PDB 1PDB . "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-N-Methylanilino Pyridopyrimidine Antifolate Complex With Hu" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 23 no PDB 1S3U . "Structure Determination Of Tetrahydroquinazoline Antifolates In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 24 no PDB 1S3V . "Structure Determination Of Tetrahydroquinazoline Antifolates In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 25 no PDB 1S3W . "Structure Determination Of Tetrahydroquinazoline Antifoaltes In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 26 no PDB 1U71 . "Understanding The Role Of Leu22 Variants In Methotrexate Resistance: Comparison Of Wild-type And Leu22arg Variant Mouse And Hum" . . . . . 99.47 186 99.46 99.46 1.61e-132 . . . . 17096 1 27 no PDB 1U72 . "Understanding The Role Of Leu22 Variants In Methotrexate Resistance: Comparison Of Wild-Type And Leu22arg Variant Mouse And Hum" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 28 no PDB 1YHO . "Solution Structure Of Human Dihydrofolate Reductase Complexed With Trimethoprim And Nadph, 25 Structures" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 29 no PDB 2C2S . "Human Dihydrofolate Reductase Complexed With Nadph And 2,4- Diamino-5-(1-O-Carboranylmethyl)-6-Methylpyrimidine, A Novel Boron " . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 30 no PDB 2C2T . "Human Dihydrofolate Reductase Complexed With Nadph And 2,4- Diamino-5-((7,8-Dicarbaundecaboran-7-Yl)methyl)-6- Methylpyrimidine" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 31 no PDB 2DHF . "Crystal Structures Of Recombinant Human Dihydrofolate Reductase Complexed With Folate And 5-Deazofolate" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 32 no PDB 2W3A . "Human Dihydrofolate Reductase Complexed With Nadph And Trimethoprim" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 33 no PDB 2W3B . "Human Dihydrofolate Reductase Complexed With Nadph And A Lipophilic Antifolate Selective For Mycobacterium Avium Dhfr, 6-((2,5-" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 34 no PDB 2W3M . "Human Dihydrofolate Reductase Complexed With Nadph And Folate" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 35 no PDB 3EIG . "Crystal Structure Of A Methotrexate-Resistant Mutant Of Human Dihydrofolate Reductase" . . . . . 99.47 186 98.92 99.46 9.69e-132 . . . . 17096 1 36 no PDB 3F8Y . "Correlations Of Human Dihydrofolate Reductase With Structural Data For Human Active Site Mutant Enzyme Complexes" . . . . . 100.00 187 99.47 100.00 1.09e-133 . . . . 17096 1 37 no PDB 3F8Z . "Human Dihydrofolate Reductase Structural Data With Active Site Mutant Enzyme Complexes" . . . . . 100.00 187 98.93 99.47 6.24e-133 . . . . 17096 1 38 no PDB 3F91 . "Structural Data For Human Active Site Mutant Enzyme Complexes" . . . . . 100.00 187 98.93 98.93 2.50e-132 . . . . 17096 1 39 no PDB 3FS6 . "Correlations Of Inhibitor Kinetics For Pneumocystis Jirovecii And Human Dihydrofolate Reductase With Structural Data For Human " . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 40 no PDB 3GHC . "Design, Synthesis, And X-Ray Crystal Structure Of Classical And Nonclassical 2-Amino-4-Oxo-5-Substituted-6-Thieno[2,3- D]pyrimi" . . . . . 99.47 186 98.92 99.46 4.98e-132 . . . . 17096 1 41 no PDB 3GHV . "Human Dihydrofolate Reductase Q35kN64F DOUBLE MUTANT INHIBITOR Complex" . . . . . 99.47 186 98.92 99.46 1.52e-131 . . . . 17096 1 42 no PDB 3GHW . "Human Dihydrofolate Reductase Inhibitor Complex" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 43 no PDB 3GI2 . "Human Dihydrofolate Reductase Q35k Mutant Inhibitor Complex" . . . . . 100.00 187 99.47 100.00 1.09e-133 . . . . 17096 1 44 no PDB 3GYF . "Human Dhfr With Z-Isomer In Orthorhombic Lattice" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 45 no PDB 3L3R . "Structural, Computational And Kinetic Data For Antifolate Interactions Against Pneumocystis Jirovecii, Pneumocystis Carinii And" . . . . . 99.47 186 99.46 100.00 6.80e-133 . . . . 17096 1 46 no PDB 3N0H . "Hdhfr Double Mutant Q35sN64F TRIMETHOPRIM BINARY COMPLEX" . . . . . 99.47 186 98.92 98.92 2.27e-131 . . . . 17096 1 47 no PDB 3NTZ . "Design, Synthesis, Biological Evaluation And X-Ray Crystal Structures Of Novel Classical 6,5,6-Tricyclicbenzo[4,5]thieno[2,3-D]" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 48 no PDB 3NU0 . "Design, Synthesis, Biological Evaluation And X-ray Crystal Structure Of Novel Classical 6,5,6-tricyclicbenzo[4,5]thieno[2,3-d]p" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 49 no PDB 3NXO . "Perferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" . . . . . 99.47 186 99.46 100.00 3.23e-133 . . . . 17096 1 50 no PDB 3NXR . "Perferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 51 no PDB 3NXT . "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E-And Z-Isomers Of A Se" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 52 no PDB 3NXV . "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 53 no PDB 3NXX . "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 54 no PDB 3NXY . "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alernate Binding Modes Observed Fro The E- And Z-Isomers Of A Se" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 55 no PDB 3NZD . "Structural Analysis Of Pneumocystis Carinii And Human Dhfr Complexes With Nadph And A Series Of Five 5-(Omega-Carboxy(Alkyloxy(" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 56 no PDB 3OAF . "Structural And Kinetic Data For Antifolate Interactions Against Pneumocystis Jirovecii, Pneumocystis Carinii And Human Dihydrof" . . . . . 99.47 186 98.92 98.92 2.27e-131 . . . . 17096 1 57 no PDB 3S3V . "Human Dihydrofolate Reductase Q35kN64F DOUBLE MUTANT BINARY COMPLEX With Trimethoprim" . . . . . 99.47 186 98.92 99.46 1.52e-131 . . . . 17096 1 58 no PDB 3S7A . "Human Dihydrofolate Reductase Binary Complex With Pt684" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 59 no PDB 4DDR . "Human Dihydrofolate Reductase Complexed With Nadph And P218" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 60 no PDB 4G95 . "Hdhfr-oag Binary Complex" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 61 no PDB 4KAK . "Crystal Structure Of Human Dihydrofolate Reductase Complexed With Nadph And 6-ethyl-5-[(3s)-3-[3-methoxy-5-(pyridine-4-yl)pheny" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 62 no PDB 4KBN . "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3-(3,5- Pyrimidine)]-phenyl-prop-1-yn-1-yl}-6-ethyl-pyrimidine-2,4" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 63 no PDB 4KD7 . "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5(pyridine-4-yl)phenyl]prop-1-yn-1-yl}-6-ethyl-pyrimidi" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 64 no PDB 4KEB . "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5-(isoquin-5-yl)phenyl]but-1-yn-1-yl}6-ethylpyrimidine-" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 65 no PDB 4KFJ . "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5-(isoquin-5-yl)phenyl]prop-1-yn-1-yl}6-ethylprimidine-" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 66 no PDB 4M6J . "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadph" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 67 no PDB 4M6K . "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadp+ And Folate" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 68 no PDB 4M6L . "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadp+ And 5,10-dideazatetrahydrofolic Acid" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 69 no PDB 4QHV . "Crystal Structure Of Human Dihydrofolate Reductase As Complex With Pyridopyrimidine 22 (n~6~-methyl-n~6~-[4-(propan-2-yl) Pheny" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 70 no PDB 4QJC . "Human Dihydrofolate Reductase Ternary Complex With Nadph And Inhibitor 26 (n~6~-methyl-n~6~-(3,4,5-trifluorophenyl)pyrido[2,3-d" . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 71 no DBJ BAG35526 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 72 no DBJ BAG56693 . "unnamed protein product [Homo sapiens]" . . . . . 72.19 135 100.00 100.00 4.05e-92 . . . . 17096 1 73 no DBJ BAG59770 . "unnamed protein product [Homo sapiens]" . . . . . 65.78 129 100.00 100.00 2.89e-83 . . . . 17096 1 74 no DBJ BAJ20267 . "dihydrofolate reductase [synthetic construct]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 75 no EMBL CAA23765 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 76 no EMBL CAA25409 . "dihydrofolate reductase [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 77 no GB AAA58484 . "dihydrofolate reductase (EC 1.5.1.3) [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 78 no GB AAA58485 . "dihydrofolate reductase [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 79 no GB AAH00192 . "Dihydrofolate reductase [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 80 no GB AAH03584 . "DHFR protein [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 81 no GB AAH70280 . "Dihydrofolate reductase [Homo sapiens]" . . . . . 100.00 187 99.47 100.00 7.56e-134 . . . . 17096 1 82 no PRF 0905195A . reductase,dihydrofolate . . . . . 99.47 186 100.00 100.00 1.75e-133 . . . . 17096 1 83 no PRF 0906214A . reductase,dihydrofolate . . . . . 99.47 186 98.39 99.46 1.95e-131 . . . . 17096 1 84 no REF NP_000782 . "dihydrofolate reductase isoform 1 [Homo sapiens]" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 1 85 no REF NP_001277283 . "dihydrofolate reductase isoform 2 [Homo sapiens]" . . . . . 72.19 135 100.00 100.00 4.05e-92 . . . . 17096 1 86 no REF NP_001277286 . "dihydrofolate reductase isoform 3 [Homo sapiens]" . . . . . 65.78 129 100.00 100.00 2.89e-83 . . . . 17096 1 87 no REF XP_001099963 . "PREDICTED: dihydrofolate reductase, partial [Macaca mulatta]" . . . . . 100.00 207 97.33 98.40 6.37e-131 . . . . 17096 1 88 no REF XP_001110551 . "PREDICTED: dihydrofolate reductase [Macaca mulatta]" . . . . . 100.00 262 97.86 98.93 3.08e-132 . . . . 17096 1 89 no SP P00374 . "RecName: Full=Dihydrofolate reductase" . . . . . 100.00 187 100.00 100.00 2.17e-134 . . . . 17096 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 . MET . 17096 1 2 . VAL . 17096 1 3 . GLY . 17096 1 4 . SER . 17096 1 5 . LEU . 17096 1 6 . ASN . 17096 1 7 . CYS . 17096 1 8 . ILE . 17096 1 9 . VAL . 17096 1 10 . ALA . 17096 1 11 . VAL . 17096 1 12 . SER . 17096 1 13 . GLN . 17096 1 14 . ASN . 17096 1 15 . MET . 17096 1 16 . GLY . 17096 1 17 . ILE . 17096 1 18 . GLY . 17096 1 19 . LYS . 17096 1 20 . ASN . 17096 1 21 . GLY . 17096 1 22 . ASP . 17096 1 23 . LEU . 17096 1 24 . PRO . 17096 1 25 . TRP . 17096 1 26 . PRO . 17096 1 27 . PRO . 17096 1 28 . LEU . 17096 1 29 . ARG . 17096 1 30 . ASN . 17096 1 31 . GLU . 17096 1 32 . PHE . 17096 1 33 . ARG . 17096 1 34 . TYR . 17096 1 35 . PHE . 17096 1 36 . GLN . 17096 1 37 . ARG . 17096 1 38 . MET . 17096 1 39 . THR . 17096 1 40 . THR . 17096 1 41 . THR . 17096 1 42 . SER . 17096 1 43 . SER . 17096 1 44 . VAL . 17096 1 45 . GLU . 17096 1 46 . GLY . 17096 1 47 . LYS . 17096 1 48 . GLN . 17096 1 49 . ASN . 17096 1 50 . LEU . 17096 1 51 . VAL . 17096 1 52 . ILE . 17096 1 53 . MET . 17096 1 54 . GLY . 17096 1 55 . LYS . 17096 1 56 . LYS . 17096 1 57 . THR . 17096 1 58 . TRP . 17096 1 59 . PHE . 17096 1 60 . SER . 17096 1 61 . ILE . 17096 1 62 . PRO . 17096 1 63 . GLU . 17096 1 64 . LYS . 17096 1 65 . ASN . 17096 1 66 . ARG . 17096 1 67 . PRO . 17096 1 68 . LEU . 17096 1 69 . LYS . 17096 1 70 . GLY . 17096 1 71 . ARG . 17096 1 72 . ILE . 17096 1 73 . ASN . 17096 1 74 . LEU . 17096 1 75 . VAL . 17096 1 76 . LEU . 17096 1 77 . SER . 17096 1 78 . ARG . 17096 1 79 . GLU . 17096 1 80 . LEU . 17096 1 81 . LYS . 17096 1 82 . GLU . 17096 1 83 . PRO . 17096 1 84 . PRO . 17096 1 85 . GLN . 17096 1 86 . GLY . 17096 1 87 . ALA . 17096 1 88 . HIS . 17096 1 89 . PHE . 17096 1 90 . LEU . 17096 1 91 . SER . 17096 1 92 . ARG . 17096 1 93 . SER . 17096 1 94 . LEU . 17096 1 95 . ASP . 17096 1 96 . ASP . 17096 1 97 . ALA . 17096 1 98 . LEU . 17096 1 99 . LYS . 17096 1 100 . LEU . 17096 1 101 . THR . 17096 1 102 . GLU . 17096 1 103 . GLN . 17096 1 104 . PRO . 17096 1 105 . GLU . 17096 1 106 . LEU . 17096 1 107 . ALA . 17096 1 108 . ASN . 17096 1 109 . LYS . 17096 1 110 . VAL . 17096 1 111 . ASP . 17096 1 112 . MET . 17096 1 113 . VAL . 17096 1 114 . TRP . 17096 1 115 . ILE . 17096 1 116 . VAL . 17096 1 117 . GLY . 17096 1 118 . GLY . 17096 1 119 . SER . 17096 1 120 . SER . 17096 1 121 . VAL . 17096 1 122 . TYR . 17096 1 123 . LYS . 17096 1 124 . GLU . 17096 1 125 . ALA . 17096 1 126 . MET . 17096 1 127 . ASN . 17096 1 128 . HIS . 17096 1 129 . PRO . 17096 1 130 . GLY . 17096 1 131 . HIS . 17096 1 132 . LEU . 17096 1 133 . LYS . 17096 1 134 . LEU . 17096 1 135 . PHE . 17096 1 136 . VAL . 17096 1 137 . THR . 17096 1 138 . ARG . 17096 1 139 . ILE . 17096 1 140 . MET . 17096 1 141 . GLN . 17096 1 142 . ASP . 17096 1 143 . PHE . 17096 1 144 . GLU . 17096 1 145 . SER . 17096 1 146 . ASP . 17096 1 147 . THR . 17096 1 148 . PHE . 17096 1 149 . PHE . 17096 1 150 . PRO . 17096 1 151 . GLU . 17096 1 152 . ILE . 17096 1 153 . ASP . 17096 1 154 . LEU . 17096 1 155 . GLU . 17096 1 156 . LYS . 17096 1 157 . TYR . 17096 1 158 . LYS . 17096 1 159 . LEU . 17096 1 160 . LEU . 17096 1 161 . PRO . 17096 1 162 . GLU . 17096 1 163 . TYR . 17096 1 164 . PRO . 17096 1 165 . GLY . 17096 1 166 . VAL . 17096 1 167 . LEU . 17096 1 168 . SER . 17096 1 169 . ASP . 17096 1 170 . VAL . 17096 1 171 . GLN . 17096 1 172 . GLU . 17096 1 173 . GLU . 17096 1 174 . LYS . 17096 1 175 . GLY . 17096 1 176 . ILE . 17096 1 177 . LYS . 17096 1 178 . TYR . 17096 1 179 . LYS . 17096 1 180 . PHE . 17096 1 181 . GLU . 17096 1 182 . VAL . 17096 1 183 . TYR . 17096 1 184 . GLU . 17096 1 185 . LYS . 17096 1 186 . ASN . 17096 1 187 . ASP . 17096 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 . MET 1 1 17096 1 . VAL 2 2 17096 1 . GLY 3 3 17096 1 . SER 4 4 17096 1 . LEU 5 5 17096 1 . ASN 6 6 17096 1 . CYS 7 7 17096 1 . ILE 8 8 17096 1 . VAL 9 9 17096 1 . ALA 10 10 17096 1 . VAL 11 11 17096 1 . SER 12 12 17096 1 . GLN 13 13 17096 1 . ASN 14 14 17096 1 . MET 15 15 17096 1 . GLY 16 16 17096 1 . ILE 17 17 17096 1 . GLY 18 18 17096 1 . LYS 19 19 17096 1 . ASN 20 20 17096 1 . GLY 21 21 17096 1 . ASP 22 22 17096 1 . LEU 23 23 17096 1 . PRO 24 24 17096 1 . TRP 25 25 17096 1 . PRO 26 26 17096 1 . PRO 27 27 17096 1 . LEU 28 28 17096 1 . ARG 29 29 17096 1 . ASN 30 30 17096 1 . GLU 31 31 17096 1 . PHE 32 32 17096 1 . ARG 33 33 17096 1 . TYR 34 34 17096 1 . PHE 35 35 17096 1 . GLN 36 36 17096 1 . ARG 37 37 17096 1 . MET 38 38 17096 1 . THR 39 39 17096 1 . THR 40 40 17096 1 . THR 41 41 17096 1 . SER 42 42 17096 1 . SER 43 43 17096 1 . VAL 44 44 17096 1 . GLU 45 45 17096 1 . GLY 46 46 17096 1 . LYS 47 47 17096 1 . GLN 48 48 17096 1 . ASN 49 49 17096 1 . LEU 50 50 17096 1 . VAL 51 51 17096 1 . ILE 52 52 17096 1 . MET 53 53 17096 1 . GLY 54 54 17096 1 . LYS 55 55 17096 1 . LYS 56 56 17096 1 . THR 57 57 17096 1 . TRP 58 58 17096 1 . PHE 59 59 17096 1 . SER 60 60 17096 1 . ILE 61 61 17096 1 . PRO 62 62 17096 1 . GLU 63 63 17096 1 . LYS 64 64 17096 1 . ASN 65 65 17096 1 . ARG 66 66 17096 1 . PRO 67 67 17096 1 . LEU 68 68 17096 1 . LYS 69 69 17096 1 . GLY 70 70 17096 1 . ARG 71 71 17096 1 . ILE 72 72 17096 1 . ASN 73 73 17096 1 . LEU 74 74 17096 1 . VAL 75 75 17096 1 . LEU 76 76 17096 1 . SER 77 77 17096 1 . ARG 78 78 17096 1 . GLU 79 79 17096 1 . LEU 80 80 17096 1 . LYS 81 81 17096 1 . GLU 82 82 17096 1 . PRO 83 83 17096 1 . PRO 84 84 17096 1 . GLN 85 85 17096 1 . GLY 86 86 17096 1 . ALA 87 87 17096 1 . HIS 88 88 17096 1 . PHE 89 89 17096 1 . LEU 90 90 17096 1 . SER 91 91 17096 1 . ARG 92 92 17096 1 . SER 93 93 17096 1 . LEU 94 94 17096 1 . ASP 95 95 17096 1 . ASP 96 96 17096 1 . ALA 97 97 17096 1 . LEU 98 98 17096 1 . LYS 99 99 17096 1 . LEU 100 100 17096 1 . THR 101 101 17096 1 . GLU 102 102 17096 1 . GLN 103 103 17096 1 . PRO 104 104 17096 1 . GLU 105 105 17096 1 . LEU 106 106 17096 1 . ALA 107 107 17096 1 . ASN 108 108 17096 1 . LYS 109 109 17096 1 . VAL 110 110 17096 1 . ASP 111 111 17096 1 . MET 112 112 17096 1 . VAL 113 113 17096 1 . TRP 114 114 17096 1 . ILE 115 115 17096 1 . VAL 116 116 17096 1 . GLY 117 117 17096 1 . GLY 118 118 17096 1 . SER 119 119 17096 1 . SER 120 120 17096 1 . VAL 121 121 17096 1 . TYR 122 122 17096 1 . LYS 123 123 17096 1 . GLU 124 124 17096 1 . ALA 125 125 17096 1 . MET 126 126 17096 1 . ASN 127 127 17096 1 . HIS 128 128 17096 1 . PRO 129 129 17096 1 . GLY 130 130 17096 1 . HIS 131 131 17096 1 . LEU 132 132 17096 1 . LYS 133 133 17096 1 . LEU 134 134 17096 1 . PHE 135 135 17096 1 . VAL 136 136 17096 1 . THR 137 137 17096 1 . ARG 138 138 17096 1 . ILE 139 139 17096 1 . MET 140 140 17096 1 . GLN 141 141 17096 1 . ASP 142 142 17096 1 . PHE 143 143 17096 1 . GLU 144 144 17096 1 . SER 145 145 17096 1 . ASP 146 146 17096 1 . THR 147 147 17096 1 . PHE 148 148 17096 1 . PHE 149 149 17096 1 . PRO 150 150 17096 1 . GLU 151 151 17096 1 . ILE 152 152 17096 1 . ASP 153 153 17096 1 . LEU 154 154 17096 1 . GLU 155 155 17096 1 . LYS 156 156 17096 1 . TYR 157 157 17096 1 . LYS 158 158 17096 1 . LEU 159 159 17096 1 . LEU 160 160 17096 1 . PRO 161 161 17096 1 . GLU 162 162 17096 1 . TYR 163 163 17096 1 . PRO 164 164 17096 1 . GLY 165 165 17096 1 . VAL 166 166 17096 1 . LEU 167 167 17096 1 . SER 168 168 17096 1 . ASP 169 169 17096 1 . VAL 170 170 17096 1 . GLN 171 171 17096 1 . GLU 172 172 17096 1 . GLU 173 173 17096 1 . LYS 174 174 17096 1 . GLY 175 175 17096 1 . ILE 176 176 17096 1 . LYS 177 177 17096 1 . TYR 178 178 17096 1 . LYS 179 179 17096 1 . PHE 180 180 17096 1 . GLU 181 181 17096 1 . VAL 182 182 17096 1 . TYR 183 183 17096 1 . GLU 184 184 17096 1 . LYS 185 185 17096 1 . ASN 186 186 17096 1 . ASP 187 187 17096 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 17096 _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 $DHFR . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli W3110 trpA33 . . . . . . . . . . . . . . . . . . . 17096 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 17096 _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 $DHFR . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pMONDHFR . . . . . . 17096 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17096 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '85% H2O/15% 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 'potassium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 17096 1 2 EDTA 'natural abundance' . . . . . . 0.1 . . mM . . . . 17096 1 3 DTT 'natural abundance' . . . . . . 3 . . mM . . . . 17096 1 4 'sodium azide' 'natural abundance' . . . . . . 5 . . mM . . . . 17096 1 5 DHFR '[U-100% 19F-tryptophan]' . . 1 $DHFR . . 0.89 . . mM . . . . 17096 1 6 urea 'natural abundance' . . . . . . . 0 5 M . . . . 17096 1 7 H2O 'natural abundance' . . . . . . 85 . . % . . . . 17096 1 8 D2O 'natural abundance' . . . . . . 15 . . % . . . . 17096 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 17096 _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 7.2 . pH 17096 1 pressure 1 . atm 17096 1 temperature 295 . K 17096 1 stop_ save_ ############################ # Computer software used # ############################ save_KALEIDAGRAPH _Software.Sf_category software _Software.Sf_framecode KALEIDAGRAPH _Software.Entry_ID 17096 _Software.ID 1 _Software.Name KaleidaGraph _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Synergy Software, Reading, PA' . . 17096 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'exponential fits' 17096 1 stop_ save_ save_VNMR _Software.Sf_category software _Software.Sf_framecode VNMR _Software.Entry_ID 17096 _Software.ID 2 _Software.Name VNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 17096 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 17096 2 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 17096 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'Nalorac Proton/Fluorine probe' _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VXR-500 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 470.3 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 17096 _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 Varian VXR-500 . 470.3 'Nalorac Proton/Fluorine probe' . . 17096 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 17096 _Experiment_list.ID 1 _Experiment_list.Details Stopped-flow 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 '19F NMR' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17096 1 stop_ save_ save_Chemical_rate_list _Chemical_rate_list.Sf_category chemical_rates _Chemical_rate_list.Sf_framecode Chemical_rate_list _Chemical_rate_list.Entry_ID 17096 _Chemical_rate_list.ID 1 _Chemical_rate_list.Sample_condition_list_ID 1 _Chemical_rate_list.Sample_condition_list_label $sample_conditions_1 _Chemical_rate_list.Details . _Chemical_rate_list.Text_data_format . _Chemical_rate_list.Text_data . loop_ _Chemical_rate_experiment.Experiment_ID _Chemical_rate_experiment.Experiment_name _Chemical_rate_experiment.Sample_ID _Chemical_rate_experiment.Sample_label _Chemical_rate_experiment.Sample_state _Chemical_rate_experiment.Entry_ID _Chemical_rate_experiment.Chemical_rate_list_ID 1 '19F NMR' 1 $sample_1 isotropic 17096 1 stop_ loop_ _Chemical_rate_software.Software_ID _Chemical_rate_software.Software_label _Chemical_rate_software.Method_ID _Chemical_rate_software.Method_label _Chemical_rate_software.Entry_ID _Chemical_rate_software.Chemical_rate_list_ID 1 $KALEIDAGRAPH . . 17096 1 2 $VNMR . . 17096 1 stop_ loop_ _Chemical_rate.ID _Chemical_rate.Assembly_ID _Chemical_rate.Assembly_atom_ID _Chemical_rate.Entity_assembly_ID _Chemical_rate.Entity_ID _Chemical_rate.Comp_index_ID _Chemical_rate.Seq_ID _Chemical_rate.Comp_ID _Chemical_rate.Atom_ID _Chemical_rate.Atom_type _Chemical_rate.Atom_isotope_number _Chemical_rate.Val_type _Chemical_rate.Val _Chemical_rate.Val_min _Chemical_rate.Val_max _Chemical_rate.Val_err _Chemical_rate.Val_units _Chemical_rate.Resonance_ID _Chemical_rate.Auth_entity_assembly_ID _Chemical_rate.Auth_seq_ID _Chemical_rate.Auth_comp_ID _Chemical_rate.Auth_atom_ID _Chemical_rate.Entry_ID _Chemical_rate.Chemical_rate_list_ID 1 1 . 1 1 . . . . . . . 0.010 . . 0.002 MM-1 . . . . . 17096 1 2 1 . 1 1 . . . . . . . 0.015 . . 0.001 MM-1 . . . . . 17096 1 3 1 . 1 1 . . . . . . . 0.020 . . 0.003 MM-1 . . . . . 17096 1 4 1 . 1 1 . . . . . . . 0.015 . . 0.004 MM-1 . . . . . 17096 1 stop_ save_