data_25019 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential backbone HN, N, Ca and Cb assignments of E.coli dihydrofolate reductase-folate binary complex at pH 7.0 and 308 K ; _BMRB_accession_number 25019 _BMRB_flat_file_name bmr25019.str _Entry_type original _Submission_date 2014-06-13 _Accession_date 2014-06-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; This entry includes the sequential backbone HN, N, Ca and Cb assignments of E.coli dihydrofolate reductase-folate binary complex at pH 7.0 and 308 K. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'Puthenpurackal Narayanan' Sunilkumar . . 2 Maeno Akihiro . . 3 Wada Yuji . . 4 Tate Shin-ichi . . 5 Akasaka Kazuyuki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 140 "13C chemical shifts" 295 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-11-20 update BMRB 'update entry citation' 2014-07-14 original author 'original release' stop_ _Original_release_date 2015-11-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequential backbone resonance assignments of the E. coli dihydrofolate reductase Gly67Val mutant: folate complex ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26482924 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'Puthenpurackal Narayanan' Sunilkumar . . 2 Maeno Akihiro . . 3 Wada Yuji . . 4 Tate Shin-ichi . . 5 Akasaka Kazuyuki . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2015 _Details . loop_ _Keyword 'dhfr folate complex' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DHFR-folate _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DHFR $DHFR folate $entity_FOL stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DHFR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DHFR _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MISLIAALAVDRVIGMENAM PWNLPADLAWFKRNTLNKPV IMGRHTWESIGRPLPGRKNI ILSSQPGTDDRVTWVKSVDE AIAACGDVPEIMVIGGGRVY EQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEF HDADAQNSHSYCFEILERR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 SER 4 LEU 5 ILE 6 ALA 7 ALA 8 LEU 9 ALA 10 VAL 11 ASP 12 ARG 13 VAL 14 ILE 15 GLY 16 MET 17 GLU 18 ASN 19 ALA 20 MET 21 PRO 22 TRP 23 ASN 24 LEU 25 PRO 26 ALA 27 ASP 28 LEU 29 ALA 30 TRP 31 PHE 32 LYS 33 ARG 34 ASN 35 THR 36 LEU 37 ASN 38 LYS 39 PRO 40 VAL 41 ILE 42 MET 43 GLY 44 ARG 45 HIS 46 THR 47 TRP 48 GLU 49 SER 50 ILE 51 GLY 52 ARG 53 PRO 54 LEU 55 PRO 56 GLY 57 ARG 58 LYS 59 ASN 60 ILE 61 ILE 62 LEU 63 SER 64 SER 65 GLN 66 PRO 67 GLY 68 THR 69 ASP 70 ASP 71 ARG 72 VAL 73 THR 74 TRP 75 VAL 76 LYS 77 SER 78 VAL 79 ASP 80 GLU 81 ALA 82 ILE 83 ALA 84 ALA 85 CYS 86 GLY 87 ASP 88 VAL 89 PRO 90 GLU 91 ILE 92 MET 93 VAL 94 ILE 95 GLY 96 GLY 97 GLY 98 ARG 99 VAL 100 TYR 101 GLU 102 GLN 103 PHE 104 LEU 105 PRO 106 LYS 107 ALA 108 GLN 109 LYS 110 LEU 111 TYR 112 LEU 113 THR 114 HIS 115 ILE 116 ASP 117 ALA 118 GLU 119 VAL 120 GLU 121 GLY 122 ASP 123 THR 124 HIS 125 PHE 126 PRO 127 ASP 128 TYR 129 GLU 130 PRO 131 ASP 132 ASP 133 TRP 134 GLU 135 SER 136 VAL 137 PHE 138 SER 139 GLU 140 PHE 141 HIS 142 ASP 143 ALA 144 ASP 145 ALA 146 GLN 147 ASN 148 SER 149 HIS 150 SER 151 TYR 152 CYS 153 PHE 154 GLU 155 ILE 156 LEU 157 GLU 158 ARG 159 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 11492 Dihydrofolate_Reductase_from_E._coli 100.00 158 99.37 99.37 2.64e-111 BMRB 4554 "Dihydrofolate reductase" 100.00 159 100.00 100.00 6.63e-114 PDB 1DDR "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Urea" 100.00 159 100.00 100.00 6.63e-114 PDB 1DDS "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate" 100.00 159 100.00 100.00 6.63e-114 PDB 1DHI "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.00 159 98.74 99.37 2.47e-112 PDB 1DHJ "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.00 159 98.11 98.74 3.29e-111 PDB 1DRA "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 98.74 100.00 1.84e-112 PDB 1DRB "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 98.74 99.37 1.01e-111 PDB 1DRE "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1DRH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 4.07e-113 PDB 1DYH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 4.07e-113 PDB 1DYI "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 4.07e-113 PDB 1DYJ "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 4.07e-113 PDB 1JOL "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.00 159 99.37 100.00 4.07e-113 PDB 1JOM "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.00 159 99.37 100.00 4.07e-113 PDB 1RA1 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RA2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RA3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RA8 "Dihydrofolate Reductase Complexed With Folate And 2- Monophosphoadenosine 5'-diphosphoribose" 100.00 159 99.37 100.00 4.07e-113 PDB 1RA9 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RB2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RB3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RC4 "Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized " 100.00 159 99.37 100.00 4.07e-113 PDB 1RD7 "Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RE7 "Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RF7 "Structure Of Dihydrofolate Reductase Complexed With Dihydrofolate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RG7 "Dihydrofolate Reductase Complexed With Methotrexate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RH3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX1 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (reduced Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX2 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX3 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX4 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And 2'-monophosphoadenosine 5'- Diphosphorib" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX5 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX6 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosph" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX7 "Structure Of Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX8 "Dihydrofolate Reductase Complexed With Folate And 2'- Monophosphoadenosine 5'-Diphosphoribose" 100.00 159 99.37 100.00 4.07e-113 PDB 1RX9 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 4.07e-113 PDB 1TDR "Expression, Characterization, And Crystallographic Analysis Of Telluromethionyl Dihydrofolate Reductase" 100.00 159 98.74 100.00 1.46e-112 PDB 2ANO "Crystal Structure Of E.coli Dihydrofolate Reductase In Complex With Nadph And The Inhibitor Ms-sh08-17" 100.00 159 99.37 100.00 4.07e-113 PDB 2ANQ "Crystal Structure Of E.coli Dhfr In Complex With Nadph And The Inhibitor Compound 10a." 100.00 159 99.37 100.00 4.07e-113 PDB 2DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.00 159 98.74 100.00 4.22e-112 PDB 2INQ "Neutron Crystal Structure Of Escherichia Coli Dihydrofolate Reductase Bound To The Anti-Cancer Drug, Methotrexate" 100.00 159 99.37 100.00 4.07e-113 PDB 3DAU "Crystal Structure Of The Ternary Mtx Nadph Complex Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 100.00 100.00 6.63e-114 PDB 3DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.00 159 99.37 100.00 4.07e-113 PDB 3K74 "Disruption Of Protein Dynamics By An Allosteric Effector Antibody" 100.00 159 100.00 100.00 6.63e-114 PDB 3KFY "Dynamic Switching And Partial Occupancies Of A Small Molecule Inhibitor Complex Of Dhfr" 100.00 159 99.37 100.00 4.07e-113 PDB 3OCH "Chemically Self-Assembled Antibody Nanorings (Csans): Design And Characterization Of An Anti-Cd3 Igm Biomimetic" 100.00 159 99.37 100.00 4.07e-113 PDB 3QL0 "Crystal Structure Of N23pp/s148a Mutant Of E. Coli Dihydrofolate Reductase" 100.63 160 98.13 98.75 3.90e-110 PDB 3QL3 "Re-refined Coordinates For Pdb Entry 1rx2" 100.00 159 99.37 100.00 4.07e-113 PDB 3QYL "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.00 159 99.37 100.00 4.07e-113 PDB 3QYO "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.00 159 99.37 100.00 4.07e-113 PDB 3R33 "Evidence For Dynamic Motion In Proteins As A Mechanism For Ligand Dissociation" 100.00 159 99.37 100.00 4.07e-113 PDB 4DFR "Crystal Structures Of Escherichia Coli And Lactobacillus Casei Dihydrofolate Reductase Refined At 1.7 Angstroms Resolution. I. " 100.00 159 98.74 100.00 1.46e-112 PDB 4EIG "Ca1698 Camel Antibody Fragment In Complex With Dhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4EIZ "Structure Of Nb113 Bound To Apodhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4EJ1 "Binding Of Nb113 Camelid Antibody Fragment With The Binary Dhfr:folate Complex" 100.00 159 100.00 100.00 6.63e-114 PDB 4FHB "Enhancing Dhfr Catalysis By Binding Of An Allosteric Regulator Nanobody (nb179)" 100.00 159 100.00 100.00 6.63e-114 PDB 4I13 "Nanobody Ca1697 Binding To The Dhfr.folate Binary Complex" 100.00 159 100.00 100.00 6.63e-114 PDB 4I1N "R104a-ca1697 Nanobody Binding To The Binary Dhfr.folate Complex" 100.00 159 100.00 100.00 6.63e-114 PDB 4KJJ "Cryogenic Wt Dhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4KJK "Room Temperature Wt Dhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4KJL "Room Temperature N23pps148a Dhfr" 100.63 160 98.13 98.75 3.90e-110 PDB 4NX6 "Single Room Temperature Model Of Dhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4NX7 "Single Cryogenic Temperature Model Of Dhfr" 100.00 159 100.00 100.00 6.63e-114 PDB 4P3Q "Room-temperature Wt Dhfr, Time-averaged Ensemble" 100.00 159 100.00 100.00 6.63e-114 PDB 4P3R "Cryogenic Wt Dhfr, Time-averaged Ensemble" 100.00 159 100.00 100.00 6.63e-114 PDB 4P66 "Electrostatics Of Active Site Microenvironments Of E. Coli Dhfr" 100.00 159 98.11 98.11 1.26e-110 PDB 4P68 "Electrostatics Of Active Site Microenvironments For E. Coli Dhfr" 100.00 159 98.11 98.11 1.05e-110 PDB 4PSS "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.00 159 99.37 99.37 2.24e-112 PDB 4PST "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 277 K" 100.00 159 99.37 99.37 2.24e-112 PDB 4PSY "100k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 99.37 99.37 2.24e-112 PDB 4PTH "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.00 159 99.37 99.37 2.24e-112 PDB 4PTJ "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 277k" 100.00 159 99.37 99.37 2.24e-112 PDB 4QLE "Crystal Structure Of I14a Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 99.37 4.16e-113 PDB 4QLF "Crystal Structure Of I14g Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 99.37 1.32e-112 PDB 4QLG "Crystal Structure Of I14v Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 100.00 1.10e-113 PDB 4RGC "277k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 99.37 99.37 2.24e-112 PDB 5CC9 "L28f E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucleotide" 100.00 159 99.37 99.37 2.57e-113 PDB 5CCC "Wild-type E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucle" 100.00 159 100.00 100.00 6.63e-114 PDB 5DFR "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 99.37 100.00 4.07e-113 PDB 6DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.00 159 99.37 100.00 4.07e-113 PDB 7DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.00 159 99.37 100.00 4.07e-113 DBJ BAA05974 "fusion protein, composed of HCV p21 (NS2), E.coli dihydroforate reductase, substrate polypeptide for HCV serine proteinase and " 99.37 847 100.00 100.00 1.22e-105 DBJ BAB33474 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. Sakai]" 100.00 159 99.37 99.37 2.47e-112 DBJ BAB96616 "dihydrofolate reductase [Escherichia coli str. K12 substr. W3110]" 100.00 159 100.00 100.00 6.63e-114 DBJ BAG75573 "dihydrofolate reductase [Escherichia coli SE11]" 100.00 159 100.00 100.00 6.63e-114 DBJ BAI23410 "dihydrofolate reductase [Escherichia coli O26:H11 str. 11368]" 100.00 159 100.00 100.00 6.63e-114 EMBL CAA28755 "unnamed protein product [Escherichia coli]" 100.00 159 98.74 99.37 5.37e-112 EMBL CAD01243 "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 159 97.48 98.74 7.29e-112 EMBL CAP74618 "Dihydrofolate reductase [Escherichia coli LF82]" 100.00 159 100.00 100.00 6.63e-114 EMBL CAQ30568 "dihydrofolate reductase [Escherichia coli BL21(DE3)]" 100.00 159 100.00 100.00 6.63e-114 EMBL CAQ87642 "dihydrofolate reductase [Escherichia fergusonii ATCC 35469]" 100.00 159 100.00 100.00 6.63e-114 GB AAA87976 "dihydrofolate reductase [Escherichia coli]" 100.00 159 100.00 100.00 6.63e-114 GB AAC73159 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 6.63e-114 GB AAG54351 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. EDL933]" 100.00 159 99.37 99.37 2.47e-112 GB AAN41711 "dihydrofolate reductase type I [Shigella flexneri 2a str. 301]" 100.00 159 100.00 100.00 6.63e-114 GB AAN78554 "Dihydrofolate reductase [Escherichia coli CFT073]" 100.00 204 100.00 100.00 1.02e-113 PIR AC0513 "dihydrofolate reductase type I [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 159 97.48 98.74 7.29e-112 REF NP_308078 "dihydrofolate reductase [Escherichia coli O157:H7 str. Sakai]" 100.00 159 99.37 99.37 2.47e-112 REF NP_414590 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 6.63e-114 REF NP_454699 "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 159 97.48 98.74 7.29e-112 REF NP_706004 "dihydrofolate reductase [Shigella flexneri 2a str. 301]" 100.00 159 100.00 100.00 6.63e-114 REF WP_000378105 "MULTISPECIES: dihydrofolate reductase [Proteobacteria]" 100.00 196 100.00 100.00 1.21e-113 SP P0ABQ4 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.63e-114 SP P0ABQ5 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.63e-114 SP P0ABQ6 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.63e-114 stop_ save_ ############# # Ligands # ############# save_FOL _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_FOL (FOLIC ACID)" _BMRB_code FOL _PDB_code FOL _Molecular_mass 441.397 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? NA2 NA2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4A C4A C . 0 . ? N5 N5 N . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? N8 N8 N . 0 . ? C8A C8A C . 0 . ? C9 C9 C . 0 . ? N10 N10 N . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C C C . 0 . ? O O O . 0 . ? N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE1 OE1 O . 0 . ? OE2 OE2 O . 0 . ? CT CT C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? H7 H7 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? HN0 HN0 H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? H15 H15 H . 0 . ? H16 H16 H . 0 . ? HN HN H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HG1 HG1 H . 0 . ? HG2 HG2 H . 0 . ? HOE2 HOE2 H . 0 . ? HO2 HO2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? SING N1 C8A ? ? SING N1 HN1 ? ? SING C2 NA2 ? ? DOUB C2 N3 ? ? SING NA2 HN21 ? ? SING NA2 HN22 ? ? SING N3 C4 ? ? DOUB C4 O4 ? ? SING C4 C4A ? ? SING C4A N5 ? ? DOUB C4A C8A ? ? DOUB N5 C6 ? ? SING C6 C7 ? ? SING C6 C9 ? ? DOUB C7 N8 ? ? SING C7 H7 ? ? SING N8 C8A ? ? SING C9 N10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING N10 C14 ? ? SING N10 HN0 ? ? DOUB C11 C12 ? ? SING C11 C16 ? ? SING C11 C ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 H13 ? ? SING C14 C15 ? ? DOUB C15 C16 ? ? SING C15 H15 ? ? SING C16 H16 ? ? DOUB C O ? ? SING C N ? ? SING N CA ? ? SING N HN ? ? SING CA CB ? ? SING CA CT ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CG CD ? ? SING CG HG1 ? ? SING CG HG2 ? ? DOUB CD OE1 ? ? SING CD OE2 ? ? SING OE2 HOE2 ? ? DOUB CT O1 ? ? SING CT O2 ? ? SING O2 HO2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DHFR 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DHFR 'recombinant technology' . Escherichia coli . pTP64-1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DHFR 1.2 mM '[U-100% 13C; U-100% 15N]' $entity_FOL 1.2 mM 'natural abundance' 'TRIS buffer' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR _Saveframe_category software _Name CCPNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01715 . mM pH 7 . pH pressure 1 . atm temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DHFR _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET CA C 55.378 0.000 1 2 1 1 MET CB C 32.860 0.000 1 3 2 2 ILE H H 9.377 0.002 1 4 2 2 ILE CA C 61.552 0.000 1 5 2 2 ILE CB C 39.227 0.000 1 6 2 2 ILE N N 124.931 0.018 1 7 3 3 SER H H 9.391 0.001 1 8 3 3 SER CA C 56.464 0.000 1 9 3 3 SER CB C 65.937 0.000 1 10 3 3 SER N N 125.938 0.019 1 11 4 4 LEU H H 8.528 0.006 1 12 4 4 LEU CA C 53.875 0.000 1 13 4 4 LEU CB C 43.737 0.000 1 14 4 4 LEU N N 122.200 0.010 1 15 5 5 ILE H H 8.607 0.003 1 16 5 5 ILE CA C 58.362 0.000 1 17 5 5 ILE CB C 43.346 0.000 1 18 5 5 ILE N N 120.271 0.012 1 19 6 6 ALA H H 8.502 0.004 1 20 6 6 ALA CA C 53.013 0.000 1 21 6 6 ALA CB C 25.030 0.000 1 22 6 6 ALA N N 126.562 0.014 1 23 7 7 ALA H H 7.615 0.001 1 24 7 7 ALA CA C 50.486 0.000 1 25 7 7 ALA CB C 19.419 0.000 1 26 7 7 ALA N N 122.266 0.019 1 27 8 8 LEU H H 8.951 0.002 1 28 8 8 LEU CA C 53.767 0.000 1 29 8 8 LEU CB C 45.612 0.000 1 30 8 8 LEU N N 122.912 0.033 1 31 9 9 ALA H H 8.626 0.003 1 32 9 9 ALA CA C 50.018 0.000 1 33 9 9 ALA CB C 19.514 0.000 1 34 9 9 ALA N N 124.834 0.015 1 35 10 10 VAL H H 7.770 0.003 1 36 10 10 VAL CA C 65.366 0.000 1 37 10 10 VAL CB C 31.679 0.000 1 38 10 10 VAL N N 118.798 0.013 1 39 11 11 ASP H H 8.924 0.004 1 40 11 11 ASP CA C 55.962 0.000 1 41 11 11 ASP CB C 39.521 0.000 1 42 11 11 ASP N N 121.950 0.045 1 43 12 12 ARG H H 8.427 0.004 1 44 12 12 ARG CA C 57.826 0.000 1 45 12 12 ARG CB C 27.124 0.000 1 46 12 12 ARG N N 108.226 0.010 1 47 13 13 VAL H H 6.841 0.002 1 48 13 13 VAL CA C 64.879 0.000 1 49 13 13 VAL CB C 32.892 0.000 1 50 13 13 VAL N N 120.781 0.005 1 51 14 14 ILE H H 7.910 0.003 1 52 14 14 ILE CA C 60.078 0.000 1 53 14 14 ILE CB C 40.015 0.000 1 54 14 14 ILE N N 121.535 0.019 1 55 15 15 GLY H H 8.589 0.002 1 56 15 15 GLY CA C 45.891 0.000 1 57 15 15 GLY N N 110.401 0.007 1 58 16 16 MET H H 8.326 0.002 1 59 16 16 MET CA C 55.578 0.000 1 60 16 16 MET CB C 32.696 0.000 1 61 16 16 MET N N 119.609 0.024 1 62 17 17 GLU H H 8.656 0.002 1 63 17 17 GLU CA C 58.710 0.000 1 64 17 17 GLU CB C 29.022 0.000 1 65 17 17 GLU N N 121.315 0.010 1 66 18 18 ASN H H 8.251 0.003 1 67 18 18 ASN CA C 53.687 0.000 1 68 18 18 ASN CB C 38.738 0.000 1 69 18 18 ASN N N 115.717 0.033 1 70 19 19 ALA H H 7.845 0.001 1 71 19 19 ALA CA C 51.865 0.000 1 72 19 19 ALA CB C 19.018 0.036 1 73 19 19 ALA N N 122.378 0.027 1 74 20 20 MET H H 7.997 0.002 1 75 20 20 MET CA C 52.622 0.000 1 76 20 20 MET CB C 31.299 0.000 1 77 20 20 MET N N 120.174 0.010 1 78 21 21 PRO CA C 63.360 0.000 1 79 21 21 PRO CB C 31.155 0.000 1 80 22 22 TRP H H 6.394 0.003 1 81 22 22 TRP CA C 55.154 0.000 1 82 22 22 TRP CB C 30.133 0.000 1 83 22 22 TRP N N 114.488 0.010 1 84 23 23 ASN H H 9.356 0.004 1 85 23 23 ASN CA C 54.244 0.000 1 86 23 23 ASN CB C 40.364 0.000 1 87 23 23 ASN N N 119.121 0.009 1 88 24 24 LEU H H 9.047 0.003 1 89 24 24 LEU CA C 50.889 0.000 1 90 24 24 LEU CB C 44.915 0.000 1 91 24 24 LEU N N 123.088 0.034 1 92 25 25 PRO CA C 65.570 0.000 1 93 25 25 PRO CB C 31.104 0.000 1 94 26 26 ALA H H 9.001 0.004 1 95 26 26 ALA CA C 55.558 0.000 1 96 26 26 ALA CB C 18.730 0.000 1 97 26 26 ALA N N 119.768 0.042 1 98 27 27 ASP H H 7.436 0.001 1 99 27 27 ASP CA C 57.184 0.000 1 100 27 27 ASP CB C 43.886 0.000 1 101 27 27 ASP N N 118.874 0.005 1 102 28 28 LEU H H 7.615 0.001 1 103 28 28 LEU CA C 57.863 0.000 1 104 28 28 LEU CB C 40.651 0.000 1 105 28 28 LEU N N 121.688 0.014 1 106 29 29 ALA H H 7.993 0.002 1 107 29 29 ALA CA C 55.095 0.000 1 108 29 29 ALA CB C 17.298 0.000 1 109 29 29 ALA N N 120.738 0.011 1 110 30 30 TRP H H 7.543 0.002 1 111 30 30 TRP CA C 60.359 0.000 1 112 30 30 TRP CB C 29.293 0.000 1 113 30 30 TRP N N 124.073 0.006 1 114 31 31 PHE H H 9.078 0.001 1 115 31 31 PHE CA C 61.799 0.000 1 116 31 31 PHE CB C 38.292 0.000 1 117 31 31 PHE N N 123.496 0.014 1 118 32 32 LYS H H 8.703 0.001 1 119 32 32 LYS CA C 60.516 0.000 1 120 32 32 LYS CB C 32.571 0.000 1 121 32 32 LYS N N 123.539 0.011 1 122 33 33 ARG H H 8.257 0.005 1 123 33 33 ARG CA C 59.142 0.000 1 124 33 33 ARG CB C 29.359 0.000 1 125 33 33 ARG N N 117.515 0.004 1 126 34 34 ASN H H 7.136 0.001 1 127 34 34 ASN CA C 54.539 0.000 1 128 34 34 ASN CB C 38.753 0.000 1 129 34 34 ASN N N 111.484 0.017 1 130 35 35 THR H H 7.094 0.004 1 131 35 35 THR CA C 62.339 0.000 1 132 35 35 THR CB C 71.427 0.000 1 133 35 35 THR N N 107.409 0.014 1 134 36 36 LEU H H 7.531 0.002 1 135 36 36 LEU CA C 57.267 0.000 1 136 36 36 LEU CB C 42.357 0.000 1 137 36 36 LEU N N 122.197 0.013 1 138 37 37 ASN H H 7.814 0.002 1 139 37 37 ASN CA C 54.674 0.000 1 140 37 37 ASN CB C 37.189 0.000 1 141 37 37 ASN N N 113.700 0.022 1 142 38 38 LYS H H 7.783 0.007 1 143 38 38 LYS CA C 54.141 0.000 1 144 38 38 LYS CB C 34.014 0.000 1 145 38 38 LYS N N 119.678 0.010 1 146 39 39 PRO CA C 62.252 0.000 1 147 39 39 PRO CB C 32.464 0.000 1 148 40 40 VAL H H 8.672 0.006 1 149 40 40 VAL CA C 57.078 0.000 1 150 40 40 VAL CB C 34.499 0.000 1 151 40 40 VAL N N 114.367 0.050 1 152 41 41 ILE H H 8.518 0.000 1 153 41 41 ILE CA C 59.508 0.022 1 154 41 41 ILE CB C 39.929 0.000 1 155 41 41 ILE N N 122.172 0.001 1 156 42 42 MET H H 8.969 0.005 1 157 42 42 MET CA C 52.226 0.000 1 158 42 42 MET CB C 40.232 0.000 1 159 42 42 MET N N 124.908 0.098 1 160 43 43 GLY H H 8.991 0.002 1 161 43 43 GLY CA C 44.127 0.000 1 162 43 43 GLY N N 106.041 0.008 1 163 44 44 ARG H H 8.268 0.001 1 164 44 44 ARG CA C 60.157 0.000 1 165 44 44 ARG CB C 30.748 0.000 1 166 44 44 ARG N N 119.762 0.026 1 167 46 46 THR CA C 67.875 0.000 1 168 47 47 TRP H H 7.886 0.003 1 169 47 47 TRP CA C 60.006 0.000 1 170 47 47 TRP CB C 29.483 0.000 1 171 47 47 TRP N N 123.357 0.048 1 172 48 48 GLU H H 8.366 0.001 1 173 48 48 GLU CA C 58.729 0.000 1 174 48 48 GLU CB C 28.916 0.000 1 175 48 48 GLU N N 117.768 0.007 1 176 49 49 SER H H 7.599 0.001 1 177 49 49 SER CA C 60.908 0.000 1 178 49 49 SER CB C 63.765 0.000 1 179 49 49 SER N N 114.229 0.009 1 180 50 50 ILE H H 7.836 0.002 1 181 50 50 ILE CA C 65.220 0.000 1 182 50 50 ILE CB C 38.994 0.000 1 183 50 50 ILE N N 122.040 0.067 1 184 51 51 GLY H H 7.540 0.002 1 185 51 51 GLY CA C 46.059 0.000 1 186 51 51 GLY N N 105.239 0.012 1 187 52 52 ARG H H 6.874 0.002 1 188 52 52 ARG CA C 53.264 0.000 1 189 52 52 ARG CB C 28.526 0.000 1 190 52 52 ARG N N 116.389 0.014 1 191 53 53 PRO CA C 61.894 0.000 1 192 53 53 PRO CB C 31.407 0.000 1 193 54 54 LEU H H 9.284 0.002 1 194 54 54 LEU CA C 52.524 0.000 1 195 54 54 LEU CB C 40.580 0.000 1 196 54 54 LEU N N 126.241 0.007 1 197 56 56 GLY CA C 46.662 0.000 1 198 57 57 ARG H H 7.180 0.003 1 199 57 57 ARG CA C 54.648 0.000 1 200 57 57 ARG CB C 36.054 0.000 1 201 57 57 ARG N N 118.248 0.064 1 202 58 58 LYS H H 7.325 0.002 1 203 58 58 LYS CA C 56.198 0.000 1 204 58 58 LYS CB C 32.406 0.000 1 205 58 58 LYS N N 123.478 0.017 1 206 59 59 ASN H H 8.968 0.002 1 207 59 59 ASN CA C 53.824 0.000 1 208 59 59 ASN CB C 41.110 0.000 1 209 59 59 ASN N N 126.056 0.014 1 210 60 60 ILE H H 8.820 0.001 1 211 60 60 ILE CA C 59.894 0.000 1 212 60 60 ILE CB C 39.578 0.000 1 213 60 60 ILE N N 126.782 0.009 1 214 61 61 ILE H H 8.761 0.002 1 215 61 61 ILE CA C 57.995 0.000 1 216 61 61 ILE CB C 36.303 0.000 1 217 61 61 ILE N N 127.158 0.017 1 218 62 62 LEU H H 8.797 0.003 1 219 62 62 LEU CA C 53.452 0.000 1 220 62 62 LEU CB C 43.292 0.000 1 221 62 62 LEU N N 128.921 0.031 1 222 63 63 SER H H 8.806 0.073 1 223 63 63 SER CA C 57.031 0.000 1 224 63 63 SER CB C 65.711 0.000 1 225 63 63 SER N N 119.642 0.000 1 226 68 68 THR H H 7.223 0.004 1 227 68 68 THR CA C 60.961 0.000 1 228 68 68 THR CB C 69.417 0.000 1 229 68 68 THR N N 107.158 0.024 1 230 69 69 ASP H H 7.451 0.007 1 231 69 69 ASP CA C 55.502 0.000 1 232 69 69 ASP CB C 42.863 0.000 1 233 69 69 ASP N N 122.159 0.010 1 234 70 70 ASP H H 8.618 0.002 1 235 70 70 ASP CA C 54.597 0.000 1 236 70 70 ASP CB C 40.229 0.000 1 237 70 70 ASP N N 126.096 0.045 1 238 71 71 ARG H H 8.807 0.003 1 239 71 71 ARG CA C 57.289 0.000 1 240 71 71 ARG CB C 31.350 0.000 1 241 71 71 ARG N N 118.603 0.011 1 242 72 72 VAL H H 7.077 0.004 1 243 72 72 VAL CA C 58.152 0.000 1 244 72 72 VAL CB C 33.397 0.000 1 245 72 72 VAL N N 108.209 0.007 1 246 73 73 THR H H 7.717 0.005 1 247 73 73 THR CA C 62.606 0.000 1 248 73 73 THR CB C 70.894 0.000 1 249 73 73 THR N N 116.968 0.018 1 250 74 74 TRP H H 8.771 0.002 1 251 74 74 TRP CA C 56.228 0.000 1 252 74 74 TRP CB C 28.920 0.000 1 253 74 74 TRP N N 129.232 0.042 1 254 75 75 VAL H H 9.126 0.002 1 255 75 75 VAL CA C 58.934 0.000 1 256 75 75 VAL CB C 35.802 0.000 1 257 75 75 VAL N N 116.170 0.019 1 258 76 76 LYS H H 8.570 0.003 1 259 76 76 LYS CA C 56.240 0.000 1 260 76 76 LYS CB C 33.809 0.000 1 261 76 76 LYS N N 116.355 0.019 1 262 77 77 SER H H 7.308 0.001 1 263 77 77 SER CA C 56.222 0.000 1 264 77 77 SER CB C 67.848 0.000 1 265 77 77 SER N N 112.226 0.033 1 266 78 78 VAL H H 8.752 0.003 1 267 78 78 VAL CA C 66.709 0.000 1 268 78 78 VAL CB C 31.926 0.000 1 269 78 78 VAL N N 122.924 0.027 1 270 79 79 ASP H H 8.281 0.001 1 271 79 79 ASP CA C 57.770 0.000 1 272 79 79 ASP CB C 40.000 0.000 1 273 79 79 ASP N N 117.738 0.026 1 274 80 80 GLU H H 7.844 0.001 1 275 80 80 GLU CA C 59.152 0.000 1 276 80 80 GLU CB C 31.023 0.000 1 277 80 80 GLU N N 120.722 0.025 1 278 81 81 ALA H H 8.282 0.001 1 279 81 81 ALA CA C 55.691 0.000 1 280 81 81 ALA CB C 18.015 0.000 1 281 81 81 ALA N N 122.448 0.009 1 282 82 82 ILE H H 8.096 0.001 1 283 82 82 ILE CA C 65.713 0.000 1 284 82 82 ILE CB C 38.380 0.000 1 285 82 82 ILE N N 116.399 0.006 1 286 83 83 ALA H H 8.052 0.001 1 287 83 83 ALA CA C 55.236 0.000 1 288 83 83 ALA CB C 17.497 0.000 1 289 83 83 ALA N N 123.974 0.025 1 290 84 84 ALA H H 7.943 0.001 1 291 84 84 ALA CA C 53.806 0.000 1 292 84 84 ALA CB C 17.934 0.000 1 293 84 84 ALA N N 119.184 0.018 1 294 85 85 CYS H H 7.398 0.001 1 295 85 85 CYS CA C 62.120 0.000 1 296 85 85 CYS CB C 27.809 0.000 1 297 85 85 CYS N N 114.550 0.021 1 298 86 86 GLY H H 7.154 0.001 1 299 86 86 GLY CA C 45.301 0.000 1 300 86 86 GLY N N 103.385 0.022 1 301 87 87 ASP H H 8.419 0.003 1 302 87 87 ASP CA C 53.616 0.000 1 303 87 87 ASP CB C 39.719 0.000 1 304 87 87 ASP N N 122.226 0.046 1 305 88 88 VAL H H 7.205 0.002 1 306 88 88 VAL CA C 58.318 0.000 1 307 88 88 VAL CB C 31.947 0.000 1 308 88 88 VAL N N 114.893 0.019 1 309 89 89 PRO CA C 64.945 0.000 1 310 89 89 PRO CB C 32.447 0.000 1 311 90 90 GLU H H 7.713 0.001 1 312 90 90 GLU CA C 55.870 0.000 1 313 90 90 GLU CB C 32.909 0.000 1 314 90 90 GLU N N 116.963 0.018 1 315 91 91 ILE H H 8.672 0.003 1 316 91 91 ILE CA C 61.099 0.000 1 317 91 91 ILE CB C 41.779 0.000 1 318 91 91 ILE N N 129.882 0.010 1 319 92 92 MET H H 7.991 0.003 1 320 92 92 MET CA C 51.972 0.000 1 321 92 92 MET CB C 30.698 0.000 1 322 92 92 MET N N 121.884 0.008 1 323 93 93 VAL H H 9.183 0.003 1 324 93 93 VAL CA C 62.104 0.000 1 325 93 93 VAL CB C 32.074 0.000 1 326 93 93 VAL N N 124.506 0.029 1 327 94 94 ILE H H 8.817 0.002 1 328 94 94 ILE CA C 60.842 0.000 1 329 94 94 ILE CB C 39.718 0.000 1 330 94 94 ILE N N 118.277 0.021 1 331 95 95 GLY H H 6.116 0.004 1 332 95 95 GLY CA C 41.937 0.000 1 333 95 95 GLY N N 104.719 0.018 1 334 96 96 GLY H H 7.647 0.002 1 335 96 96 GLY CA C 46.418 0.000 1 336 96 96 GLY N N 108.483 0.006 1 337 98 98 ARG CA C 58.548 0.000 1 338 98 98 ARG CB C 29.735 0.000 1 339 99 99 VAL H H 7.341 0.002 1 340 99 99 VAL CA C 66.619 0.000 1 341 99 99 VAL CB C 31.591 0.000 1 342 99 99 VAL N N 120.836 0.026 1 343 100 100 TYR H H 8.705 0.002 1 344 100 100 TYR CA C 60.487 0.000 1 345 100 100 TYR CB C 37.334 0.000 1 346 100 100 TYR N N 118.288 0.015 1 347 101 101 GLU H H 8.134 0.002 1 348 101 101 GLU CA C 59.977 0.000 1 349 101 101 GLU CB C 29.900 0.000 1 350 101 101 GLU N N 116.817 0.000 1 351 102 102 GLN H H 7.756 0.002 1 352 102 102 GLN CA C 58.500 0.000 1 353 102 102 GLN CB C 30.051 0.000 1 354 102 102 GLN N N 115.361 0.018 1 355 103 103 PHE H H 7.805 0.002 1 356 103 103 PHE CA C 60.282 0.000 1 357 103 103 PHE CB C 42.044 0.000 1 358 103 103 PHE N N 112.590 0.006 1 359 104 104 LEU H H 8.257 0.001 1 360 104 104 LEU CA C 60.638 0.000 1 361 104 104 LEU CB C 38.865 0.000 1 362 104 104 LEU N N 123.563 0.011 1 363 105 105 PRO CA C 65.741 0.000 1 364 105 105 PRO CB C 31.456 0.000 1 365 106 106 LYS H H 7.473 0.001 1 366 106 106 LYS CA C 55.124 0.000 1 367 106 106 LYS CB C 34.541 0.000 1 368 106 106 LYS N N 112.587 0.010 1 369 107 107 ALA H H 7.991 0.006 1 370 107 107 ALA CA C 52.520 0.000 1 371 107 107 ALA CB C 20.931 0.000 1 372 107 107 ALA N N 122.778 0.029 1 373 108 108 GLN H H 9.222 0.002 1 374 108 108 GLN CA C 55.782 0.000 1 375 108 108 GLN CB C 32.191 0.000 1 376 108 108 GLN N N 118.082 0.017 1 377 109 109 LYS H H 7.758 0.006 1 378 109 109 LYS CA C 56.320 0.000 1 379 109 109 LYS CB C 36.977 0.000 1 380 109 109 LYS N N 120.419 0.012 1 381 110 110 LEU H H 8.987 0.003 1 382 110 110 LEU CA C 53.106 0.000 1 383 110 110 LEU CB C 44.875 0.000 1 384 110 110 LEU N N 122.210 0.021 1 385 111 111 TYR H H 9.421 0.002 1 386 111 111 TYR CA C 56.063 0.000 1 387 111 111 TYR CB C 38.728 0.000 1 388 111 111 TYR N N 122.083 0.018 1 389 112 112 LEU H H 9.612 0.002 1 390 112 112 LEU CA C 52.943 0.000 1 391 112 112 LEU CB C 44.802 0.000 1 392 112 112 LEU N N 123.500 0.011 1 393 113 113 THR H H 8.038 0.002 1 394 113 113 THR CA C 60.264 0.000 1 395 113 113 THR CB C 69.756 0.000 1 396 113 113 THR N N 117.917 0.038 1 397 114 114 HIS H H 9.155 0.006 1 398 114 114 HIS CA C 54.622 0.000 1 399 114 114 HIS CB C 29.909 0.000 1 400 114 114 HIS N N 126.403 0.019 1 401 115 115 ILE H H 9.151 0.002 1 402 115 115 ILE CA C 61.264 0.000 1 403 115 115 ILE CB C 39.501 0.000 1 404 115 115 ILE N N 128.145 0.009 1 405 116 116 ASP H H 8.163 0.002 1 406 116 116 ASP CA C 53.855 0.000 1 407 116 116 ASP CB C 38.991 0.000 1 408 116 116 ASP N N 129.582 0.016 1 409 117 117 ALA H H 8.077 0.001 1 410 117 117 ALA CA C 51.168 0.000 1 411 117 117 ALA CB C 21.689 0.000 1 412 117 117 ALA N N 125.045 0.022 1 413 118 118 GLU H H 8.461 0.001 1 414 118 118 GLU CA C 55.705 0.000 1 415 118 118 GLU CB C 29.976 0.000 1 416 118 118 GLU N N 122.626 0.019 1 417 119 119 VAL H H 8.479 0.002 1 418 119 119 VAL CA C 59.886 0.000 1 419 119 119 VAL CB C 35.228 0.000 1 420 119 119 VAL N N 122.206 0.030 1 421 120 120 GLU H H 8.405 0.001 1 422 120 120 GLU CA C 55.987 0.000 1 423 120 120 GLU CB C 29.828 0.000 1 424 120 120 GLU N N 124.946 0.023 1 425 121 121 GLY H H 7.990 0.003 1 426 121 121 GLY CA C 45.469 0.000 1 427 121 121 GLY N N 110.281 0.032 1 428 122 122 ASP H H 8.163 0.000 1 429 122 122 ASP CA C 53.918 0.000 1 430 122 122 ASP CB C 42.086 0.000 1 431 122 122 ASP N N 117.501 0.004 1 432 123 123 THR H H 8.024 0.004 1 433 123 123 THR CA C 61.903 0.000 1 434 123 123 THR CB C 70.246 0.000 1 435 123 123 THR N N 115.582 0.006 1 436 124 124 HIS H H 8.782 0.003 1 437 124 124 HIS CA C 54.128 0.000 1 438 124 124 HIS CB C 31.430 0.000 1 439 124 124 HIS N N 121.903 0.011 1 440 125 125 PHE H H 8.972 0.001 1 441 125 125 PHE CA C 57.638 0.000 1 442 125 125 PHE CB C 40.174 0.000 1 443 125 125 PHE N N 124.943 0.075 1 444 126 126 PRO CA C 62.731 0.006 1 445 126 126 PRO CB C 31.846 0.000 1 446 127 127 ASP H H 7.906 0.004 1 447 127 127 ASP CA C 55.017 0.000 1 448 127 127 ASP CB C 41.198 0.000 1 449 127 127 ASP N N 117.842 0.176 1 450 128 128 TYR H H 7.186 0.000 1 451 128 128 TYR CA C 55.109 0.000 1 452 128 128 TYR CB C 38.763 0.000 1 453 128 128 TYR N N 118.362 0.007 1 454 129 129 GLU H H 8.872 0.004 1 455 129 129 GLU CA C 53.618 0.000 1 456 129 129 GLU CB C 29.476 0.000 1 457 129 129 GLU N N 123.982 0.019 1 458 130 130 PRO CA C 65.762 0.000 1 459 130 130 PRO CB C 32.138 0.000 1 460 131 131 ASP H H 8.710 0.004 1 461 131 131 ASP CA C 56.266 0.000 1 462 131 131 ASP CB C 40.491 0.000 1 463 131 131 ASP N N 114.439 0.032 1 464 132 132 ASP H H 8.011 0.006 1 465 132 132 ASP CA C 54.901 0.000 1 466 132 132 ASP CB C 42.267 0.000 1 467 132 132 ASP N N 117.551 0.016 1 468 133 133 TRP H H 7.618 0.005 1 469 133 133 TRP CA C 56.543 0.000 1 470 133 133 TRP CB C 33.226 0.000 1 471 133 133 TRP N N 119.523 0.030 1 472 134 134 GLU H H 9.398 0.002 1 473 134 134 GLU CA C 54.351 0.000 1 474 134 134 GLU CB C 32.288 0.000 1 475 134 134 GLU N N 123.028 0.020 1 476 135 135 SER H H 8.954 0.001 1 477 135 135 SER CA C 58.614 0.000 1 478 135 135 SER CB C 62.356 0.000 1 479 135 135 SER N N 121.501 0.017 1 480 136 136 VAL H H 8.921 0.003 1 481 136 136 VAL CA C 61.208 0.000 1 482 136 136 VAL CB C 32.459 0.000 1 483 136 136 VAL N N 121.880 0.004 1 484 137 137 PHE H H 7.834 0.003 1 485 137 137 PHE CA C 58.469 0.000 1 486 137 137 PHE CB C 43.005 0.000 1 487 137 137 PHE N N 123.510 0.008 1 488 138 138 SER H H 7.484 0.001 1 489 138 138 SER CA C 57.075 0.000 1 490 138 138 SER CB C 64.999 0.000 1 491 138 138 SER N N 119.895 0.016 1 492 139 139 GLU H H 8.612 0.001 1 493 139 139 GLU CA C 56.256 0.000 1 494 139 139 GLU CB C 35.020 0.000 1 495 139 139 GLU N N 125.643 0.023 1 496 140 140 PHE H H 8.543 0.004 1 497 140 140 PHE CA C 58.528 0.000 1 498 140 140 PHE CB C 40.742 0.000 1 499 140 140 PHE N N 129.120 0.112 1 500 141 141 HIS H H 7.943 0.001 1 501 141 141 HIS CA C 54.188 0.000 1 502 141 141 HIS CB C 31.268 0.000 1 503 141 141 HIS N N 123.202 0.023 1 504 142 142 ASP H H 7.905 0.006 1 505 142 142 ASP CA C 53.227 0.000 1 506 142 142 ASP CB C 42.666 0.000 1 507 142 142 ASP N N 120.459 0.028 1 508 143 143 ALA H H 8.018 0.000 1 509 143 143 ALA CA C 52.956 0.000 1 510 143 143 ALA CB C 18.713 0.000 1 511 143 143 ALA N N 122.831 0.001 1 512 144 144 ASP H H 8.998 0.001 1 513 144 144 ASP CA C 53.256 0.000 1 514 144 144 ASP CB C 41.368 0.000 1 515 144 144 ASP N N 121.067 0.007 1 516 145 145 ALA H H 8.033 0.000 1 517 145 145 ALA CA C 54.763 0.000 1 518 145 145 ALA CB C 18.505 0.000 1 519 145 145 ALA N N 117.634 0.000 1 520 146 146 GLN H H 8.048 0.001 1 521 146 146 GLN CA C 56.694 0.000 1 522 146 146 GLN CB C 31.225 0.000 1 523 146 146 GLN N N 113.403 0.008 1 524 147 147 ASN H H 8.232 0.002 1 525 147 147 ASN CA C 53.004 0.000 1 526 147 147 ASN CB C 41.345 0.000 1 527 147 147 ASN N N 119.410 0.008 1 528 148 148 SER H H 8.723 0.001 1 529 148 148 SER CA C 61.955 0.000 1 530 148 148 SER CB C 64.234 0.000 1 531 148 148 SER N N 117.560 0.020 1 532 149 149 HIS H H 7.138 0.001 1 533 149 149 HIS CA C 55.793 0.000 1 534 149 149 HIS CB C 35.522 0.000 1 535 149 149 HIS N N 119.379 0.015 1 536 150 150 SER H H 8.488 0.004 1 537 150 150 SER CA C 58.564 0.000 1 538 150 150 SER CB C 64.510 0.000 1 539 150 150 SER N N 112.877 0.008 1 540 151 151 TYR H H 7.608 0.003 1 541 151 151 TYR CA C 54.880 0.000 1 542 151 151 TYR CB C 39.071 0.000 1 543 151 151 TYR N N 115.011 0.020 1 544 152 152 CYS H H 8.225 0.002 1 545 152 152 CYS CA C 54.979 0.000 1 546 152 152 CYS CB C 30.078 0.000 1 547 152 152 CYS N N 118.619 0.012 1 548 153 153 PHE H H 8.355 0.001 1 549 153 153 PHE CA C 55.294 0.000 1 550 153 153 PHE CB C 40.470 0.000 1 551 153 153 PHE N N 128.196 0.023 1 552 154 154 GLU H H 9.668 0.002 1 553 154 154 GLU CA C 54.848 0.000 1 554 154 154 GLU CB C 34.545 0.000 1 555 154 154 GLU N N 124.000 0.014 1 556 155 155 ILE H H 8.650 0.002 1 557 155 155 ILE CA C 60.088 0.000 1 558 155 155 ILE CB C 40.646 0.000 1 559 155 155 ILE N N 124.132 0.019 1 560 156 156 LEU H H 9.154 0.003 1 561 156 156 LEU CA C 53.692 0.000 1 562 156 156 LEU CB C 45.944 0.000 1 563 156 156 LEU N N 126.086 0.042 1 564 157 157 GLU H H 9.253 0.001 1 565 157 157 GLU CA C 54.761 0.000 1 566 157 157 GLU CB C 33.786 0.000 1 567 157 157 GLU N N 119.976 0.006 1 568 158 158 ARG H H 8.065 0.001 1 569 158 158 ARG CA C 57.013 0.000 1 570 158 158 ARG CB C 30.684 0.000 1 571 158 158 ARG N N 127.113 0.019 1 572 159 159 ARG H H 7.961 0.002 1 573 159 159 ARG CA C 58.310 0.000 1 574 159 159 ARG CB C 30.943 0.000 1 575 159 159 ARG N N 131.645 0.014 1 stop_ save_