data_11492 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Dihydrofolate Reductase from E.coli G67 deletion mutant ; _BMRB_accession_number 11492 _BMRB_flat_file_name bmr11492.str _Entry_type original _Submission_date 2012-03-30 _Accession_date 2012-04-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nakashima Atsushi . . 2 Wada Yuji . . 3 Tate Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 289 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-06 original author . stop_ _Original_release_date 2012-08-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone Assignment of Dihydrofolate Reductase from E.coli G67 deletion mutant' _Citation_status 'in preparation' _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nakashima Atsushi . . 2 Wada Yuji . . 3 Tate Shin-ichi . . stop_ _Journal_abbreviation 'Not known' _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 . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monomer $Dihydrofolate_Reductase_from_E._coli NAP $entity_NAP FOL $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_Dihydrofolate_Reductase_from_E._coli _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dihydrofolate_Reductase_from_E._coli _Molecular_mass 17943.3 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 158 _Mol_residue_sequence ; MISLIAALAVDRVIGMENAM PWNLPADLAWFKRNTLNKPV IMGRHTWESIGRPLPGRKNI ILSSQPTDDRVTWVKSVDEA IAACGDVPEIMVIGGGRVYE QFLPKAQKLYLTHIDAEVEG DTHFPDYEPDDWESVFSEFH DADAQNSHSYCFEILERR ; 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 THR 68 ASP 69 ASP 70 ARG 71 VAL 72 THR 73 TRP 74 VAL 75 LYS 76 SER 77 VAL 78 ASP 79 GLU 80 ALA 81 ILE 82 ALA 83 ALA 84 CYS 85 GLY 86 ASP 87 VAL 88 PRO 89 GLU 90 ILE 91 MET 92 VAL 93 ILE 94 GLY 95 GLY 96 GLY 97 ARG 98 VAL 99 TYR 100 GLU 101 GLN 102 PHE 103 LEU 104 PRO 105 LYS 106 ALA 107 GLN 108 LYS 109 LEU 110 TYR 111 LEU 112 THR 113 HIS 114 ILE 115 ASP 116 ALA 117 GLU 118 VAL 119 GLU 120 GLY 121 ASP 122 THR 123 HIS 124 PHE 125 PRO 126 ASP 127 TYR 128 GLU 129 PRO 130 ASP 131 ASP 132 TRP 133 GLU 134 SER 135 VAL 136 PHE 137 SER 138 GLU 139 PHE 140 HIS 141 ASP 142 ALA 143 ASP 144 ALA 145 GLN 146 ASN 147 SER 148 HIS 149 SER 150 TYR 151 CYS 152 PHE 153 GLU 154 ILE 155 LEU 156 GLU 157 ARG 158 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-21 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 25019 DHFR 100.63 159 99.37 99.37 2.52e-111 BMRB 4554 "Dihydrofolate reductase" 100.63 159 99.37 99.37 2.52e-111 PDB 1DDR "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Urea" 100.63 159 99.37 99.37 2.52e-111 PDB 1DDS "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate" 100.63 159 99.37 99.37 2.52e-111 PDB 1DHI "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.63 159 98.11 98.74 1.00e-109 PDB 1DHJ "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.63 159 97.48 98.11 1.38e-108 PDB 1DRA "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.63 159 98.11 99.37 6.99e-110 PDB 1DRB "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.63 159 98.11 98.74 4.24e-109 PDB 1DRE "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1DRH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.63 159 98.74 99.37 2.29e-110 PDB 1DYH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.63 159 98.74 99.37 2.29e-110 PDB 1DYI "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.63 159 98.74 99.37 2.29e-110 PDB 1DYJ "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.63 159 98.74 99.37 2.29e-110 PDB 1JOL "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.63 159 98.74 99.37 2.29e-110 PDB 1JOM "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.63 159 98.74 99.37 2.29e-110 PDB 1RA1 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RA2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RA3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RA8 "Dihydrofolate Reductase Complexed With Folate And 2- Monophosphoadenosine 5'-diphosphoribose" 100.63 159 98.74 99.37 2.29e-110 PDB 1RA9 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RB2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RB3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RC4 "Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized " 100.63 159 98.74 99.37 2.29e-110 PDB 1RD7 "Dihydrofolate Reductase Complexed With Folate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RE7 "Dihydrofolate Reductase Complexed With Folate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RF7 "Structure Of Dihydrofolate Reductase Complexed With Dihydrofolate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RG7 "Dihydrofolate Reductase Complexed With Methotrexate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RH3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX1 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (reduced Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX2 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX3 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX4 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And 2'-monophosphoadenosine 5'- Diphosphorib" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX5 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX6 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosph" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX7 "Structure Of Dihydrofolate Reductase Complexed With Folate" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX8 "Dihydrofolate Reductase Complexed With Folate And 2'- Monophosphoadenosine 5'-Diphosphoribose" 100.63 159 98.74 99.37 2.29e-110 PDB 1RX9 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.63 159 98.74 99.37 2.29e-110 PDB 1TDR "Expression, Characterization, And Crystallographic Analysis Of Telluromethionyl Dihydrofolate Reductase" 100.63 159 98.11 99.37 7.22e-110 PDB 2ANO "Crystal Structure Of E.coli Dihydrofolate Reductase In Complex With Nadph And The Inhibitor Ms-sh08-17" 100.63 159 98.74 99.37 2.29e-110 PDB 2ANQ "Crystal Structure Of E.coli Dhfr In Complex With Nadph And The Inhibitor Compound 10a." 100.63 159 98.74 99.37 2.29e-110 PDB 2DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.63 159 98.11 99.37 1.75e-109 PDB 2INQ "Neutron Crystal Structure Of Escherichia Coli Dihydrofolate Reductase Bound To The Anti-Cancer Drug, Methotrexate" 100.63 159 98.74 99.37 2.29e-110 PDB 3DAU "Crystal Structure Of The Ternary Mtx Nadph Complex Of Escherichia Coli Dihydrofolate Reductase" 100.63 159 99.37 99.37 2.52e-111 PDB 3DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.63 159 98.74 99.37 2.29e-110 PDB 3K74 "Disruption Of Protein Dynamics By An Allosteric Effector Antibody" 100.63 159 99.37 99.37 2.52e-111 PDB 3KFY "Dynamic Switching And Partial Occupancies Of A Small Molecule Inhibitor Complex Of Dhfr" 100.63 159 98.74 99.37 2.29e-110 PDB 3OCH "Chemically Self-Assembled Antibody Nanorings (Csans): Design And Characterization Of An Anti-Cd3 Igm Biomimetic" 100.63 159 98.74 99.37 2.29e-110 PDB 3QL0 "Crystal Structure Of N23pp/s148a Mutant Of E. Coli Dihydrofolate Reductase" 101.27 160 97.50 98.13 1.69e-107 PDB 3QL3 "Re-refined Coordinates For Pdb Entry 1rx2" 100.63 159 98.74 99.37 2.29e-110 PDB 3QYL "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.63 159 98.74 99.37 2.29e-110 PDB 3QYO "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.63 159 98.74 99.37 2.29e-110 PDB 3R33 "Evidence For Dynamic Motion In Proteins As A Mechanism For Ligand Dissociation" 100.63 159 98.74 99.37 2.29e-110 PDB 4DFR "Crystal Structures Of Escherichia Coli And Lactobacillus Casei Dihydrofolate Reductase Refined At 1.7 Angstroms Resolution. I. " 100.63 159 98.11 99.37 7.22e-110 PDB 4EIG "Ca1698 Camel Antibody Fragment In Complex With Dhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4EIZ "Structure Of Nb113 Bound To Apodhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4EJ1 "Binding Of Nb113 Camelid Antibody Fragment With The Binary Dhfr:folate Complex" 100.63 159 99.37 99.37 2.52e-111 PDB 4FHB "Enhancing Dhfr Catalysis By Binding Of An Allosteric Regulator Nanobody (nb179)" 100.63 159 99.37 99.37 2.52e-111 PDB 4I13 "Nanobody Ca1697 Binding To The Dhfr.folate Binary Complex" 100.63 159 99.37 99.37 2.52e-111 PDB 4I1N "R104a-ca1697 Nanobody Binding To The Binary Dhfr.folate Complex" 100.63 159 99.37 99.37 2.52e-111 PDB 4KJJ "Cryogenic Wt Dhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4KJK "Room Temperature Wt Dhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4KJL "Room Temperature N23pps148a Dhfr" 101.27 160 97.50 98.13 1.69e-107 PDB 4NX6 "Single Room Temperature Model Of Dhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4NX7 "Single Cryogenic Temperature Model Of Dhfr" 100.63 159 99.37 99.37 2.52e-111 PDB 4P3Q "Room-temperature Wt Dhfr, Time-averaged Ensemble" 100.63 159 99.37 99.37 2.52e-111 PDB 4P3R "Cryogenic Wt Dhfr, Time-averaged Ensemble" 100.63 159 99.37 99.37 2.52e-111 PDB 4P66 "Electrostatics Of Active Site Microenvironments Of E. Coli Dhfr" 100.63 159 97.48 97.48 5.07e-108 PDB 4P68 "Electrostatics Of Active Site Microenvironments For E. Coli Dhfr" 100.63 159 97.48 97.48 4.60e-108 PDB 4PSS "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.63 159 98.74 98.74 9.39e-110 PDB 4PST "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 277 K" 100.63 159 98.74 98.74 9.39e-110 PDB 4PSY "100k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.63 159 98.74 98.74 9.39e-110 PDB 4PTH "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.63 159 98.74 98.74 9.39e-110 PDB 4PTJ "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 277k" 100.63 159 98.74 98.74 9.39e-110 PDB 4QLE "Crystal Structure Of I14a Dhfr Mutant Complexed With Folate And Nadp+" 100.63 159 98.74 98.74 1.67e-110 PDB 4QLF "Crystal Structure Of I14g Dhfr Mutant Complexed With Folate And Nadp+" 100.63 159 98.74 98.74 3.96e-110 PDB 4QLG "Crystal Structure Of I14v Dhfr Mutant Complexed With Folate And Nadp+" 100.63 159 98.74 99.37 4.70e-111 PDB 4RGC "277k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.63 159 98.74 98.74 9.39e-110 PDB 5CC9 "L28f E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucleotide" 100.63 159 98.74 98.74 1.09e-110 PDB 5CCC "Wild-type E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucle" 100.63 159 99.37 99.37 2.52e-111 PDB 5DFR "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.63 159 98.74 99.37 2.29e-110 PDB 6DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.63 159 98.74 99.37 2.29e-110 PDB 7DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.63 159 98.74 99.37 2.29e-110 DBJ BAA05974 "fusion protein, composed of HCV p21 (NS2), E.coli dihydroforate reductase, substrate polypeptide for HCV serine proteinase and " 100.00 847 99.37 99.37 4.54e-103 DBJ BAB33474 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. Sakai]" 100.63 159 98.74 98.74 9.09e-110 DBJ BAB96616 "dihydrofolate reductase [Escherichia coli str. K12 substr. W3110]" 100.63 159 99.37 99.37 2.52e-111 DBJ BAG75573 "dihydrofolate reductase [Escherichia coli SE11]" 100.63 159 99.37 99.37 2.52e-111 DBJ BAI23410 "dihydrofolate reductase [Escherichia coli O26:H11 str. 11368]" 100.63 159 99.37 99.37 2.52e-111 EMBL CAA28755 "unnamed protein product [Escherichia coli]" 100.63 159 98.11 98.74 2.11e-109 EMBL CAP74618 "Dihydrofolate reductase [Escherichia coli LF82]" 100.63 159 99.37 99.37 2.52e-111 EMBL CAQ30568 "dihydrofolate reductase [Escherichia coli BL21(DE3)]" 100.63 159 99.37 99.37 2.52e-111 EMBL CAQ87642 "dihydrofolate reductase [Escherichia fergusonii ATCC 35469]" 100.63 159 99.37 99.37 2.52e-111 EMBL CAQ96940 "dihydrofolate reductase [Escherichia coli IAI1]" 100.63 159 99.37 99.37 2.52e-111 GB AAA87976 "dihydrofolate reductase [Escherichia coli]" 100.63 159 99.37 99.37 2.52e-111 GB AAC73159 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.63 159 99.37 99.37 2.52e-111 GB AAG54351 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. EDL933]" 100.63 159 98.74 98.74 9.09e-110 GB AAN41711 "dihydrofolate reductase type I [Shigella flexneri 2a str. 301]" 100.63 159 99.37 99.37 2.52e-111 GB AAN78554 "Dihydrofolate reductase [Escherichia coli CFT073]" 100.63 204 99.37 99.37 3.90e-111 REF NP_308078 "dihydrofolate reductase [Escherichia coli O157:H7 str. Sakai]" 100.63 159 98.74 98.74 9.09e-110 REF NP_414590 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.63 159 99.37 99.37 2.52e-111 REF NP_706004 "dihydrofolate reductase [Shigella flexneri 2a str. 301]" 100.63 159 99.37 99.37 2.52e-111 REF WP_000378105 "MULTISPECIES: dihydrofolate reductase [Proteobacteria]" 100.63 196 99.37 99.37 6.04e-111 REF WP_000624372 "dihydrofolate reductase [Escherichia coli]" 100.63 159 98.74 98.74 9.09e-110 SP P0ABQ4 "RecName: Full=Dihydrofolate reductase" 100.63 159 99.37 99.37 2.52e-111 SP P0ABQ5 "RecName: Full=Dihydrofolate reductase" 100.63 159 99.37 99.37 2.52e-111 SP P0ABQ6 "RecName: Full=Dihydrofolate reductase" 100.63 159 99.37 99.37 2.52e-111 stop_ save_ ############# # Ligands # ############# save_NAP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' _BMRB_code NAP _PDB_code NAP _Molecular_mass 743.405 _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 PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O5B O5B O . 0 . ? C5B C5B C . 0 . ? C4B C4B C . 0 . ? O4B O4B O . 0 . ? C3B C3B C . 0 . ? O3B O3B O . 0 . ? C2B C2B C . 0 . ? O2B O2B O . 0 . ? C1B C1B C . 0 . ? N9A N9A N . 0 . ? C8A C8A C . 0 . ? N7A N7A N . 0 . ? C5A C5A C . 0 . ? C6A C6A C . 0 . ? N6A N6A N . 0 . ? N1A N1A N . 0 . ? C2A C2A C . 0 . ? N3A N3A N . 0 . ? C4A C4A C . 0 . ? O3 O3 O . 0 . ? PN PN P . 0 . ? O1N O1N O . 0 . ? O2N O2N O . -1 . ? O5D O5D O . 0 . ? C5D C5D C . 0 . ? C4D C4D C . 0 . ? O4D O4D O . 0 . ? C3D C3D C . 0 . ? O3D O3D O . 0 . ? C2D C2D C . 0 . ? O2D O2D O . 0 . ? C1D C1D C . 0 . ? N1N N1N N . 1 . ? C2N C2N C . 0 . ? C3N C3N C . 0 . ? C7N C7N C . 0 . ? O7N O7N O . 0 . ? N7N N7N N . 0 . ? C4N C4N C . 0 . ? C5N C5N C . 0 . ? C6N C6N C . 0 . ? P2B P2B P . 0 . ? O1X O1X O . 0 . ? O2X O2X O . 0 . ? O3X O3X O . 0 . ? HOA2 HOA2 H . 0 . ? H51A H51A H . 0 . ? H52A H52A H . 0 . ? H4B H4B H . 0 . ? H3B H3B H . 0 . ? HO3A HO3A H . 0 . ? H2B H2B H . 0 . ? H1B H1B H . 0 . ? H8A H8A H . 0 . ? H61A H61A H . 0 . ? H62A H62A H . 0 . ? H2A H2A H . 0 . ? H51N H51N H . 0 . ? H52N H52N H . 0 . ? H4D H4D H . 0 . ? H3D H3D H . 0 . ? HO3N HO3N H . 0 . ? H2D H2D H . 0 . ? HO2N HO2N H . 0 . ? H1D H1D H . 0 . ? H2N H2N H . 0 . ? H71N H71N H . 0 . ? H72N H72N H . 0 . ? H4N H4N H . 0 . ? H5N H5N H . 0 . ? H6N H6N H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 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 DOUB PA O1A ? ? SING PA O2A ? ? SING PA O5B ? ? SING PA O3 ? ? SING O2A HOA2 ? ? SING O5B C5B ? ? SING C5B C4B ? ? SING C5B H51A ? ? SING C5B H52A ? ? SING C4B O4B ? ? SING C4B C3B ? ? SING C4B H4B ? ? SING O4B C1B ? ? SING C3B O3B ? ? SING C3B C2B ? ? SING C3B H3B ? ? SING O3B HO3A ? ? SING C2B O2B ? ? SING C2B C1B ? ? SING C2B H2B ? ? SING O2B P2B ? ? SING C1B N9A ? ? SING C1B H1B ? ? SING N9A C8A ? ? SING N9A C4A ? ? DOUB C8A N7A ? ? SING C8A H8A ? ? SING N7A C5A ? ? SING C5A C6A ? ? DOUB C5A C4A ? ? SING C6A N6A ? ? DOUB C6A N1A ? ? SING N6A H61A ? ? SING N6A H62A ? ? SING N1A C2A ? ? DOUB C2A N3A ? ? SING C2A H2A ? ? SING N3A C4A ? ? SING O3 PN ? ? DOUB PN O1N ? ? SING PN O2N ? ? SING PN O5D ? ? SING O5D C5D ? ? SING C5D C4D ? ? SING C5D H51N ? ? SING C5D H52N ? ? SING C4D O4D ? ? SING C4D C3D ? ? SING C4D H4D ? ? SING O4D C1D ? ? SING C3D O3D ? ? SING C3D C2D ? ? SING C3D H3D ? ? SING O3D HO3N ? ? SING C2D O2D ? ? SING C2D C1D ? ? SING C2D H2D ? ? SING O2D HO2N ? ? SING C1D N1N ? ? SING C1D H1D ? ? SING N1N C2N ? ? DOUB N1N C6N ? ? DOUB C2N C3N ? ? SING C2N H2N ? ? SING C3N C7N ? ? SING C3N C4N ? ? DOUB C7N O7N ? ? SING C7N N7N ? ? SING N7N H71N ? ? SING N7N H72N ? ? DOUB C4N C5N ? ? SING C4N H4N ? ? SING C5N C6N ? ? SING C5N H5N ? ? SING C6N H6N ? ? DOUB P2B O1X ? ? SING P2B O2X ? ? SING P2B O3X ? ? SING O2X HOP2 ? ? SING O3X HOP3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_FOL _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common '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 $Dihydrofolate_Reductase_from_E._coli 'E. coli' 562 Eubacteria . 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 $Dihydrofolate_Reductase_from_E._coli 'recombinant technology' 'E. coli' Escherichia coli . pET22b 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 $Dihydrofolate_Reductase_from_E._coli 1 mM '[U-100% 13C; U-100% 15N]' 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' EDTA 1 mM 'natural abundance' DTT 1 mM 'natural abundance' 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 6 mM 'natural abundance' 'FOLIC ACID' 10 mM 'natural abundance' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_KUJIRA _Saveframe_category software _Name Kujira _Version . loop_ _Vendor _Address _Electronic_address RIKEN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 0.1 . M pH 6.8 . 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 CBCA(CO)NH' '3D HNCACB' '3D HN(CO)CA' 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 monomer _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 55.433 0.300 1 2 1 1 MET CB C 32.792 0.300 1 3 2 2 ILE H H 9.429 0.030 1 4 2 2 ILE CA C 61.634 0.300 1 5 2 2 ILE CB C 39.203 0.300 1 6 2 2 ILE N N 124.770 0.300 1 7 3 3 SER H H 9.414 0.030 1 8 3 3 SER CA C 56.449 0.300 1 9 3 3 SER CB C 65.582 0.300 1 10 3 3 SER N N 126.161 0.300 1 11 4 4 LEU H H 8.566 0.030 1 12 4 4 LEU CA C 53.945 0.300 1 13 4 4 LEU CB C 44.073 0.300 1 14 4 4 LEU N N 121.992 0.300 1 15 5 5 ILE H H 8.597 0.030 1 16 5 5 ILE CA C 58.095 0.300 1 17 5 5 ILE CB C 43.447 0.300 1 18 5 5 ILE N N 120.275 0.300 1 19 6 6 ALA H H 8.639 0.030 1 20 6 6 ALA CA C 52.841 0.300 1 21 6 6 ALA N N 126.514 0.300 1 22 7 7 ALA C C 175.250 0.300 1 23 7 7 ALA CA C 50.739 0.300 1 24 8 8 LEU H H 9.154 0.030 1 25 8 8 LEU CA C 54.137 0.300 1 26 8 8 LEU CB C 45.947 0.300 1 27 8 8 LEU N N 123.544 0.300 1 28 9 9 ALA H H 8.513 0.030 1 29 9 9 ALA CA C 50.055 0.300 1 30 9 9 ALA N N 125.853 0.300 1 31 10 10 VAL H H 7.592 0.030 1 32 10 10 VAL CA C 65.049 0.300 1 33 10 10 VAL CB C 32.092 0.300 1 34 10 10 VAL N N 118.190 0.300 1 35 11 11 ASP H H 9.057 0.030 1 36 11 11 ASP CA C 56.134 0.300 1 37 11 11 ASP CB C 39.308 0.300 1 38 11 11 ASP N N 122.777 0.300 1 39 12 12 ARG H H 8.491 0.030 1 40 12 12 ARG CA C 57.657 0.300 1 41 12 12 ARG CB C 27.783 0.300 1 42 12 12 ARG N N 107.402 0.300 1 43 13 13 VAL H H 7.119 0.030 1 44 13 13 VAL CA C 65.557 0.300 1 45 13 13 VAL CB C 33.073 0.300 1 46 13 13 VAL N N 120.745 0.300 1 47 15 15 GLY H H 7.478 0.030 1 48 15 15 GLY CA C 46.045 0.300 1 49 15 15 GLY N N 110.593 0.300 1 50 16 16 MET H H 8.537 0.030 1 51 16 16 MET CA C 55.363 0.300 1 52 16 16 MET CB C 29.606 0.300 1 53 16 16 MET N N 119.406 0.300 1 54 18 18 ASN C C 173.721 0.300 1 55 18 18 ASN CA C 54.312 0.300 1 56 18 18 ASN CB C 38.818 0.300 1 57 19 19 ALA H H 7.726 0.030 1 58 19 19 ALA CA C 50.844 0.300 1 59 19 19 ALA CB C 21.793 0.300 1 60 19 19 ALA N N 121.115 0.300 1 61 20 20 MET H H 8.264 0.030 1 62 20 20 MET CA C 52.385 0.300 1 63 20 20 MET N N 119.799 0.300 1 64 23 23 ASN C C 172.775 0.300 1 65 23 23 ASN CA C 53.822 0.300 1 66 23 23 ASN CB C 40.219 0.300 1 67 24 24 LEU H H 9.518 0.030 1 68 24 24 LEU N N 125.458 0.300 1 69 25 25 PRO C C 179.695 0.300 1 70 25 25 PRO CA C 65.697 0.300 1 71 25 25 PRO CB C 31.391 0.300 1 72 26 26 ALA H H 9.248 0.030 1 73 26 26 ALA CA C 55.328 0.300 1 74 26 26 ALA CB C 19.585 0.300 1 75 26 26 ALA N N 120.320 0.300 1 76 27 27 ASP H H 7.487 0.030 1 77 27 27 ASP CA C 56.537 0.300 1 78 27 27 ASP CB C 43.898 0.300 1 79 27 27 ASP N N 118.475 0.300 1 80 28 28 LEU H H 7.610 0.030 1 81 28 28 LEU CA C 57.780 0.300 1 82 28 28 LEU CB C 40.639 0.300 1 83 28 28 LEU N N 121.622 0.300 1 84 29 29 ALA H H 7.870 0.030 1 85 29 29 ALA CA C 55.276 0.300 1 86 29 29 ALA CB C 17.834 0.300 1 87 29 29 ALA N N 120.802 0.300 1 88 30 30 TRP H H 7.467 0.030 1 89 30 30 TRP CA C 60.267 0.300 1 90 30 30 TRP CB C 29.535 0.300 1 91 30 30 TRP N N 124.168 0.300 1 92 31 31 PHE H H 9.055 0.030 1 93 31 31 PHE CA C 61.577 0.300 1 94 31 31 PHE CB C 38.012 0.300 1 95 31 31 PHE N N 123.524 0.300 1 96 32 32 LYS H H 8.699 0.030 1 97 32 32 LYS CA C 60.478 0.300 1 98 32 32 LYS CB C 32.793 0.300 1 99 32 32 LYS N N 124.291 0.300 1 100 33 33 ARG H H 8.114 0.030 1 101 33 33 ARG CA C 59.163 0.300 1 102 33 33 ARG CB C 29.955 0.300 1 103 33 33 ARG N N 117.228 0.300 1 104 34 34 ASN H H 7.111 0.030 1 105 34 34 ASN CA C 54.732 0.300 1 106 34 34 ASN CB C 39.343 0.300 1 107 34 34 ASN N N 111.573 0.300 1 108 35 35 THR H H 7.157 0.030 1 109 35 35 THR CA C 62.177 0.300 1 110 35 35 THR CB C 70.522 0.300 1 111 35 35 THR N N 107.498 0.300 1 112 36 36 LEU H H 7.514 0.030 1 113 36 36 LEU CA C 57.203 0.300 1 114 36 36 LEU CB C 42.391 0.300 1 115 36 36 LEU N N 122.022 0.300 1 116 37 37 ASN H H 7.943 0.030 1 117 37 37 ASN CA C 55.048 0.300 1 118 37 37 ASN CB C 37.767 0.300 1 119 37 37 ASN N N 113.425 0.300 1 120 38 38 LYS H H 7.899 0.030 1 121 38 38 LYS CA C 54.347 0.300 1 122 38 38 LYS CB C 34.194 0.300 1 123 38 38 LYS N N 119.607 0.300 1 124 39 39 PRO C C 175.959 0.300 1 125 39 39 PRO CA C 62.369 0.300 1 126 39 39 PRO CB C 32.232 0.300 1 127 40 40 VAL H H 8.762 0.030 1 128 40 40 VAL CA C 56.922 0.300 1 129 40 40 VAL CB C 34.229 0.300 1 130 40 40 VAL N N 113.509 0.300 1 131 41 41 ILE H H 8.520 0.030 1 132 41 41 ILE CA C 59.934 0.300 1 133 41 41 ILE CB C 40.429 0.300 1 134 41 41 ILE N N 121.926 0.300 1 135 42 42 MET H H 9.066 0.030 1 136 42 42 MET CA C 52.461 0.300 1 137 42 42 MET CB C 40.541 0.300 1 138 42 42 MET N N 123.795 0.300 1 139 43 43 GLY H H 9.197 0.030 1 140 43 43 GLY CA C 44.288 0.300 1 141 43 43 GLY N N 105.869 0.300 1 142 44 44 ARG H H 7.655 0.030 1 143 44 44 ARG CA C 61.073 0.300 1 144 44 44 ARG CB C 30.803 0.300 1 145 44 44 ARG N N 118.959 0.300 1 146 45 45 HIS H H 7.483 0.030 1 147 45 45 HIS CA C 58.341 0.300 1 148 45 45 HIS CB C 33.509 0.300 1 149 45 45 HIS N N 113.453 0.300 1 150 46 46 THR C C 176.180 0.300 1 151 47 47 TRP H H 8.421 0.030 1 152 47 47 TRP CA C 60.090 0.300 1 153 47 47 TRP CB C 29.902 0.300 1 154 47 47 TRP N N 124.247 0.300 1 155 48 48 GLU H H 8.230 0.030 1 156 48 48 GLU CA C 59.146 0.300 1 157 48 48 GLU CB C 29.413 0.300 1 158 48 48 GLU N N 118.049 0.300 1 159 49 49 SER H H 7.750 0.030 1 160 49 49 SER CA C 60.618 0.300 1 161 49 49 SER CB C 63.550 0.300 1 162 49 49 SER N N 114.028 0.300 1 163 50 50 ILE H H 7.591 0.030 1 164 50 50 ILE CA C 64.997 0.300 1 165 50 50 ILE CB C 38.993 0.300 1 166 50 50 ILE N N 123.106 0.300 1 167 51 51 GLY H H 7.586 0.030 1 168 51 51 GLY CA C 46.010 0.300 1 169 51 51 GLY N N 104.642 0.300 1 170 52 52 ARG H H 6.829 0.030 1 171 52 52 ARG CA C 53.366 0.300 1 172 52 52 ARG CB C 29.326 0.300 1 173 52 52 ARG N N 116.760 0.300 1 174 53 53 PRO C C 177.188 0.300 1 175 53 53 PRO CA C 62.054 0.300 1 176 53 53 PRO CB C 31.882 0.300 1 177 54 54 LEU H H 9.457 0.030 1 178 54 54 LEU CA C 52.245 0.300 1 179 54 54 LEU CB C 40.850 0.300 1 180 54 54 LEU N N 126.356 0.300 1 181 56 56 GLY C C 173.169 0.300 1 182 56 56 GLY CA C 46.780 0.300 1 183 57 57 ARG H H 7.273 0.030 1 184 57 57 ARG CA C 54.627 0.300 1 185 57 57 ARG CB C 36.015 0.300 1 186 57 57 ARG N N 118.324 0.300 1 187 58 58 LYS H H 7.405 0.030 1 188 58 58 LYS CA C 56.239 0.300 1 189 58 58 LYS CB C 32.617 0.300 1 190 58 58 LYS N N 123.424 0.300 1 191 59 59 ASN H H 9.240 0.030 1 192 59 59 ASN CA C 53.752 0.300 1 193 59 59 ASN CB C 40.639 0.300 1 194 59 59 ASN N N 126.899 0.300 1 195 60 60 ILE H H 8.798 0.030 1 196 60 60 ILE CA C 60.618 0.300 1 197 60 60 ILE CB C 27.328 0.300 1 198 60 60 ILE N N 126.490 0.300 1 199 61 61 ILE CA C 58.936 0.300 1 200 61 61 ILE CB C 28.378 0.300 1 201 62 62 LEU H H 8.392 0.030 1 202 62 62 LEU CA C 53.453 0.300 1 203 62 62 LEU CB C 42.882 0.300 1 204 62 62 LEU N N 127.578 0.300 1 205 63 63 SER H H 8.370 0.030 1 206 63 63 SER CA C 58.166 0.300 1 207 63 63 SER N N 115.511 0.300 1 208 64 64 SER C C 175.139 0.300 1 209 64 64 SER CA C 60.618 0.300 1 210 65 65 GLN H H 8.711 0.030 1 211 65 65 GLN CA C 53.156 0.300 1 212 65 65 GLN CB C 30.480 0.300 1 213 65 65 GLN N N 122.820 0.300 1 214 69 69 ASP C C 177.409 0.300 1 215 69 69 ASP CA C 55.503 0.300 1 216 69 69 ASP CB C 40.850 0.300 1 217 70 70 ARG H H 9.060 0.030 1 218 70 70 ARG CA C 57.579 0.300 1 219 70 70 ARG CB C 40.780 0.300 1 220 70 70 ARG N N 118.846 0.300 1 221 71 71 VAL H H 7.315 0.030 1 222 71 71 VAL CA C 58.968 0.300 1 223 71 71 VAL CB C 42.041 0.300 1 224 71 71 VAL N N 110.030 0.300 1 225 75 75 LYS H H 8.394 0.030 1 226 75 75 LYS CA C 55.695 0.300 1 227 75 75 LYS CB C 33.563 0.300 1 228 75 75 LYS N N 116.961 0.300 1 229 76 76 SER H H 7.219 0.030 1 230 76 76 SER CA C 57.080 0.300 1 231 76 76 SER CB C 66.037 0.300 1 232 76 76 SER N N 109.568 0.300 1 233 77 77 VAL H H 8.901 0.030 1 234 77 77 VAL CA C 67.362 0.300 1 235 77 77 VAL CB C 31.826 0.300 1 236 77 77 VAL N N 122.773 0.300 1 237 78 78 ASP H H 8.392 0.030 1 238 78 78 ASP CA C 57.832 0.300 1 239 78 78 ASP CB C 40.430 0.300 1 240 78 78 ASP N N 118.092 0.300 1 241 79 79 GLU H H 7.891 0.030 1 242 79 79 GLU CA C 59.251 0.300 1 243 79 79 GLU CB C 30.866 0.300 1 244 79 79 GLU N N 120.742 0.300 1 245 80 80 ALA H H 8.180 0.030 1 246 80 80 ALA CA C 55.626 0.300 1 247 80 80 ALA CB C 18.289 0.300 1 248 80 80 ALA N N 122.526 0.300 1 249 81 81 ILE H H 7.949 0.030 1 250 81 81 ILE CA C 65.540 0.300 1 251 81 81 ILE CB C 38.573 0.300 1 252 81 81 ILE N N 115.870 0.300 1 253 82 82 ALA H H 8.109 0.030 1 254 82 82 ALA CA C 55.293 0.300 1 255 82 82 ALA CB C 18.184 0.300 1 256 82 82 ALA N N 124.236 0.300 1 257 83 83 ALA H H 8.079 0.030 1 258 83 83 ALA CA C 53.910 0.300 1 259 83 83 ALA CB C 18.465 0.300 1 260 83 83 ALA N N 119.445 0.300 1 261 84 84 CYS H H 7.418 0.030 1 262 84 84 CYS CA C 61.809 0.300 1 263 84 84 CYS CB C 28.379 0.300 1 264 84 84 CYS N N 114.560 0.300 1 265 85 85 GLY H H 7.242 0.030 1 266 85 85 GLY CA C 45.397 0.300 1 267 85 85 GLY N N 103.379 0.300 1 268 86 86 ASP H H 8.510 0.030 1 269 86 86 ASP CA C 53.629 0.300 1 270 86 86 ASP CB C 39.904 0.300 1 271 86 86 ASP N N 122.648 0.300 1 272 87 87 VAL H H 7.224 0.030 1 273 87 87 VAL CA C 58.516 0.300 1 274 87 87 VAL CB C 32.442 0.300 1 275 87 87 VAL N N 114.468 0.300 1 276 88 88 PRO C C 177.850 0.300 1 277 88 88 PRO CA C 64.892 0.300 1 278 88 88 PRO CB C 32.302 0.300 1 279 89 89 GLU H H 7.739 0.030 1 280 89 89 GLU CA C 56.011 0.300 1 281 89 89 GLU CB C 33.073 0.300 1 282 89 89 GLU N N 117.022 0.300 1 283 90 90 ILE H H 8.780 0.030 1 284 90 90 ILE CA C 61.318 0.300 1 285 90 90 ILE CB C 41.410 0.300 1 286 90 90 ILE N N 130.160 0.300 1 287 91 91 MET H H 7.908 0.030 1 288 91 91 MET CA C 51.948 0.300 1 289 91 91 MET CB C 30.621 0.300 1 290 91 91 MET N N 121.963 0.300 1 291 92 92 VAL H H 9.388 0.030 1 292 92 92 VAL CA C 62.282 0.300 1 293 92 92 VAL CB C 31.493 0.300 1 294 92 92 VAL N N 125.096 0.300 1 295 93 93 ILE H H 8.976 0.030 1 296 93 93 ILE CA C 60.846 0.300 1 297 93 93 ILE CB C 31.531 0.300 1 298 93 93 ILE N N 119.646 0.300 1 299 94 94 GLY H H 6.214 0.030 1 300 94 94 GLY CA C 46.815 0.300 1 301 94 94 GLY N N 103.238 0.300 1 302 95 95 GLY H H 8.172 0.030 1 303 95 95 GLY CA C 46.850 0.300 1 304 95 95 GLY N N 111.944 0.300 1 305 96 96 GLY C C 175.013 0.300 1 306 96 96 GLY CA C 49.373 0.300 1 307 97 97 ARG H H 9.308 0.030 1 308 97 97 ARG CA C 58.463 0.300 1 309 97 97 ARG CB C 29.815 0.300 1 310 97 97 ARG N N 122.315 0.300 1 311 98 98 VAL H H 7.309 0.030 1 312 98 98 VAL CA C 68.079 0.300 1 313 98 98 VAL CB C 31.952 0.300 1 314 98 98 VAL N N 122.213 0.300 1 315 99 99 TYR H H 9.558 0.030 1 316 99 99 TYR CA C 60.478 0.300 1 317 99 99 TYR CB C 38.047 0.300 1 318 99 99 TYR N N 119.721 0.300 1 319 100 100 GLU H H 8.096 0.030 1 320 100 100 GLU CA C 60.197 0.300 1 321 100 100 GLU CB C 29.990 0.300 1 322 100 100 GLU N N 116.193 0.300 1 323 101 101 GLN H H 7.247 0.030 1 324 101 101 GLN CA C 58.270 0.300 1 325 101 101 GLN CB C 32.477 0.300 1 326 101 101 GLN N N 114.367 0.300 1 327 102 102 PHE H H 7.993 0.030 1 328 102 102 PHE CA C 60.460 0.300 1 329 102 102 PHE CB C 41.866 0.300 1 330 102 102 PHE N N 113.298 0.300 1 331 103 103 LEU H H 8.383 0.030 1 332 103 103 LEU CA C 60.933 0.300 1 333 103 103 LEU CB C 38.958 0.300 1 334 103 103 LEU N N 123.664 0.300 1 335 104 104 PRO C C 177.425 0.300 1 336 104 104 PRO CA C 65.633 0.300 1 337 104 104 PRO CB C 31.574 0.300 1 338 105 105 LYS H H 7.446 0.030 1 339 105 105 LYS CA C 55.477 0.300 1 340 105 105 LYS CB C 34.825 0.300 1 341 105 105 LYS N N 112.880 0.300 1 342 106 106 ALA H H 7.954 0.030 1 343 106 106 ALA CA C 52.578 0.300 1 344 106 106 ALA CB C 21.337 0.300 1 345 106 106 ALA N N 122.417 0.300 1 346 107 107 GLN H H 9.239 0.030 1 347 107 107 GLN CA C 55.941 0.300 1 348 107 107 GLN CB C 31.812 0.300 1 349 107 107 GLN N N 118.501 0.300 1 350 108 108 LYS H H 7.813 0.030 1 351 108 108 LYS CA C 56.221 0.300 1 352 108 108 LYS CB C 37.101 0.300 1 353 108 108 LYS N N 120.748 0.300 1 354 109 109 LEU H H 9.041 0.030 1 355 109 109 LEU CA C 53.156 0.300 1 356 109 109 LEU CB C 44.633 0.300 1 357 109 109 LEU N N 122.131 0.300 1 358 110 110 TYR H H 9.478 0.030 1 359 110 110 TYR CA C 56.029 0.300 1 360 110 110 TYR CB C 38.538 0.300 1 361 110 110 TYR N N 122.537 0.300 1 362 111 111 LEU H H 9.612 0.030 1 363 111 111 LEU CA C 52.946 0.300 1 364 111 111 LEU CB C 44.738 0.300 1 365 111 111 LEU N N 123.600 0.300 1 366 112 112 THR H H 8.295 0.030 1 367 112 112 THR CA C 60.109 0.300 1 368 112 112 THR CB C 69.155 0.300 1 369 112 112 THR N N 118.035 0.300 1 370 113 113 HIS H H 9.238 0.030 1 371 113 113 HIS CA C 54.838 0.300 1 372 113 113 HIS CB C 30.340 0.300 1 373 113 113 HIS N N 126.627 0.300 1 374 114 114 ILE H H 9.118 0.030 1 375 114 114 ILE CA C 60.916 0.300 1 376 114 114 ILE CB C 39.519 0.300 1 377 114 114 ILE N N 127.444 0.300 1 378 115 115 ASP H H 8.328 0.030 1 379 115 115 ASP CA C 53.681 0.300 1 380 115 115 ASP CB C 38.678 0.300 1 381 115 115 ASP N N 130.156 0.300 1 382 116 116 ALA H H 7.776 0.030 1 383 116 116 ALA CA C 51.404 0.300 1 384 116 116 ALA CB C 20.882 0.300 1 385 116 116 ALA N N 124.471 0.300 1 386 117 117 GLU H H 8.544 0.030 1 387 117 117 GLU CA C 55.573 0.300 1 388 117 117 GLU CB C 29.464 0.300 1 389 117 117 GLU N N 124.149 0.300 1 390 118 118 VAL H H 8.163 0.030 1 391 118 118 VAL CA C 58.865 0.300 1 392 118 118 VAL CB C 35.627 0.300 1 393 118 118 VAL N N 119.194 0.300 1 394 119 119 GLU H H 8.369 0.030 1 395 119 119 GLU CA C 56.449 0.300 1 396 119 119 GLU CB C 30.270 0.300 1 397 119 119 GLU N N 124.255 0.300 1 398 120 120 GLY H H 8.349 0.030 1 399 120 120 GLY CA C 45.953 0.300 1 400 120 120 GLY N N 107.000 0.300 1 401 121 121 ASP H H 8.553 0.030 1 402 121 121 ASP CA C 52.724 0.300 1 403 121 121 ASP CB C 42.189 0.300 1 404 121 121 ASP N N 116.518 0.300 1 405 122 122 THR H H 7.465 0.030 1 406 122 122 THR CA C 62.044 0.300 1 407 122 122 THR N N 114.256 0.300 1 408 123 123 HIS C C 173.894 0.300 1 409 123 123 HIS CA C 56.169 0.300 1 410 123 123 HIS CB C 33.283 0.300 1 411 124 124 PHE H H 9.155 0.030 1 412 124 124 PHE CA C 56.939 0.300 1 413 124 124 PHE CB C 41.480 0.300 1 414 124 124 PHE N N 125.107 0.300 1 415 125 125 PRO CA C 62.657 0.300 1 416 125 125 PRO CB C 31.990 0.300 1 417 126 126 ASP H H 8.069 0.030 1 418 126 126 ASP CA C 54.643 0.300 1 419 126 126 ASP CB C 40.773 0.300 1 420 126 126 ASP N N 117.780 0.300 1 421 127 127 TYR H H 7.443 0.030 1 422 127 127 TYR CA C 55.660 0.300 1 423 127 127 TYR CB C 39.553 0.300 1 424 127 127 TYR N N 119.252 0.300 1 425 128 128 GLU H H 8.796 0.030 1 426 128 128 GLU CA C 53.506 0.300 1 427 128 128 GLU CB C 29.710 0.300 1 428 128 128 GLU N N 123.456 0.300 1 429 129 129 PRO C C 178.403 0.300 1 430 129 129 PRO CA C 65.872 0.300 1 431 129 129 PRO CB C 32.652 0.300 1 432 130 130 ASP H H 8.966 0.030 1 433 130 130 ASP CA C 56.484 0.300 1 434 130 130 ASP CB C 40.359 0.300 1 435 130 130 ASP N N 114.896 0.300 1 436 131 131 ASP H H 8.152 0.030 1 437 131 131 ASP CA C 55.100 0.300 1 438 131 131 ASP CB C 41.305 0.300 1 439 131 131 ASP N N 118.186 0.300 1 440 132 132 TRP H H 7.776 0.030 1 441 132 132 TRP CA C 56.344 0.300 1 442 132 132 TRP CB C 34.159 0.300 1 443 132 132 TRP N N 119.631 0.300 1 444 133 133 GLU H H 9.553 0.030 1 445 133 133 GLU CA C 54.522 0.300 1 446 133 133 GLU CB C 32.793 0.300 1 447 133 133 GLU N N 122.928 0.300 1 448 134 134 SER H H 9.002 0.030 1 449 134 134 SER CA C 58.743 0.300 1 450 134 134 SER CB C 62.270 0.300 1 451 134 134 SER N N 121.491 0.300 1 452 135 135 VAL H H 9.050 0.030 1 453 135 135 VAL CA C 61.283 0.300 1 454 135 135 VAL CB C 32.667 0.300 1 455 135 135 VAL N N 121.776 0.300 1 456 136 136 PHE H H 7.881 0.030 1 457 136 136 PHE CA C 58.534 0.300 1 458 136 136 PHE CB C 43.022 0.300 1 459 136 136 PHE N N 123.567 0.300 1 460 137 137 SER H H 7.525 0.030 1 461 137 137 SER CA C 57.220 0.300 1 462 137 137 SER CB C 64.741 0.300 1 463 137 137 SER N N 119.791 0.300 1 464 138 138 GLU H H 8.690 0.030 1 465 138 138 GLU CA C 56.537 0.300 1 466 138 138 GLU CB C 35.035 0.300 1 467 138 138 GLU N N 125.649 0.300 1 468 139 139 PHE H H 8.629 0.030 1 469 139 139 PHE CA C 58.779 0.300 1 470 139 139 PHE CB C 40.815 0.300 1 471 139 139 PHE N N 129.306 0.300 1 472 140 140 HIS H H 7.916 0.030 1 473 140 140 HIS CA C 54.382 0.300 1 474 140 140 HIS CB C 31.251 0.300 1 475 140 140 HIS N N 123.303 0.300 1 476 141 141 ASP H H 7.979 0.030 1 477 141 141 ASP CA C 53.401 0.300 1 478 141 141 ASP CB C 42.531 0.300 1 479 141 141 ASP N N 120.533 0.300 1 480 142 142 ALA H H 8.097 0.030 1 481 142 142 ALA CA C 52.963 0.300 1 482 142 142 ALA CB C 19.130 0.300 1 483 142 142 ALA N N 122.692 0.300 1 484 143 143 ASP H H 8.886 0.030 1 485 143 143 ASP CA C 53.243 0.300 1 486 143 143 ASP CB C 41.515 0.300 1 487 143 143 ASP N N 120.828 0.300 1 488 144 144 ALA H H 8.132 0.030 1 489 144 144 ALA CA C 54.908 0.300 1 490 144 144 ALA CB C 18.465 0.300 1 491 144 144 ALA N N 117.920 0.300 1 492 145 145 GLN H H 8.020 0.030 1 493 145 145 GLN CA C 56.694 0.300 1 494 145 145 GLN CB C 31.111 0.300 1 495 145 145 GLN N N 113.340 0.300 1 496 146 146 ASN H H 8.194 0.030 1 497 146 146 ASN CA C 53.034 0.300 1 498 146 146 ASN CB C 41.025 0.300 1 499 146 146 ASN N N 119.651 0.300 1 500 147 147 SER H H 8.904 0.030 1 501 147 147 SER CA C 61.599 0.300 1 502 147 147 SER CB C 63.550 0.300 1 503 147 147 SER N N 117.339 0.300 1 504 148 148 HIS H H 7.070 0.030 1 505 148 148 HIS CA C 54.925 0.300 1 506 148 148 HIS CB C 35.175 0.300 1 507 148 148 HIS N N 117.826 0.300 1 508 149 149 SER H H 8.621 0.030 1 509 149 149 SER CA C 58.691 0.300 1 510 149 149 SER CB C 64.111 0.300 1 511 149 149 SER N N 113.611 0.300 1 512 150 150 TYR H H 7.646 0.030 1 513 150 150 TYR CA C 54.978 0.300 1 514 150 150 TYR CB C 39.133 0.300 1 515 150 150 TYR N N 115.122 0.300 1 516 151 151 CYS H H 8.241 0.030 1 517 151 151 CYS CA C 55.171 0.300 1 518 151 151 CYS CB C 30.515 0.300 1 519 151 151 CYS N N 118.720 0.300 1 520 152 152 PHE H H 8.437 0.030 1 521 152 152 PHE CA C 55.611 0.300 1 522 152 152 PHE CB C 40.359 0.300 1 523 152 152 PHE N N 111.047 0.300 1 524 153 153 GLU H H 9.771 0.030 1 525 153 153 GLU CA C 55.031 0.300 1 526 153 153 GLU CB C 34.649 0.300 1 527 153 153 GLU N N 124.280 0.300 1 528 154 154 ILE H H 8.632 0.030 1 529 154 154 ILE CA C 60.267 0.300 1 530 154 154 ILE CB C 40.640 0.300 1 531 154 154 ILE N N 124.185 0.300 1 532 155 155 LEU H H 9.302 0.030 1 533 155 155 LEU CA C 53.523 0.300 1 534 155 155 LEU CB C 45.719 0.300 1 535 155 155 LEU N N 126.472 0.300 1 536 156 156 GLU H H 9.341 0.030 1 537 156 156 GLU CA C 54.820 0.300 1 538 156 156 GLU CB C 33.773 0.300 1 539 156 156 GLU N N 120.017 0.300 1 540 157 157 ARG H H 8.225 0.030 1 541 157 157 ARG CA C 57.465 0.300 1 542 157 157 ARG CB C 30.901 0.300 1 543 157 157 ARG N N 126.829 0.300 1 544 158 158 ARG H H 7.980 0.030 1 545 158 158 ARG CA C 58.341 0.300 1 546 158 158 ARG CB C 31.214 0.300 1 547 158 158 ARG N N 131.547 0.300 1 stop_ save_