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HEADER TRANSFERASE 24-OCT-01 1K8O TITLE SOLUTION STRUCTURE OF THE LIPOIC ACID-BEARING DOMAIN OF THE TITLE 2 E2 COMPONENT OF HUMAN, MITOCHONDRIAL BRANCHED-CHAIN ALPHA- TITLE 3 KETOACID DEHYDROGENASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: E2 COMPONENT OF BRANCHED-CHAIN AHPHA-KETOACID COMPND 3 DEHYDROGENASE; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: LIPOIC ACID-BEARING DOMAIN; COMPND 6 SYNONYM: DIHYDROLIPOAMIDE BRANCHED CHAIN TRANSACYLASE; COMPND 7 EC: 2.3.1.-; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B KEYWDS LIPOYL ACID BEARING, HUMAN BCKD, EXPERIMENTAL NMR DATA EXPDTA NMR, 20 STRUCTURES AUTHOR C.-F.CHANG,H.-T.CHOU,J.L.CHUANG,D.T.CHUANG,T.-H.HUANG REVDAT 3 01-APR-03 1K8O 1 JRNL REVDAT 2 04-DEC-02 1K8O 1 REMARK REVDAT 1 14-NOV-01 1K8O 0 JRNL AUTH C.-F.CHANG,H.-T.CHOU,J.L.CHUANG,D.T.CHUANG, JRNL AUTH 2 T.-H.HUANG JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE LIPOIC JRNL TITL 2 ACID-BEARING DOMAIN OF HUMAN MITOCHONDRIAL JRNL TITL 3 BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE JRNL TITL 4 COMPLEX JRNL REF J.BIOL.CHEM. V. 277 15865 2002 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.0 REMARK 3 AUTHORS : NILGES ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1K8O COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB014698. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 310 REMARK 210 PH : 7.5; 7.5 REMARK 210 IONIC STRENGTH : 100MM NACL; 100MM NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM PROTEIN U-15N; 50MM REMARK 210 PHOSPHATE BUFFER, PH7.5, 100MM REMARK 210 NACL, 0.02% (W/V) NAN3; 2MM REMARK 210 PROTEIN U-15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER, PH7.5, 100MM REMARK 210 NACL, 0.02% (W/V) NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, HNHA, REMARK 210 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE, AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.0, AURELIA 2.0.6, REMARK 210 ARIA 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURE WITH THE LOWEST REMARK 210 ENERGY AND ACCEPTABLE COVALENT REMARK 210 GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 1 HIS A 88 REMARK 465 1 HIS A 89 REMARK 465 1 HIS A 90 REMARK 465 1 HIS A 91 REMARK 465 1 HIS A 92 REMARK 465 1 HIS A 93 REMARK 465 2 HIS A 88 REMARK 465 2 HIS A 89 REMARK 465 2 HIS A 90 REMARK 465 2 HIS A 91 REMARK 465 2 HIS A 92 REMARK 465 2 HIS A 93 REMARK 465 3 HIS A 88 REMARK 465 3 HIS A 89 REMARK 465 3 HIS A 90 REMARK 465 3 HIS A 91 REMARK 465 3 HIS A 92 REMARK 465 3 HIS A 93 REMARK 465 4 HIS A 88 REMARK 465 4 HIS A 89 REMARK 465 4 HIS A 90 REMARK 465 4 HIS A 91 REMARK 465 4 HIS A 92 REMARK 465 4 HIS A 93 REMARK 465 5 HIS A 88 REMARK 465 5 HIS A 89 REMARK 465 5 HIS A 90 REMARK 465 5 HIS A 91 REMARK 465 5 HIS A 92 REMARK 465 5 HIS A 93 REMARK 465 6 HIS A 88 REMARK 465 6 HIS A 89 REMARK 465 6 HIS A 90 REMARK 465 6 HIS A 91 REMARK 465 6 HIS A 92 REMARK 465 6 HIS A 93 REMARK 465 7 HIS A 88 REMARK 465 7 HIS A 89 REMARK 465 7 HIS A 90 REMARK 465 7 HIS A 91 REMARK 465 7 HIS A 92 REMARK 465 7 HIS A 93 REMARK 465 8 HIS A 88 REMARK 465 8 HIS A 89 REMARK 465 8 HIS A 90 REMARK 465 8 HIS A 91 REMARK 465 8 HIS A 92 REMARK 465 8 HIS A 93 REMARK 465 9 HIS A 88 REMARK 465 9 HIS A 89 REMARK 465 9 HIS A 90 REMARK 465 9 HIS A 91 REMARK 465 9 HIS A 92 REMARK 465 9 HIS A 93 REMARK 465 10 HIS A 88 REMARK 465 10 HIS A 89 REMARK 465 10 HIS A 90 REMARK 465 10 HIS A 91 REMARK 465 10 HIS A 92 REMARK 465 10 HIS A 93 REMARK 465 11 HIS A 88 REMARK 465 11 HIS A 89 REMARK 465 11 HIS A 90 REMARK 465 11 HIS A 91 REMARK 465 11 HIS A 92 REMARK 465 11 HIS A 93 REMARK 465 12 HIS A 88 REMARK 465 12 HIS A 89 REMARK 465 12 HIS A 90 REMARK 465 12 HIS A 91 REMARK 465 12 HIS A 92 REMARK 465 12 HIS A 93 REMARK 465 13 HIS A 88 REMARK 465 13 HIS A 89 REMARK 465 13 HIS A 90 REMARK 465 13 HIS A 91 REMARK 465 13 HIS A 92 REMARK 465 13 HIS A 93 REMARK 465 14 HIS A 88 REMARK 465 14 HIS A 89 REMARK 465 14 HIS A 90 REMARK 465 14 HIS A 91 REMARK 465 14 HIS A 92 REMARK 465 14 HIS A 93 REMARK 465 15 HIS A 88 REMARK 465 15 HIS A 89 REMARK 465 15 HIS A 90 REMARK 465 15 HIS A 91 REMARK 465 15 HIS A 92 REMARK 465 15 HIS A 93 REMARK 465 16 HIS A 88 REMARK 465 16 HIS A 89 REMARK 465 16 HIS A 90 REMARK 465 16 HIS A 91 REMARK 465 16 HIS A 92 REMARK 465 16 HIS A 93 REMARK 465 17 HIS A 88 REMARK 465 17 HIS A 89 REMARK 465 17 HIS A 90 REMARK 465 17 HIS A 91 REMARK 465 17 HIS A 92 REMARK 465 17 HIS A 93 REMARK 465 18 HIS A 88 REMARK 465 18 HIS A 89 REMARK 465 18 HIS A 90 REMARK 465 18 HIS A 91 REMARK 465 18 HIS A 92 REMARK 465 18 HIS A 93 REMARK 465 19 HIS A 88 REMARK 465 19 HIS A 89 REMARK 465 19 HIS A 90 REMARK 465 19 HIS A 91 REMARK 465 19 HIS A 92 REMARK 465 19 HIS A 93 REMARK 465 20 HIS A 88 REMARK 465 20 HIS A 89 REMARK 465 20 HIS A 90 REMARK 465 20 HIS A 91 REMARK 465 20 HIS A 92 REMARK 465 20 HIS A 93 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 THR A 20 CA THR A 20 CB 0.022 REMARK 500 2 GLU A 87 C GLU A 87 O 0.018 REMARK 500 3 GLU A 87 C GLU A 87 O 0.018 REMARK 500 4 ARG A 53 CA ARG A 53 CB 0.018 REMARK 500 4 GLU A 87 C GLU A 87 O 0.018 REMARK 500 5 ARG A 53 CA ARG A 53 CB 0.019 REMARK 500 6 GLU A 87 C GLU A 87 O 0.018 REMARK 500 7 GLU A 87 C GLU A 87 O 0.018 REMARK 500 8 GLU A 87 C GLU A 87 O 0.019 REMARK 500 9 THR A 20 CA THR A 20 CB 0.024 REMARK 500 9 GLU A 87 C GLU A 87 O 0.018 REMARK 500 10 ARG A 53 CA ARG A 53 CB 0.021 REMARK 500 10 GLU A 87 C GLU A 87 O 0.018 REMARK 500 12 ILE A 12 CA ILE A 12 CB 0.019 REMARK 500 13 ILE A 68 CA ILE A 68 C -0.020 REMARK 500 13 ILE A 68 C ALA A 69 N -0.021 REMARK 500 13 GLU A 87 C GLU A 87 O 0.021 REMARK 500 14 ARG A 53 CA ARG A 53 CB 0.020 REMARK 500 14 GLU A 87 C GLU A 87 O 0.018 REMARK 500 15 GLU A 87 C GLU A 87 O 0.018 REMARK 500 16 GLU A 87 C GLU A 87 O 0.018 REMARK 500 17 GLU A 87 C GLU A 87 O 0.019 REMARK 500 18 ARG A 53 CA ARG A 53 C 0.019 REMARK 500 18 GLU A 87 C GLU A 87 O 0.018 REMARK 500 19 CYS A 39 CA CYS A 39 CB 0.021 REMARK 500 19 GLU A 87 C GLU A 87 O 0.018 REMARK 500 20 ARG A 53 CA ARG A 53 CB 0.019 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 THR A 20 CA - CB - CG2 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ASP A 11 N - CA - C ANGL. DEV. = 4.4 DEGREES REMARK 500 9 THR A 20 CA - CB - CG2 ANGL. DEV. = 3.7 DEGREES REMARK 500 10 ARG A 17 N - CA - C ANGL. DEV. = -3.3 DEGREES REMARK 500 13 VAL A 5 N - CA - C ANGL. DEV. = -3.2 DEGREES REMARK 500 18 LYS A 84 N - CA - C ANGL. DEV. = 4.1 DEGREES REMARK 500 20 LYS A 84 N - CA - C ANGL. DEV. = 4.1 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1K8M RELATED DB: PDB REMARK 900 1K8M CONTAINS THE AVERAGE STRUCTURE OF THE SAME PROTEIN REMARK 900 RELATED ID: 5078 RELATED DB: BMRB REMARK 900 5078 CONTAINS CHEMICAL SHIFT LISTS EXCLUDING FIRST MET DBREF 1K8O A 2 85 UNP P11182 ODB2_HUMAN 62 145 SEQADV 1K8O MET A 1 UNP P11182 INITIATING MET SEQADV 1K8O LEU A 86 UNP P11182 HIS TAG SEQADV 1K8O GLU A 87 UNP P11182 HIS TAG SEQADV 1K8O HIS A 88 UNP P11182 HIS TAG SEQADV 1K8O HIS A 89 UNP P11182 HIS TAG SEQADV 1K8O HIS A 90 UNP P11182 HIS TAG SEQADV 1K8O HIS A 91 UNP P11182 HIS TAG SEQADV 1K8O HIS A 92 UNP P11182 HIS TAG SEQADV 1K8O HIS A 93 UNP P11182 HIS TAG SEQRES 1 A 93 MET GLY GLN VAL VAL GLN PHE LYS LEU SER ASP ILE GLY SEQRES 2 A 93 GLU GLY ILE ARG GLU VAL THR VAL LYS GLU TRP TYR VAL SEQRES 3 A 93 LYS GLU GLY ASP THR VAL SER GLN PHE ASP SER ILE CYS SEQRES 4 A 93 GLU VAL GLN SER ASP LYS ALA SER VAL THR ILE THR SER SEQRES 5 A 93 ARG TYR ASP GLY VAL ILE LYS LYS LEU TYR TYR ASN LEU SEQRES 6 A 93 ASP ASP ILE ALA TYR VAL GLY LYS PRO LEU VAL ASP ILE SEQRES 7 A 93 GLU THR GLU ALA LEU LYS ASP LEU GLU HIS HIS HIS HIS SEQRES 8 A 93 HIS HIS SHEET 1 A 3 VAL A 5 LYS A 8 0 SHEET 2 A 3 PRO A 74 GLU A 79 -1 O ILE A 78 N VAL A 5 SHEET 3 A 3 VAL A 57 LYS A 60 -1 N VAL A 57 O GLU A 79 SHEET 1 B 4 SER A 47 THR A 49 0 SHEET 2 B 4 CYS A 39 GLN A 42 -1 N VAL A 41 O VAL A 48 SHEET 3 B 4 VAL A 19 TRP A 24 -1 N GLU A 23 O GLU A 40 SHEET 4 B 4 ILE A 68 ALA A 69 -1 O ALA A 69 N VAL A 19 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1