HEADER CARRIER PROTEIN 24-OCT-02 1O78 TITLE BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (1.3S) TITLE 2 [10-48] DELETION MUTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: BIOTIN CARBOXYL CARRIER PROTEIN OF METHYLMALONYL- COMPND 3 COA CARBOXYL-TRANSFERASE; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: TRANSCARBOXYLASE, 1.3S SUBUNIT; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: RESIDUES 10-48 DELETION MUTANT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PROPIONIBACTERIUM FREUDENREICHII SOURCE 3 SUBSP. SHERMANII; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PTAC1.3DELTA10-48, PCY216 KEYWDS TRANSCARBOXYLASE,CARBOXYL CARRIER, TRANSFERASE EXPDTA NMR, 20 STRUCTURES AUTHOR M.M.JANK,J.D.SADOWSKY,C.PEIKERT,S.BERGER REVDAT 1 21-NOV-02 1O78 0 JRNL AUTH M.M.JANK,J.D.SADOWSKY,C.PEIKERT,S.BERGER JRNL TITL NMR STUDIES ON THE SOLUTION STRUCTURE OF A JRNL TITL 2 DELETION MUTANT OF THE TRANSCARBOXYLASE BIOTIN JRNL TITL 3 CARRIER SUBUNIT. JRNL REF INT.J.BIOL.MACROMOL. V. 30 233 2002 JRNL REFN ASTM IJBMDR UK ISSN 0141-8130 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.V.REDDY,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN REMARK 1 TITL HIGH RESOLUTION SOLUTION STRUCTURE OF THE 1.3S REMARK 1 TITL 2 SUBUNIT OF TRANSCARBOXYLASE FROM PROPIONIBACTERIUM REMARK 1 TITL 3 SHERMANII(DAGGER) REMARK 1 REF BIOCHEMISTRY V. 39 2509 2000 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.M.JANK,S.BOKORNY,K.-H.ROEHM,S.BERGER REMARK 1 TITL EXPRESSION AND BIOTINYLATION OF A MUTANT OF THE REMARK 1 TITL 2 TRANSCARBOXYLASE CARRIER PROTEIN FROM PROPIONI REMARK 1 TITL 3 SHERMANII REMARK 1 REF PROTEIN EXPRESSION PURIF. V. 17 123 1999 REMARK 1 REFN ASTM PEXPEJ US ISSN 1046-5928 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER NUMBER OF NON-HYDROGEN ATOMS USED IN REMARK 3 REFINEMENT. PROTEIN ATOMS : 604 NUCLEIC ACID REMARK 3 ATOMS : 0 HETEROGEN ATOMS : 0 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DGSA, REFINEMENT WITH NOES AND REMARK 3 HYDROGEN-BOND CONSTRAINTS REMARK 4 REMARK 4 1O78 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 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI. REMARK 100 THE EBI ID CODE IS EBI-11596. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : 2 MM AMMONIUM ACETATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2.3 MM PROTEIN, N15/C13 REMARK 210 LABELED TC 1.3S [10-48], REMARK 210 BIOTIN (UNLABELED) COVALENTLY REMARK 210 ATTACHED TO LYS 89 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC-NOESY, HNCA, HNCO, REMARK 210 CBCANH, CBCA(CO)NH, HN(CA)CO, REMARK 210 HCACO, HN-HSQC-TOCSY, REMARK 210 HBHA(CBCACO)NH, (H)N(CA)NNH, REMARK 210 HCCH-TOCSY, 2D 15N-1H HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR, PROCHECK 3.5.3, AQUA REMARK 210 2.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 600 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. BIOTIN WAS UNLABELED REMARK 210 AND NOT INCLUDED IN THE STRUCTURE CALCULATION. 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 THR A 6 159.55 59.06 REMARK 500 1 GLU A 33 145.68 59.77 REMARK 500 2 VAL A 74 164.41 56.44 REMARK 500 3 GLU A 33 155.65 59.82 REMARK 500 4 VAL A 5 137.72 61.14 REMARK 500 5 LYS A 12 -88.42 55.24 REMARK 500 5 MET A 49 -83.29 59.04 REMARK 500 5 THR A 53 -74.74 61.00 REMARK 500 5 ALA A 73 142.82 61.82 REMARK 500 6 GLU A 70 143.45 61.27 REMARK 500 7 VAL A 7 160.90 57.75 REMARK 500 8 THR A 53 -83.80 56.81 REMARK 500 9 LYS A 2 -72.62 62.94 REMARK 500 9 GLU A 33 142.32 61.21 REMARK 500 10 THR A 53 -92.28 52.10 REMARK 500 11 LYS A 4 -88.92 54.91 REMARK 500 11 THR A 53 -64.99 65.70 REMARK 500 12 GLU A 70 135.79 61.61 REMARK 500 12 VAL A 74 139.71 60.86 REMARK 500 13 GLU A 70 135.94 61.97 REMARK 500 14 LYS A 4 155.11 59.94 REMARK 500 14 LEU A 22 127.96 61.52 REMARK 500 14 GLU A 52 -92.48 54.08 REMARK 500 14 THR A 53 -89.78 51.67 REMARK 500 15 GLU A 33 157.62 59.85 REMARK 500 16 GLU A 70 132.39 61.95 REMARK 500 17 MET A 51 -85.67 57.04 REMARK 500 17 GLU A 52 -77.15 62.86 REMARK 500 17 THR A 53 -92.92 44.77 REMARK 500 17 ARG A 71 -42.63 74.09 REMARK 500 18 VAL A 7 151.11 60.05 REMARK 500 18 MET A 51 -63.28 65.58 REMARK 500 18 GLU A 52 -65.15 67.76 REMARK 500 18 THR A 53 -103.46 52.45 REMARK 500 19 LYS A 12 164.92 57.38 REMARK 500 20 THR A 53 -59.96 66.84 DBREF 1O78 A 1 9 UNP P02904 BCCP_PROFR 1 9 DBREF 1O78 A 10 84 UNP P02904 BCCP_PROFR 49 123 SEQRES 1 A 84 MET LYS LEU LYS VAL THR VAL ASN GLY ALA GLY LYS ALA SEQRES 2 A 84 GLY GLU GLY GLU ILE PRO ALA PRO LEU ALA GLY THR VAL SEQRES 3 A 84 SER LYS ILE LEU VAL LYS GLU GLY ASP THR VAL LYS ALA SEQRES 4 A 84 GLY GLN THR VAL LEU VAL LEU GLU ALA MET LYS MET GLU SEQRES 5 A 84 THR GLU ILE ASN ALA PRO THR ASP GLY LYS VAL GLU LYS SEQRES 6 A 84 VAL LEU VAL LYS GLU ARG ASP ALA VAL GLN GLY GLY GLN SEQRES 7 A 84 GLY LEU ILE LYS ILE GLY SHEET 1 AA 3 LYS A 28 ILE A 29 0 SHEET 2 AA 3 THR A 42 VAL A 45 -1 N VAL A 45 O LYS A 28 SHEET 3 AA 3 ILE A 55 ASN A 56 -1 O ILE A 55 N VAL A 43 SHEET 1 AB 3 THR A 36 VAL A 37 0 SHEET 2 AB 3 GLY A 61 VAL A 66 -1 O GLY A 61 N VAL A 37 SHEET 3 AB 3 ILE A 81 ILE A 83 -1 O LYS A 82 N GLU A 64 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