HEADER CARRIER PROTEIN 04-MAR-98 1A6X TITLE STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO- TITLE 2 BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, TITLE 3 49 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL- COMPND 3 COA CARBOXYLASE; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: CARBOXYL-TERMINAL FRAGMENT, RESIDUES 70 - 156; COMPND 6 SYNONYM: APO-BCCP87; COMPND 7 EC: 6.4.1.2; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 STRAIN: BL21 (DE3); SOURCE 4 CELL_LINE: BL21; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTM53 KEYWDS ACETYL-COA CARBOXYLASE, BIOTIN CARBOXYL CARRIER PROTEIN, KEYWDS 2 NUCLEAR MAGNETIC RESONANCE, BACKBONE DYNAMICS EXPDTA NMR, 49 STRUCTURES AUTHOR X.YAO,D.WEI,C.SODEN JUNIOR,M.F.SUMMERS,D.BECKETT REVDAT 2 01-APR-03 1A6X 1 JRNL REVDAT 1 14-OCT-98 1A6X 0 JRNL AUTH X.YAO,D.WEI,C.SODEN JR.,M.F.SUMMERS,D.BECKETT JRNL TITL STRUCTURE OF THE CARBOXY-TERMINAL FRAGMENT OF THE JRNL TITL 2 APO-BIOTIN CARBOXYL CARRIER SUBUNIT OF ESCHERICHIA JRNL TITL 3 COLI ACETYL-COA CARBOXYLASE. JRNL REF BIOCHEMISTRY V. 36 15089 1997 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 1A6X 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 (2007-03-16) REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : PHOSPHATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY, COSY, HSQC, REMARK 210 NOESY-HSQC, TOCSY-HSQC AND T1, REMARK 210 T2, NOE MEASUREMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : GE OMEGA PSG REMARK 210 SPECTROMETER MANUFACTURER : GE REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 49 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 49 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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 ALA A 74 -62.06 71.46 REMARK 500 1 ALA A 76 -62.02 74.52 REMARK 500 1 GLU A 77 134.02 62.75 REMARK 500 2 GLU A 71 152.35 64.69 REMARK 500 3 ILE A 78 -66.88 69.07 REMARK 500 4 SER A 79 -82.44 72.35 REMARK 500 5 SER A 79 -92.37 60.26 REMARK 500 6 SER A 79 -41.07 87.93 REMARK 500 8 ILE A 78 -86.65 66.58 REMARK 500 11 ALA A 75 -62.08 74.54 REMARK 500 11 ILE A 78 144.18 65.57 REMARK 500 12 SER A 79 -51.95 81.99 REMARK 500 13 ALA A 75 -67.18 68.94 REMARK 500 13 SER A 79 -58.96 73.45 REMARK 500 16 ALA A 74 157.21 61.83 REMARK 500 16 ALA A 76 -62.63 74.53 REMARK 500 18 ALA A 72 154.54 59.77 REMARK 500 18 GLU A 77 154.06 68.86 REMARK 500 19 ALA A 74 -61.97 74.50 REMARK 500 19 ALA A 75 -62.06 72.20 REMARK 500 22 GLU A 71 -65.25 68.60 REMARK 500 22 ILE A 78 127.86 63.50 REMARK 500 23 ALA A 76 144.52 61.93 REMARK 500 28 ALA A 74 155.14 59.60 REMARK 500 28 GLU A 77 149.33 69.57 REMARK 500 29 ALA A 72 160.07 64.01 REMARK 500 29 ALA A 75 162.92 64.00 REMARK 500 31 ILE A 78 155.33 65.04 REMARK 500 32 ALA A 76 -61.98 74.51 REMARK 500 32 GLU A 77 157.35 59.41 REMARK 500 34 ALA A 76 -62.94 70.73 REMARK 500 35 ILE A 78 166.52 55.98 REMARK 500 37 GLU A 71 -59.48 74.61 REMARK 500 37 GLU A 77 139.36 61.28 REMARK 500 38 GLU A 71 121.32 66.99 REMARK 500 38 ALA A 72 168.53 59.57 REMARK 500 39 ALA A 74 -61.92 75.04 REMARK 500 39 ALA A 76 152.13 60.89 REMARK 500 40 GLU A 71 151.83 59.50 REMARK 500 40 GLU A 77 138.06 64.23 REMARK 500 41 ILE A 78 153.68 63.74 REMARK 500 42 GLU A 77 120.34 60.12 REMARK 500 43 ALA A 76 -62.06 74.49 REMARK 500 43 GLU A 77 168.57 60.34 REMARK 500 44 ALA A 72 166.00 59.67 REMARK 500 44 ALA A 74 -62.10 71.47 REMARK 500 47 GLU A 71 -65.98 69.36 REMARK 500 47 ALA A 76 -63.89 69.80 REMARK 500 49 GLU A 77 142.99 66.24 DBREF 1A6X A 70 156 UNP P0ABD8 BCCP_ECOLI 70 156 SEQRES 1 A 87 MET GLU ALA PRO ALA ALA ALA GLU ILE SER GLY HIS ILE SEQRES 2 A 87 VAL ARG SER PRO MET VAL GLY THR PHE TYR ARG THR PRO SEQRES 3 A 87 SER PRO ASP ALA LYS ALA PHE ILE GLU VAL GLY GLN LYS SEQRES 4 A 87 VAL ASN VAL GLY ASP THR LEU CYS ILE VAL GLU ALA MET SEQRES 5 A 87 LYS MET MET ASN GLN ILE GLU ALA ASP LYS SER GLY THR SEQRES 6 A 87 VAL LYS ALA ILE LEU VAL GLU SER GLY GLN PRO VAL GLU SEQRES 7 A 87 PHE ASP GLU PRO LEU VAL VAL ILE GLU SHEET 1 A 3 THR A 90 TYR A 92 0 SHEET 2 A 3 THR A 114 ALA A 120 -1 N GLU A 119 O THR A 90 SHEET 3 A 3 MET A 123 GLU A 128 -1 N ILE A 127 O LEU A 115 SHEET 1 B 2 VAL A 135 ILE A 138 0 SHEET 2 B 2 VAL A 153 ILE A 155 -1 N VAL A 154 O LYS A 136 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