Header list of 1bbl.pdb file
Complete list - 16 202 Bytes
HEADER GLYCOLYSIS 20-FEB-92 1BBL TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE TITLE 2 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE TITLE 3 DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 EC: 2.3.1.61; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562 KEYWDS GLYCOLYSIS EXPDTA SOLUTION NMR AUTHOR G.M.CLORE,M.A.ROBIEN,A.M.GRONENBORN REVDAT 3 16-FEB-22 1BBL 1 REMARK REVDAT 2 24-FEB-09 1BBL 1 VERSN REVDAT 1 31-JAN-94 1BBL 0 JRNL AUTH M.A.ROBIEN,G.M.CLORE,J.G.OMICHINSKI,R.N.PERHAM,E.APPELLA, JRNL AUTH 2 K.SAKAGUCHI,A.M.GRONENBORN JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING JRNL TITL 2 DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM JRNL TITL 3 THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF JRNL TITL 4 ESCHERICHIA COLI. JRNL REF BIOCHEMISTRY V. 31 3463 1992 JRNL REFN ISSN 0006-2960 JRNL PMID 1554728 JRNL DOI 10.1021/BI00128A021 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL REMARK 3 STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS REMARK 3 ABOVE. THE STRUCTURES ARE BASED ON 630 INTERPROTON REMARK 3 DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; AND 46 REMARK 3 PHI AND 35 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 20 REMARK 3 CHI1 SIDE CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM REMARK 3 COUPLING CONSTANTS AND NOE DATA. THE LATTER ARE OBTAINED REMARK 3 USING THE CONFORMATIONAL GRID SEARCH PROGRAM STEREOSEARCH REMARK 3 (M.NILGES,G.M.CLORE,A.M.GRONENBORN (1990) BIOPOLYMERS REMARK 3 29, 813-822). THE METHOD USED TO DETERMINE THE STRUCTURES REMARK 3 IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL REMARK 3 SIMULATED ANNEALING METHOD (M.NILGES,G.M.CLORE, REMARK 3 A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)). REMARK 3 REMARK 3 THIS ENTRY CONTAINS THE SIMULATED ANNEALING RESONANCE REMARK 3 MINIMIZED AVERAGE STRUCTURE. THE COORDINATES OF 56 REMARK 3 INDIVIDUAL STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK REMARK 3 ENTRY 1BAL. (SA)R RESTRAINED MINIMIZED MEAN STRUCTURE WAS REMARK 3 DERIVED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL SA REMARK 3 STRUCTURES BEST FITTED TO RESIDUES 14 - 30 AND 39 - 47, REMARK 3 AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED REMARK 3 MINIMIZATION. RESIDUES 1 - 11 AND 48 - 51 ARE COMPLETELY REMARK 3 DISORDERED AND ARE NOT INCLUDED IN THE COORDINATE SET. REMARK 3 REMARK 3 THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF THIS ENTRY HAS REMARK 3 NO MEANING. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF REMARK 3 ENTRY 1BAL REPRESENTS THE ATOMIC RMS DEVIATIONS OF THE 56 REMARK 3 INDIVIDUAL STRUCTURES ABOUT THE MEAN STRUCTURE. REMARK 3 REMARK 3 ALL THE INTERPROTON DISTANCE AND TORSION ANGLE RESTRAINTS REMARK 3 ARE PRESENTED IN PROTEIN DATA BANK ENTRY R1BBLMR. REMARK 4 REMARK 4 1BBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171563. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 RES C SSSEQI REMARK 465 TYR A 1 REMARK 465 ALA A 2 REMARK 465 SER A 3 REMARK 465 LEU A 4 REMARK 465 GLU A 5 REMARK 465 GLU A 6 REMARK 465 GLN A 7 REMARK 465 ASN A 8 REMARK 465 ASN A 9 REMARK 465 ASP A 10 REMARK 465 ALA A 11 REMARK 465 ALA A 49 REMARK 465 LYS A 50 REMARK 465 ALA A 51 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),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 23 CG HIS A 23 ND1 -0.115 REMARK 500 HIS A 47 CG HIS A 47 ND1 -0.115 REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 24 89.58 50.81 REMARK 500 THR A 33 32.43 -78.38 REMARK 500 VAL A 35 78.18 -68.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 17 0.16 SIDE CHAIN REMARK 500 ARG A 18 0.29 SIDE CHAIN REMARK 500 ARG A 38 0.23 SIDE CHAIN REMARK 500 ARG A 41 0.17 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BAL RELATED DB: PDB DBREF 1BBL A 2 51 UNP P07016 ODO2_ECOLI 103 152 SEQRES 1 A 51 TYR ALA SER LEU GLU GLU GLN ASN ASN ASP ALA LEU SER SEQRES 2 A 51 PRO ALA ILE ARG ARG LEU LEU ALA GLU HIS ASN LEU ASP SEQRES 3 A 51 ALA SER ALA ILE LYS GLY THR GLY VAL GLY GLY ARG LEU SEQRES 4 A 51 THR ARG GLU ASP VAL GLU LYS HIS LEU ALA LYS ALA HELIX 1 1 ALA A 15 HIS A 23 1 9 HELIX 2 2 ASP A 26 ILE A 30 5 5 HELIX 3 3 THR A 40 LEU A 48 1 9 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
Complete list - 16 202 Bytes