Header list of 1qjo.pdb file
Complete list - n 31 2 Bytes
HEADER DIHYDROLIPOAMIDE ACETYLTRANSFERASE 29-JUN-99 1QJO
TITLE INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHERICHIA
TITLE 2 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIPOAMIDE BINDING DOMAIN OF E2P;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BL21(DE3);
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 5 GENE: E2P_ECOLI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS DIHYDROLIPOAMIDE ACETYLTRANSFERASE, LIPOYL DOMAIN, PYRUVATE
KEYWDS 2 DEHYDROGENASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR D.D.JONES,M.J.HOWARD,R.N.PERHAM
REVDAT 5 31-JAN-18 1QJO 1 SOURCE JRNL REMARK
REVDAT 4 24-FEB-09 1QJO 1 VERSN
REVDAT 3 21-JUL-00 1QJO 1 JRNL
REVDAT 2 04-JUL-00 1QJO 1 JRNL
REVDAT 1 30-JUN-99 1QJO 0
JRNL AUTH D.D.JONES,K.M.STOTT,M.J.HOWARD,R.N.PERHAM
JRNL TITL RESTRICTED MOTION OF THE LIPOYL-LYSINE SWINGING ARM IN THE
JRNL TITL 2 PYRUVATE DEHYDROGENASE COMPLEX OF ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 39 8448 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10913250
JRNL DOI 10.1021/BI992978I
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.J.HOWARD,H.J.CHAUHAN,G.J.DOMINGO,C.FULLER,R.N.PERHAM
REMARK 1 TITL PROTEIN-PROTEIN INTERACTION REVEALED BY NMR T(2) RELAXATION
REMARK 1 TITL 2 EXPERIMENTS: THE LIPOYL DOMAIN AND E1 COMPONENT OF THE
REMARK 1 TITL 3 PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX OF BACILLUS
REMARK 1 TITL 4 STEAROTHERMOPHILUS
REMARK 1 REF J.MOL.BIOL. V. 295 1023 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 10656808
REMARK 1 DOI 10.1006/JMBI.1999.3391
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE N-TERMINAL MET IS AN ARTIFACT OF
REMARK 3 THE EXPRESSION SYSTEM USED AND NO RESTRAINTS WERE USED TO
REMARK 3 CALCULATE ITS PART IN THE STRUCTURE.
REMARK 4
REMARK 4 1QJO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1290001228.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20MM NAPI
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/ 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQFCOSY; HMQC
REMARK 210 -NOESY; HMQC-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG
REMARK 210 METHOD USED : XPLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 1 GLU A 75 CB GLU A 75 CG 0.118
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 ASP A 63 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 3 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 ASP A 63 CB - CG - OD2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 6 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 7 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 8 ASP A 26 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 9 ASP A 13 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 9 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 9 ASP A 40 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 10 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 10 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 10 PHE A 74 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 11 ASP A 13 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 11 ASP A 13 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 11 ASP A 26 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 11 ASP A 40 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 11 ASP A 40 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 11 ASP A 63 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 12 ASP A 13 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 12 ASP A 26 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 12 ASP A 40 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 13 ASP A 13 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 13 GLU A 14 OE1 - CD - OE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 13 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 14 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 15 ASP A 40 CB - CG - OD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 19 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 20 ASP A 13 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 21 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 22 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 22 GLU A 56 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 23 ASP A 40 CB - CG - OD2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 23 ASP A 63 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 23 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 24 ASP A 63 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 26 ASP A 40 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 27 ASP A 13 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 28 ASP A 63 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 29 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 29 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 29 ASP A 63 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 30 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 30 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 30 ASP A 63 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
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 1 PRO A 8 -90.72 -66.58
REMARK 500 1 ASP A 13 -106.33 -9.95
REMARK 500 1 GLU A 31 -16.54 60.49
REMARK 500 1 SER A 33 138.44 -36.57
REMARK 500 1 ASP A 40 -106.25 -111.02
REMARK 500 1 LYS A 58 52.54 -90.65
REMARK 500 1 SER A 69 132.92 -38.31
REMARK 500 1 ILE A 71 -63.99 -23.12
REMARK 500 1 VAL A 76 73.60 -60.30
REMARK 500 1 GLU A 77 -155.30 83.22
REMARK 500 1 ALA A 79 50.91 4.31
REMARK 500 2 VAL A 2 161.24 -48.91
REMARK 500 2 ALA A 30 173.83 -57.45
REMARK 500 2 GLU A 31 -18.67 62.79
REMARK 500 2 LEU A 34 -64.52 -92.77
REMARK 500 2 GLU A 38 -142.96 -131.49
REMARK 500 2 ASP A 40 58.06 28.61
REMARK 500 2 LYS A 41 -6.39 159.02
REMARK 500 2 ALA A 42 140.73 -179.27
REMARK 500 2 GLU A 77 82.25 -58.19
REMARK 500 2 ALA A 79 153.12 114.16
REMARK 500 3 VAL A 2 103.34 10.67
REMARK 500 3 ILE A 10 64.14 -53.49
REMARK 500 3 GLU A 14 149.17 41.40
REMARK 500 3 VAL A 24 91.95 -59.37
REMARK 500 3 ALA A 30 157.58 -44.05
REMARK 500 3 GLU A 31 -20.05 61.49
REMARK 500 3 LYS A 41 -6.83 -24.31
REMARK 500 3 LYS A 66 154.59 149.94
REMARK 500 3 THR A 67 103.59 -25.09
REMARK 500 3 ILE A 71 -58.25 -22.75
REMARK 500 3 VAL A 76 33.92 -54.39
REMARK 500 3 ALA A 79 -90.41 97.43
REMARK 500 4 VAL A 2 119.58 85.48
REMARK 500 4 VAL A 7 122.71 -20.75
REMARK 500 4 PRO A 8 -172.10 -65.36
REMARK 500 4 ASP A 9 45.08 -65.66
REMARK 500 4 ILE A 10 48.61 -80.25
REMARK 500 4 MET A 21 -51.69 -20.30
REMARK 500 4 VAL A 24 94.99 -54.24
REMARK 500 4 GLU A 31 -21.55 118.89
REMARK 500 4 LEU A 34 -57.25 -29.99
REMARK 500 4 ASP A 40 59.78 -3.94
REMARK 500 4 VAL A 76 56.27 -91.15
REMARK 500 4 GLU A 77 -173.27 66.26
REMARK 500 4 ALA A 79 -102.02 -156.73
REMARK 500 5 VAL A 2 123.88 -11.73
REMARK 500 5 ASP A 9 53.77 -69.20
REMARK 500 5 ILE A 10 21.14 -70.87
REMARK 500 5 ASP A 13 -74.02 -77.89
REMARK 500
REMARK 500 THIS ENTRY HAS 459 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DPC RELATED DB: PDB
DBREF 1QJO A 2 80 UNP P06959 ODP2_ECOLI 207 284
SEQRES 1 A 80 MET VAL LYS GLU VAL ASN VAL PRO ASP ILE GLY GLY ASP
SEQRES 2 A 80 GLU VAL GLU VAL THR GLU VAL MET VAL LYS VAL GLY ASP
SEQRES 3 A 80 LYS VAL ALA ALA GLU GLN SER LEU ILE THR VAL GLU GLY
SEQRES 4 A 80 ASP LYS ALA SER MET GLU VAL PRO ALA PRO PHE ALA GLY
SEQRES 5 A 80 VAL VAL LYS GLU LEU LYS VAL ASN VAL GLY ASP LYS VAL
SEQRES 6 A 80 LYS THR GLY SER LEU ILE MET ILE PHE GLU VAL GLU GLY
SEQRES 7 A 80 ALA ALA
SHEET 1 A 4 VAL A 2 ASN A 6 0
SHEET 2 A 4 LEU A 70 VAL A 76 -1 O MET A 72 N VAL A 5
SHEET 3 A 4 GLY A 52 LYS A 58 -1 O VAL A 53 N GLU A 75
SHEET 4 A 4 ASP A 26 VAL A 28 -1 O VAL A 28 N GLY A 52
SHEET 1 B 4 ALA A 42 PRO A 47 0
SHEET 2 B 4 LEU A 34 GLY A 39 -1 N LEU A 34 O VAL A 46
SHEET 3 B 4 VAL A 15 VAL A 20 -1 O GLU A 16 N GLU A 38
SHEET 4 B 4 ASP A 63 VAL A 65 -1 O VAL A 65 N VAL A 15
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
Complete list - n 31 2 Bytes