Header list of 1lab.pdb file
Complete list - v 29 2 Bytes
HEADER TRANSFERASE (ACYLTRANSFERASE) 02-SEP-92 1LAB
TITLE THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS
TITLE 2 STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.1.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 GENE: BACILLUS STEAROTHERMOPHILUS;
SOURCE 5 EXPRESSION_SYSTEM_GENE: BACILLUS STEAROTHERMOPHILUS
KEYWDS TRANSFERASE (ACYLTRANSFERASE)
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR F.DARDEL,A.L.DAVIS,E.D.LAUE,R.N.PERHAM
REVDAT 4 29-NOV-17 1LAB 1 REMARK HELIX
REVDAT 3 24-FEB-09 1LAB 1 VERSN
REVDAT 2 15-OCT-94 1LAB 1 COMPND SOURCE
REVDAT 1 15-JUL-93 1LAB 0
JRNL AUTH F.DARDEL,A.L.DAVIS,E.D.LAUE,R.N.PERHAM
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM
JRNL TITL 2 BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE
JRNL TITL 3 MULTIENZYME COMPLEX.
JRNL REF J.MOL.BIOL. V. 229 1037 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8445635
JRNL DOI 10.1006/JMBI.1993.1103
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.DARDEL,E.D.LAUE,R.N.PERHAM
REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 OF THE LIPOYL DOMAIN OF THE BACILLUS STEAROTHERMOPHILUS
REMARK 1 TITL 3 PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
REMARK 1 REF EUR.J.BIOCHEM. V. 201 203 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LAB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174627.
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 : 11
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 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 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 1 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 GLU A 28 OE1 - CD - OE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 2 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 VAL A 34 CG1 - CB - CG2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 2 VAL A 34 CA - C - N ANGL. DEV. = -14.8 DEGREES
REMARK 500 2 CYS A 36 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 2 ASP A 76 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 ASP A 76 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 PHE A 2 N - CA - C ANGL. DEV. = -22.0 DEGREES
REMARK 500 3 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 3 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 GLU A 31 N - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 3 GLU A 31 CA - C - O ANGL. DEV. = 13.2 DEGREES
REMARK 500 3 GLU A 31 CA - C - N ANGL. DEV. = -23.1 DEGREES
REMARK 500 3 GLU A 31 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 3 ASP A 32 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 3 ASP A 32 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 3 GLU A 37 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 3 ILE A 58 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 3 VAL A 68 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 4 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 4 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 4 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 ASN A 30 CA - C - N ANGL. DEV. = -14.5 DEGREES
REMARK 500 4 GLU A 31 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 4 GLU A 31 N - CA - C ANGL. DEV. = 40.8 DEGREES
REMARK 500 4 GLU A 31 CA - C - O ANGL. DEV. = 13.2 DEGREES
REMARK 500 4 GLU A 31 CA - C - N ANGL. DEV. = -24.0 DEGREES
REMARK 500 4 GLU A 31 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 4 ASP A 32 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 4 VAL A 55 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 4 ILE A 58 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 4 VAL A 68 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 5 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 5 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 5 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 5 GLU A 31 OE1 - CD - OE2 ANGL. DEV. = -40.1 DEGREES
REMARK 500 5 GLU A 31 CG - CD - OE1 ANGL. DEV. = 47.5 DEGREES
REMARK 500 5 GLU A 31 CG - CD - OE2 ANGL. DEV. = -35.7 DEGREES
REMARK 500 5 GLU A 37 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 5 ILE A 47 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 5 ILE A 58 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 5 GLY A 69 N - CA - C ANGL. DEV. = -16.0 DEGREES
REMARK 500 5 TYR A 80 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 6 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 6 ASN A 30 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 97 ANGLE DEVIATIONS.
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 GLU A 3 -160.97 -117.81
REMARK 500 1 PRO A 7 80.93 -42.48
REMARK 500 1 ASP A 8 -72.64 -121.70
REMARK 500 1 ILE A 9 40.58 37.41
REMARK 500 1 VAL A 19 -61.76 -93.85
REMARK 500 1 PRO A 25 174.79 -8.61
REMARK 500 1 ASP A 27 -85.24 8.79
REMARK 500 1 ASP A 32 -55.22 -177.34
REMARK 500 1 ASP A 33 -137.74 18.13
REMARK 500 1 ASP A 41 -72.43 -7.58
REMARK 500 1 PRO A 48 -167.09 -62.93
REMARK 500 1 LEU A 56 -79.20 -38.06
REMARK 500 1 VAL A 60 75.92 -113.62
REMARK 500 1 PRO A 61 -83.53 -49.76
REMARK 500 1 THR A 67 -155.45 -117.87
REMARK 500 1 LEU A 72 -67.19 -135.23
REMARK 500 1 PRO A 78 68.34 -53.09
REMARK 500 2 PRO A 7 82.04 -66.12
REMARK 500 2 ASP A 8 -80.68 -123.87
REMARK 500 2 ILE A 9 26.13 41.96
REMARK 500 2 PRO A 25 162.82 -39.17
REMARK 500 2 ASP A 27 -100.94 11.79
REMARK 500 2 ASP A 32 28.32 -175.93
REMARK 500 2 LEU A 35 -160.21 -106.13
REMARK 500 2 ASP A 41 -67.25 -6.73
REMARK 500 2 ALA A 43 -168.57 -102.75
REMARK 500 2 ILE A 47 79.54 -117.20
REMARK 500 2 PRO A 48 -166.01 -62.29
REMARK 500 2 LEU A 56 -76.88 -29.10
REMARK 500 2 VAL A 60 67.96 -117.93
REMARK 500 2 PRO A 61 -78.08 -41.93
REMARK 500 2 THR A 67 -151.70 -99.84
REMARK 500 2 LEU A 72 -70.44 -139.90
REMARK 500 3 PRO A 7 89.19 -56.31
REMARK 500 3 ASP A 8 -82.05 -122.45
REMARK 500 3 ILE A 9 37.00 36.80
REMARK 500 3 HIS A 14 -51.88 -131.90
REMARK 500 3 GLU A 31 78.74 47.26
REMARK 500 3 ASP A 32 31.50 -155.43
REMARK 500 3 ASP A 33 -168.70 -117.22
REMARK 500 3 LEU A 35 -84.85 -125.54
REMARK 500 3 ASP A 41 -59.49 -3.78
REMARK 500 3 GLU A 46 -73.32 -120.50
REMARK 500 3 LEU A 56 -76.02 -30.48
REMARK 500 3 VAL A 60 79.97 -119.71
REMARK 500 3 PRO A 61 -107.66 -34.80
REMARK 500 3 THR A 67 -144.78 -116.87
REMARK 500 3 LEU A 72 -66.84 -145.99
REMARK 500 3 ALA A 77 -49.95 -140.79
REMARK 500 4 PHE A 2 102.96 16.37
REMARK 500
REMARK 500 THIS ENTRY HAS 181 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 24 PRO A 25 1 -70.90
REMARK 500 ILE A 47 PRO A 48 3 82.65
REMARK 500 ILE A 47 PRO A 48 4 90.04
REMARK 500 LEU A 6 PRO A 7 5 148.03
REMARK 500 ALA A 77 PRO A 78 5 -143.90
REMARK 500 ILE A 47 PRO A 48 6 83.39
REMARK 500 LEU A 6 PRO A 7 7 148.60
REMARK 500 ILE A 47 PRO A 48 7 84.30
REMARK 500 LYS A 24 PRO A 25 8 -60.08
REMARK 500 ALA A 77 PRO A 78 8 -62.64
REMARK 500 ILE A 47 PRO A 48 9 87.58
REMARK 500 LEU A 6 PRO A 7 11 145.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LIP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LAC RELATED DB: PDB
DBREF 1LAB A 1 80 UNP P11961 ODP2_BACST 1 80
SEQRES 1 A 80 ALA PHE GLU PHE LYS LEU PRO ASP ILE GLY GLU GLY ILE
SEQRES 2 A 80 HIS GLU GLY GLU ILE VAL LYS TRP PHE VAL LYS PRO GLY
SEQRES 3 A 80 ASP GLU VAL ASN GLU ASP ASP VAL LEU CYS GLU VAL GLN
SEQRES 4 A 80 ASN ASP LYS ALA VAL VAL GLU ILE PRO SER PRO VAL LYS
SEQRES 5 A 80 GLY LYS VAL LEU GLU ILE LEU VAL PRO GLU GLY THR VAL
SEQRES 6 A 80 ALA THR VAL GLY GLN THR LEU ILE THR LEU ASP ALA PRO
SEQRES 7 A 80 GLY TYR
SHEET 1 A 4 ALA A 1 PHE A 4 0
SHEET 2 A 4 ILE A 73 PRO A 78 -1
SHEET 3 A 4 GLY A 53 LEU A 59 -1
SHEET 4 A 4 ASP A 27 VAL A 29 -1
SHEET 1 B 4 ALA A 43 ILE A 47 0
SHEET 2 B 4 CYS A 36 ASN A 40 -1
SHEET 3 B 4 GLU A 15 VAL A 19 -1
SHEET 4 B 4 GLY A 63 VAL A 68 -1
CISPEP 1 LYS A 24 PRO A 25 2 13.21
CISPEP 2 ALA A 77 PRO A 78 2 -22.73
CISPEP 3 ALA A 77 PRO A 78 3 -22.09
CISPEP 4 LYS A 24 PRO A 25 10 29.71
CISPEP 5 ALA A 77 PRO A 78 10 -24.56
SITE 1 LIP 1 LYS A 42
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 - v 29 2 Bytes