Header list of 1du2.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 13-JAN-00 1DU2
TITLE SOLUTION STRUCTURE OF THE THETA SUBUNIT OF DNA POLYMERASE III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE III;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THETA SUBUNIT;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCM869
KEYWDS DNA POLYMERASE, ALPHA HELIX, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.KENIRY,H.A.BERTHON,J.-Y.YANG,C.S.MILES,N.E.DIXON
REVDAT 4 16-FEB-22 1DU2 1 REMARK
REVDAT 3 24-FEB-09 1DU2 1 VERSN
REVDAT 2 01-APR-03 1DU2 1 JRNL
REVDAT 1 31-MAY-00 1DU2 0
JRNL AUTH M.A.KENIRY,H.A.BERTHON,J.Y.YANG,C.S.MILES,N.E.DIXON
JRNL TITL NMR SOLUTION STRUCTURE OF THE THETA SUBUNIT OF DNA
JRNL TITL 2 POLYMERASE III FROM ESCHERICHIA COLI.
JRNL REF PROTEIN SCI. V. 9 721 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 10794414
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.2 AND 6.1, SPSCAN 1.0.53, DYANA 1.5
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), GLASER (SPSCAN),
REMARK 3 GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 819
REMARK 3 RESTRAINTS, 511 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 300
REMARK 3 DIHEDRAL ANGLE RESTRAINTS AND 8 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS
REMARK 4
REMARK 4 1DU2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010367.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 0.03; 0.03; 0.03
REMARK 210 PRESSURE : AAMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM THETA SUBUNIT U-15N; 10 MM
REMARK 210 PHOSPHATE BUFFER PH 6.5;; 1 MM
REMARK 210 THETA SUBUNIT U-15N,13C; 10 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.5; 1 MM
REMARK 210 THETA SUBUNIT; 10 MM PHOSPHATE
REMARK 210 BUFFER PH 6.5;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; HNHA; HNHB; 3D_
REMARK 210 13C-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; VXRS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.10
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY DOUBLE AND TRIPLE
REMARK 210 RESONANCE HETERONUCLEAR NMR SPECTROSCOPY TECHNIQUES. THERE IS
REMARK 210 EVIDENCE OF SUBSTANTIAL CONFORMATIONAL EXCHANGE IN SECTIONS OF
REMARK 210 THE CHAIN THAT SEVERELY LIMIT THE PRECISION OF THE STRUCTURE IN
REMARK 210 THESE REGIONS OF THE MOLECULE. SPECIFICALLY, CONFORMATIONAL
REMARK 210 EXCHANGE OCCURS IN THE REGIONS D19-M33 AND L55-S63.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG A 53 H LEU A 56 1.50
REMARK 500 O GLU A 46 H ARG A 49 1.50
REMARK 500 O GLU A 12 H VAL A 16 1.51
REMARK 500 O PRO A 34 H ILE A 36 1.52
REMARK 500 O HIS A 47 H TRP A 51 1.53
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 LEU A 2 71.47 -168.07
REMARK 500 1 ALA A 6 93.25 63.94
REMARK 500 1 LEU A 8 107.26 163.69
REMARK 500 1 ASP A 9 49.02 -172.63
REMARK 500 1 ALA A 21 -78.78 -57.35
REMARK 500 1 VAL A 25 -79.00 -117.55
REMARK 500 1 LYS A 28 118.10 -177.43
REMARK 500 1 GLU A 29 -37.12 -33.75
REMARK 500 1 ARG A 30 -61.31 71.96
REMARK 500 1 ASN A 32 64.05 63.75
REMARK 500 1 VAL A 35 57.02 -67.53
REMARK 500 1 GLU A 43 -78.11 -90.73
REMARK 500 1 GLU A 54 -37.73 -33.41
REMARK 500 1 ARG A 55 -31.17 -39.44
REMARK 500 1 LEU A 56 69.34 -174.06
REMARK 500 1 ALA A 58 151.62 64.05
REMARK 500 1 HIS A 59 -76.60 70.70
REMARK 500 1 ARG A 60 168.90 68.44
REMARK 500 1 LEU A 61 158.57 66.08
REMARK 500 1 ALA A 62 -68.19 -159.94
REMARK 500 1 SER A 63 100.31 63.16
REMARK 500 1 SER A 67 118.48 60.32
REMARK 500 1 LEU A 69 83.10 69.85
REMARK 500 1 PRO A 70 -164.26 -74.98
REMARK 500 1 GLU A 72 156.26 -42.58
REMARK 500 1 LYS A 74 152.56 62.06
REMARK 500 1 LEU A 75 64.00 67.59
REMARK 500 2 LYS A 3 -167.46 -165.27
REMARK 500 2 ASN A 4 90.02 66.96
REMARK 500 2 ALA A 6 105.05 75.38
REMARK 500 2 LEU A 8 76.53 61.17
REMARK 500 2 ASP A 9 51.05 -166.75
REMARK 500 2 ALA A 22 -152.20 59.43
REMARK 500 2 ALA A 23 125.50 65.65
REMARK 500 2 ALA A 26 -34.51 -38.50
REMARK 500 2 PHE A 27 70.39 -153.67
REMARK 500 2 LYS A 28 18.12 -146.25
REMARK 500 2 VAL A 35 56.32 -69.08
REMARK 500 2 GLU A 43 -72.76 -82.88
REMARK 500 2 LEU A 48 -33.17 -38.50
REMARK 500 2 GLU A 54 -33.60 -34.42
REMARK 500 2 LEU A 56 63.32 66.39
REMARK 500 2 ALA A 58 -38.20 -37.35
REMARK 500 2 ARG A 60 126.61 -178.64
REMARK 500 2 ALA A 62 -67.09 -178.00
REMARK 500 2 SER A 63 76.31 63.25
REMARK 500 2 VAL A 64 -99.00 -113.55
REMARK 500 2 LEU A 66 94.83 78.85
REMARK 500 2 TYR A 71 -46.24 -131.01
REMARK 500 2 GLU A 72 93.46 54.12
REMARK 500
REMARK 500 THIS ENTRY HAS 496 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DU2 A 1 76 UNP P0ABS8 HOLE_ECOLI 1 76
SEQRES 1 A 76 MET LEU LYS ASN LEU ALA LYS LEU ASP GLN THR GLU MET
SEQRES 2 A 76 ASP LYS VAL ASN VAL ASP LEU ALA ALA ALA GLY VAL ALA
SEQRES 3 A 76 PHE LYS GLU ARG TYR ASN MET PRO VAL ILE ALA GLU ALA
SEQRES 4 A 76 VAL GLU ARG GLU GLN PRO GLU HIS LEU ARG SER TRP PHE
SEQRES 5 A 76 ARG GLU ARG LEU ILE ALA HIS ARG LEU ALA SER VAL ASN
SEQRES 6 A 76 LEU SER ARG LEU PRO TYR GLU PRO LYS LEU LYS
HELIX 1 1 GLN A 10 ALA A 22 1 13
HELIX 2 2 ALA A 37 GLN A 44 1 8
HELIX 3 3 GLU A 46 GLU A 54 1 9
HELIX 4 4 ARG A 55 ILE A 57 5 3
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
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