Header list of 1olg.pdb file
Complete list - 23 20 Bytes
HEADER ANTI-ONCOGENE 13-JUN-94 1OLG
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
TITLE 2 P53 BY MULTI-DIMENSIONAL NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ANTI-ONCOGENE
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 5 23-FEB-22 1OLG 1 REMARK
REVDAT 4 24-FEB-09 1OLG 1 VERSN
REVDAT 3 01-APR-03 1OLG 1 JRNL
REVDAT 2 08-MAR-95 1OLG 1 REMARK
REVDAT 1 26-JAN-95 1OLG 0
JRNL AUTH G.M.CLORE,J.G.OMICHINSKI,K.SAKAGUCHI,N.ZAMBRANO,H.SAKAMOTO,
JRNL AUTH 2 E.APPELLA,A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
JRNL TITL 2 P53 BY MULTIDIMENSIONAL NMR.
JRNL REF SCIENCE V. 265 386 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 8023159
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 THE 3D STRUCTURE OF THE OLIGOMERIZATION DOMAIN (RESIDUES
REMARK 3 319 - 360) OF P53 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED
REMARK 3 AND -FILTERED NMR IS BASED ON 3824 EXPERIMENTAL RESTRAINTS
REMARK 3 COMPRISING THE FOLLOWING INTRA- AND INTER-SUBUNIT
REMARK 3 RESTRAINTS: (A) INTRASUBUNIT: 840 SEQUENTIAL (|I-J|=1),
REMARK 3 744 SHORT RANGE (1 < |I-J| >=5) AND 72 LONG RANGE
REMARK 3 (|I-J| >5) INTERRESIDUES AND INTRARESIDUE APPROXIMATE
REMARK 3 INTERPROTON DISTANCE RESTRAINTS, 136 DISTANCE RESTRAINTS
REMARK 3 FOR 68 HYDROGEN BONDS, 268 TORSION ANGLE (144 PHI, 104 CHI1
REMARK 3 AND 20 CHI2) RESTRAINTS, AND 144 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS. (B) INTERSUBUNIT: 72 A-B/C-D,
REMARK 3 758 A-C/B-D, 10 A-D/B-C APPROXIMATE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS, AND 24 DISTANCE RESTRAINTS FOR 12 HYDROGEN
REMARK 3 BONDS INVOLVING THE A-C/B-D SUBUNITS. IN ADDITION, THERE
REMARK 3 ARE A TOTAL OF 38 CALPHA AND 38 CB CHEMICAL SHIFT
REMARK 3 RESTRAINTS PER SUBUNIT THAT HAVE BEEN INCORPORATED
REMARK 3 INTO THE REFINEMENT [J. KUSZWESKI, J. QIN, A.M. GRONENBORN
REMARK 3 AND G.M. CLORE, J. MAGN RESON. SER IN PRESS (1994)]
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. AND
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT. 29, 317-324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE JRNL REFERENCE.
REMARK 3
REMARK 3 THE STRUCTURE PRESENTED IN THIS ENTRY IS THE RESTRAINED
REMARK 3 MINIMIZED AVERAGE STRUCTURE (SA)R. THIS IS OBTAINED BY
REMARK 3 FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 35
REMARK 3 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO
REMARK 3 RESIDUES 324 - 356 OF ALL FOUR SUBUNITS AND SUBJECTING THE
REMARK 3 RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE
REMARK 3 QUANTITY PRESENTED IN COLUMNS 61 - 66 IN THIS SET OF
REMARK 3 COORDINATES (THE B-FACTOR FIELD IN X-RAY STRUCTURES) GIVES
REMARK 3 THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA
REMARK 3 STRUCTURES AND THE MEAN STRUCTURE. THE NUMBERS IN COLUMNS
REMARK 3 61 - 66 OF THE INDIVIDUAL STRUCTURES HAVE NO MEANING. NOTE
REMARK 3 THAT RESIDUES 319 - 323 AT THE N-TERMINUS AND RESIDUES 357
REMARK 3 - 360 AT THE C-TERMINUS ARE DISORDERED. THE SET OF 35
REMARK 3 STRUCTURES IS PRESENTED IN PROTEIN DATA BANK ENTRY 1OLH.
REMARK 4
REMARK 4 1OLG 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_1000175466.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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: 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 LYS A 320 -74.36 68.94
REMARK 500 LYS A 321 135.74 67.72
REMARK 500 GLU A 326 -174.99 -58.70
REMARK 500 PHE A 328 -165.33 -112.87
REMARK 500 LYS B 320 -74.65 69.83
REMARK 500 LYS B 321 135.74 67.89
REMARK 500 GLU B 326 -175.08 -59.01
REMARK 500 PHE B 328 -165.39 -113.04
REMARK 500 LYS C 320 116.35 57.32
REMARK 500 LYS C 321 -127.71 -161.07
REMARK 500 PRO C 322 -137.97 -40.58
REMARK 500 GLU C 326 -173.91 -57.97
REMARK 500 PHE C 328 -162.84 -113.14
REMARK 500 LYS D 320 -75.43 69.86
REMARK 500 LYS D 321 135.67 68.29
REMARK 500 GLU D 326 -174.99 -58.62
REMARK 500 PHE D 328 -165.46 -112.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OLH RELATED DB: PDB
DBREF 1OLG A 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1OLG B 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1OLG C 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1OLG D 319 360 UNP P04637 P53_HUMAN 319 360
SEQRES 1 A 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 A 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 A 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 A 42 GLU PRO GLY
SEQRES 1 B 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 B 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 B 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 B 42 GLU PRO GLY
SEQRES 1 C 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 C 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 C 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 C 42 GLU PRO GLY
SEQRES 1 D 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 D 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 D 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 D 42 GLU PRO GLY
HELIX 1 1 GLY A 334 GLY A 356 1 23
HELIX 2 2 GLY B 334 GLY B 356 1 23
HELIX 3 3 GLY C 334 GLY C 356 1 23
HELIX 4 4 GLY D 334 GLY D 356 1 23
SHEET 1 A 2 TYR A 327 ARG A 333 0
SHEET 2 A 2 TYR C 327 ARG C 333 -1 N PHE C 328 O ILE A 332
SHEET 1 B 2 TYR B 327 ARG B 333 0
SHEET 2 B 2 TYR D 327 ARG D 333 -1 N PHE D 328 O ILE B 332
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 - 23 20 Bytes