HEADER ANTI-ONCOGENE 12-MAR-95 1SAF
TITLE HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN
TITLE 2 OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR SUPPRESSOR P53;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 OTHER_DETAILS: SAD STRUCTURES
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
NUMMDL 76
AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 4 11-JAN-12 1SAF 1 VERSN
REVDAT 3 24-FEB-09 1SAF 1 VERSN
REVDAT 2 01-APR-03 1SAF 1 JRNL
REVDAT 1 15-OCT-95 1SAF 0
SPRSDE 01-JUL-08 1SAF 1SAJ
JRNL AUTH G.M.CLORE,J.ERNST,R.CLUBB,J.G.OMICHINSKI,W.M.KENNEDY,
JRNL AUTH 2 K.SAKAGUCHI,E.APPELLA,A.M.GRONENBORN
JRNL TITL REFINED SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
JRNL TITL 2 THE TUMOUR SUPPRESSOR P53.
JRNL REF NAT.STRUCT.BIOL. V. 2 321 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7796267
JRNL DOI 10.1038/NSB0495-321
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.CLORE,J.G.OMICHINSKI,K.SAKAGUCHI,N.ZAMBRANO,H.SAKAMOTO,
REMARK 1 AUTH 2 E.APPELLA,A.M.GRONENBORN
REMARK 1 TITL INTERHELICAL ANGLES IN THE SOLUTION STRUCTURE OF THE
REMARK 1 TITL 2 OLIGOMERIZATION DOMAIN OF P53: CORRECTION
REMARK 1 REF SCIENCE V. 267 1515 1995
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.M.CLORE,J.G.OMICHINSKI,K.SAKAGUCHI,N.ZAMBRANO,H.SAKAMOTO,
REMARK 1 AUTH 2 E.APPELLA,A.M.GRONENBORN
REMARK 1 TITL HIGH-RESOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
REMARK 1 TITL 2 P53 BY MULTIDIMENSIONAL NMR
REMARK 1 REF SCIENCE V. 265 386 1994
REMARK 1 REFN ISSN 0036-8075
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 4472 EXPERIMENTAL RESTRAINTS
REMARK 3 COMPRISING THE FOLLOWING INTRA- AND INTER-SUBUNIT
REMARK 3 RESTRAINTS:
REMARK 3
REMARK 3 (A) INTRASUBUNIT: 852 SEQUENTIAL (|I-J|=1), 712 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 76 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES AND 740 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, 136 DISTANCE RESTRAINTS FOR 68
REMARK 3 HYDROGEN BONDS, 284 TORSION ANGLE (144 PHI, 104 CHI1, AND
REMARK 3 36 CHI2) RESTRAINTS, AND 144 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS.
REMARK 3
REMARK 3 (B) INTERSUBUNIT: 244 A-B/C-D, 876 A-C/B-D, 40 A-D/B-C
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS, 40 DISTANCE
REMARK 3 RESTRAINTS FOR 20 HYDROGEN BONDS INVOLVING THE A-C/B-D
REMARK 3 SUBUNITS, AND 36 DISTANCE RESTRAINTS FOR 4 WATER MOLECULES.
REMARK 3 IN ADDITION, THERE ARE A TOTAL OF 38 CALPHA AND 35 CB
REMARK 3 CHEMICAL SHIFT RESTRAINTS PER SUBUNIT THAT HAVE BEEN
REMARK 3 INCORPORATED INTO THE REFINEMENT [J. KUSZWESKI, J. QIN,
REMARK 3 A.M. GRONENBORN AND G.M. CLORE, J. MAGN RESON. SER B 106,
REMARK 3 92-96 (1995)].
REMARK 3
REMARK 3 THE 76 STRUCTURES PRESENTED IN PDB ENTRIES 1SAF, 1SAH, AND
REMARK 3 1SAJ ARE CALCULATED WITH THE FOLLOWING VALUES FOR THE HARD
REMARK 3 SPHERE EFFECTIVE VAN DER WAALS RADII USED IN QUARTIC VAN
REMARK 3 DER WAALS REPULSION TERM. IN THE SOURCE REFERENCE, THESE
REMARK 3 STRUCTURES ARE REFERRED TO AS <SAD>. H(POLAR) = 0.95
REMARK 3 ANGSTROMS, H (NON-POLAR) = 1.00 ANGSTROMS, N = 1.30
REMARK 3 ANGSTROMS, C = 1.40 ANGSTROMS, C(AROMATIC) = 1.35
REMARK 3 ANGSTROMS, O = 1.20 ANGSTROMS, AND S = 1.60 ANGSTROMS.
REMARK 3 THESE VALUES CORRESPOND TO THE HARD SPHERE EFFECTIVE VAN
REMARK 3 DER WAALS RADII EMPLOYED BY THE PROGRAMS DISMAN AND DIANA.
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. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT. 229, 317-324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE SOURCE REFERENCE.
REMARK 3
REMARK 3 ENTRY 1SAL CONTAINS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE
REMARK 3 COORDINATES OF THE INDIVIDUAL 76 DYNAMICAL SIMULATED
REMARK 3 ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 326 - 354
REMARK 3 OF ALL FOUR SUBUNITS, AND SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION. THE QUANTITY
REMARK 3 PRESENTED IN COLUMNS 61 - 66 IN THIS SET OF COORDINATES
REMARK 3 (THE B-FACTOR COLUMN IN X-RAY STRUCTURES) GIVES THE
REMARK 3 AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES
REMARK 3 AND THE MEAN STRUCTURE. THE NUMBERS IN COLUMNS 61 - 66 OF
REMARK 3 THE INDIVIDUAL STRUCTURES HAVE NO MEANING. NOTE THAT
REMARK 3 RESIDUES 319 - 323 AT THE N-TERMINUS AND RESIDUES 357 - 360
REMARK 3 AT THE C-TERMINUS ARE COMPLETELY DISORDERED.
REMARK 4
REMARK 4 1SAF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : 76
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 1 LYS A 320 -168.10 58.45
REMARK 500 1 LYS A 321 82.55 42.00
REMARK 500 1 PRO A 322 -82.15 -62.33
REMARK 500 1 LYS B 320 -168.11 58.55
REMARK 500 1 LYS B 321 82.67 41.97
REMARK 500 1 PRO B 322 -82.20 -62.46
REMARK 500 1 LYS C 320 -168.03 58.50
REMARK 500 1 LYS C 321 82.58 41.94
REMARK 500 1 PRO C 322 -82.17 -62.45
REMARK 500 1 LYS D 320 -168.05 58.34
REMARK 500 1 LYS D 321 82.57 42.02
REMARK 500 1 PRO D 322 -82.20 -62.43
REMARK 500 2 LYS A 320 -89.95 58.26
REMARK 500 2 LYS A 321 87.86 60.76
REMARK 500 2 PRO A 322 -151.81 -59.04
REMARK 500 2 ASP A 324 -164.43 -79.69
REMARK 500 2 GLU A 358 159.94 -49.39
REMARK 500 2 LYS B 320 -89.88 58.16
REMARK 500 2 LYS B 321 87.83 60.80
REMARK 500 2 PRO B 322 -151.81 -59.06
REMARK 500 2 ASP B 324 -164.36 -79.66
REMARK 500 2 GLU B 358 159.91 -49.38
REMARK 500 2 LYS C 320 -89.83 58.17
REMARK 500 2 LYS C 321 87.83 60.76
REMARK 500 2 PRO C 322 -151.74 -59.11
REMARK 500 2 ASP C 324 -164.42 -79.78
REMARK 500 2 GLU C 358 159.91 -49.51
REMARK 500 2 LYS D 320 -89.93 58.24
REMARK 500 2 LYS D 321 87.90 60.79
REMARK 500 2 PRO D 322 -151.72 -59.08
REMARK 500 2 ASP D 324 -164.39 -79.76
REMARK 500 2 GLU D 358 159.87 -49.49
REMARK 500 3 LYS A 320 -87.88 60.53
REMARK 500 3 LYS A 321 80.69 65.50
REMARK 500 3 PRO A 322 85.25 -61.19
REMARK 500 3 PRO A 359 -80.99 -62.98
REMARK 500 3 LYS B 320 -87.80 60.41
REMARK 500 3 LYS B 321 80.68 65.51
REMARK 500 3 PRO B 322 85.30 -61.27
REMARK 500 3 PRO B 359 -81.17 -63.03
REMARK 500 3 LYS C 320 -87.86 60.50
REMARK 500 3 LYS C 321 80.67 65.60
REMARK 500 3 PRO C 322 85.21 -61.19
REMARK 500 3 PRO C 359 -81.08 -63.01
REMARK 500 3 LYS D 320 -87.93 60.48
REMARK 500 3 LYS D 321 80.73 65.50
REMARK 500 3 PRO D 322 85.20 -61.28
REMARK 500 3 PRO D 359 -81.00 -62.96
REMARK 500 4 LYS A 321 143.08 61.06
REMARK 500 4 PRO A 322 -82.60 -64.17
REMARK 500
REMARK 500 THIS ENTRY HAS 1131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SAL RELATED DB: PDB
DBREF 1SAF A 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1SAF B 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1SAF C 319 360 UNP P04637 P53_HUMAN 319 360
DBREF 1SAF 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
FORMUL 5 HOH *4(H2 O)
HELIX 1 1 ARG A 335 ALA A 355 1 21
HELIX 2 2 ARG B 335 ALA B 355 1 21
HELIX 3 3 ARG C 335 ALA C 355 1 21
HELIX 4 4 ARG D 335 ALA D 355 1 21
SHEET 1 A 2 TYR A 327 ARG A 333 0
SHEET 2 A 2 TYR C 327 ARG C 333 -1 N ILE C 332 O PHE A 328
SHEET 1 B 2 TYR B 327 ARG B 333 0
SHEET 2 B 2 TYR D 327 ARG D 333 -1 N ILE D 332 O PHE B 328
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
(ATOM LINES ARE NOT SHOWN.)
END