HEADER DNA-BINDING PROTEIN 19-SEP-03 1UOL
TITLE CRYSTAL STRUCTURE OF THE HUMAN P53 CORE DOMAIN MUTANT
TITLE 2 M133L/V203A/N239Y/N268D AT 1.9 A RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DNA BINDING (CORE) DOMAIN, RESIDUES 94-312;
COMPND 5 SYNONYM: TUMOR SUPPRESSOR P53, PHOSPHOPROTEIN P53, ANTIGEN
COMPND 6 NY-CO-13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA-BINDING PROTEIN, P53, DNA-BINDING DOMAIN, TUMOR
KEYWDS 2 SUPPRESSOR, SECOND-SITE SUPPRESSOR MUTATION, SUPERSTABLE
KEYWDS 3 MUTANT, APOPTOSIS, TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.JOERGER,M.D.ALLEN,A.R.FERSHT
REVDAT 3 24-FEB-09 1UOL 1 VERSN
REVDAT 2 26-MAY-05 1UOL 1 JRNL REMARK HET LINK
REVDAT 2 2 HETATM
REVDAT 1 16-OCT-03 1UOL 0
JRNL AUTH A.C.JOERGER,M.D.ALLEN,A.R.FERSHT
JRNL TITL CRYSTAL STRUCTURE OF A SUPERSTABLE MUTANT OF HUMAN
JRNL TITL 2 P53 CORE DOMAIN. INSIGHTS INTO THE MECHANISM OF
JRNL TITL 3 RESCUING ONCOGENIC MUTATIONS
JRNL REF J.BIOL.CHEM. V. 279 1291 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14534297
JRNL DOI 10.1074/JBC.M309732200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.NIKOLOVA,J.HENKEL,D.P.LANE,A.R.FERSHT
REMARK 1 TITL SEMIRATIONAL DESIGN OF ACTIVE TUMOR SUPPRESSOR P53
REMARK 1 TITL 2 DNA BINDING DOMAIN WITH ENHANCED STABILITY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 14675 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 9843948
REMARK 1 DOI 10.1073/PNAS.95.25.14675
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.CHO,S.GORINA,P.D.JEFFREY,N.P.PAVLETICH
REMARK 1 TITL CRYSTAL STRUCTURE OF A P53 TUMOR SUPPRESSOR-DNA
REMARK 1 TITL 2 COMPLEX: UNDERSTANDING TUMORIGENIC MUTATIONS
REMARK 1 REF SCIENCE V. 265 346 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 8023157
REMARK 1 DOI 10.1126/SCIENCE.8023157
REMARK 2
REMARK 2 RESOLUTION. 1.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.9
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.6
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 38078
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3072
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 391
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UOL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-03.
REMARK 100 THE PDBE ID CODE IS EBI-13352.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38078
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 35.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION MET 133 LEU, VAL 203 ALA, ASN 239 TYR
REMARK 400 AND ASN 268 ASP IN CHAINS A AND B
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 94
REMARK 465 SER A 95
REMARK 465 LYS A 291
REMARK 465 LYS A 292
REMARK 465 GLY A 293
REMARK 465 GLU A 294
REMARK 465 PRO A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 GLU A 298
REMARK 465 LEU A 299
REMARK 465 PRO A 300
REMARK 465 PRO A 301
REMARK 465 GLY A 302
REMARK 465 SER A 303
REMARK 465 THR A 304
REMARK 465 LYS A 305
REMARK 465 ARG A 306
REMARK 465 ALA A 307
REMARK 465 LEU A 308
REMARK 465 PRO A 309
REMARK 465 ASN A 310
REMARK 465 ASN A 311
REMARK 465 THR A 312
REMARK 465 SER B 94
REMARK 465 SER B 95
REMARK 465 LYS B 291
REMARK 465 LYS B 292
REMARK 465 GLY B 293
REMARK 465 GLU B 294
REMARK 465 PRO B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 GLU B 298
REMARK 465 LEU B 299
REMARK 465 PRO B 300
REMARK 465 PRO B 301
REMARK 465 GLY B 302
REMARK 465 SER B 303
REMARK 465 THR B 304
REMARK 465 LYS B 305
REMARK 465 ARG B 306
REMARK 465 ALA B 307
REMARK 465 LEU B 308
REMARK 465 PRO B 309
REMARK 465 ASN B 310
REMARK 465 ASN B 311
REMARK 465 THR B 312
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 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 B 120 -14.75 -49.63
REMARK 500 ALA B 138 18.20 56.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 179 ND1
REMARK 620 2 CYS A 176 SG 107.0
REMARK 620 3 CYS A 238 SG 106.7 109.6
REMARK 620 4 CYS A 242 SG 106.8 109.4 116.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 179 ND1
REMARK 620 2 CYS B 238 SG 107.7
REMARK 620 3 CYS B 176 SG 104.2 108.5
REMARK 620 4 CYS B 242 SG 106.3 118.2 111.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A1U RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE DETERMINATION OF A P53
REMARK 900 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED
REMARK 900 AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1AIE RELATED DB: PDB
REMARK 900 P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1DT7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE C-TERMINAL
REMARK 900 NEGATIVE REGULATORY DOMAIN OF P53 IN A
REMARK 900 COMPLEX WITH CA2+-BOUND S100B(BB)
REMARK 900 RELATED ID: 1GZH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BRCT DOMAINS OF
REMARK 900 HUMAN 53BP1 BOUND TO THE P53 TUMOR
REMARK 900 SUPRESSOR
REMARK 900 RELATED ID: 1H26 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P53
REMARK 900 RELATED ID: 1HS5 RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER
REMARK 900 RELATED ID: 1KZY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 53BP1 BRCT REGION
REMARK 900 COMPLEXED TOTUMOR SUPPRESSOR P53
REMARK 900 RELATED ID: 1MA3 RELATED DB: PDB
REMARK 900 STRUCTURE OF A SIR2 ENZYME BOUND TO AN
REMARK 900 ACETYLATED P53PEPTIDE
REMARK 900 RELATED ID: 1OLG RELATED DB: PDB
REMARK 900 P53 (OLIGOMERIZATION DOMAIN) (NMR, MINIMIZED
REMARK 900 AVERAGE STRUCTURE)
REMARK 900 RELATED ID: 1OLH RELATED DB: PDB
REMARK 900 P53 (OLIGOMERIZATION DOMAIN) (NMR, 35
REMARK 900 STRUCTURES)
REMARK 900 RELATED ID: 1PES RELATED DB: PDB
REMARK 900 TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN)
REMARK 900 (P53TET) (NMR, MINIMIZED AVERAGE STRUCTURE)
REMARK 900 RELATED ID: 1PET RELATED DB: PDB
REMARK 900 TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN)
REMARK 900 (P53TET) (NMR, 19 STRUCTURES)
REMARK 900 RELATED ID: 1SAE RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAC STRUCTURES)
REMARK 900 RELATED ID: 1SAF RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAD STRUCTURES)
REMARK 900 RELATED ID: 1SAG RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAC STRUCTURES)
REMARK 900 RELATED ID: 1SAH RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAD STRUCTURES)
REMARK 900 RELATED ID: 1SAI RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAC STRUCTURES)
REMARK 900 RELATED ID: 1SAJ RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAD STRUCTURES)
REMARK 900 RELATED ID: 1SAK RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAC STRUCTURES)
REMARK 900 RELATED ID: 1SAL RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAD STRUCTURES)
REMARK 900 RELATED ID: 1TSR RELATED DB: PDB
REMARK 900 P53 CORE DOMAIN IN COMPLEX WITH
REMARK 900 DEOXYRIBONUCLEIC ACID
REMARK 900 RELATED ID: 1TUP RELATED DB: PDB
REMARK 900 TUMOR SUPPRESSOR P53 COMPLEXED WITH
REMARK 900 DEOXYRIBONUCLEIC ACID
REMARK 900 RELATED ID: 1YCQ RELATED DB: PDB
REMARK 900 XENOPUS LAEVIS MDM2 BOUND TO THE
REMARK 900 TRANSACTIVATION DOMAIN OF HUMAN P53
REMARK 900 RELATED ID: 1YCR RELATED DB: PDB
REMARK 900 MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF
REMARK 900 P53
REMARK 900 RELATED ID: 1YCS RELATED DB: PDB
REMARK 900 P53-53BP2 COMPLEX
REMARK 900 RELATED ID: 3SAK RELATED DB: PDB
REMARK 900 HIGH RESOLUTION SOLUTION NMR STRUCTURE OF
REMARK 900 THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-
REMARK 900 DIMENSIONAL NMR (SAC STRUCTURES)
DBREF 1UOL A 94 312 UNP P04637 P53_HUMAN 94 312
DBREF 1UOL B 94 312 UNP P04637 P53_HUMAN 94 312
SEQADV 1UOL LEU A 133 UNP P04637 MET 133 ENGINEERED MUTATION
SEQADV 1UOL ALA A 203 UNP P04637 VAL 203 ENGINEERED MUTATION
SEQADV 1UOL TYR A 239 UNP P04637 ASN 239 ENGINEERED MUTATION
SEQADV 1UOL ASP A 268 UNP P04637 ASN 268 ENGINEERED MUTATION
SEQADV 1UOL LEU B 133 UNP P04637 MET 133 ENGINEERED MUTATION
SEQADV 1UOL ALA B 203 UNP P04637 VAL 203 ENGINEERED MUTATION
SEQADV 1UOL TYR B 239 UNP P04637 ASN 239 ENGINEERED MUTATION
SEQADV 1UOL ASP B 268 UNP P04637 ASN 268 ENGINEERED MUTATION
SEQRES 1 A 219 SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER
SEQRES 2 A 219 TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA
SEQRES 3 A 219 LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS
SEQRES 4 A 219 LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU
SEQRES 5 A 219 TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG
SEQRES 6 A 219 ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU
SEQRES 7 A 219 VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP
SEQRES 8 A 219 SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL
SEQRES 9 A 219 GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN
SEQRES 10 A 219 THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO
SEQRES 11 A 219 GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR
SEQRES 12 A 219 MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG
SEQRES 13 A 219 PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY
SEQRES 14 A 219 ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS
SEQRES 15 A 219 ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN
SEQRES 16 A 219 LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO
SEQRES 17 A 219 GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR
SEQRES 1 B 219 SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER
SEQRES 2 B 219 TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA
SEQRES 3 B 219 LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS
SEQRES 4 B 219 LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU
SEQRES 5 B 219 TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG
SEQRES 6 B 219 ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU
SEQRES 7 B 219 VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP
SEQRES 8 B 219 SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL
SEQRES 9 B 219 GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN
SEQRES 10 B 219 THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO
SEQRES 11 B 219 GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR
SEQRES 12 B 219 MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG
SEQRES 13 B 219 PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY
SEQRES 14 B 219 ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS
SEQRES 15 B 219 ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN
SEQRES 16 B 219 LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO
SEQRES 17 B 219 GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR
HET ZN A1300 1
HET ZN B1300 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *391(H2 O1)
HELIX 1 1 HIS A 178 CYS A 182 5 5
HELIX 2 2 CYS A 277 ARG A 290 1 14
HELIX 3 3 HIS B 178 CYS B 182 5 5
HELIX 4 4 CYS B 277 ARG B 290 1 14
SHEET 1 AA 4 ARG A 110 GLY A 112 0
SHEET 2 AA 4 CYS A 141 TRP A 146 -1 O GLN A 144 N GLY A 112
SHEET 3 AA 4 THR A 230 TYR A 236 -1 O THR A 230 N LEU A 145
SHEET 4 AA 4 ILE A 195 VAL A 197 -1 O ARG A 196 N ASN A 235
SHEET 1 AB 7 CYS A 124 SER A 127 0
SHEET 2 AB 7 LYS A 132 CYS A 135 -1 O LYS A 132 N SER A 127
SHEET 3 AB 7 LEU A 264 VAL A 274 1 O GLU A 271 N LEU A 133
SHEET 4 AB 7 ILE A 251 GLU A 258 -1 O ILE A 251 N VAL A 272
SHEET 5 AB 7 ARG A 156 TYR A 163 -1 O ARG A 156 N GLU A 258
SHEET 6 AB 7 HIS A 214 PRO A 219 -1 O VAL A 216 N ALA A 159
SHEET 7 AB 7 GLU A 204 ASP A 207 -1 O GLU A 204 N VAL A 217
SHEET 1 BA 4 ARG B 110 GLY B 112 0
SHEET 2 BA 4 CYS B 141 TRP B 146 -1 O GLN B 144 N GLY B 112
SHEET 3 BA 4 THR B 230 TYR B 236 -1 O THR B 230 N LEU B 145
SHEET 4 BA 4 ILE B 195 VAL B 197 -1 O ARG B 196 N ASN B 235
SHEET 1 BB 7 CYS B 124 SER B 127 0
SHEET 2 BB 7 LYS B 132 CYS B 135 -1 O LYS B 132 N SER B 127
SHEET 3 BB 7 LEU B 264 VAL B 274 1 O GLU B 271 N LEU B 133
SHEET 4 BB 7 ILE B 251 GLU B 258 -1 O ILE B 251 N VAL B 272
SHEET 5 BB 7 ARG B 156 TYR B 163 -1 O ARG B 156 N GLU B 258
SHEET 6 BB 7 HIS B 214 PRO B 219 -1 O VAL B 216 N ALA B 159
SHEET 7 BB 7 GLU B 204 ASP B 207 -1 O GLU B 204 N VAL B 217
LINK ZN ZN A1300 ND1 HIS A 179 1555 1555 2.02
LINK ZN ZN A1300 SG CYS A 176 1555 1555 2.41
LINK ZN ZN A1300 SG CYS A 238 1555 1555 2.35
LINK ZN ZN A1300 SG CYS A 242 1555 1555 2.35
LINK ZN ZN B1300 SG CYS B 238 1555 1555 2.41
LINK ZN ZN B1300 SG CYS B 176 1555 1555 2.38
LINK ZN ZN B1300 SG CYS B 242 1555 1555 2.32
LINK ZN ZN B1300 ND1 HIS B 179 1555 1555 2.01
SITE 1 AC1 4 CYS A 176 HIS A 179 CYS A 238 CYS A 242
SITE 1 AC2 4 CYS B 176 HIS B 179 CYS B 238 CYS B 242
CRYST1 65.000 71.000 104.800 90.00 90.00 90.00 P 21 21 21 8
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 0.015385 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
