HEADER TRANSCRIPTION 08-AUG-06 2J0Z
TITLE P53 TETRAMERIZATION DOMAIN WILD TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: TETRAMERIZATION DOMAIN, RESIDUES 326-356;
COMPND 5 SYNONYM: P53, TUMOR SUPPRESSOR P53, PHOSPHOPROTEIN P53,
COMPND 6 ANTIGEN NY-CO-13
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS P53, ZINC, ACTIVATOR, APOPTOSIS, WILD TYPE, CELL CYCLE,
KEYWDS 2 ACETYLATION, DNA-BINDING, POLYMORPHISM, TETRAMERIZATION
KEYWDS 3 DOMAIN, TRANSCRIPTION REGULATION, ANTI-ONCOGENE, NUCLEAR
KEYWDS 4 PROTEIN, PHOSPHORYLATION, LI-FRAUMENI SYNDROME, HOST-VIRUS
KEYWDS 5 INTERACTION, DISEASE MUTATION, ALTERNATIVE SPLICING,
KEYWDS 6 GLYCOPROTEIN, TRANSCRIPTION, METAL-BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR R.J.CARBAJO,P.MORA,M.M.SANCHEZ DEL PINO,E.PEREZ-PAYA,
AUTHOR 2 A.PINEDA-LUCENA
REVDAT 3 24-FEB-09 2J0Z 1 VERSN
REVDAT 2 25-DEC-07 2J0Z 1 JRNL ATOM
REVDAT 1 28-AUG-07 2J0Z 0
JRNL AUTH P.MORA,R.J.CARBAJO,A.PINEDA-LUCENA,
JRNL AUTH 2 M.M.SANCHEZ DEL PINO,E.PEREZ-PAYA
JRNL TITL SOLVENT-EXPOSED RESIDUES LOCATED IN THE BETA-SHEET
JRNL TITL 2 MODULATE THE STABILITY OF THE TETRAMERIZATION
JRNL TITL 3 DOMAIN OF P53--A STRUCTURAL AND COMBINATORIAL
JRNL TITL 4 APPROACH.
JRNL REF PROTEINS V. 71 1670 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18076077
JRNL DOI 10.1002/PROT.21854
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
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,READ,
REMARK 3 RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2J0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-06.
REMARK 100 THE PDBE ID CODE IS EBI-29618.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300.0
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 5% D2O/95% WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : OTHER
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY
REMARK 210 METHOD USED : CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17
REMARK 210
REMARK 210 REMARK: NONE
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 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 1 TYR C 327 150.99 61.82
REMARK 500 2 LEU D 330 98.65 -160.43
REMARK 500 4 TYR A 327 140.64 63.15
REMARK 500 5 TYR B 327 97.15 60.29
REMARK 500 5 GLN B 331 88.53 -69.33
REMARK 500 5 TYR D 327 110.60 60.55
REMARK 500 6 TYR B 327 118.75 62.55
REMARK 500 6 GLN B 331 84.44 -69.94
REMARK 500 6 TYR D 327 112.69 61.15
REMARK 500 7 TYR B 327 96.53 60.33
REMARK 500 7 TYR D 327 152.79 61.69
REMARK 500 8 TYR A 327 106.64 60.46
REMARK 500 8 TYR B 327 96.30 60.32
REMARK 500 8 TYR C 327 139.37 63.21
REMARK 500 10 TYR B 327 98.00 60.56
REMARK 500 11 TYR C 327 101.84 60.06
REMARK 500 13 TYR B 327 111.11 60.55
REMARK 500 13 TYR C 327 115.39 61.76
REMARK 500 13 TYR D 327 110.13 60.21
REMARK 500 14 TYR B 327 110.61 60.67
REMARK 500 14 TYR C 327 112.22 61.04
REMARK 500 14 THR C 329 95.22 -60.39
REMARK 500 14 TYR D 327 137.80 63.44
REMARK 500 15 TYR B 327 142.84 63.25
REMARK 500 15 TYR C 327 113.60 61.05
REMARK 500 15 TYR D 327 147.55 62.63
REMARK 500 16 TYR A 327 113.56 61.26
REMARK 500 17 TYR C 327 111.62 60.82
REMARK 500 17 TYR D 327 113.84 61.37
REMARK 500 18 TYR A 327 101.65 60.12
REMARK 500 18 TYR B 327 111.37 60.59
REMARK 500 18 TYR C 327 144.17 62.90
REMARK 500 19 TYR A 327 146.78 62.70
REMARK 500 19 TYR B 327 116.11 61.98
REMARK 500 19 PHE C 328 88.60 -150.44
REMARK 500 20 TYR C 327 108.61 60.24
REMARK 500 20 TYR D 327 128.85 63.39
REMARK 500 21 TYR B 327 135.65 63.39
REMARK 500 21 TYR C 327 112.00 60.90
REMARK 500 22 TYR A 327 111.28 60.62
REMARK 500 22 TYR B 327 109.91 60.34
REMARK 500 22 TYR D 327 109.89 60.23
REMARK 500 23 TYR A 327 112.98 61.21
REMARK 500 23 TYR B 327 149.03 62.38
REMARK 500 24 TYR C 327 111.07 60.52
REMARK 500 25 TYR A 327 112.62 60.90
REMARK 500 25 TYR C 327 112.96 61.29
REMARK 500 25 TYR D 327 102.04 60.66
REMARK 500 27 TYR A 327 111.68 60.83
REMARK 500 27 TYR B 327 115.57 61.86
REMARK 500 27 TYR C 327 114.55 61.59
REMARK 500 27 TYR D 327 98.36 60.34
REMARK 500 28 TYR A 327 113.12 61.25
REMARK 500 28 TYR D 327 110.61 60.55
REMARK 500 29 GLN B 331 83.72 -66.10
REMARK 500 29 TYR D 327 110.56 60.43
REMARK 500 29 GLN D 331 84.04 -66.05
REMARK 500 30 TYR B 327 141.04 63.19
REMARK 500 30 TYR C 327 116.11 61.99
REMARK 500
REMARK 500 REMARK: NULL
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: 1C26 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF P53 TETRAMERIZATION
REMARK 900 DOMAIN
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: 1JSP RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF CBP BROMODOMAIN IN COMPLEX
REMARK 900 WITH P53 PEPTIDE
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: 1UOL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN P53 CORE
REMARK 900 DOMAIN MUTANT M133L/V203A/N239Y/N268D AT 1
REMARK 900 .9 A RESOLUTION.
REMARK 900 RELATED ID: 1XQH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF
REMARK 900 THEMETHYLTRANSFERASE SET9 (ALSO KNOWN AS SET7
REMARK 900 /9) WITH A P53PEPTIDE AND SAH
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: 2AC0 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF DNA RECOGNITION BY P53
REMARK 900 TETRAMERS(COMPLEX I)
REMARK 900 RELATED ID: 2ADY RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF DNA RECOGNITION BY P53
REMARK 900 TETRAMERS(COMPLEX IV)
REMARK 900 RELATED ID: 2AHI RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF DNA RECOGNITION BY P53
REMARK 900 TETRAMERS(COMPLEX III)
REMARK 900 RELATED ID: 2ATA RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF DNA RECOGNITION BY P53
REMARK 900 TETRAMERS(COMPLEX II)
REMARK 900 RELATED ID: 2B3G RELATED DB: PDB
REMARK 900 P53N (FRAGMENT 33-60) BOUND TO RPA70N
REMARK 900 RELATED ID: 2BIM RELATED DB: PDB
REMARK 900 HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-
REMARK 900 N239Y-N268D-R273H
REMARK 900 RELATED ID: 2BIN RELATED DB: PDB
REMARK 900 HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-
REMARK 900 V203A-N239Y-N268D
REMARK 900 RELATED ID: 2BIO RELATED DB: PDB
REMARK 900 HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-
REMARK 900 N239Y-R249S-N268D
REMARK 900 RELATED ID: 2BIP RELATED DB: PDB
REMARK 900 HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-
REMARK 900 V203A-N239Y-R249S-N268D
REMARK 900 RELATED ID: 2BIQ RELATED DB: PDB
REMARK 900 HUMAN P53 CORE DOMAIN MUTANT T123A-M133L-
REMARK 900 H168R-V203A-N239Y-R249S-N268D
REMARK 900 RELATED ID: 2F1X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRAF-LIKE DOMAIN
REMARK 900 OF HAUSP/USP7BOUND TO A P53 PEPTIDE
REMARK 900 RELATED ID: 2FEJ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN P53 DNA BINDING
REMARK 900 DOMAIN.
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)
REMARK 900 RELATED ID: 2J10 RELATED DB: PDB
REMARK 900 P53 TETRAMERIZATION DOMAIN MUTANT T329K Q331K
REMARK 900 RELATED ID: 2J11 RELATED DB: PDB
REMARK 900 P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G
REMARK 900 Q331G
REMARK 900 RELATED ID: 2TOH RELATED DB: PDB
REMARK 900 TYROSINE HYDROXYLASE CATALYTIC AND
REMARK 900 TETRAMERIZATION DOMAINS FROM RAT
DBREF 2J0Z A 326 356 UNP P04637 P53_HUMAN 326 356
DBREF 2J0Z B 326 356 UNP P04637 P53_HUMAN 326 356
DBREF 2J0Z C 326 356 UNP P04637 P53_HUMAN 326 356
DBREF 2J0Z D 326 356 UNP P04637 P53_HUMAN 326 356
SEQRES 1 A 31 GLU TYR PHE THR LEU GLN ILE ARG GLY ARG GLU ARG PHE
SEQRES 2 A 31 GLU MET PHE ARG GLU LEU ASN GLU ALA LEU GLU LEU LYS
SEQRES 3 A 31 ASP ALA GLN ALA GLY
SEQRES 1 B 31 GLU TYR PHE THR LEU GLN ILE ARG GLY ARG GLU ARG PHE
SEQRES 2 B 31 GLU MET PHE ARG GLU LEU ASN GLU ALA LEU GLU LEU LYS
SEQRES 3 B 31 ASP ALA GLN ALA GLY
SEQRES 1 C 31 GLU TYR PHE THR LEU GLN ILE ARG GLY ARG GLU ARG PHE
SEQRES 2 C 31 GLU MET PHE ARG GLU LEU ASN GLU ALA LEU GLU LEU LYS
SEQRES 3 C 31 ASP ALA GLN ALA GLY
SEQRES 1 D 31 GLU TYR PHE THR LEU GLN ILE ARG GLY ARG GLU ARG PHE
SEQRES 2 D 31 GLU MET PHE ARG GLU LEU ASN GLU ALA LEU GLU LEU LYS
SEQRES 3 D 31 ASP ALA GLN ALA GLY
HELIX 1 1 GLY A 334 ALA A 355 1 22
HELIX 2 2 GLY B 334 ALA B 355 1 22
HELIX 3 3 GLY C 334 GLN C 354 1 21
HELIX 4 4 GLY D 334 ALA D 355 1 22
SHEET 1 AA 2 PHE A 328 ILE A 332 0
SHEET 2 AA 2 PHE B 328 ILE B 332 -1 O PHE B 328 N ILE A 332
SHEET 1 CA 2 PHE C 328 ILE C 332 0
SHEET 2 CA 2 PHE D 328 ILE D 332 -1 O PHE D 328 N ILE C 332
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 4
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
