HEADER DNA BINDING PROTEIN/DNA 09-DEC-12 4IBV
TITLE HUMAN P53 CORE DOMAIN WITH HOT SPOT MUTATION R273C AND SECOND-SITE
TITLE 2 SUPPRESSOR MUTATION S240R IN SEQUENCE-SPECIFIC COMPLEX WITH DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN;
COMPND 5 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: P53, TP53;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-27-B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS METAL-BINDING, LOOP-SHEET-HELIX MOTIF, TRANSCRIPTION, ACTIVATOR,
KEYWDS 2 ANTI-ONCOGENE, APOPTOSIS, CELL CYCLE, DISEASE MUTATION, RESCUE
KEYWDS 3 MUTATION, TUMOR SUPPRESSOR, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ELDAR,H.ROZENBERG,Y.DISKIN-POSNER,Z.SHAKKED
REVDAT 4 20-SEP-23 4IBV 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4IBV 1 REMARK
REVDAT 2 23-OCT-13 4IBV 1 JRNL
REVDAT 1 14-AUG-13 4IBV 0
JRNL AUTH A.ELDAR,H.ROZENBERG,Y.DISKIN-POSNER,R.ROHS,Z.SHAKKED
JRNL TITL STRUCTURAL STUDIES OF P53 INACTIVATION BY DNA-CONTACT
JRNL TITL 2 MUTATIONS AND ITS RESCUE BY SUPPRESSOR MUTATIONS VIA
JRNL TITL 3 ALTERNATIVE PROTEIN-DNA INTERACTIONS.
JRNL REF NUCLEIC ACIDS RES. V. 41 8748 2013
JRNL REFN ISSN 0305-1048
JRNL PMID 23863845
JRNL DOI 10.1093/NAR/GKT630
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1405
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 13262
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.2472 - 3.5839 0.99 2670 129 0.1415 0.2031
REMARK 3 2 3.5839 - 2.8448 0.99 2591 138 0.1604 0.2253
REMARK 3 3 2.8448 - 2.4852 0.99 2581 143 0.1839 0.2552
REMARK 3 4 2.4852 - 2.2580 0.97 2460 156 0.1786 0.2581
REMARK 3 5 2.2580 - 2.1000 0.87 2293 101 0.1808 0.2416
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.03
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1947
REMARK 3 ANGLE : 1.210 2674
REMARK 3 CHIRALITY : 0.078 284
REMARK 3 PLANARITY : 0.006 315
REMARK 3 DIHEDRAL : 18.445 771
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 94:176)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3767 25.6079 -2.3676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1111
REMARK 3 T33: 0.1951 T12: -0.0215
REMARK 3 T13: -0.0482 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 2.9767 L22: 2.2381
REMARK 3 L33: 0.8200 L12: -1.3751
REMARK 3 L13: 0.5526 L23: -0.0615
REMARK 3 S TENSOR
REMARK 3 S11: -0.1187 S12: 0.1088 S13: 0.4307
REMARK 3 S21: 0.1479 S22: -0.1087 S23: -0.5258
REMARK 3 S31: -0.1170 S32: 0.0083 S33: 0.1585
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 177:194)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4378 14.6569 -5.0018
REMARK 3 T TENSOR
REMARK 3 T11: 0.2177 T22: 0.2567
REMARK 3 T33: 0.2000 T12: -0.0533
REMARK 3 T13: 0.0365 T23: -0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 5.3704 L22: 5.5512
REMARK 3 L33: 2.4400 L12: -4.0558
REMARK 3 L13: -1.6458 L23: -0.0730
REMARK 3 S TENSOR
REMARK 3 S11: -0.1224 S12: 0.5668 S13: -1.1194
REMARK 3 S21: -0.1411 S22: -0.0810 S23: 0.5387
REMARK 3 S31: 0.1850 S32: -0.5748 S33: 0.3273
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 195:277)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1358 19.3778 -4.4248
REMARK 3 T TENSOR
REMARK 3 T11: 0.1051 T22: 0.0986
REMARK 3 T33: 0.0598 T12: 0.0034
REMARK 3 T13: 0.0189 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 3.5249 L22: 3.2864
REMARK 3 L33: 1.9552 L12: -1.4821
REMARK 3 L13: 1.0769 L23: -0.0491
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: 0.2402 S13: 0.0414
REMARK 3 S21: 0.0028 S22: -0.1132 S23: -0.1962
REMARK 3 S31: 0.0274 S32: 0.0436 S33: 0.0894
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 278:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2072 44.0953 -1.2346
REMARK 3 T TENSOR
REMARK 3 T11: 0.2927 T22: 0.1374
REMARK 3 T33: 0.4119 T12: 0.0154
REMARK 3 T13: -0.0888 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 7.6206 L22: 3.5404
REMARK 3 L33: 5.9927 L12: 1.6681
REMARK 3 L13: 2.5955 L23: 4.3642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: -0.5907 S13: 0.9941
REMARK 3 S21: -0.1285 S22: -0.1361 S23: -0.0898
REMARK 3 S31: -0.4998 S32: -0.3605 S33: 0.1235
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 1:11)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5000 40.1717 0.5263
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.2587
REMARK 3 T33: 0.1554 T12: 0.0175
REMARK 3 T13: 0.0005 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.3616 L22: 0.1298
REMARK 3 L33: 6.5309 L12: 0.0838
REMARK 3 L13: 0.2190 L23: 1.2145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0434 S13: 0.0751
REMARK 3 S21: 0.1097 S22: 0.1589 S23: -0.0377
REMARK 3 S31: 0.1131 S32: 0.1951 S33: -0.1659
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000076558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : SILICON (111)
REMARK 200 OPTICS : PT COATED SI MIRROR IN
REMARK 200 KIRKPATRICK-BAEZ GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13264
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.25500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2AC0, CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:2.4 PROTEIN/DNA RATIO, 16% PEG 3350,
REMARK 280 0.18M NH4F, PH 6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.81550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.15100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.81550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.15100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 ASP A 184
REMARK 465 SER A 185
REMARK 465 ASP A 186
REMARK 465 DG B 12
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 114 CD1 CD2
REMARK 470 LEU A 188 CD1 CD2
REMARK 470 GLU A 221 CG CD OE1 OE2
REMARK 470 ASP A 228 CB CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC B 1 O5' - C5' - C4' ANGL. DEV. = -6.7 DEGREES
REMARK 500 DG B 4 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA B 6 O4' - C4' - C3' ANGL. DEV. = -3.3 DEGREES
REMARK 500 DC B 11 C1' - O4' - C4' ANGL. DEV. = -7.3 DEGREES
REMARK 500 DC B 11 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
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 PRO A 223 156.01 -45.36
REMARK 500 VAL A 225 126.51 165.90
REMARK 500
REMARK 500 REMARK: NULL
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 A 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 176 SG
REMARK 620 2 HIS A 179 ND1 105.6
REMARK 620 3 CYS A 238 SG 108.9 114.1
REMARK 620 4 CYS A 242 SG 114.4 100.6 112.9
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IBQ RELATED DB: PDB
REMARK 900 RELATED ID: 4IBS RELATED DB: PDB
REMARK 900 RELATED ID: 4IBT RELATED DB: PDB
REMARK 900 RELATED ID: 4IBU RELATED DB: PDB
REMARK 900 RELATED ID: 4IBW RELATED DB: PDB
REMARK 900 RELATED ID: 4IBY RELATED DB: PDB
REMARK 900 RELATED ID: 4IBZ RELATED DB: PDB
REMARK 900 RELATED ID: 4IJT RELATED DB: PDB
DBREF 4IBV A 94 293 UNP P04637 P53_HUMAN 94 293
DBREF 4IBV B 1 12 PDB 4IBV 4IBV 1 12
SEQADV 4IBV ARG A 240 UNP P04637 SER 240 ENGINEERED MUTATION
SEQADV 4IBV CYS A 273 UNP P04637 ARG 273 ENGINEERED MUTATION
SEQRES 1 A 200 SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER
SEQRES 2 A 200 TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA
SEQRES 3 A 200 LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS
SEQRES 4 A 200 MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU
SEQRES 5 A 200 TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG
SEQRES 6 A 200 ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU
SEQRES 7 A 200 VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP
SEQRES 8 A 200 SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL
SEQRES 9 A 200 GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN
SEQRES 10 A 200 THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO
SEQRES 11 A 200 GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR
SEQRES 12 A 200 MET CYS ASN ARG SER CYS MET GLY GLY MET ASN ARG ARG
SEQRES 13 A 200 PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY
SEQRES 14 A 200 ASN LEU LEU GLY ARG ASN SER PHE GLU VAL CYS VAL CYS
SEQRES 15 A 200 ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN
SEQRES 16 A 200 LEU ARG LYS LYS GLY
SEQRES 1 B 12 DC DG DG DG DC DA DT DG DC DC DC DG
HET EDO A 301 4
HET EDO A 302 4
HET EDO A 303 8
HET EDO A 304 4
HET EDO A 305 8
HET EDO A 306 4
HET EDO A 307 4
HET ZN A 308 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 7(C2 H6 O2)
FORMUL 10 ZN ZN 2+
FORMUL 11 HOH *164(H2 O)
HELIX 1 1 CYS A 176 CYS A 182 1 7
HELIX 2 2 CYS A 277 GLY A 293 1 17
SHEET 1 A 4 ARG A 110 GLY A 112 0
SHEET 2 A 4 THR A 140 TRP A 146 -1 O TRP A 146 N ARG A 110
SHEET 3 A 4 THR A 230 TYR A 236 -1 O THR A 230 N LEU A 145
SHEET 4 A 4 ILE A 195 GLU A 198 -1 N ARG A 196 O ASN A 235
SHEET 1 B 7 CYS A 124 SER A 127 0
SHEET 2 B 7 LYS A 132 CYS A 135 -1 O LYS A 132 N SER A 127
SHEET 3 B 7 LEU A 264 VAL A 274 1 O GLU A 271 N MET A 133
SHEET 4 B 7 ILE A 251 GLU A 258 -1 N LEU A 257 O LEU A 265
SHEET 5 B 7 ARG A 156 TYR A 163 -1 N ARG A 156 O GLU A 258
SHEET 6 B 7 HIS A 214 PRO A 219 -1 O VAL A 218 N VAL A 157
SHEET 7 B 7 GLU A 204 ASP A 207 -1 N GLU A 204 O VAL A 217
LINK SG CYS A 176 ZN ZN A 308 1555 1555 2.28
LINK ND1 HIS A 179 ZN ZN A 308 1555 1555 2.09
LINK SG CYS A 238 ZN ZN A 308 1555 1555 2.39
LINK SG CYS A 242 ZN ZN A 308 1555 1555 2.30
SITE 1 AC1 5 PRO A 177 HIS A 178 ARG A 181 CYS A 182
SITE 2 AC1 5 GLY A 244
SITE 1 AC2 9 THR A 140 SER A 166 GLN A 167 HIS A 168
SITE 2 AC2 9 MET A 169 THR A 170 GLU A 171 GLU A 198
SITE 3 AC2 9 HOH A 482
SITE 1 AC3 7 ASN A 131 PRO A 152 ASP A 259 SER A 260
SITE 2 AC3 7 SER A 261 HOH A 405 HOH A 484
SITE 1 AC4 7 GLY A 154 THR A 155 ARG A 156 PRO A 219
SITE 2 AC4 7 EDO A 305 EDO A 306 HOH A 426
SITE 1 AC5 5 LYS A 101 THR A 102 GLY A 154 SER A 260
SITE 2 AC5 5 EDO A 304
SITE 1 AC6 8 PRO A 151 PRO A 152 PRO A 153 THR A 155
SITE 2 AC6 8 TYR A 220 PRO A 222 EDO A 304 HOH A 498
SITE 1 AC7 4 GLU A 180 ARG A 181 SER A 183 PRO A 191
SITE 1 AC8 4 CYS A 176 HIS A 179 CYS A 238 CYS A 242
CRYST1 137.631 50.302 34.008 90.00 93.46 90.00 C 1 2 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 0.007266 0.000000 0.000439 0.00000
SCALE2 0.000000 0.019880 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029459 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
