HEADER DNA BINDING PROTEIN 18-MAY-17 5O1D
TITLE P53 CANCER MUTANT Y220C IN COMPLEX WITH COMPOUND MB481
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 94-312;
COMPND 5 SYNONYM: ANTIGEN NY-CO-13,PHOSPHOPROTEIN P53,TUMOR SUPPRESSOR P53;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TP53, P53;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS P53, TUMOR SUPPRESSOR, CANCER MUTATION, PROTEIN STABILIZATION, SMALL-
KEYWDS 2 MOLECULE STABILIZERS, CANCER THERAPY, DNA BINDING PROTEIN, MOLECULAR
KEYWDS 3 CHAPERONES
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.JOERGER,M.R.BAUER,M.G.J.BAUD,A.R.FERSHT
REVDAT 2 17-JAN-24 5O1D 1 REMARK
REVDAT 1 09-MAY-18 5O1D 0
JRNL AUTH M.G.J.BAUD,M.R.BAUER,L.VERDUCI,F.A.DINGLER,K.J.PATEL,
JRNL AUTH 2 D.HORIL ROY,A.C.JOERGER,A.R.FERSHT
JRNL TITL AMINOBENZOTHIAZOLE DERIVATIVES STABILIZE THE THERMOLABILE
JRNL TITL 2 P53 CANCER MUTANT Y220C AND SHOW ANTICANCER ACTIVITY IN
JRNL TITL 3 P53-Y220C CELL LINES.
JRNL REF EUR J MED CHEM V. 152 101 2018
JRNL REFN ISSN 1768-3254
JRNL PMID 29702446
JRNL DOI 10.1016/J.EJMECH.2018.04.035
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 105218
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 5231
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 29.6377 - 4.2219 0.98 3555 158 0.1592 0.1453
REMARK 3 2 4.2219 - 3.3526 0.99 3418 180 0.1488 0.1656
REMARK 3 3 3.3526 - 2.9292 0.98 3355 165 0.1608 0.1760
REMARK 3 4 2.9292 - 2.6616 0.99 3378 177 0.1589 0.1726
REMARK 3 5 2.6616 - 2.4709 0.99 3361 176 0.1582 0.1745
REMARK 3 6 2.4709 - 2.3253 0.99 3354 166 0.1509 0.1475
REMARK 3 7 2.3253 - 2.2089 0.99 3360 163 0.1456 0.1619
REMARK 3 8 2.2089 - 2.1127 0.99 3310 188 0.1382 0.1789
REMARK 3 9 2.1127 - 2.0314 1.00 3326 190 0.1358 0.1607
REMARK 3 10 2.0314 - 1.9613 1.00 3362 154 0.1345 0.1440
REMARK 3 11 1.9613 - 1.9000 1.00 3333 176 0.1268 0.1650
REMARK 3 12 1.9000 - 1.8457 1.00 3318 183 0.1302 0.1521
REMARK 3 13 1.8457 - 1.7971 1.00 3304 213 0.1190 0.1542
REMARK 3 14 1.7971 - 1.7533 1.00 3311 183 0.1112 0.1251
REMARK 3 15 1.7533 - 1.7134 1.00 3307 173 0.1124 0.1394
REMARK 3 16 1.7134 - 1.6770 1.00 3293 192 0.1167 0.1545
REMARK 3 17 1.6770 - 1.6434 1.00 3317 177 0.1139 0.1551
REMARK 3 18 1.6434 - 1.6124 1.00 3300 175 0.1194 0.1608
REMARK 3 19 1.6124 - 1.5836 1.00 3326 153 0.1215 0.1671
REMARK 3 20 1.5836 - 1.5568 1.00 3340 182 0.1194 0.1542
REMARK 3 21 1.5568 - 1.5317 1.00 3325 154 0.1279 0.1473
REMARK 3 22 1.5317 - 1.5081 1.00 3295 184 0.1326 0.1600
REMARK 3 23 1.5081 - 1.4859 1.00 3292 172 0.1433 0.1941
REMARK 3 24 1.4859 - 1.4650 1.00 3325 177 0.1531 0.2068
REMARK 3 25 1.4650 - 1.4452 1.00 3291 163 0.1586 0.1899
REMARK 3 26 1.4452 - 1.4264 1.00 3310 187 0.1704 0.2107
REMARK 3 27 1.4264 - 1.4086 1.00 3317 172 0.1714 0.1963
REMARK 3 28 1.4086 - 1.3916 1.00 3284 189 0.1815 0.2325
REMARK 3 29 1.3916 - 1.3755 1.00 3298 154 0.1976 0.2133
REMARK 3 30 1.3755 - 1.3600 1.00 3322 155 0.2070 0.2363
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.720
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 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 : 0.005 3254
REMARK 3 ANGLE : 0.801 4444
REMARK 3 CHIRALITY : 0.082 485
REMARK 3 PLANARITY : 0.006 588
REMARK 3 DIHEDRAL : 14.156 1230
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5O1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976250
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105340
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
REMARK 200 RESOLUTION RANGE LOW (A) : 29.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2J1X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 6 MG/ML PROTEIN IN
REMARK 280 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR
REMARK 280 BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000,
REMARK 280 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH
REMARK 280 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE
REMARK 280 GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 32.58800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.66050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.59250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.66050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.58800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.59250
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 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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 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 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 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 LYS A 120 CG CD CE NZ
REMARK 470 ARG A 209 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 290 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 ARG B 209 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 280 NE CZ NH1 NH2
REMARK 470 GLU B 287 CG CD OE1 OE2
REMARK 470 ARG B 290 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 291 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 261 O HOH A 501 2.04
REMARK 500 OE2 GLU A 258 O HOH A 502 2.10
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 LEU A 188 -45.88 -132.30
REMARK 500 LEU B 188 -50.63 -121.66
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 176 SG
REMARK 620 2 HIS A 179 ND1 106.4
REMARK 620 3 CYS A 238 SG 110.4 106.5
REMARK 620 4 CYS A 242 SG 110.8 105.4 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 176 SG
REMARK 620 2 HIS B 179 ND1 105.7
REMARK 620 3 CYS B 238 SG 111.4 106.8
REMARK 620 4 CYS B 242 SG 111.1 105.5 115.6
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9GW A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9GW B 404
DBREF 5O1D A 94 312 UNP P04637 P53_HUMAN 94 312
DBREF 5O1D B 94 312 UNP P04637 P53_HUMAN 94 312
SEQADV 5O1D LEU A 133 UNP P04637 MET 133 ENGINEERED MUTATION
SEQADV 5O1D ALA A 203 UNP P04637 VAL 203 ENGINEERED MUTATION
SEQADV 5O1D CYS A 220 UNP P04637 TYR 220 ENGINEERED MUTATION
SEQADV 5O1D TYR A 239 UNP P04637 ASN 239 ENGINEERED MUTATION
SEQADV 5O1D ASP A 268 UNP P04637 ASN 268 ENGINEERED MUTATION
SEQADV 5O1D LEU B 133 UNP P04637 MET 133 ENGINEERED MUTATION
SEQADV 5O1D ALA B 203 UNP P04637 VAL 203 ENGINEERED MUTATION
SEQADV 5O1D CYS B 220 UNP P04637 TYR 220 ENGINEERED MUTATION
SEQADV 5O1D TYR B 239 UNP P04637 ASN 239 ENGINEERED MUTATION
SEQADV 5O1D 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 CYS 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 CYS 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 A 401 1
HET 9GW A 402 20
HET ZN B 401 1
HET GOL B 402 6
HET GOL B 403 6
HET 9GW B 404 20
HETNAM ZN ZINC ION
HETNAM 9GW 3-IODANYL-2-OXIDANYL-5-PROPOXY-4-PYRROL-1-YL-BENZOIC
HETNAM 2 9GW ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 9GW 2(C14 H14 I N O4)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 9 HOH *405(H2 O)
HELIX 1 AA1 GLN A 165 MET A 169 5 5
HELIX 2 AA2 HIS A 178 CYS A 182 5 5
HELIX 3 AA3 CYS A 277 LYS A 292 1 16
HELIX 4 AA4 HIS B 178 CYS B 182 5 5
HELIX 5 AA5 CYS B 277 LYS B 291 1 15
SHEET 1 AA1 4 ARG A 110 GLY A 112 0
SHEET 2 AA1 4 CYS A 141 TRP A 146 -1 O GLN A 144 N GLY A 112
SHEET 3 AA1 4 THR A 230 TYR A 236 -1 O THR A 230 N LEU A 145
SHEET 4 AA1 4 ILE A 195 VAL A 197 -1 N ARG A 196 O ASN A 235
SHEET 1 AA2 7 CYS A 124 SER A 127 0
SHEET 2 AA2 7 LYS A 132 CYS A 135 -1 O LYS A 132 N SER A 127
SHEET 3 AA2 7 LEU A 264 VAL A 274 1 O GLU A 271 N LEU A 133
SHEET 4 AA2 7 ILE A 251 GLU A 258 -1 N LEU A 257 O LEU A 265
SHEET 5 AA2 7 ARG A 156 TYR A 163 -1 N MET A 160 O ILE A 254
SHEET 6 AA2 7 HIS A 214 PRO A 219 -1 O VAL A 218 N VAL A 157
SHEET 7 AA2 7 GLU A 204 ASP A 207 -1 N LEU A 206 O SER A 215
SHEET 1 AA3 4 ARG B 110 GLY B 112 0
SHEET 2 AA3 4 CYS B 141 TRP B 146 -1 O GLN B 144 N GLY B 112
SHEET 3 AA3 4 THR B 230 TYR B 236 -1 O THR B 230 N LEU B 145
SHEET 4 AA3 4 ILE B 195 VAL B 197 -1 N ARG B 196 O ASN B 235
SHEET 1 AA4 7 CYS B 124 SER B 127 0
SHEET 2 AA4 7 LYS B 132 CYS B 135 -1 O LYS B 132 N SER B 127
SHEET 3 AA4 7 LEU B 264 VAL B 274 1 O GLU B 271 N LEU B 133
SHEET 4 AA4 7 ILE B 251 GLU B 258 -1 N LEU B 257 O LEU B 265
SHEET 5 AA4 7 ARG B 156 TYR B 163 -1 N MET B 160 O ILE B 254
SHEET 6 AA4 7 HIS B 214 PRO B 219 -1 O VAL B 218 N VAL B 157
SHEET 7 AA4 7 GLU B 204 ASP B 207 -1 N GLU B 204 O VAL B 217
LINK SG CYS A 176 ZN ZN A 401 1555 1555 2.34
LINK ND1 HIS A 179 ZN ZN A 401 1555 1555 1.99
LINK SG CYS A 238 ZN ZN A 401 1555 1555 2.32
LINK SG CYS A 242 ZN ZN A 401 1555 1555 2.32
LINK SG CYS B 176 ZN ZN B 401 1555 1555 2.33
LINK ND1 HIS B 179 ZN ZN B 401 1555 1555 2.06
LINK SG CYS B 238 ZN ZN B 401 1555 1555 2.33
LINK SG CYS B 242 ZN ZN B 401 1555 1555 2.31
SITE 1 AC1 4 CYS A 176 HIS A 179 CYS A 238 CYS A 242
SITE 1 AC2 11 LEU A 145 VAL A 147 THR A 150 PRO A 151
SITE 2 AC2 11 PRO A 152 CYS A 220 GLU A 221 PRO A 223
SITE 3 AC2 11 THR A 230 HOH A 510 HOH A 611
SITE 1 AC3 4 CYS B 176 HIS B 179 CYS B 238 CYS B 242
SITE 1 AC4 4 SER B 241 CYS B 275 ALA B 276 HOH B 550
SITE 1 AC5 6 ARG B 174 GLN B 192 ASP B 207 PHE B 212
SITE 2 AC5 6 HIS B 214 HOH B 572
SITE 1 AC6 10 LEU B 145 VAL B 147 THR B 150 PRO B 151
SITE 2 AC6 10 PRO B 152 CYS B 220 GLU B 221 PRO B 223
SITE 3 AC6 10 HOH B 506 HOH B 626
CRYST1 65.176 71.185 105.321 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 0.015343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014048 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009495 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
