HEADER DNA BINDING PROTEIN 04-JAN-18 6FF9
TITLE MUTANT R280K OF HUMAN P53
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ANTIGEN NY-CO-13,PHOSPHOPROTEIN P53,TUMOR SUPPRESSOR P53;
COMPND 5 ENGINEERED: YES;
COMPND 6 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, MUTANT, DNA BINDING, ANTICANCER THERAPY, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.G.TROVAO,A.S.GOMES,B.PINHEIRO,A.L.CARVALHO,M.J.ROMAO
REVDAT 2 17-JAN-24 6FF9 1 REMARK
REVDAT 1 25-APR-18 6FF9 0
JRNL AUTH A.S.GOMES,F.TROVAO,B.ANDRADE PINHEIRO,F.FREIRE,S.GOMES,
JRNL AUTH 2 C.OLIVEIRA,L.DOMINGUES,M.J.ROMAO,L.SARAIVA,A.L.CARVALHO
JRNL TITL THE CRYSTAL STRUCTURE OF THE R280K MUTANT OF HUMAN P53
JRNL TITL 2 EXPLAINS THE LOSS OF DNA BINDING.
JRNL REF INT J MOL SCI V. 19 2018
JRNL REFN ESSN 1422-0067
JRNL PMID 29652801
JRNL DOI 10.3390/IJMS19041184
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 47903
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2440
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 2.0510 - 1.9990 0.95 3472 207 0.2660 0.3140
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.102
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -21.21000
REMARK 3 B22 (A**2) : 43.98000
REMARK 3 B33 (A**2) : -22.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.7510
REMARK 3 OPERATOR: H, K, L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 : 6
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: A
REMARK 3 SELECTION : B
REMARK 3 ATOM PAIRS NUMBER : 21798
REMARK 3 RMSD : 0.110
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: A
REMARK 3 SELECTION : C
REMARK 3 ATOM PAIRS NUMBER : 22280
REMARK 3 RMSD : 0.090
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: A
REMARK 3 SELECTION : D
REMARK 3 ATOM PAIRS NUMBER : 21778
REMARK 3 RMSD : 0.110
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: B
REMARK 3 SELECTION : C
REMARK 3 ATOM PAIRS NUMBER : 22126
REMARK 3 RMSD : 0.100
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: B
REMARK 3 SELECTION : D
REMARK 3 ATOM PAIRS NUMBER : 22324
REMARK 3 RMSD : 0.080
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: C
REMARK 3 SELECTION : D
REMARK 3 ATOM PAIRS NUMBER : 22220
REMARK 3 RMSD : 0.100
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6FF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-17
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 : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50430
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.83300
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
REMARK 200 STARTING MODEL: 2OCJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.72250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 VAL A 225 O
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 C 227 O HOH C 401 2.17
REMARK 500 OG1 THR B 123 O HOH B 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 141 CB CYS C 141 SG -0.100
REMARK 500 CYS D 141 CB CYS D 141 SG -0.111
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 267 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 273 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 110 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 267 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 282 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 282 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP C 228 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG C 267 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG D 273 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 282 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 282 NE - CZ - NH2 ANGL. DEV. = -3.8 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 SER C 183 58.69 -90.82
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 176 SG
REMARK 620 2 CYS A 238 SG 113.1
REMARK 620 3 CYS A 242 SG 114.4 113.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 176 SG
REMARK 620 2 CYS B 238 SG 111.1
REMARK 620 3 CYS B 242 SG 119.7 116.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 176 SG
REMARK 620 2 CYS C 238 SG 111.7
REMARK 620 3 CYS C 242 SG 118.5 118.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 176 SG
REMARK 620 2 CYS D 238 SG 109.5
REMARK 620 3 CYS D 242 SG 114.0 113.8
REMARK 620 N 1 2
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
DBREF 6FF9 A 97 289 UNP P04637 P53_HUMAN 58 250
DBREF 6FF9 B 97 289 UNP P04637 P53_HUMAN 58 250
DBREF 6FF9 C 97 289 UNP P04637 P53_HUMAN 58 250
DBREF 6FF9 D 97 289 UNP P04637 P53_HUMAN 58 250
SEQADV 6FF9 LYS A 280 UNP P04637 ARG 241 ENGINEERED MUTATION
SEQADV 6FF9 LYS B 280 UNP P04637 ARG 241 ENGINEERED MUTATION
SEQADV 6FF9 LYS C 280 UNP P04637 ARG 241 ENGINEERED MUTATION
SEQADV 6FF9 LYS D 280 UNP P04637 ARG 241 ENGINEERED MUTATION
SEQRES 1 A 193 VAL PRO SER GLN LYS THR TYR GLN GLY SER TYR GLY PHE
SEQRES 2 A 193 ARG LEU GLY PHE LEU HIS SER GLY THR ALA LYS SER VAL
SEQRES 3 A 193 THR CYS THR TYR SER PRO ALA LEU ASN LYS MET PHE CYS
SEQRES 4 A 193 GLN LEU ALA LYS THR CYS PRO VAL GLN LEU TRP VAL ASP
SEQRES 5 A 193 SER THR PRO PRO PRO GLY THR ARG VAL ARG ALA MET ALA
SEQRES 6 A 193 ILE TYR LYS GLN SER GLN HIS MET THR GLU VAL VAL ARG
SEQRES 7 A 193 ARG CYS PRO HIS HIS GLU ARG CYS SER ASP SER ASP GLY
SEQRES 8 A 193 LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN
SEQRES 9 A 193 LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN THR PHE ARG
SEQRES 10 A 193 HIS SER VAL VAL VAL PRO TYR GLU PRO PRO GLU VAL GLY
SEQRES 11 A 193 SER ASP CYS THR THR ILE HIS TYR ASN TYR MET CYS ASN
SEQRES 12 A 193 SER SER CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU
SEQRES 13 A 193 THR ILE ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU
SEQRES 14 A 193 GLY ARG ASN SER PHE GLU VAL ARG VAL CYS ALA CYS PRO
SEQRES 15 A 193 GLY LYS ASP ARG ARG THR GLU GLU GLU ASN LEU
SEQRES 1 B 193 VAL PRO SER GLN LYS THR TYR GLN GLY SER TYR GLY PHE
SEQRES 2 B 193 ARG LEU GLY PHE LEU HIS SER GLY THR ALA LYS SER VAL
SEQRES 3 B 193 THR CYS THR TYR SER PRO ALA LEU ASN LYS MET PHE CYS
SEQRES 4 B 193 GLN LEU ALA LYS THR CYS PRO VAL GLN LEU TRP VAL ASP
SEQRES 5 B 193 SER THR PRO PRO PRO GLY THR ARG VAL ARG ALA MET ALA
SEQRES 6 B 193 ILE TYR LYS GLN SER GLN HIS MET THR GLU VAL VAL ARG
SEQRES 7 B 193 ARG CYS PRO HIS HIS GLU ARG CYS SER ASP SER ASP GLY
SEQRES 8 B 193 LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN
SEQRES 9 B 193 LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN THR PHE ARG
SEQRES 10 B 193 HIS SER VAL VAL VAL PRO TYR GLU PRO PRO GLU VAL GLY
SEQRES 11 B 193 SER ASP CYS THR THR ILE HIS TYR ASN TYR MET CYS ASN
SEQRES 12 B 193 SER SER CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU
SEQRES 13 B 193 THR ILE ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU
SEQRES 14 B 193 GLY ARG ASN SER PHE GLU VAL ARG VAL CYS ALA CYS PRO
SEQRES 15 B 193 GLY LYS ASP ARG ARG THR GLU GLU GLU ASN LEU
SEQRES 1 C 193 VAL PRO SER GLN LYS THR TYR GLN GLY SER TYR GLY PHE
SEQRES 2 C 193 ARG LEU GLY PHE LEU HIS SER GLY THR ALA LYS SER VAL
SEQRES 3 C 193 THR CYS THR TYR SER PRO ALA LEU ASN LYS MET PHE CYS
SEQRES 4 C 193 GLN LEU ALA LYS THR CYS PRO VAL GLN LEU TRP VAL ASP
SEQRES 5 C 193 SER THR PRO PRO PRO GLY THR ARG VAL ARG ALA MET ALA
SEQRES 6 C 193 ILE TYR LYS GLN SER GLN HIS MET THR GLU VAL VAL ARG
SEQRES 7 C 193 ARG CYS PRO HIS HIS GLU ARG CYS SER ASP SER ASP GLY
SEQRES 8 C 193 LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN
SEQRES 9 C 193 LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN THR PHE ARG
SEQRES 10 C 193 HIS SER VAL VAL VAL PRO TYR GLU PRO PRO GLU VAL GLY
SEQRES 11 C 193 SER ASP CYS THR THR ILE HIS TYR ASN TYR MET CYS ASN
SEQRES 12 C 193 SER SER CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU
SEQRES 13 C 193 THR ILE ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU
SEQRES 14 C 193 GLY ARG ASN SER PHE GLU VAL ARG VAL CYS ALA CYS PRO
SEQRES 15 C 193 GLY LYS ASP ARG ARG THR GLU GLU GLU ASN LEU
SEQRES 1 D 193 VAL PRO SER GLN LYS THR TYR GLN GLY SER TYR GLY PHE
SEQRES 2 D 193 ARG LEU GLY PHE LEU HIS SER GLY THR ALA LYS SER VAL
SEQRES 3 D 193 THR CYS THR TYR SER PRO ALA LEU ASN LYS MET PHE CYS
SEQRES 4 D 193 GLN LEU ALA LYS THR CYS PRO VAL GLN LEU TRP VAL ASP
SEQRES 5 D 193 SER THR PRO PRO PRO GLY THR ARG VAL ARG ALA MET ALA
SEQRES 6 D 193 ILE TYR LYS GLN SER GLN HIS MET THR GLU VAL VAL ARG
SEQRES 7 D 193 ARG CYS PRO HIS HIS GLU ARG CYS SER ASP SER ASP GLY
SEQRES 8 D 193 LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN
SEQRES 9 D 193 LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN THR PHE ARG
SEQRES 10 D 193 HIS SER VAL VAL VAL PRO TYR GLU PRO PRO GLU VAL GLY
SEQRES 11 D 193 SER ASP CYS THR THR ILE HIS TYR ASN TYR MET CYS ASN
SEQRES 12 D 193 SER SER CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU
SEQRES 13 D 193 THR ILE ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU
SEQRES 14 D 193 GLY ARG ASN SER PHE GLU VAL ARG VAL CYS ALA CYS PRO
SEQRES 15 D 193 GLY LYS ASP ARG ARG THR GLU GLU GLU ASN LEU
HET ZN A 301 1
HET ZN B 301 1
HET ZN C 301 1
HET ZN D 301 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 HOH *336(H2 O)
HELIX 1 AA1 GLN A 104 GLY A 108 5 5
HELIX 2 AA2 GLN A 165 MET A 169 5 5
HELIX 3 AA3 CYS A 176 ARG A 181 1 6
HELIX 4 AA4 CYS A 277 ASN A 288 1 12
HELIX 5 AA5 GLN B 165 MET B 169 5 5
HELIX 6 AA6 CYS B 176 CYS B 182 1 7
HELIX 7 AA7 CYS B 277 ASN B 288 1 12
HELIX 8 AA8 GLN C 165 MET C 169 5 5
HELIX 9 AA9 CYS C 176 ARG C 181 1 6
HELIX 10 AB1 CYS C 277 ASN C 288 1 12
HELIX 11 AB2 GLN D 165 MET D 169 5 5
HELIX 12 AB3 CYS D 176 CYS D 182 1 7
HELIX 13 AB4 CYS D 277 ASN D 288 1 12
SHEET 1 AA1 4 ARG A 110 GLY A 112 0
SHEET 2 AA1 4 CYS A 141 TRP A 146 -1 O TRP A 146 N ARG A 110
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 PHE A 134 N THR A 125
SHEET 3 AA2 7 LEU A 264 VAL A 274 1 O GLU A 271 N MET 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 ARG A 156 O GLU A 258
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 GLU A 204 O VAL A 217
SHEET 1 AA3 4 ARG B 110 GLY B 112 0
SHEET 2 AA3 4 CYS B 141 TRP B 146 -1 O TRP B 146 N ARG B 110
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 PHE B 134 N THR B 125
SHEET 3 AA4 7 LEU B 264 VAL B 274 1 O GLU B 271 N MET 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
SHEET 1 AA5 4 ARG C 110 GLY C 112 0
SHEET 2 AA5 4 CYS C 141 TRP C 146 -1 O TRP C 146 N ARG C 110
SHEET 3 AA5 4 THR C 230 TYR C 236 -1 O THR C 230 N LEU C 145
SHEET 4 AA5 4 ILE C 195 VAL C 197 -1 N ARG C 196 O ASN C 235
SHEET 1 AA6 7 CYS C 124 SER C 127 0
SHEET 2 AA6 7 LYS C 132 CYS C 135 -1 O PHE C 134 N THR C 125
SHEET 3 AA6 7 LEU C 264 VAL C 274 1 O GLU C 271 N MET C 133
SHEET 4 AA6 7 ILE C 251 GLU C 258 -1 N LEU C 257 O LEU C 265
SHEET 5 AA6 7 ARG C 156 TYR C 163 -1 N ARG C 156 O GLU C 258
SHEET 6 AA6 7 HIS C 214 PRO C 219 -1 O VAL C 218 N VAL C 157
SHEET 7 AA6 7 GLU C 204 ASP C 207 -1 N GLU C 204 O VAL C 217
SHEET 1 AA7 4 ARG D 110 GLY D 112 0
SHEET 2 AA7 4 CYS D 141 TRP D 146 -1 O TRP D 146 N ARG D 110
SHEET 3 AA7 4 THR D 230 TYR D 236 -1 O THR D 230 N LEU D 145
SHEET 4 AA7 4 ILE D 195 VAL D 197 -1 N ARG D 196 O ASN D 235
SHEET 1 AA8 7 CYS D 124 SER D 127 0
SHEET 2 AA8 7 LYS D 132 CYS D 135 -1 O PHE D 134 N THR D 125
SHEET 3 AA8 7 LEU D 264 VAL D 274 1 O GLU D 271 N MET D 133
SHEET 4 AA8 7 ILE D 251 GLU D 258 -1 N LEU D 257 O LEU D 265
SHEET 5 AA8 7 ARG D 156 TYR D 163 -1 N ARG D 156 O GLU D 258
SHEET 6 AA8 7 HIS D 214 PRO D 219 -1 O VAL D 218 N VAL D 157
SHEET 7 AA8 7 GLU D 204 ASP D 207 -1 N GLU D 204 O VAL D 217
LINK SG CYS A 176 ZN ZN A 301 1555 1555 2.36
LINK SG CYS A 238 ZN ZN A 301 1555 1555 2.34
LINK SG CYS A 242 ZN ZN A 301 1555 1555 2.27
LINK SG CYS B 176 ZN ZN B 301 1555 1555 2.39
LINK SG CYS B 238 ZN ZN B 301 1555 1555 2.38
LINK SG CYS B 242 ZN ZN B 301 1555 1555 2.13
LINK SG CYS C 176 ZN ZN C 301 1555 1555 2.36
LINK SG CYS C 238 ZN ZN C 301 1555 1555 2.38
LINK SG CYS C 242 ZN ZN C 301 1555 1555 2.15
LINK SG CYS D 176 ZN ZN D 301 1555 1555 2.42
LINK SG CYS D 238 ZN ZN D 301 1555 1555 2.35
LINK SG CYS D 242 ZN ZN D 301 1555 1555 2.19
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
SITE 1 AC3 4 CYS C 176 HIS C 179 CYS C 238 CYS C 242
SITE 1 AC4 4 CYS D 176 HIS D 179 CYS D 238 CYS D 242
CRYST1 68.569 69.445 83.335 90.00 90.04 90.00 P 1 21 1 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 0.014584 0.000000 0.000010 0.00000
SCALE2 0.000000 0.014400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
