HEADER DNA BINDING PROTEIN 23-MAR-09 3GPM
TITLE STRUCTURE OF THE TRIMERIC FORM OF THE E113G PCNA MUTANT PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PCNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: POL30, YBR0811, YBR088C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET11-A
KEYWDS DNA DAMAGE, DNA REPAIR, DNA REPLICATION, DNA-BINDING, ISOPEPTIDE
KEYWDS 2 BOND, NUCLEUS, UBL CONJUGATION, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.FREUDENTHAL,L.GAKHAR,S.RAMASWAMY,M.T.WASHINGTON
REVDAT 3 06-SEP-23 3GPM 1 REMARK
REVDAT 2 20-OCT-21 3GPM 1 SEQADV
REVDAT 1 16-JUN-09 3GPM 0
JRNL AUTH B.D.FREUDENTHAL,L.GAKHAR,S.RAMASWAMY,M.T.WASHINGTON
JRNL TITL A CHARGED RESIDUE AT THE SUBUNIT INTERFACE OF PCNA PROMOTES
JRNL TITL 2 TRIMER FORMATION BY DESTABILIZING ALTERNATE SUBUNIT
JRNL TITL 3 INTERACTIONS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 65 560 2009
JRNL REFN ISSN 0907-4449
JRNL PMID 19465770
JRNL DOI 10.1107/S0907444909011329
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 5860
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 + TEST SET) : 0.275
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 282
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 439
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 19
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.25
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.699
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.669
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.347
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1989 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2687 ; 1.376 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 253 ; 7.225 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;40.990 ;25.244
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 363 ;21.069 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;21.184 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 321 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1451 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 972 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1362 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 77 ; 0.154 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 22 ; 0.161 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1288 ; 0.555 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2038 ; 1.010 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 766 ; 0.764 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 649 ; 1.320 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3GPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052155.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : SAGGITAL FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6146
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.56
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 9.84
REMARK 200 R MERGE FOR SHELL (I) : 0.29400
REMARK 200 R SYM FOR SHELL (I) : 0.29400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1PLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE AND 0.1 M
REMARK 280 SODIUM CITRATE, PH 5.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 61.04650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.04650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.04650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.04650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.04650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.04650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 61.04650
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.04650
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.04650
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.04650
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.04650
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.04650
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 61.04650
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.04650
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.04650
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.04650
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.04650
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.04650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 BIOMT1 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 61.04650
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 61.04650
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -61.04650
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 61.04650
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 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 ASN A 255
REMARK 465 ASP A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
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 PRO A 191 C - N - CD ANGL. DEV. = -18.1 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 LYS A 20 -25.81 103.92
REMARK 500 ASP A 21 40.43 -99.10
REMARK 500 GLN A 24 -0.28 51.87
REMARK 500 THR A 85 52.99 92.51
REMARK 500 ASP A 86 63.80 -165.90
REMARK 500 THR A 87 44.98 97.23
REMARK 500 ASP A 109 32.52 73.15
REMARK 500 ASP A 120 88.96 65.43
REMARK 500 PRO A 184 -104.78 -50.42
REMARK 500 PHE A 185 179.09 73.22
REMARK 500 VAL A 186 119.66 176.57
REMARK 500 GLU A 189 -105.76 -120.17
REMARK 500 HIS A 190 -103.14 -43.58
REMARK 500 PRO A 191 -122.25 -119.22
REMARK 500 GLU A 192 -78.90 -64.17
REMARK 500 THR A 193 56.74 15.06
REMARK 500 LYS A 210 -35.39 -33.71
REMARK 500 LYS A 242 99.27 -31.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF THE NON-TRIMERIC FORM OF THE E113G PCNA MUTANT PROTEIN
DBREF 3GPM A 1 258 UNP P15873 PCNA_YEAST 1 258
SEQADV 3GPM GLY A 113 UNP P15873 GLU 113 ENGINEERED MUTATION
SEQRES 1 A 258 MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS
SEQRES 2 A 258 ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL
SEQRES 3 A 258 ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA
SEQRES 4 A 258 VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE
SEQRES 5 A 258 GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO
SEQRES 6 A 258 VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS ILE
SEQRES 7 A 258 LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU ILE
SEQRES 8 A 258 ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU
SEQRES 9 A 258 ASP THR LYS LYS ASP ARG ILE ALA GLY TYR SER LEU LYS
SEQRES 10 A 258 LEU MET ASP ILE ASP ALA ASP PHE LEU LYS ILE GLU GLU
SEQRES 11 A 258 LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU
SEQRES 12 A 258 PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP
SEQRES 13 A 258 SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS PHE
SEQRES 14 A 258 VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE
SEQRES 15 A 258 LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE
SEQRES 16 A 258 LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY
SEQRES 17 A 258 ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU
SEQRES 18 A 258 SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO
SEQRES 19 A 258 ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN
SEQRES 20 A 258 PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU
HELIX 1 1 ALA A 9 GLY A 18 1 10
HELIX 2 2 GLY A 53 PHE A 57 5 5
HELIX 3 3 LEU A 72 GLY A 82 1 11
HELIX 4 4 SER A 141 SER A 155 1 15
HELIX 5 5 ALA A 209 LYS A 217 1 9
HELIX 6 6 GLY A 218 SER A 220 5 3
SHEET 1 A 5 GLU A 59 CYS A 62 0
SHEET 2 A 5 LEU A 2 LYS A 5 -1 N LYS A 5 O GLU A 59
SHEET 3 A 5 THR A 89 ALA A 92 -1 O LEU A 90 N ALA A 4
SHEET 4 A 5 SER A 98 PHE A 103 -1 O ILE A 100 N ILE A 91
SHEET 5 A 5 ALA A 112 LYS A 117 -1 O TYR A 114 N LEU A 101
SHEET 1 B 9 VAL A 66 ASP A 71 0
SHEET 2 B 9 LEU A 25 LYS A 31 -1 N CYS A 30 O VAL A 66
SHEET 3 B 9 GLY A 34 VAL A 40 -1 O ILE A 36 N GLN A 29
SHEET 4 B 9 LEU A 46 ILE A 52 -1 O ILE A 52 N ILE A 35
SHEET 5 B 9 GLY A 244 LEU A 250 -1 O GLN A 247 N SER A 49
SHEET 6 B 9 ALA A 235 LEU A 241 -1 N LEU A 241 O GLY A 244
SHEET 7 B 9 ARG A 224 LEU A 229 -1 N GLY A 226 O GLN A 238
SHEET 8 B 9 SER A 135 PRO A 140 -1 N LEU A 137 O ILE A 227
SHEET 9 B 9 LYS A 196 MET A 199 -1 O LYS A 196 N SER A 138
SHEET 1 C 4 SER A 177 ILE A 182 0
SHEET 2 C 4 THR A 166 ASP A 172 -1 N PHE A 169 O VAL A 180
SHEET 3 C 4 SER A 157 THR A 163 -1 N ASN A 159 O VAL A 170
SHEET 4 C 4 VAL A 203 GLY A 208 -1 O PHE A 207 N ILE A 158
CRYST1 122.093 122.093 122.093 90.00 90.00 90.00 P 21 3 12
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 0.008190 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
