HEADER PROTEIN BINDING/TRANSFERASE 11-JUN-12 4FJ3
TITLE 14-3-3 ISOFORM ZETA IN COMPLEX WITH A DIPHOYPHORYLATED C-RAF PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN ZETA/DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-230;
COMPND 5 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE;
COMPND 9 CHAIN: P;
COMPND 10 FRAGMENT: UNP RESIDUES 229-264;
COMPND 11 SYNONYM: PROTO-ONCOGENE C-RAF, CRAF, RAF-1;
COMPND 12 EC: 2.7.11.1;
COMPND 13 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: YWHAZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS 14-3-3 FOLD, ALL ALPHA-HELICAL, ADAPTER PROTEIN, PROTEIN BINDING-
KEYWDS 2 TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.OTTMANN,M.MOLZAN
REVDAT 2 10-JUL-13 4FJ3 1 JRNL
REVDAT 1 05-SEP-12 4FJ3 0
JRNL AUTH M.MOLZAN,C.OTTMANN
JRNL TITL SYNERGISTIC BINDING OF THE PHOSPHORYLATED S233- AND
JRNL TITL 2 S259-BINDING SITES OF C-RAF TO ONE 14-3-3ZETA DIMER
JRNL REF J.MOL.BIOL. V. 423 486 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22922483
JRNL DOI 10.1016/J.JMB.2012.08.009
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0093
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 61868
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3094
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4009
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.1430
REMARK 3 BIN FREE R VALUE SET COUNT : 218
REMARK 3 BIN FREE R VALUE : 0.1990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3609
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 587
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 1.03000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.167
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3860 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5241 ; 1.724 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 503 ; 4.946 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 197 ;38.333 ;24.924
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 737 ;15.049 ;15.041
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;16.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 585 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2919 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 10953 ; 4.498 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 588 ;18.412 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3784 ;13.826 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 300 5
REMARK 3 1 B 1 B 300 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 849 ; 0.200 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 786 ; 0.530 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 849 ; 3.380 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 786 ; 4.970 ;10.000
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4FJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : AL2/AL2
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61869
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.310
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA-ACETATE PH 7.0, 0.8 M NAH2PO4
REMARK 280 AND 1.2 M K2HPO4 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 36.07000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.07000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.21500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P
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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 70
REMARK 465 GLY A 71
REMARK 465 ALA A 72
REMARK 465 ASP A 204
REMARK 465 THR A 205
REMARK 465 LEU A 206
REMARK 465 SER A 207
REMARK 465 GLU A 208
REMARK 465 GLU A 209
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 70
REMARK 465 GLY B 71
REMARK 465 ALA B 134
REMARK 465 GLY B 135
REMARK 465 ASP B 136
REMARK 465 ASP B 204
REMARK 465 THR B 205
REMARK 465 GLN P 229
REMARK 465 HIS P 236
REMARK 465 ALA P 237
REMARK 465 PHE P 238
REMARK 465 THR P 239
REMARK 465 PHE P 240
REMARK 465 ASN P 241
REMARK 465 THR P 242
REMARK 465 SER P 243
REMARK 465 SER P 244
REMARK 465 PRO P 245
REMARK 465 SER P 246
REMARK 465 SER P 247
REMARK 465 GLU P 248
REMARK 465 GLY P 249
REMARK 465 SER P 250
REMARK 465 LEU P 251
REMARK 465 SER P 252
REMARK 465 GLN P 253
REMARK 465 ARG P 254
REMARK 465 GLN P 255
REMARK 465 HIS P 264
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 3 NZ
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 LYS A 75 CD CE NZ
REMARK 470 GLN A 76 CG CD OE1 NE2
REMARK 470 LYS A 103 NZ
REMARK 470 LYS A 139 CD CE NZ
REMARK 470 LYS A 158 NZ
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 LYS A 212 CE NZ
REMARK 470 GLU B 5 CD OE1 OE2
REMARK 470 LYS B 68 CE NZ
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 LYS B 75 CE NZ
REMARK 470 LYS B 103 CD CE
REMARK 470 ASP B 137 CG OD1 OD2
REMARK 470 LYS B 157 NZ
REMARK 470 GLU B 202 CG CD OE1 OE2
REMARK 470 GLU B 208 CG CD OE1 OE2
REMARK 470 GLU B 209 CG CD OE1 OE2
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 SER B 230 OG
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 NE2 GLN B 15 O HOH B 566 2.06
REMARK 500 CD1 LEU A 216 O HOH A 389 2.18
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 LYS A 27 CE LYS A 27 NZ -0.161
REMARK 500 PHE A 174 CZ PHE A 174 CE2 0.130
REMARK 500 LYS B 27 CE LYS B 27 NZ -0.163
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 LEU A 203 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU B 90 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU B 90 CB - CG - CD2 ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASP A 137 36.12 -92.84
REMARK 500 SER A 184 72.18 -119.97
REMARK 500 PHE B 104 -53.75 -128.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IQJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA IN COMPLEX WITH
REMARK 900 RAF1 PEPTIDE (10MER)
REMARK 900 RELATED ID: 3NKX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN 14-3-3 ZETA IN COMPLEX WITH RAF1
REMARK 900 PEPTIDE (10MER)
REMARK 900 RELATED ID: 1A4O RELATED DB: PDB
REMARK 900 14-3-3 PROTEIN ZETA ISOFORM
DBREF 4FJ3 A 1 230 UNP P63104 1433Z_HUMAN 1 230
DBREF 4FJ3 B 1 230 UNP P63104 1433Z_HUMAN 1 230
DBREF 4FJ3 P 229 264 UNP P04049 RAF1_HUMAN 229 264
SEQADV 4FJ3 GLY A -4 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 ALA A -3 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 MET A -2 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 GLY A -1 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 SER A 0 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 GLY B -4 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 ALA B -3 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 MET B -2 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 GLY B -1 UNP P63104 EXPRESSION TAG
SEQADV 4FJ3 SER B 0 UNP P63104 EXPRESSION TAG
SEQRES 1 A 235 GLY ALA MET GLY SER MET ASP LYS ASN GLU LEU VAL GLN
SEQRES 2 A 235 LYS ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR ASP ASP
SEQRES 3 A 235 MET ALA ALA CYS MET LYS SER VAL THR GLU GLN GLY ALA
SEQRES 4 A 235 GLU LEU SER ASN GLU GLU ARG ASN LEU LEU SER VAL ALA
SEQRES 5 A 235 TYR LYS ASN VAL VAL GLY ALA ARG ARG SER SER TRP ARG
SEQRES 6 A 235 VAL VAL SER SER ILE GLU GLN LYS THR GLU GLY ALA GLU
SEQRES 7 A 235 LYS LYS GLN GLN MET ALA ARG GLU TYR ARG GLU LYS ILE
SEQRES 8 A 235 GLU THR GLU LEU ARG ASP ILE CYS ASN ASP VAL LEU SER
SEQRES 9 A 235 LEU LEU GLU LYS PHE LEU ILE PRO ASN ALA SER GLN ALA
SEQRES 10 A 235 GLU SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 A 235 TYR ARG TYR LEU ALA GLU VAL ALA ALA GLY ASP ASP LYS
SEQRES 12 A 235 LYS GLY ILE VAL ASP GLN SER GLN GLN ALA TYR GLN GLU
SEQRES 13 A 235 ALA PHE GLU ILE SER LYS LYS GLU MET GLN PRO THR HIS
SEQRES 14 A 235 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 A 235 TYR TYR GLU ILE LEU ASN SER PRO GLU LYS ALA CYS SER
SEQRES 16 A 235 LEU ALA LYS THR ALA PHE ASP GLU ALA ILE ALA GLU LEU
SEQRES 17 A 235 ASP THR LEU SER GLU GLU SER TYR LYS ASP SER THR LEU
SEQRES 18 A 235 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 A 235 SER
SEQRES 1 B 235 GLY ALA MET GLY SER MET ASP LYS ASN GLU LEU VAL GLN
SEQRES 2 B 235 LYS ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR ASP ASP
SEQRES 3 B 235 MET ALA ALA CYS MET LYS SER VAL THR GLU GLN GLY ALA
SEQRES 4 B 235 GLU LEU SER ASN GLU GLU ARG ASN LEU LEU SER VAL ALA
SEQRES 5 B 235 TYR LYS ASN VAL VAL GLY ALA ARG ARG SER SER TRP ARG
SEQRES 6 B 235 VAL VAL SER SER ILE GLU GLN LYS THR GLU GLY ALA GLU
SEQRES 7 B 235 LYS LYS GLN GLN MET ALA ARG GLU TYR ARG GLU LYS ILE
SEQRES 8 B 235 GLU THR GLU LEU ARG ASP ILE CYS ASN ASP VAL LEU SER
SEQRES 9 B 235 LEU LEU GLU LYS PHE LEU ILE PRO ASN ALA SER GLN ALA
SEQRES 10 B 235 GLU SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 B 235 TYR ARG TYR LEU ALA GLU VAL ALA ALA GLY ASP ASP LYS
SEQRES 12 B 235 LYS GLY ILE VAL ASP GLN SER GLN GLN ALA TYR GLN GLU
SEQRES 13 B 235 ALA PHE GLU ILE SER LYS LYS GLU MET GLN PRO THR HIS
SEQRES 14 B 235 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 B 235 TYR TYR GLU ILE LEU ASN SER PRO GLU LYS ALA CYS SER
SEQRES 16 B 235 LEU ALA LYS THR ALA PHE ASP GLU ALA ILE ALA GLU LEU
SEQRES 17 B 235 ASP THR LEU SER GLU GLU SER TYR LYS ASP SER THR LEU
SEQRES 18 B 235 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 B 235 SER
SEQRES 1 P 36 GLN HIS ARG TYR SEP THR PRO HIS ALA PHE THR PHE ASN
SEQRES 2 P 36 THR SER SER PRO SER SER GLU GLY SER LEU SER GLN ARG
SEQRES 3 P 36 GLN ARG SER THR SEP THR PRO ASN VAL HIS
MODRES 4FJ3 SEP P 233 SER PHOSPHOSERINE
MODRES 4FJ3 SEP P 259 SER PHOSPHOSERINE
HET SEP P 233 10
HET SEP P 259 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 3 SEP 2(C3 H8 N O6 P)
FORMUL 4 HOH *587(H2 O)
HELIX 1 1 ASP A 2 ALA A 16 1 15
HELIX 2 2 ARG A 18 GLU A 31 1 14
HELIX 3 3 SER A 37 LYS A 68 1 32
HELIX 4 4 LYS A 74 PHE A 104 1 31
HELIX 5 5 PHE A 104 ALA A 109 1 6
HELIX 6 6 GLN A 111 VAL A 132 1 22
HELIX 7 7 LYS A 138 MET A 160 1 23
HELIX 8 8 HIS A 164 ILE A 181 1 18
HELIX 9 9 SER A 184 GLU A 202 1 19
HELIX 10 10 TYR A 211 SER A 230 1 20
HELIX 11 11 LYS B 3 ALA B 16 1 14
HELIX 12 12 ARG B 18 GLN B 32 1 15
HELIX 13 13 SER B 37 THR B 69 1 33
HELIX 14 14 GLU B 73 PHE B 104 1 32
HELIX 15 15 PHE B 104 ALA B 109 1 6
HELIX 16 16 GLN B 111 VAL B 132 1 22
HELIX 17 17 LYS B 138 MET B 160 1 23
HELIX 18 18 HIS B 164 ILE B 181 1 18
HELIX 19 19 SER B 184 GLU B 202 1 19
HELIX 20 20 SER B 207 GLU B 209 5 3
HELIX 21 21 SER B 210 SER B 230 1 21
LINK C TYR P 232 N SEP P 233 1555 1555 1.33
LINK C SEP P 233 N THR P 234 1555 1555 1.34
LINK C THR P 258 N SEP P 259 1555 1555 1.33
LINK C SEP P 259 N THR P 260 1555 1555 1.34
CRYST1 72.140 102.430 113.890 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 0.013862 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009763 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008780 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
