HEADER SIGNALING PROTEIN 15-SEP-05 2C1J
TITLE MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND
TITLE 2 PHOSPHOACETYLATED HISTONE H3 BY 14-3-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN ZETA/DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H3 ACETYLPHOSPHOPEPTIDE;
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: 14-3-3, HISTONE H3 ACETYLPHOSPHOPEPTIDE (RESIDUES 7-14);
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834 PLYS/S;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PACYC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS SIGNALING PROTEIN-COMPLEX, NUCLEOSOME, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.I.WELBURN,N.MACDONALD,M.E.M.NOBLE,A.NGUYEN,M.B.YAFFE,D.CLYNES,
AUTHOR 2 J.G.MOGGS,G.ORPHANIDES,S.THOMSON,J.W.EDMUNDS,A.L.CLAYTON,
AUTHOR 3 J.A.ENDICOTT,L.C.MAHADEVAN
REVDAT 6 13-DEC-23 2C1J 1 REMARK
REVDAT 5 29-JUL-20 2C1J 1 SOURCE LINK
REVDAT 4 18-SEP-13 2C1J 1 KEYWDS REMARK
REVDAT 3 13-JUL-11 2C1J 1 VERSN
REVDAT 2 24-FEB-09 2C1J 1 VERSN
REVDAT 1 02-NOV-05 2C1J 0
JRNL AUTH N.MACDONALD,J.P.I.WELBURN,M.E.M.NOBLE,A.NGUYEN,M.B.YAFFE,
JRNL AUTH 2 D.CLYNES,J.G.MOGGS,G.ORPHANIDES,S.THOMSON,J.W.EDMUNDS,
JRNL AUTH 3 A.L.CLAYTON,J.A.ENDICOTT,L.C.MAHADEVAN
JRNL TITL MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND
JRNL TITL 2 PHOSPHOACETYLATED HISTONE H3 BY 14-3-3.
JRNL REF MOL.CELL V. 20 199 2005
JRNL REFN ISSN 1097-2765
JRNL PMID 16246723
JRNL DOI 10.1016/J.MOLCEL.2005.08.032
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 20689
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1113
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1492
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : UNVERIFIED
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.67000
REMARK 3 B22 (A**2) : -3.11000
REMARK 3 B33 (A**2) : 2.92000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.525
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.336
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.296
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.333
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3852 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5164 ; 1.527 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 468 ; 6.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;41.963 ;25.319
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 748 ;21.680 ;15.040
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 570 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2834 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1988 ; 0.271 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2651 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 198 ; 0.197 ; 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): 56 ; 0.250 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.144 ; 0.200
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): 2420 ; 0.479 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3768 ; 0.859 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1615 ; 1.380 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1396 ; 2.261 ; 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 : 2
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 230 2
REMARK 3 1 B 1 B 230 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 920 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 920 ; .04 ; .05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 921 ; .26 ; .50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 921 ; .26 ; .50
REMARK 3 TIGHT THERMAL 1 A (A**2): 920 ; .06 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 920 ; .06 ; .50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 921 ; .47 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 921 ; .47 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 7 C 14 2
REMARK 3 1 D 7 D 14 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 32 ; .12 ; .05
REMARK 3 TIGHT POSITIONAL 2 D (A): 32 ; .12 ; .05
REMARK 3 MEDIUM POSITIONAL 2 C (A): 30 ; .45 ; .50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 30 ; .45 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 32 ; .06 ; .50
REMARK 3 TIGHT THERMAL 2 D (A**2): 32 ; .06 ; .50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 30 ; .55 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 30 ; .55 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 230
REMARK 3 RESIDUE RANGE : C 7 C 14
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7910 -.0840 12.3520
REMARK 3 T TENSOR
REMARK 3 T11: -.0944 T22: .0299
REMARK 3 T33: -.0500 T12: -.0099
REMARK 3 T13: -.0544 T23: -.0938
REMARK 3 L TENSOR
REMARK 3 L11: 1.4529 L22: 2.4902
REMARK 3 L33: 1.9700 L12: .9249
REMARK 3 L13: -.9665 L23: -1.7620
REMARK 3 S TENSOR
REMARK 3 S11: .4054 S12: -.2752 S13: .2820
REMARK 3 S21: .2436 S22: .0230 S23: -.0329
REMARK 3 S31: -.4959 S32: .1852 S33: -.4284
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 230
REMARK 3 RESIDUE RANGE : D 7 D 14
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6550 -34.2530 22.1320
REMARK 3 T TENSOR
REMARK 3 T11: -.0793 T22: .0231
REMARK 3 T33: .0134 T12: .0862
REMARK 3 T13: -.0142 T23: .0434
REMARK 3 L TENSOR
REMARK 3 L11: 2.2674 L22: 2.1352
REMARK 3 L33: 1.0948 L12: 1.6453
REMARK 3 L13: -.7089 L23: -.2676
REMARK 3 S TENSOR
REMARK 3 S11: -.4607 S12: -.2623 S13: -.6693
REMARK 3 S21: .0308 S22: .0667 S23: -.2847
REMARK 3 S31: .2197 S32: .2246 S33: .3940
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 2C1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1290025634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 21.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1QJA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH7.0, 23% ETHYLENE
REMARK 280 GLYCOL, PH 7.00
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 36.20650
REMARK 290 SMTRY3 2 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: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 MET A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 GLN A -1
REMARK 465 ASP A 0
REMARK 465 ASP A 231
REMARK 465 THR A 232
REMARK 465 GLN A 233
REMARK 465 GLY A 234
REMARK 465 ASP A 235
REMARK 465 GLU A 236
REMARK 465 ALA A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 GLY A 240
REMARK 465 GLU A 241
REMARK 465 GLY A 242
REMARK 465 GLY A 243
REMARK 465 GLU A 244
REMARK 465 ASN A 245
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 SER B -2
REMARK 465 GLN B -1
REMARK 465 ASP B 0
REMARK 465 ASP B 231
REMARK 465 THR B 232
REMARK 465 GLN B 233
REMARK 465 GLY B 234
REMARK 465 ASP B 235
REMARK 465 GLU B 236
REMARK 465 ALA B 237
REMARK 465 GLU B 238
REMARK 465 ALA B 239
REMARK 465 GLY B 240
REMARK 465 GLU B 241
REMARK 465 GLY B 242
REMARK 465 GLY B 243
REMARK 465 GLU B 244
REMARK 465 ASN B 245
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 SER A 230 OG
REMARK 470 SER B 230 OG
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 D 8 O - C - N ANGL. DEV. = -26.6 DEGREES
REMARK 500 ALY D 9 C - N - CA ANGL. DEV. = 17.2 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 ALA A 23 -75.28 -57.25
REMARK 500 ALA A 24 -37.23 -37.84
REMARK 500 SER A 57 -76.07 -62.85
REMARK 500 SER A 58 -55.71 -23.70
REMARK 500 ASP A 96 -76.50 -24.19
REMARK 500 PHE A 104 -73.13 -105.65
REMARK 500 ALA A 134 -26.70 152.05
REMARK 500 ASP A 136 -64.16 85.95
REMARK 500 ILE A 181 -64.58 -96.13
REMARK 500 SER A 210 4.88 -150.53
REMARK 500 ALA B 23 -72.08 -61.87
REMARK 500 SER B 28 -73.82 -55.27
REMARK 500 VAL B 29 -62.61 -27.38
REMARK 500 THR B 88 -70.53 -50.79
REMARK 500 ASP B 96 -78.23 -19.15
REMARK 500 PHE B 104 -77.91 -102.85
REMARK 500 ALA B 134 -29.42 159.83
REMARK 500 ASP B 136 -63.00 86.49
REMARK 500 ILE B 181 -64.50 -95.99
REMARK 500 ASP B 204 0.92 -69.29
REMARK 500 GLU B 209 -4.45 -56.56
REMARK 500 SER B 210 -0.34 -145.99
REMARK 500 THR C 11 -54.19 -23.79
REMARK 500 ARG D 8 157.45 -40.89
REMARK 500 THR D 11 -50.73 -24.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY D 13 LYS D 14 -128.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG D 8 -32.34
REMARK 500 ALY D 9 24.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IB1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 14-3-3 ZETA: SEROTONIN N-ACETYLTRANSFERASE
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1QJA RELATED DB: PDB
REMARK 900 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)
REMARK 900 RELATED ID: 1QJB RELATED DB: PDB
REMARK 900 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)
DBREF 2C1J A -12 0 PDB 2C1J 2C1J -12 0
DBREF 2C1J A 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 2C1J B -12 0 PDB 2C1J 2C1J -12 0
DBREF 2C1J B 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 2C1J C 7 14 PDB 2C1J 2C1J 7 14
DBREF 2C1J D 7 14 PDB 2C1J 2C1J 7 14
SEQRES 1 A 258 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 258 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 3 A 258 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 4 A 258 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 5 A 258 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 6 A 258 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 7 A 258 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 8 A 258 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 9 A 258 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 10 A 258 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 11 A 258 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 12 A 258 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 13 A 258 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 14 A 258 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 15 A 258 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 16 A 258 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 17 A 258 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 18 A 258 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 19 A 258 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 20 A 258 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 B 258 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 258 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 3 B 258 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 4 B 258 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 5 B 258 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 6 B 258 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 7 B 258 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 8 B 258 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 9 B 258 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 10 B 258 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 11 B 258 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 12 B 258 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 13 B 258 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 14 B 258 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 15 B 258 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 16 B 258 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 17 B 258 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 18 B 258 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 19 B 258 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 20 B 258 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 C 8 ALA ARG ALY SEP THR GLY GLY LYS
SEQRES 1 D 8 ALA ARG ALY SEP THR GLY GLY LYS
MODRES 2C1J ALY C 9 LYS N(6)-ACETYLLYSINE
MODRES 2C1J SEP C 10 SER PHOSPHOSERINE
MODRES 2C1J ALY D 9 LYS N(6)-ACETYLLYSINE
MODRES 2C1J SEP D 10 SER PHOSPHOSERINE
HET ALY C 9 12
HET SEP C 10 10
HET ALY D 9 12
HET SEP D 10 10
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 3 ALY 2(C8 H16 N2 O3)
FORMUL 3 SEP 2(C3 H8 N O6 P)
FORMUL 5 HOH *86(H2 O)
HELIX 1 1 ASP A 2 ALA A 16 1 15
HELIX 2 2 ARG A 18 GLN A 32 1 15
HELIX 3 3 SER A 37 GLN A 67 1 31
HELIX 4 4 ALA A 72 PHE A 104 1 33
HELIX 5 5 GLN A 111 GLU A 131 1 21
HELIX 6 6 ASP A 136 MET A 160 1 25
HELIX 7 7 HIS A 164 ILE A 181 1 18
HELIX 8 8 SER A 184 ALA A 201 1 18
HELIX 9 9 GLU A 202 LEU A 206 5 5
HELIX 10 10 SER A 207 GLU A 209 5 3
HELIX 11 11 SER A 210 SER A 230 1 21
HELIX 12 12 ASP B 2 ALA B 16 1 15
HELIX 13 13 ARG B 18 GLN B 32 1 15
HELIX 14 14 SER B 37 THR B 69 1 33
HELIX 15 15 ALA B 72 PHE B 104 1 33
HELIX 16 16 GLN B 111 GLU B 131 1 21
HELIX 17 17 ASP B 136 MET B 160 1 25
HELIX 18 18 HIS B 164 ILE B 181 1 18
HELIX 19 19 SER B 184 ALA B 201 1 18
HELIX 20 20 GLU B 202 LEU B 206 5 5
HELIX 21 21 SER B 207 GLU B 209 5 3
HELIX 22 22 SER B 210 SER B 230 1 21
LINK C ARG C 8 N ALY C 9 1555 1555 1.85
LINK C ALY C 9 N SEP C 10 1555 1555 1.79
LINK C SEP C 10 N THR C 11 1555 1555 1.33
LINK C ARG D 8 N ALY D 9 1555 1555 1.36
LINK C ALY D 9 N SEP D 10 1555 1555 1.34
LINK C SEP D 10 N THR D 11 1555 1555 1.32
CISPEP 1 ALA A 133 ALA A 134 0 -6.39
CISPEP 2 ALA B 133 ALA B 134 0 -11.19
CISPEP 3 GLY C 13 LYS C 14 0 -21.66
CRYST1 71.191 72.413 71.160 90.00 102.96 90.00 P 1 21 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 0.014047 0.000000 0.003233 0.00000
SCALE2 0.000000 0.013810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014420 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
