HEADER TRANSFERASE 30-NOV-05 2C7Z
TITLE PLANT ENZYME CRYSTAL FORM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-KETOACYL-COA THIOLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 38-441;
COMPND 5 SYNONYM: BETA-KETOTHIOLASE 2, ACETYL-COA ACYLTRANSFERASE 2,
COMPND 6 PEROXISOMAL 3-OXOACYL-COA THIOLASE 2, PEROXISOME DEFECTIVE PROTEIN 1;
COMPND 7 EC: 2.3.1.16;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS FATTY ACID METABOLISM, TRANSFERASE, OXYLIPIN SYNTHESIS, LIPID
KEYWDS 2 SYNTHESIS, ACYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SUNDARAMOORTHY,E.MICOSSI,M.S.ALPHEY,G.A.LEONARD,W.N.HUNTER
REVDAT 4 13-DEC-23 2C7Z 1 REMARK
REVDAT 3 13-JUL-11 2C7Z 1 VERSN
REVDAT 2 24-FEB-09 2C7Z 1 VERSN
REVDAT 1 17-MAY-06 2C7Z 0
JRNL AUTH R.SUNDARAMOORTHY,E.MICOSSI,M.S.ALPHEY,V.GERMAIN,J.H.BRYCE,
JRNL AUTH 2 S.M.SMITH,G.A.LEONARD,W.N.HUNTER
JRNL TITL THE CRYSTAL STRUCTURE OF A PLANT 3-KETOACYL-COA THIOLASE
JRNL TITL 2 REVEALS THE POTENTIAL FOR REDOX CONTROL OF PEROXISOMAL FATTY
JRNL TITL 3 ACID BETA-OXIDATION.
JRNL REF J.MOL.BIOL. V. 359 347 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16630629
JRNL DOI 10.1016/J.JMB.2006.03.032
REMARK 2
REMARK 2 RESOLUTION. 2.37 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) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 13748
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 725
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) : 2.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 752
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2900
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 53.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.64000
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): 0.632
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.324
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.276
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2910 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3946 ; 1.269 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 394 ; 5.644 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;34.582 ;24.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 466 ;16.722 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;18.396 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 463 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2183 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1407 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2000 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 146 ; 0.180 ; 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): 50 ; 0.217 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.102 ; 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): 2001 ; 0.460 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3116 ; 0.806 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 996 ; 1.145 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 830 ; 1.883 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 259
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2740 14.6320 5.4600
REMARK 3 T TENSOR
REMARK 3 T11: -0.0338 T22: -0.2261
REMARK 3 T33: -0.4115 T12: -0.0349
REMARK 3 T13: -0.0113 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 4.3963 L22: 5.7636
REMARK 3 L33: 2.1186 L12: -3.5734
REMARK 3 L13: 1.3057 L23: -1.3712
REMARK 3 S TENSOR
REMARK 3 S11: 0.2854 S12: 0.1565 S13: -0.3244
REMARK 3 S21: -0.8783 S22: 0.0396 S23: 0.1466
REMARK 3 S31: 0.1268 S32: 0.0110 S33: -0.3250
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 260 A 292
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4760 5.1600 0.3380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5985 T22: -0.0790
REMARK 3 T33: 1.3035 T12: -0.0775
REMARK 3 T13: -0.8726 T23: 0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 6.6359 L22: 7.4566
REMARK 3 L33: 2.3981 L12: -3.7480
REMARK 3 L13: -3.1705 L23: 0.3004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1832 S12: 0.7340 S13: -2.7816
REMARK 3 S21: -2.0018 S22: 0.2449 S23: 3.3416
REMARK 3 S31: 0.6956 S32: -0.1316 S33: -0.4281
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 293 A 441
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7350 12.0340 18.8310
REMARK 3 T TENSOR
REMARK 3 T11: -0.2162 T22: -0.0203
REMARK 3 T33: -0.3244 T12: 0.1107
REMARK 3 T13: 0.0397 T23: 0.2432
REMARK 3 L TENSOR
REMARK 3 L11: 4.2873 L22: 7.1889
REMARK 3 L33: 2.6316 L12: -2.9831
REMARK 3 L13: 0.5507 L23: -0.9665
REMARK 3 S TENSOR
REMARK 3 S11: -0.4369 S12: -0.7866 S13: -0.8011
REMARK 3 S21: 0.3259 S22: 0.9049 S23: 1.0339
REMARK 3 S31: -0.0001 S32: -0.3575 S33: -0.4680
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2001 A 2102
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4030 14.3650 12.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: -0.0562
REMARK 3 T33: -0.3259 T12: 0.0683
REMARK 3 T13: -0.0295 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.3316 L22: 1.3636
REMARK 3 L33: 1.1192 L12: -1.0134
REMARK 3 L13: 0.2674 L23: 0.3719
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: -0.1438 S13: -0.1519
REMARK 3 S21: -0.0751 S22: 0.2549 S23: 0.1174
REMARK 3 S31: -0.0710 S32: -0.1008 S33: -0.1229
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. REGIONS WITH NO DIFFERENCE DENSITY HAVE BEEN LEFT
REMARK 3 OUT. NON DEFINED SIDE CHAINS ARE MODELLED WITH ZERO OCCUPANCY
REMARK 4
REMARK 4 2C7Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1290025856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16453
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.06000
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1AFW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% POLYETHYLENE GLYCOL 4000, 0.1M
REMARK 280 TRIS-HCL PH 8.5, 300MM MGCL2, PH 7.70
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.69750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.91050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.69750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.91050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 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 -1.000000 0.000000 0.000000 73.39500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ASP A 38
REMARK 465 GLY A 177
REMARK 465 SER A 178
REMARK 465 VAL A 179
REMARK 465 ASN A 180
REMARK 465 PRO A 181
REMARK 465 ALA A 182
REMARK 465 VAL A 183
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 184 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 205 CD OE1 NE2
REMARK 480 ARG A 206 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 249 CG CD CE NZ
REMARK 480 LYS A 254 CG CD CE NZ
REMARK 480 LYS A 275 CG CD CE NZ
REMARK 480 LYS A 277 CG CD CE NZ
REMARK 480 PHE A 280 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 LYS A 282 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 O PHE A 207 O HOH A 2042 2.17
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 GLN A 205 CG GLN A 205 CD -0.212
REMARK 500 ARG A 206 CB ARG A 206 CG -0.355
REMARK 500 LYS A 254 CB LYS A 254 CG -0.582
REMARK 500 LYS A 275 CB LYS A 275 CG 0.250
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 LYS A 254 CA - CB - CG ANGL. DEV. = 29.2 DEGREES
REMARK 500 LYS A 254 CB - CG - CD ANGL. DEV. = 26.5 DEGREES
REMARK 500 LYS A 282 CB - CG - CD ANGL. DEV. = 21.4 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 ARG A 67 -0.92 66.99
REMARK 500 ASP A 99 137.45 -174.81
REMARK 500 THR A 243 -151.84 -127.54
REMARK 500 PHE A 280 -82.41 -108.85
REMARK 500 ASP A 283 35.76 -97.16
REMARK 500 GLU A 362 47.45 -108.09
REMARK 500 PRO A 394 37.82 -86.68
REMARK 500 LEU A 395 -106.90 31.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C7Y RELATED DB: PDB
REMARK 900 PLANT ENZYME
DBREF 2C7Z A 38 441 UNP Q9S7M3 THIK2_ARATH 38 441
SEQRES 1 A 404 ASP SER ALA ALA TYR GLN ARG THR SER LEU TYR GLY ASP
SEQRES 2 A 404 ASP VAL VAL ILE VAL ALA ALA HIS ARG THR PRO LEU CYS
SEQRES 3 A 404 LYS SER LYS ARG GLY ASN PHE LYS ASP THR TYR PRO ASP
SEQRES 4 A 404 ASP LEU LEU ALA PRO VAL LEU ARG ALA LEU ILE GLU LYS
SEQRES 5 A 404 THR ASN LEU ASN PRO SER GLU VAL GLY ASP ILE VAL VAL
SEQRES 6 A 404 GLY THR VAL LEU ALA PRO GLY SER GLN ARG ALA SER GLU
SEQRES 7 A 404 CYS ARG MET ALA ALA PHE TYR ALA GLY PHE PRO GLU THR
SEQRES 8 A 404 VAL ALA VAL ARG THR VAL ASN ARG GLN CYS SER SER GLY
SEQRES 9 A 404 LEU GLN ALA VAL ALA ASP VAL ALA ALA ALA ILE LYS ALA
SEQRES 10 A 404 GLY PHE TYR ASP ILE GLY ILE GLY ALA GLY LEU GLU SER
SEQRES 11 A 404 MET THR THR ASN PRO MET ALA TRP GLU GLY SER VAL ASN
SEQRES 12 A 404 PRO ALA VAL LYS LYS PHE ALA GLN ALA GLN ASN CYS LEU
SEQRES 13 A 404 LEU PRO MET GLY VAL THR SER GLU ASN VAL ALA GLN ARG
SEQRES 14 A 404 PHE GLY VAL SER ARG GLN GLU GLN ASP GLN ALA ALA VAL
SEQRES 15 A 404 ASP SER HIS ARG LYS ALA ALA ALA ALA THR ALA ALA GLY
SEQRES 16 A 404 LYS PHE LYS ASP GLU ILE ILE PRO VAL LYS THR LYS LEU
SEQRES 17 A 404 VAL ASP PRO LYS THR GLY ASP GLU LYS PRO ILE THR VAL
SEQRES 18 A 404 SER VAL ASP ASP GLY ILE ARG PRO THR THR THR LEU ALA
SEQRES 19 A 404 SER LEU GLY LYS LEU LYS PRO VAL PHE LYS LYS ASP GLY
SEQRES 20 A 404 THR THR THR ALA GLY ASN SER SER GLN VAL SER ASP GLY
SEQRES 21 A 404 ALA GLY ALA VAL LEU LEU MET LYS ARG SER VAL ALA MET
SEQRES 22 A 404 GLN LYS GLY LEU PRO VAL LEU GLY VAL PHE ARG THR PHE
SEQRES 23 A 404 ALA ALA VAL GLY VAL ASP PRO ALA ILE MET GLY ILE GLY
SEQRES 24 A 404 PRO ALA VAL ALA ILE PRO ALA ALA VAL LYS ALA ALA GLY
SEQRES 25 A 404 LEU GLU LEU ASP ASP ILE ASP LEU PHE GLU ILE ASN GLU
SEQRES 26 A 404 ALA PHE ALA SER GLN PHE VAL TYR CYS ARG ASN LYS LEU
SEQRES 27 A 404 GLY LEU ASP PRO GLU LYS ILE ASN VAL ASN GLY GLY ALA
SEQRES 28 A 404 MET ALA ILE GLY HIS PRO LEU GLY ALA THR GLY ALA ARG
SEQRES 29 A 404 CYS VAL ALA THR LEU LEU HIS GLU MET LYS ARG ARG GLY
SEQRES 30 A 404 LYS ASP CYS ARG PHE GLY VAL VAL SER MET CYS ILE GLY
SEQRES 31 A 404 THR GLY MET GLY ALA ALA ALA VAL PHE GLU ARG GLY ASP
SEQRES 32 A 404 GLY
FORMUL 2 HOH *102(H2 O)
HELIX 1 1 PRO A 75 ASN A 91 1 17
HELIX 2 2 ASN A 93 VAL A 97 5 5
HELIX 3 3 SER A 110 ALA A 123 1 14
HELIX 4 4 GLY A 141 ALA A 154 1 14
HELIX 5 5 LYS A 184 GLY A 208 1 25
HELIX 6 6 SER A 210 GLY A 232 1 23
HELIX 7 7 THR A 269 GLY A 274 1 6
HELIX 8 8 ARG A 306 LYS A 312 1 7
HELIX 9 9 ILE A 335 ALA A 348 1 14
HELIX 10 10 GLU A 351 ILE A 355 5 5
HELIX 11 11 PHE A 364 LEU A 375 1 12
HELIX 12 12 ASP A 378 LYS A 381 5 4
HELIX 13 13 GLY A 387 GLY A 392 1 6
HELIX 14 14 PRO A 394 GLY A 396 5 3
HELIX 15 15 ALA A 397 GLY A 414 1 18
SHEET 1 AA 4 TYR A 42 LEU A 47 0
SHEET 2 AA 4 GLY A 318 GLY A 327 -1 O PHE A 323 N SER A 46
SHEET 3 AA 4 VAL A 52 ARG A 59 -1 O VAL A 52 N PHE A 320
SHEET 4 AA 4 SER A 295 LYS A 305 -1 O ALA A 300 N HIS A 58
SHEET 1 AB 5 TYR A 42 LEU A 47 0
SHEET 2 AB 5 GLY A 318 GLY A 327 -1 O PHE A 323 N SER A 46
SHEET 3 AB 5 MET A 430 ARG A 438 -1 O GLY A 431 N VAL A 326
SHEET 4 AB 5 PHE A 419 CYS A 425 -1 O GLY A 420 N PHE A 436
SHEET 5 AB 5 LEU A 357 ILE A 360 1 O LEU A 357 N VAL A 421
SHEET 1 AC 2 VAL A 241 VAL A 246 0
SHEET 2 AC 2 GLU A 253 VAL A 258 -1 O LYS A 254 N LEU A 245
SSBOND 1 CYS A 138 CYS A 192 1555 1555 2.04
CRYST1 73.395 95.821 56.125 90.00 90.00 90.00 P 21 21 2 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 0.013625 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010436 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
