HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-JAN-12 4DGM
TITLE CRYSTAL STRUCTURE OF MAIZE CK2 IN COMPLEX WITH THE INHIBITOR APIGENIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CK II, CK2-ALPHA;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 GENE: ACK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LOLLI,M.MAZZORANA,R.BATTISTUTTA
REVDAT 4 28-FEB-24 4DGM 1 REMARK SEQADV
REVDAT 3 02-JAN-13 4DGM 1 JRNL
REVDAT 2 05-SEP-12 4DGM 1 JRNL
REVDAT 1 01-AUG-12 4DGM 0
JRNL AUTH G.LOLLI,G.COZZA,M.MAZZORANA,E.TIBALDI,L.CESARO,
JRNL AUTH 2 A.DONELLA-DEANA,F.MEGGIO,A.VENERANDO,C.FRANCHIN,S.SARNO,
JRNL AUTH 3 R.BATTISTUTTA,L.A.PINNA
JRNL TITL INHIBITION OF PROTEIN KINASE CK2 BY FLAVONOIDS AND
JRNL TITL 2 TYRPHOSTINS. A STRUCTURAL INSIGHT.
JRNL REF BIOCHEMISTRY V. 51 6097 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22794353
JRNL DOI 10.1021/BI300531C
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 45014
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2263
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3122
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2723
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.91000
REMARK 3 B22 (A**2) : -17.84000
REMARK 3 B33 (A**2) : 18.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -18.85000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.023
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.024
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.599
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2865 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3874 ; 1.362 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 337 ; 5.254 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;37.071 ;23.986
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 516 ;14.053 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;19.553 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 406 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2187 ; 0.007 ; 0.021
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): 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 7 A 184
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8109 7.8203 11.1476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0648 T22: 0.2222
REMARK 3 T33: 0.1985 T12: 0.0090
REMARK 3 T13: -0.0175 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 2.6067 L22: 1.4437
REMARK 3 L33: 2.2680 L12: 1.2277
REMARK 3 L13: 1.3384 L23: 0.0496
REMARK 3 S TENSOR
REMARK 3 S11: -0.1297 S12: 0.1622 S13: -0.0716
REMARK 3 S21: 0.0688 S22: 0.0750 S23: -0.2963
REMARK 3 S31: -0.3278 S32: 0.2115 S33: 0.0548
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 185 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6360 -13.6213 9.1484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0928 T22: 0.2643
REMARK 3 T33: 0.3969 T12: 0.0537
REMARK 3 T13: -0.1425 T23: -0.1285
REMARK 3 L TENSOR
REMARK 3 L11: 2.2910 L22: 2.9735
REMARK 3 L33: 2.6085 L12: 0.7211
REMARK 3 L13: -0.0422 L23: -0.9592
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: -0.0407 S13: -0.5806
REMARK 3 S21: 0.1062 S22: 0.1754 S23: -0.6962
REMARK 3 S31: 0.3970 S32: 0.2487 S33: -0.2728
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 257 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5598 -21.3212 9.8579
REMARK 3 T TENSOR
REMARK 3 T11: 0.2611 T22: 0.3647
REMARK 3 T33: 0.5011 T12: 0.0032
REMARK 3 T13: -0.1290 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 1.2617 L22: 3.3565
REMARK 3 L33: 3.2237 L12: -0.7013
REMARK 3 L13: -0.4521 L23: 0.4007
REMARK 3 S TENSOR
REMARK 3 S11: -0.1461 S12: 0.0029 S13: -0.5883
REMARK 3 S21: 0.0050 S22: 0.2166 S23: 0.0042
REMARK 3 S31: 0.5762 S32: -0.0708 S33: -0.0705
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 295 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6265 -6.1796 6.2386
REMARK 3 T TENSOR
REMARK 3 T11: 0.0173 T22: 0.2635
REMARK 3 T33: 0.1075 T12: -0.0038
REMARK 3 T13: -0.0393 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 6.4504 L22: 3.5784
REMARK 3 L33: 3.4492 L12: -1.6651
REMARK 3 L13: -0.6821 L23: 0.1237
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: -0.0339 S13: -0.3294
REMARK 3 S21: 0.0802 S22: 0.3279 S23: -0.0101
REMARK 3 S31: 0.1283 S32: -0.2281 S33: -0.3681
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
REMARK 4
REMARK 4 4DGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45035
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 69.242
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : 0.44600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 10-20% PEG 4000, 0.2 M
REMARK 280 NA-ACETATE, PH 8, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 71.18150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.93750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.18150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.93750
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 NZ LYS A 77 O HOH A 586 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 HIS A 148 CG HIS A 148 CD2 0.066
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 ASN A 93 19.23 56.99
REMARK 500 ASP A 156 44.47 -149.29
REMARK 500 ASP A 175 77.66 51.43
REMARK 500 ALA A 193 153.47 60.81
REMARK 500 TYR A 234 75.80 -111.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGI A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DGO RELATED DB: PDB
REMARK 900 RELATED ID: 4DGN RELATED DB: PDB
DBREF 4DGM A 7 332 UNP P28523 CSK2A_MAIZE 2 327
SEQADV 4DGM MET A 89 UNP P28523 CYS 84 CONFLICT
SEQRES 1 A 326 SER LYS ALA ARG VAL TYR ALA ASP VAL ASN VAL LEU ARG
SEQRES 2 A 326 PRO LYS GLU TYR TRP ASP TYR GLU ALA LEU THR VAL GLN
SEQRES 3 A 326 TRP GLY GLU GLN ASP ASP TYR GLU VAL VAL ARG LYS VAL
SEQRES 4 A 326 GLY ARG GLY LYS TYR SER GLU VAL PHE GLU GLY ILE ASN
SEQRES 5 A 326 VAL ASN ASN ASN GLU LYS CYS ILE ILE LYS ILE LEU LYS
SEQRES 6 A 326 PRO VAL LYS LYS LYS LYS ILE LYS ARG GLU ILE LYS ILE
SEQRES 7 A 326 LEU GLN ASN LEU MET GLY GLY PRO ASN ILE VAL LYS LEU
SEQRES 8 A 326 LEU ASP ILE VAL ARG ASP GLN HIS SER LYS THR PRO SER
SEQRES 9 A 326 LEU ILE PHE GLU TYR VAL ASN ASN THR ASP PHE LYS VAL
SEQRES 10 A 326 LEU TYR PRO THR LEU THR ASP TYR ASP ILE ARG TYR TYR
SEQRES 11 A 326 ILE TYR GLU LEU LEU LYS ALA LEU ASP TYR CYS HIS SER
SEQRES 12 A 326 GLN GLY ILE MET HIS ARG ASP VAL LYS PRO HIS ASN VAL
SEQRES 13 A 326 MET ILE ASP HIS GLU LEU ARG LYS LEU ARG LEU ILE ASP
SEQRES 14 A 326 TRP GLY LEU ALA GLU PHE TYR HIS PRO GLY LYS GLU TYR
SEQRES 15 A 326 ASN VAL ARG VAL ALA SER ARG TYR PHE LYS GLY PRO GLU
SEQRES 16 A 326 LEU LEU VAL ASP LEU GLN ASP TYR ASP TYR SER LEU ASP
SEQRES 17 A 326 MET TRP SER LEU GLY CYS MET PHE ALA GLY MET ILE PHE
SEQRES 18 A 326 ARG LYS GLU PRO PHE PHE TYR GLY HIS ASP ASN HIS ASP
SEQRES 19 A 326 GLN LEU VAL LYS ILE ALA LYS VAL LEU GLY THR ASP GLY
SEQRES 20 A 326 LEU ASN VAL TYR LEU ASN LYS TYR ARG ILE GLU LEU ASP
SEQRES 21 A 326 PRO GLN LEU GLU ALA LEU VAL GLY ARG HIS SER ARG LYS
SEQRES 22 A 326 PRO TRP LEU LYS PHE MET ASN ALA ASP ASN GLN HIS LEU
SEQRES 23 A 326 VAL SER PRO GLU ALA ILE ASP PHE LEU ASP LYS LEU LEU
SEQRES 24 A 326 ARG TYR ASP HIS GLN GLU ARG LEU THR ALA LEU GLU ALA
SEQRES 25 A 326 MET THR HIS PRO TYR PHE GLN GLN VAL ARG ALA ALA GLU
SEQRES 26 A 326 ASN
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET PEG A 405 7
HET AGI A 406 20
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM AGI 5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE
HETSYN EDO ETHYLENE GLYCOL
HETSYN AGI APIGENIN
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 PEG C4 H10 O3
FORMUL 7 AGI C15 H10 O5
FORMUL 8 HOH *165(H2 O)
HELIX 1 1 ASP A 14 ARG A 19 1 6
HELIX 2 2 PRO A 20 ASP A 25 1 6
HELIX 3 3 TYR A 26 LEU A 29 5 4
HELIX 4 4 GLU A 35 ASP A 37 5 3
HELIX 5 5 LYS A 74 MET A 89 1 16
HELIX 6 6 ASP A 120 TYR A 125 1 6
HELIX 7 7 PRO A 126 LEU A 128 5 3
HELIX 8 8 THR A 129 GLN A 150 1 22
HELIX 9 9 LYS A 158 HIS A 160 5 3
HELIX 10 10 ASP A 175 ALA A 179 5 5
HELIX 11 11 SER A 194 LYS A 198 5 5
HELIX 12 12 GLY A 199 VAL A 204 1 6
HELIX 13 13 TYR A 211 PHE A 227 1 17
HELIX 14 14 ASP A 237 GLY A 250 1 14
HELIX 15 15 GLY A 250 TYR A 261 1 12
HELIX 16 16 ASP A 266 GLY A 274 1 9
HELIX 17 17 PRO A 280 MET A 285 5 6
HELIX 18 18 ASN A 289 VAL A 293 5 5
HELIX 19 19 SER A 294 LEU A 305 1 12
HELIX 20 20 THR A 314 HIS A 321 1 8
HELIX 21 21 PHE A 324 ASN A 332 1 9
SHEET 1 A 5 TYR A 39 ARG A 47 0
SHEET 2 A 5 SER A 51 ASN A 58 -1 O VAL A 53 N VAL A 45
SHEET 3 A 5 LYS A 64 LEU A 70 -1 O CYS A 65 N GLY A 56
SHEET 4 A 5 PRO A 109 GLU A 114 -1 O LEU A 111 N LYS A 68
SHEET 5 A 5 LEU A 97 ARG A 102 -1 N LEU A 98 O ILE A 112
SHEET 1 B 2 ILE A 152 MET A 153 0
SHEET 2 B 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 C 2 VAL A 162 ASP A 165 0
SHEET 2 C 2 LYS A 170 LEU A 173 -1 O ARG A 172 N MET A 163
CISPEP 1 GLU A 230 PRO A 231 0 -12.19
SITE 1 AC1 6 TYR A 125 MET A 221 GLY A 224 MET A 225
SITE 2 AC1 6 GLU A 230 HOH A 659
SITE 1 AC2 4 THR A 129 ASP A 130 HIS A 291 HOH A 553
SITE 1 AC3 9 VAL A 11 SER A 212 MET A 215 ARG A 312
SITE 2 AC3 9 LEU A 313 THR A 314 HOH A 516 HOH A 634
SITE 3 AC3 9 HOH A 635
SITE 1 AC4 5 ALA A 9 TYR A 12 ALA A 13 ASP A 14
SITE 2 AC4 5 GLN A 325
SITE 1 AC5 8 ARG A 278 ASP A 302 LEU A 305 ARG A 306
SITE 2 AC5 8 TYR A 307 ASP A 308 GLU A 311 HOH A 592
SITE 1 AC6 12 VAL A 45 VAL A 53 ILE A 66 LYS A 68
SITE 2 AC6 12 PHE A 113 VAL A 116 ASN A 118 MET A 163
SITE 3 AC6 12 ILE A 174 ASP A 175 HOH A 501 HOH A 581
CRYST1 142.363 59.875 45.931 90.00 103.40 90.00 C 1 2 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 0.007024 0.000000 0.001674 0.00000
SCALE2 0.000000 0.016702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022382 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
