HEADER TRANSFERASE 20-DEC-07 3BQC
TITLE HIGH PH-VALUE CRYSTAL STRUCTURE OF EMODIN IN COMPLEX WITH THE
TITLE 2 CATALYTIC SUBUNIT OF PROTEIN KINASE CK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-335;
COMPND 5 SYNONYM: CASEIN KINASE II, ALPHA CHAIN, CK II;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: CSNK2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS PROTEIN KINASE CK2, CASEIN KINASE 2, EUKARYOTIC PROTEIN KINASES,
KEYWDS 2 EMODIN, ATP-COMPETITIVE INHIBITOR, ATP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, WNT SIGNALING PATHWAY
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,J.RAAF,O.-G.ISSINGER
REVDAT 4 01-NOV-23 3BQC 1 REMARK
REVDAT 3 24-FEB-09 3BQC 1 VERSN
REVDAT 2 18-MAR-08 3BQC 1 JRNL
REVDAT 1 15-JAN-08 3BQC 0
JRNL AUTH J.RAAF,K.KLOPFFLEISCH,O.-G.ISSINGER,K.NIEFIND
JRNL TITL THE CATALYTIC SUBUNIT OF HUMAN PROTEIN KINASE CK2
JRNL TITL 2 STRUCTURALLY DEVIATES FROM ITS MAIZE HOMOLOGUE IN COMPLEX
JRNL TITL 3 WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN
JRNL REF J.MOL.BIOL. V. 377 1 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18242640
JRNL DOI 10.1016/J.JMB.2008.01.008
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 47602
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) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2557
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.1560
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2773
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61000
REMARK 3 B22 (A**2) : 0.87000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.221
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2933 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2033 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3984 ; 1.390 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4902 ; 0.930 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 341 ; 5.681 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;32.663 ;23.101
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 514 ;13.113 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;21.333 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 409 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3273 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 644 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 623 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2214 ; 0.199 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1453 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1485 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 228 ; 0.164 ; 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): 18 ; 0.132 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.321 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.173 ; 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): 2190 ; 4.889 ; 6.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 668 ; 2.283 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2747 ; 5.558 ; 9.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 5.740 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1237 ; 7.173 ; 9.000
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 : 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 3 A 10
REMARK 3 RESIDUE RANGE : A 117 A 330
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4790 -58.6640 -42.0290
REMARK 3 T TENSOR
REMARK 3 T11: -0.0424 T22: -0.0969
REMARK 3 T33: -0.0830 T12: 0.0012
REMARK 3 T13: -0.0148 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.1396 L22: 1.0075
REMARK 3 L33: 1.1315 L12: -0.0451
REMARK 3 L13: -0.0878 L23: -0.0440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: 0.0817 S13: -0.0154
REMARK 3 S21: 0.1334 S22: 0.0384 S23: -0.0590
REMARK 3 S31: -0.0513 S32: 0.0122 S33: -0.0354
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 11 A 116
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5120 -63.2740 -46.4970
REMARK 3 T TENSOR
REMARK 3 T11: -0.0245 T22: 0.0686
REMARK 3 T33: 0.0992 T12: 0.0464
REMARK 3 T13: -0.0205 T23: -0.0920
REMARK 3 L TENSOR
REMARK 3 L11: 4.9085 L22: 1.2345
REMARK 3 L33: 1.5308 L12: 2.4365
REMARK 3 L13: 0.7303 L23: 0.1832
REMARK 3 S TENSOR
REMARK 3 S11: 0.0323 S12: 0.1281 S13: -0.4884
REMARK 3 S21: 0.1374 S22: 0.0187 S23: -0.3061
REMARK 3 S31: 0.0432 S32: 0.2978 S33: -0.0510
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3BQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045835.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.84
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50159
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 34.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : 0.03600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.60700
REMARK 200 R SYM FOR SHELL (I) : 0.60700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: 1PJK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STOCK SOLUTION: 10MG/ML
REMARK 280 PROTEIN IN 500MM NACL, 25MM TRIS/HCL, PH 8.5 EMODIN STOCK
REMARK 280 SOLUTION: 10MM IN WATER PROTEIN/EMODIN MIXTURE: EQUAL VOLUMES OF
REMARK 280 PROTEIN AND EMODIN STOCK SOLUTIONS WERE MIXED AND EQUILLIBRATED
REMARK 280 FOR 30 MIN PRIOR TO CRYSTALLIZATION RESERVOIR: 30% PEG4000, 0.2M
REMARK 280 LITHIUM SULFATE, 0.1M TRIS/HCL, PH 8.5 CRYSTALLIZATION DROP: 2
REMARK 280 MIKROLITERS PROTEIN/EMODIN MIXTURE PLUS 1 MIKROLITER RESERVOIR
REMARK 280 SOLUTION, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 22.87000
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: 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 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 1
REMARK 465 SER A 2
REMARK 465 GLN A 331
REMARK 465 ALA A 332
REMARK 465 ARG A 333
REMARK 465 MET A 334
REMARK 465 GLY A 335
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 HOH A 507 O HOH A 677 2.00
REMARK 500 O HOH A 412 O HOH A 693 2.11
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 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 316 NE - CZ - NH2 ANGL. DEV. = 3.7 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 VAL A 73 -74.51 -137.68
REMARK 500 LYS A 74 116.16 -163.43
REMARK 500 ASP A 156 43.22 -149.10
REMARK 500 ASP A 175 76.18 51.27
REMARK 500 ALA A 193 162.04 60.96
REMARK 500 ASP A 205 31.30 70.80
REMARK 500 MET A 208 55.42 -94.36
REMARK 500 HIS A 234 68.99 -105.26
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 CL A 336
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMO A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PVR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ADENYLYL IMIDODIPHOSPHATE (AMPPNP)
REMARK 900 AND SULFATE
REMARK 900 RELATED ID: 2RKP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH 5,6-DICHLORO BENZIMIDAZOLE-BETA-D-
REMARK 900 RIBOFURANOSIDE
REMARK 900 RELATED ID: 1F0Q RELATED DB: PDB
REMARK 900 THE SAME INHIBITOR (EMODIN) WITH THE HOMOLOGOUS ENYZME FROM ZEA MAYS
REMARK 900 RELATED ID: 1JWH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH A NON-CATALYTIC SUBUNIT
DBREF 3BQC A 1 335 UNP P68400 CSK21_HUMAN 1 335
SEQRES 1 A 335 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR
SEQRES 2 A 335 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR
SEQRES 3 A 335 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR
SEQRES 4 A 335 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU
SEQRES 5 A 335 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL
SEQRES 6 A 335 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE
SEQRES 7 A 335 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY
SEQRES 8 A 335 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO
SEQRES 9 A 335 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN
SEQRES 10 A 335 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP
SEQRES 11 A 335 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA
SEQRES 12 A 335 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP
SEQRES 13 A 335 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG
SEQRES 14 A 335 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR
SEQRES 15 A 335 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG
SEQRES 16 A 335 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET
SEQRES 17 A 335 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET
SEQRES 18 A 335 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS
SEQRES 19 A 335 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS
SEQRES 20 A 335 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS
SEQRES 21 A 335 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU
SEQRES 22 A 335 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS
SEQRES 23 A 335 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP
SEQRES 24 A 335 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG
SEQRES 25 A 335 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 26 A 335 THR VAL VAL LYS ASP GLN ALA ARG MET GLY
HET CL A 336 1
HET CL A 337 1
HET EMO A 400 20
HETNAM CL CHLORIDE ION
HETNAM EMO 3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE
HETSYN EMO EMODIN
FORMUL 2 CL 2(CL 1-)
FORMUL 4 EMO C15 H10 O5
FORMUL 5 HOH *300(H2 O)
HELIX 1 1 PRO A 20 ASP A 25 1 6
HELIX 2 2 TYR A 26 HIS A 29 5 4
HELIX 3 3 ASN A 35 ASP A 37 5 3
HELIX 4 4 LYS A 74 ARG A 89 1 16
HELIX 5 5 ASP A 120 LEU A 124 5 5
HELIX 6 6 THR A 129 MET A 150 1 22
HELIX 7 7 LYS A 158 HIS A 160 5 3
HELIX 8 8 ASP A 175 ALA A 179 5 5
HELIX 9 9 SER A 194 LYS A 198 5 5
HELIX 10 10 GLY A 199 VAL A 204 1 6
HELIX 11 11 TYR A 211 ARG A 228 1 18
HELIX 12 12 ASP A 237 GLY A 250 1 14
HELIX 13 13 GLY A 250 TYR A 261 1 12
HELIX 14 14 ASP A 266 ILE A 272 5 7
HELIX 15 15 ARG A 280 VAL A 285 5 6
HELIX 16 16 ASN A 289 VAL A 293 5 5
HELIX 17 17 SER A 294 LEU A 305 1 12
HELIX 18 18 ASP A 308 ARG A 312 5 5
HELIX 19 19 THR A 314 GLU A 320 1 7
HELIX 20 20 HIS A 321 TYR A 325 5 5
SHEET 1 A 5 TYR A 39 ARG A 47 0
SHEET 2 A 5 SER A 51 ASN A 58 -1 O GLU A 55 N VAL A 42
SHEET 3 A 5 LYS A 64 LEU A 70 -1 O VAL A 67 N PHE A 54
SHEET 4 A 5 PRO A 109 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 A 5 LEU A 97 LYS A 102 -1 N VAL A 101 O ALA A 110
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 LYS A 170 N ASP A 165
CISPEP 1 GLU A 230 PRO A 231 0 -9.15
SITE 1 AC1 2 ARG A 80 ARG A 155
SITE 1 AC2 5 HIS A 148 THR A 314 ALA A 315 HOH A 431
SITE 2 AC2 5 HOH A 462
SITE 1 AC3 12 VAL A 53 VAL A 66 LYS A 68 ILE A 95
SITE 2 AC3 12 PHE A 113 VAL A 116 ASN A 118 MET A 163
SITE 3 AC3 12 ILE A 174 ASP A 175 HOH A 405 HOH A 432
CRYST1 58.870 45.740 63.500 90.00 111.78 90.00 P 1 21 1 2
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 0.016987 0.000000 0.006787 0.00000
SCALE2 0.000000 0.021863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016959 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
