HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-MAR-11 3R0T
TITLE CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN COMPLEX
TITLE 2 WITH THE INHIBITOR CX-5279
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-337;
COMPND 5 SYNONYM: CK II ALPHA;
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, CK2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS KINASE, CK2-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BATTISTUTTA,E.PAPINUTTO,G.LOLLI,F.PIERRE,M.HADDACH,D.M.RYCKMAN
REVDAT 3 13-SEP-23 3R0T 1 REMARK
REVDAT 2 29-OCT-14 3R0T 1 AUTHOR
REVDAT 1 07-DEC-11 3R0T 0
JRNL AUTH R.BATTISTUTTA,G.COZZA,F.PIERRE,E.PAPINUTTO,G.LOLLI,S.SARNO,
JRNL AUTH 2 S.E.O'BRIEN,A.SIDDIQUI-JAIN,M.HADDACH,K.ANDERES,D.M.RYCKMAN,
JRNL AUTH 3 F.MEGGIO,L.A.PINNA
JRNL TITL UNPRECEDENTED SELECTIVITY AND STRUCTURAL DETERMINANTS OF A
JRNL TITL 2 NEW CLASS OF PROTEIN KINASE CK2 INHIBITORS IN CLINICAL
JRNL TITL 3 TRIALS FOR THE TREATMENT OF CANCER.
JRNL REF BIOCHEMISTRY V. 50 8478 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21870818
JRNL DOI 10.1021/BI2008382
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.COZZA,M.MAZZORANA,E.PAPINUTTO,J.BAIN,M.ELLIOTT,G.DI MAIRA,
REMARK 1 AUTH 2 A.GIANONCELLI,M.A.PAGANO,S.SARNO,M.RUZZENE,R.BATTISTUTTA,
REMARK 1 AUTH 3 F.MEGGIO,S.MORO,G.ZAGOTTO,L.A.PINNA
REMARK 1 TITL QUINALIZARIN AS A POTENT, SELECTIVE AND CELL-PERMEABLE
REMARK 1 TITL 2 INHIBITOR OF PROTEIN KINASE CK2.
REMARK 1 REF BIOCHEM.J. V. 421 387 2009
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 19432557
REMARK 1 DOI 10.1042/BJ20090069
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 28526
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1420
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 35.1842 - 3.7690 0.99 3103 165 0.1437 0.1687
REMARK 3 2 3.7690 - 2.9920 0.99 3026 162 0.1456 0.1894
REMARK 3 3 2.9920 - 2.6140 1.00 3033 153 0.1662 0.2429
REMARK 3 4 2.6140 - 2.3750 0.99 2975 179 0.1725 0.2541
REMARK 3 5 2.3750 - 2.2048 0.99 3009 152 0.1654 0.2217
REMARK 3 6 2.2048 - 2.0749 0.97 2927 145 0.1638 0.2257
REMARK 3 7 2.0749 - 1.9710 0.92 2782 140 0.1662 0.2278
REMARK 3 8 1.9710 - 1.8852 0.85 2580 129 0.1825 0.2350
REMARK 3 9 1.8852 - 1.8126 0.71 2123 113 0.2041 0.2279
REMARK 3 10 1.8126 - 1.7500 0.51 1548 82 0.2385 0.3005
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 38.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.30980
REMARK 3 B22 (A**2) : 3.47990
REMARK 3 B33 (A**2) : 2.82990
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.16510
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2946
REMARK 3 ANGLE : 1.036 3976
REMARK 3 CHIRALITY : 0.075 406
REMARK 3 PLANARITY : 0.005 501
REMARK 3 DIHEDRAL : 13.608 1109
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4641 -55.6146 14.6268
REMARK 3 T TENSOR
REMARK 3 T11: 0.1667 T22: 0.1553
REMARK 3 T33: 0.2001 T12: -0.0541
REMARK 3 T13: 0.0353 T23: -0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 0.0564 L22: 0.0078
REMARK 3 L33: 0.0150 L12: 0.0243
REMARK 3 L13: 0.0083 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: 0.0526 S13: -0.0471
REMARK 3 S21: -0.0062 S22: 0.0860 S23: -0.0703
REMARK 3 S31: -0.0106 S32: -0.0466 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 14:32)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9593 -56.5547 8.8193
REMARK 3 T TENSOR
REMARK 3 T11: 0.2184 T22: 0.1470
REMARK 3 T33: 0.3446 T12: 0.0235
REMARK 3 T13: 0.0536 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 0.0139 L22: 0.0999
REMARK 3 L33: 0.0686 L12: -0.0127
REMARK 3 L13: 0.0311 L23: -0.0074
REMARK 3 S TENSOR
REMARK 3 S11: -0.2488 S12: 0.1931 S13: -0.1999
REMARK 3 S21: -0.0211 S22: 0.0957 S23: -0.1243
REMARK 3 S31: 0.1808 S32: 0.1616 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 33:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0192 -34.0681 15.6464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1317 T22: 0.2292
REMARK 3 T33: 0.2319 T12: -0.0256
REMARK 3 T13: 0.0088 T23: -0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 0.0751 L22: 0.1045
REMARK 3 L33: 0.1087 L12: -0.0117
REMARK 3 L13: 0.0879 L23: 0.0255
REMARK 3 S TENSOR
REMARK 3 S11: -0.0732 S12: 0.0348 S13: -0.0756
REMARK 3 S21: -0.0804 S22: -0.1905 S23: 0.2135
REMARK 3 S31: -0.0276 S32: 0.0701 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 52:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1118 -31.5914 11.3104
REMARK 3 T TENSOR
REMARK 3 T11: 0.1156 T22: 0.2072
REMARK 3 T33: 0.1295 T12: -0.0180
REMARK 3 T13: -0.0353 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0728 L22: 0.0127
REMARK 3 L33: 0.0385 L12: -0.0320
REMARK 3 L13: -0.0050 L23: 0.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0461 S12: 0.1432 S13: 0.2397
REMARK 3 S21: -0.1383 S22: 0.0626 S23: 0.0589
REMARK 3 S31: 0.0279 S32: -0.0798 S33: 0.0007
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 72:102)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7116 -44.4796 11.8194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1217 T22: 0.1772
REMARK 3 T33: 0.1597 T12: 0.0066
REMARK 3 T13: -0.0140 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.1791 L22: 0.2326
REMARK 3 L33: 0.1170 L12: 0.1641
REMARK 3 L13: 0.0026 L23: 0.1089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.1009 S13: -0.1852
REMARK 3 S21: 0.0915 S22: 0.0280 S23: -0.1044
REMARK 3 S31: 0.0618 S32: 0.0149 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 103:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9998 -29.1819 10.8388
REMARK 3 T TENSOR
REMARK 3 T11: 0.1312 T22: 0.1502
REMARK 3 T33: 0.1780 T12: 0.0178
REMARK 3 T13: -0.0068 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.0500 L22: 0.0814
REMARK 3 L33: 0.2482 L12: -0.0064
REMARK 3 L13: -0.0006 L23: -0.1427
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0020 S13: 0.2493
REMARK 3 S21: 0.0802 S22: 0.0149 S23: -0.1391
REMARK 3 S31: -0.0785 S32: -0.0440 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 140:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9353 -41.3947 15.1453
REMARK 3 T TENSOR
REMARK 3 T11: 0.0934 T22: 0.0745
REMARK 3 T33: 0.1054 T12: -0.0020
REMARK 3 T13: -0.0027 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 0.5752 L22: 0.4700
REMARK 3 L33: 0.2096 L12: 0.0653
REMARK 3 L13: -0.1833 L23: -0.2846
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: 0.1121 S13: -0.0482
REMARK 3 S21: 0.0253 S22: 0.0386 S23: -0.1052
REMARK 3 S31: 0.0006 S32: -0.0174 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 225:247)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7560 -31.9870 26.3692
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.0805
REMARK 3 T33: 0.1055 T12: 0.0151
REMARK 3 T13: -0.0151 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.1356 L22: 0.0378
REMARK 3 L33: 0.0555 L12: -0.0798
REMARK 3 L13: 0.0674 L23: -0.0466
REMARK 3 S TENSOR
REMARK 3 S11: -0.0772 S12: 0.0027 S13: 0.1597
REMARK 3 S21: 0.1155 S22: 0.0023 S23: -0.1846
REMARK 3 S31: -0.0997 S32: -0.0487 S33: -0.0003
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 248:329)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9085 -37.9654 18.3039
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.1009
REMARK 3 T33: 0.0675 T12: -0.0082
REMARK 3 T13: -0.0036 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.4401 L22: 0.2274
REMARK 3 L33: 0.3372 L12: -0.1399
REMARK 3 L13: -0.2005 L23: -0.0276
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: 0.1025 S13: -0.0126
REMARK 3 S21: 0.0164 S22: 0.0378 S23: -0.0172
REMARK 3 S31: 0.0227 S32: -0.1320 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-10
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 : 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) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28551
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 46.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
REMARK 200 R SYM FOR SHELL (I) : 0.46200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: PDB ENTRY 2PVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2M LI2SO4, 0.1M TRIS
REMARK 280 PH 8.5, 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 23.09200
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 ASP A 330
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 465 SER A 336
REMARK 465 SER A 337
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 VAL A 66 CA CB CG1 CG2
REMARK 480 MET A 137 CA CB CG SD CE
REMARK 480 MET A 150 CA CB CG SD CE
REMARK 480 SER A 194 CA CB OG
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 PRO A 72 7.31 -63.10
REMARK 500 LYS A 74 171.94 77.25
REMARK 500 LYS A 75 -94.80 -122.48
REMARK 500 ASP A 156 41.13 -151.35
REMARK 500 ASP A 175 76.09 53.05
REMARK 500 ALA A 193 155.33 68.87
REMARK 500 MET A 208 54.56 -92.13
REMARK 500 HIS A 234 73.11 -103.07
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 FU9 A 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 348
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 349
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 352
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PE1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN
REMARK 900 COMPLEX WITH THE INHIBITOR CX-4945
REMARK 900 RELATED ID: 3PE2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN
REMARK 900 COMPLEX WITH THE INHIBITOR CX-5011
DBREF 3R0T A 1 337 UNP P68400 CSK21_HUMAN 1 337
SEQRES 1 A 337 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR
SEQRES 2 A 337 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR
SEQRES 3 A 337 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR
SEQRES 4 A 337 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU
SEQRES 5 A 337 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL
SEQRES 6 A 337 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE
SEQRES 7 A 337 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY
SEQRES 8 A 337 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO
SEQRES 9 A 337 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN
SEQRES 10 A 337 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP
SEQRES 11 A 337 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA
SEQRES 12 A 337 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP
SEQRES 13 A 337 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG
SEQRES 14 A 337 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR
SEQRES 15 A 337 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG
SEQRES 16 A 337 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET
SEQRES 17 A 337 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET
SEQRES 18 A 337 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS
SEQRES 19 A 337 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS
SEQRES 20 A 337 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS
SEQRES 21 A 337 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU
SEQRES 22 A 337 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS
SEQRES 23 A 337 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP
SEQRES 24 A 337 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG
SEQRES 25 A 337 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 26 A 337 THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER SER
HET FU9 A 338 32
HET SO4 A 339 5
HET SO4 A 340 5
HET SO4 A 341 5
HET SO4 A 342 5
HET PEG A 343 7
HET EDO A 344 4
HET EDO A 345 4
HET EDO A 346 4
HET EDO A 347 4
HET EDO A 348 4
HET EDO A 349 4
HET EDO A 350 4
HET EDO A 351 4
HET EDO A 352 4
HETNAM FU9 3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)
HETNAM 2 FU9 PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC
HETNAM 3 FU9 ACID
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN FU9 CX-5279
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 FU9 C22 H16 F3 N5 O2
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 PEG C4 H10 O3
FORMUL 8 EDO 9(C2 H6 O2)
FORMUL 17 HOH *334(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 76 ARG A 89 1 14
HELIX 5 5 ASP A 120 TYR A 125 1 6
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 VAL A 53 N LEU A 45
SHEET 3 A 5 LYS A 64 LEU A 70 -1 O VAL A 65 N ALA A 56
SHEET 4 A 5 THR A 108 GLU A 114 -1 O LEU A 111 N LYS A 68
SHEET 5 A 5 LEU A 97 ASP A 103 -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 1.13
SITE 1 AC1 20 LEU A 45 GLY A 46 ARG A 47 VAL A 53
SITE 2 AC1 20 VAL A 66 LYS A 68 PHE A 113 GLU A 114
SITE 3 AC1 20 HIS A 115 VAL A 116 ASN A 118 MET A 163
SITE 4 AC1 20 ILE A 174 ASP A 175 EDO A 345 EDO A 351
SITE 5 AC1 20 HOH A 370 HOH A 381 HOH A 616 HOH A 636
SITE 1 AC2 6 ARG A 80 ARG A 155 ASN A 189 VAL A 192
SITE 2 AC2 6 HOH A 369 HOH A 677
SITE 1 AC3 4 ARG A 191 LYS A 198 ASN A 238 PEG A 343
SITE 1 AC4 8 ASP A 253 ARG A 278 ARG A 306 TYR A 307
SITE 2 AC4 8 ASP A 308 HOH A 397 HOH A 442 HOH A 465
SITE 1 AC5 5 LYS A 170 ARG A 172 HOH A 428 HOH A 463
SITE 2 AC5 5 HOH A 649
SITE 1 AC6 6 SER A 194 ARG A 195 TYR A 196 SO4 A 340
SITE 2 AC6 6 HOH A 433 HOH A 619
SITE 1 AC7 6 GLN A 36 TYR A 39 VAL A 101 ASP A 103
SITE 2 AC7 6 PRO A 104 ARG A 280
SITE 1 AC8 6 ASN A 118 ASP A 120 HIS A 160 FU9 A 338
SITE 2 AC8 6 EDO A 348 EDO A 351
SITE 1 AC9 4 ASP A 37 PRO A 295 HIS A 321 HOH A 620
SITE 1 BC1 5 PHE A 232 HOH A 372 HOH A 573 HOH A 621
SITE 2 BC1 5 HOH A 668
SITE 1 BC2 9 ASN A 118 THR A 119 ASP A 120 PHE A 121
SITE 2 BC2 9 PRO A 159 VAL A 162 MET A 163 ILE A 164
SITE 3 BC2 9 EDO A 345
SITE 1 BC3 6 LYS A 158 HIS A 160 SER A 194 EDO A 350
SITE 2 BC3 6 HOH A 618 HOH A 619
SITE 1 BC4 5 PRO A 159 PHE A 197 GLU A 230 EDO A 349
SITE 2 BC4 5 HOH A 618
SITE 1 BC5 5 ASN A 118 FU9 A 338 EDO A 345 HOH A 455
SITE 2 BC5 5 HOH A 575
SITE 1 BC6 7 PRO A 104 ARG A 278 LYS A 279 ASP A 302
SITE 2 BC6 7 HOH A 531 HOH A 642 HOH A 679
CRYST1 58.352 46.184 63.300 90.00 111.51 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 0.017137 0.000000 0.006753 0.00000
SCALE2 0.000000 0.021653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016980 0.00000
(ATOM LINES ARE NOT SHOWN.)
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