HEADER TRANSFERASE 12-AUG-14 4UBA
TITLE LOW-SALT STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT WITH 4'-
TITLE 2 CARBOXY-6,8-BROMO-FLAVONOL (FLC26)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-335;
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS PROTEIN KINASE CK2, ATP-COMPETITIVE INHIBITORS, HALOGEN BOND, 4'-
KEYWDS 2 CARBOXY-6, 8-BROMO-FLAVONOL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,N.BISCHOFF,B.GUERRA,A.GOLUB,O.-G.ISSINGER
REVDAT 2 29-JUL-15 4UBA 1 JRNL
REVDAT 1 01-JUL-15 4UBA 0
JRNL AUTH B.GUERRA,N.BISCHOFF,V.G.BDZHOLA,S.M.YARMOLUK,O.G.ISSINGER,
JRNL AUTH 2 A.G.GOLUB,K.NIEFIND
JRNL TITL A NOTE OF CAUTION ON THE ROLE OF HALOGEN BONDS FOR PROTEIN
JRNL TITL 2 KINASE/INHIBITOR RECOGNITION SUGGESTED BY HIGH- AND LOW-SALT
JRNL TITL 3 CK2 ALPHA COMPLEX STRUCTURES.
JRNL REF ACS CHEM.BIOL. V. 10 1654 2015
JRNL REFN ESSN 1554-8937
JRNL PMID 25961323
JRNL DOI 10.1021/ACSCHEMBIO.5B00235
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.G.GOLUB,V.G.BDZHOLA,Y.V.KYSHENIA,V.M.SAPELKIN,
REMARK 1 AUTH 2 A.O.PRYKHOD'KO,O.P.KUKHARENKO,O.V.OSTRYNSKA,S.M.YARMOLUK
REMARK 1 TITL STRUCTURE-BASED DISCOVERY OF NOVEL FLAVONOL INHIBITORS OF
REMARK 1 TITL 2 HUMAN PROTEIN KINASE CK2.
REMARK 1 REF MOL. CELL. BIOCHEM. V. 356 107 2011
REMARK 1 REFN ISSN 0300-8177
REMARK 1 PMID 21735097
REMARK 1 DOI 10.1007/S11010-011-0945-8
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.ERMAKOVA,B.BOLDYREFF,O.G.ISSINGER,K.NIEFIND
REMARK 1 TITL CRYSTAL STRUCTURE OF A C-TERMINAL DELETION MUTANT OF HUMAN
REMARK 1 TITL 2 PROTEIN KINASE CK2 CATALYTIC SUBUNIT.
REMARK 1 REF J. MOL. BIOL. V. 330 925 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12860116
REMARK 1 DOI 10.1016/S0022-2836(03)00638-7
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.NIEFIND,B.GUERRA,I.ERMAKOWA,O.G.ISSINGER
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2: INSIGHTS INTO
REMARK 1 TITL 2 BASIC PROPERTIES OF THE CK2 HOLOENZYME.
REMARK 1 REF EMBO J. V. 20 5320 2001
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 11574463
REMARK 1 DOI 10.1093/EMBOJ/20.19.5320
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 20353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1018
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 44.5526 - 5.7264 1.00 2970 155 0.1951 0.2246
REMARK 3 2 5.7264 - 4.5467 1.00 2834 150 0.1639 0.2095
REMARK 3 3 4.5467 - 3.9723 1.00 2791 147 0.1563 0.2288
REMARK 3 4 3.9723 - 3.6093 1.00 2764 145 0.1734 0.2271
REMARK 3 5 3.6093 - 3.3507 1.00 2758 146 0.2028 0.2892
REMARK 3 6 3.3507 - 3.1532 1.00 2758 145 0.2263 0.2751
REMARK 3 7 3.1532 - 2.9953 0.90 2460 130 0.2743 0.2998
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.002 5824
REMARK 3 ANGLE : 0.552 7880
REMARK 3 CHIRALITY : 0.023 810
REMARK 3 PLANARITY : 0.003 1012
REMARK 3 DIHEDRAL : 10.416 2192
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0247 -48.3778 17.8831
REMARK 3 T TENSOR
REMARK 3 T11: 0.5284 T22: 0.4625
REMARK 3 T33: 0.2003 T12: -0.0133
REMARK 3 T13: 0.0231 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 5.5164 L22: 1.4263
REMARK 3 L33: 3.2468 L12: 1.2433
REMARK 3 L13: 2.2836 L23: 0.6970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0302 S12: -0.3100 S13: -0.1529
REMARK 3 S21: 0.1503 S22: -0.0029 S23: 0.1238
REMARK 3 S31: -0.0570 S32: -0.2380 S33: -0.0722
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1995 -40.1436 0.9043
REMARK 3 T TENSOR
REMARK 3 T11: 1.1744 T22: 0.7890
REMARK 3 T33: 0.4711 T12: -0.1623
REMARK 3 T13: -0.0918 T23: 0.1954
REMARK 3 L TENSOR
REMARK 3 L11: 2.5585 L22: 2.2166
REMARK 3 L33: 5.7389 L12: 1.4437
REMARK 3 L13: -2.8564 L23: -3.5292
REMARK 3 S TENSOR
REMARK 3 S11: -0.6507 S12: 1.0443 S13: 0.1216
REMARK 3 S21: -1.6251 S22: 0.0617 S23: -0.0213
REMARK 3 S31: -0.3735 S32: -0.8052 S33: 0.1653
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6481 -38.2165 6.4448
REMARK 3 T TENSOR
REMARK 3 T11: 0.6242 T22: 0.4500
REMARK 3 T33: 0.2301 T12: -0.1253
REMARK 3 T13: 0.0293 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 3.2471 L22: 1.5190
REMARK 3 L33: 2.7253 L12: 0.4204
REMARK 3 L13: 0.2008 L23: -0.1127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0785 S12: 0.3895 S13: 0.0472
REMARK 3 S21: -0.4358 S22: 0.1153 S23: 0.0112
REMARK 3 S31: -0.0758 S32: 0.1517 S33: -0.0433
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0645 -65.6474 46.3705
REMARK 3 T TENSOR
REMARK 3 T11: 0.5675 T22: 0.5736
REMARK 3 T33: 0.2245 T12: 0.0580
REMARK 3 T13: 0.0474 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.4708 L22: 4.5700
REMARK 3 L33: 1.4394 L12: -0.7376
REMARK 3 L13: -0.1068 L23: 1.2263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.0637 S13: -0.0338
REMARK 3 S21: 0.0594 S22: -0.0261 S23: -0.0773
REMARK 3 S31: 0.1245 S32: -0.0387 S33: -0.0224
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5592 -64.0491 26.9751
REMARK 3 T TENSOR
REMARK 3 T11: 1.1511 T22: 1.3130
REMARK 3 T33: 0.6944 T12: 0.2185
REMARK 3 T13: -0.1906 T23: -0.1547
REMARK 3 L TENSOR
REMARK 3 L11: 8.6246 L22: 3.7195
REMARK 3 L33: 3.3412 L12: -4.5526
REMARK 3 L13: 3.1735 L23: -0.2032
REMARK 3 S TENSOR
REMARK 3 S11: 0.9489 S12: 2.6629 S13: 0.0249
REMARK 3 S21: -0.9373 S22: -1.3647 S23: -0.3056
REMARK 3 S31: 0.0129 S32: 1.1629 S33: 0.5117
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 130 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0786 -46.4573 36.1509
REMARK 3 T TENSOR
REMARK 3 T11: 0.6685 T22: 0.4759
REMARK 3 T33: 0.2349 T12: 0.1405
REMARK 3 T13: 0.0001 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.8518 L22: 2.6164
REMARK 3 L33: 2.3424 L12: -0.4247
REMARK 3 L13: -0.1655 L23: -0.2315
REMARK 3 S TENSOR
REMARK 3 S11: 0.2113 S12: 0.1376 S13: 0.0461
REMARK 3 S21: -0.4726 S22: -0.0899 S23: 0.0566
REMARK 3 S31: -0.2963 S32: -0.0806 S33: -0.1287
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 4UBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20425
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.995
REMARK 200 RESOLUTION RANGE LOW (A) : 44.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 59.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 30 %(W/V) PEG4000, 0.2 M
REMARK 280 AMMONIUM ACETATE, 0.1 M TRISODIUM CITRATE, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 62.07000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 93.10500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.03500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 93.10500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.03500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.07000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 GLY A 335
REMARK 465 MET B 1
REMARK 465 GLY B 335
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 47 -165.47 -110.27
REMARK 500 ASN A 61 6.03 -154.65
REMARK 500 PRO A 72 94.20 -53.42
REMARK 500 ASN A 117 85.86 -65.20
REMARK 500 ASP A 156 45.19 -158.25
REMARK 500 ASP A 175 87.21 56.07
REMARK 500 ALA A 193 157.73 67.53
REMARK 500 MET A 208 53.74 -95.86
REMARK 500 ASP A 210 -152.22 -141.91
REMARK 500 PRO A 267 1.52 -67.07
REMARK 500 ARG B 47 -166.62 -111.31
REMARK 500 ASN B 61 6.21 -153.18
REMARK 500 PRO B 72 98.45 -55.23
REMARK 500 ASN B 117 85.91 -64.62
REMARK 500 ASP B 156 45.20 -158.52
REMARK 500 ASP B 175 86.94 56.15
REMARK 500 ALA B 193 159.53 67.86
REMARK 500 MET B 208 52.32 -96.01
REMARK 500 ASP B 210 -152.29 -141.45
REMARK 500 PRO B 267 2.09 -66.98
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 3G5 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3G5 B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UB7 RELATED DB: PDB
REMARK 900 4UB7 CONTAINS THE SAME ENZYME/INHIBITOR COMPLEX AFTER
REMARK 900 CRYSTALLIZATION FROM A HIGH-SALT MEDIUM (4 M SODIUM CHLORIDE).
DBREF 4UBA A 1 335 UNP P68400 CSK21_HUMAN 1 335
DBREF 4UBA B 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
SEQRES 1 B 335 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR
SEQRES 2 B 335 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR
SEQRES 3 B 335 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR
SEQRES 4 B 335 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU
SEQRES 5 B 335 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL
SEQRES 6 B 335 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE
SEQRES 7 B 335 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY
SEQRES 8 B 335 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO
SEQRES 9 B 335 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN
SEQRES 10 B 335 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP
SEQRES 11 B 335 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA
SEQRES 12 B 335 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP
SEQRES 13 B 335 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG
SEQRES 14 B 335 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR
SEQRES 15 B 335 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG
SEQRES 16 B 335 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET
SEQRES 17 B 335 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET
SEQRES 18 B 335 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS
SEQRES 19 B 335 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS
SEQRES 20 B 335 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS
SEQRES 21 B 335 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU
SEQRES 22 B 335 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS
SEQRES 23 B 335 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP
SEQRES 24 B 335 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG
SEQRES 25 B 335 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 26 B 335 THR VAL VAL LYS ASP GLN ALA ARG MET GLY
HET 3G5 A 401 23
HET 3G5 B 401 23
HETNAM 3G5 4-(6,8-DIBROMO-3-HYDROXY-4-OXO-4H-CHROMEN-2-YL)BENZOIC
HETNAM 2 3G5 ACID
FORMUL 3 3G5 2(C16 H8 BR2 O5)
FORMUL 5 HOH *45(H2 O)
HELIX 1 AA1 PRO A 20 ASP A 25 1 6
HELIX 2 AA2 TYR A 26 HIS A 29 5 4
HELIX 3 AA3 LYS A 74 ARG A 89 1 16
HELIX 4 AA4 ASP A 120 TYR A 125 1 6
HELIX 5 AA5 THR A 129 MET A 150 1 22
HELIX 6 AA6 LYS A 158 HIS A 160 5 3
HELIX 7 AA7 SER A 194 LYS A 198 5 5
HELIX 8 AA8 GLY A 199 VAL A 204 1 6
HELIX 9 AA9 TYR A 211 PHE A 227 1 17
HELIX 10 AB1 ASP A 237 GLY A 250 1 14
HELIX 11 AB2 GLY A 250 TYR A 261 1 12
HELIX 12 AB3 ARG A 268 ILE A 272 5 5
HELIX 13 AB4 ARG A 280 VAL A 285 5 6
HELIX 14 AB5 SER A 294 LYS A 303 1 10
HELIX 15 AB6 THR A 314 GLU A 320 1 7
HELIX 16 AB7 HIS A 321 TYR A 323 5 3
HELIX 17 AB8 PHE A 324 ARG A 333 1 10
HELIX 18 AB9 PRO B 20 ASP B 25 1 6
HELIX 19 AC1 TYR B 26 HIS B 29 5 4
HELIX 20 AC2 ASN B 35 ASP B 37 5 3
HELIX 21 AC3 LYS B 74 ARG B 89 1 16
HELIX 22 AC4 ASP B 120 TYR B 125 1 6
HELIX 23 AC5 THR B 129 MET B 150 1 22
HELIX 24 AC6 LYS B 158 HIS B 160 5 3
HELIX 25 AC7 SER B 194 LYS B 198 5 5
HELIX 26 AC8 GLY B 199 VAL B 204 1 6
HELIX 27 AC9 TYR B 211 PHE B 227 1 17
HELIX 28 AD1 ASP B 237 GLY B 250 1 14
HELIX 29 AD2 GLY B 250 TYR B 261 1 12
HELIX 30 AD3 ARG B 268 ILE B 272 5 5
HELIX 31 AD4 ARG B 280 VAL B 285 5 6
HELIX 32 AD5 SER B 294 LYS B 303 1 10
HELIX 33 AD6 THR B 314 GLU B 320 1 7
HELIX 34 AD7 HIS B 321 TYR B 323 5 3
HELIX 35 AD8 PHE B 324 ARG B 333 1 10
SHEET 1 AA1 6 GLY A 34 ASN A 35 0
SHEET 2 AA1 6 LEU A 97 LYS A 102 1 O LYS A 102 N GLY A 34
SHEET 3 AA1 6 PRO A 109 GLU A 114 -1 O VAL A 112 N ASP A 99
SHEET 4 AA1 6 LYS A 64 LEU A 70 -1 N LYS A 68 O LEU A 111
SHEET 5 AA1 6 SER A 51 ASN A 58 -1 N PHE A 54 O VAL A 67
SHEET 6 AA1 6 TYR A 39 GLY A 46 -1 N VAL A 42 O GLU A 55
SHEET 1 AA2 2 ILE A 152 MET A 153 0
SHEET 2 AA2 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 AA3 2 VAL A 162 ASP A 165 0
SHEET 2 AA3 2 LYS A 170 LEU A 173 -1 O LYS A 170 N ASP A 165
SHEET 1 AA4 5 TYR B 39 GLY B 46 0
SHEET 2 AA4 5 SER B 51 ASN B 58 -1 O GLU B 55 N ARG B 43
SHEET 3 AA4 5 LYS B 64 LEU B 70 -1 O VAL B 67 N PHE B 54
SHEET 4 AA4 5 PRO B 109 PHE B 113 -1 O LEU B 111 N LYS B 68
SHEET 5 AA4 5 LEU B 97 LYS B 102 -1 N ALA B 98 O VAL B 112
SHEET 1 AA5 2 ILE B 152 MET B 153 0
SHEET 2 AA5 2 GLU B 180 PHE B 181 -1 O GLU B 180 N MET B 153
SHEET 1 AA6 2 VAL B 162 ASP B 165 0
SHEET 2 AA6 2 LYS B 170 LEU B 173 -1 O LYS B 170 N ASP B 165
CISPEP 1 GLU A 230 PRO A 231 0 -2.16
CISPEP 2 GLU B 230 PRO B 231 0 -1.38
SITE 1 AC1 11 LEU A 45 VAL A 66 LYS A 68 ILE A 95
SITE 2 AC1 11 PHE A 113 GLU A 114 HIS A 115 VAL A 116
SITE 3 AC1 11 MET A 163 ILE A 174 ASP A 175
SITE 1 AC2 10 LEU B 45 VAL B 66 LYS B 68 PHE B 113
SITE 2 AC2 10 GLU B 114 HIS B 115 VAL B 116 MET B 163
SITE 3 AC2 10 ILE B 174 ASP B 175
CRYST1 126.000 126.000 124.140 90.00 90.00 90.00 P 43 21 2 16
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 0.007937 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008055 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
