HEADER TRANSFERASE 23-JUL-15 5CSH
TITLE CRYSTAL STRUCTURE OF CK2ALPHA WITH COMPOUND 4 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-329 AND N-TERMINAL EXTENSION
COMPND 5 GSMDIEFDDDADDDGSGSGSGSGS;
COMPND 6 SYNONYM: CK II ALPHA;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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: PHAT4
KEYWDS CK2ALPHA, CK2A, FRAGMENT BASED DRUG DISCOVERY, HIGH CONCENTRATION
KEYWDS 2 SCREENING, SELECTIVE ATP COMPETITIVE INHIBITORS, SURFACE ENTROPHY
KEYWDS 3 REDUCTION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BREAR,C.DE FUSCO,K.H.GEORGIOU,D.SPRING,M.HYVONEN
REVDAT 3 10-JAN-24 5CSH 1 REMARK
REVDAT 2 10-MAY-17 5CSH 1 JRNL
REVDAT 1 27-JUL-16 5CSH 0
JRNL AUTH P.BREAR,C.DE FUSCO,K.HADJE GEORGIOU,N.J.FRANCIS-NEWTON,
JRNL AUTH 2 C.J.STUBBS,H.F.SORE,A.R.VENKITARAMAN,C.ABELL,D.R.SPRING,
JRNL AUTH 3 M.HYVONEN
JRNL TITL SPECIFIC INHIBITION OF CK2 ALPHA FROM AN ANCHOR OUTSIDE THE
JRNL TITL 2 ACTIVE SITE.
JRNL REF CHEM SCI V. 7 6839 2016
JRNL REFN ISSN 2041-6520
JRNL PMID 28451126
JRNL DOI 10.1039/C6SC02335E
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 100077
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 5042
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.65
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6349
REMARK 3 BIN R VALUE (WORKING SET) : 0.2171
REMARK 3 BIN FREE R VALUE : 0.2286
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.21
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 349
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5459
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 118
REMARK 3 SOLVENT ATOMS : 382
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.80270
REMARK 3 B22 (A**2) : -4.44760
REMARK 3 B33 (A**2) : 2.64490
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.238
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.086
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.080
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.086
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.080
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5833 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7911 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2053 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 145 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 938 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5833 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 699 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6946 ; 0.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.28
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.61
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1252 156.6080 396.1920
REMARK 3 T TENSOR
REMARK 3 T11: -0.1277 T22: 0.2756
REMARK 3 T33: -0.2055 T12: 0.0021
REMARK 3 T13: 0.0221 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.8547 L22: 1.0540
REMARK 3 L33: 5.0051 L12: 0.2407
REMARK 3 L13: 2.0990 L23: -0.9539
REMARK 3 S TENSOR
REMARK 3 S11: -0.1231 S12: -0.8439 S13: 0.0826
REMARK 3 S21: -0.0769 S22: 0.1811 S23: -0.0502
REMARK 3 S31: 0.0410 S32: -1.2371 S33: -0.0579
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9330 145.3990 355.3000
REMARK 3 T TENSOR
REMARK 3 T11: -0.0999 T22: -0.0505
REMARK 3 T33: -0.0646 T12: -0.0095
REMARK 3 T13: 0.0049 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.5066 L22: 0.4846
REMARK 3 L33: 0.9700 L12: 0.0657
REMARK 3 L13: 0.0855 L23: -0.1221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: -0.0602 S13: 0.0139
REMARK 3 S21: 0.0349 S22: -0.0271 S23: 0.0230
REMARK 3 S31: -0.0233 S32: -0.0003 S33: 0.0080
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3600 152.2960 370.6730
REMARK 3 T TENSOR
REMARK 3 T11: -0.1144 T22: 0.0326
REMARK 3 T33: -0.0078 T12: -0.0940
REMARK 3 T13: -0.0137 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 0.2353 L22: 0.0097
REMARK 3 L33: 0.6496 L12: -0.3577
REMARK 3 L13: 0.9067 L23: -0.3137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.1414 S13: 0.0746
REMARK 3 S21: 0.0340 S22: -0.0457 S23: 0.0451
REMARK 3 S31: -0.0089 S32: -0.0794 S33: 0.0029
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.14
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 111.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 3WAR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 107MM MES PH 6.5, 29% GLYCEROL
REMARK 280 ETHOXYLATE, 1 M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 167.00450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 167.00450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.14800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.57500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.14800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.57500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 167.00450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.14800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.57500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 167.00450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.14800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 34.57500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 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 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 GLY A -22
REMARK 465 SER A -21
REMARK 465 MET A -20
REMARK 465 ASP A -19
REMARK 465 ILE A -18
REMARK 465 GLU A -17
REMARK 465 PHE A -16
REMARK 465 ASP A -15
REMARK 465 ASP A -14
REMARK 465 ASP A -13
REMARK 465 ALA A -12
REMARK 465 ASP A -11
REMARK 465 ASP A -10
REMARK 465 ASP A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 SER A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 VAL A 328
REMARK 465 LYS A 329
REMARK 465 GLY B -22
REMARK 465 SER B -21
REMARK 465 MET B -20
REMARK 465 ASP B -19
REMARK 465 ILE B -18
REMARK 465 GLU B -17
REMARK 465 PHE B -16
REMARK 465 ASP B -15
REMARK 465 ASP B -14
REMARK 465 ASP B -13
REMARK 465 ALA B -12
REMARK 465 ASP B -11
REMARK 465 ASP B -10
REMARK 465 ASP B -9
REMARK 465 GLY B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 LYS B 122
REMARK 465 GLN B 123
REMARK 465 LEU B 124
REMARK 465 TYR B 125
REMARK 465 LYS B 329
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 OG SER B 21 O HOH B 501 2.07
REMARK 500 ND1 HIS A 18 O HOH A 501 2.11
REMARK 500 ND1 HIS A 276 O HOH A 502 2.12
REMARK 500 N 54E A 401 O HOH A 503 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 755 O HOH B 755 4597 0.70
REMARK 500 CE2 TYR A 255 OE1 GLN A 290 7447 1.04
REMARK 500 CZ TYR A 255 OE1 GLN A 290 7447 1.54
REMARK 500 CD2 TYR A 255 OE1 GLN A 290 7447 1.61
REMARK 500 CE2 TYR A 255 CD GLN A 290 7447 1.66
REMARK 500 OH TYR A 255 NE2 GLN A 290 7447 1.67
REMARK 500 CZ TYR A 255 CD GLN A 290 7447 1.83
REMARK 500 CE2 TYR A 255 NE2 GLN A 290 7447 1.98
REMARK 500 CZ TYR A 255 NE2 GLN A 290 7447 2.05
REMARK 500 OH TYR A 255 CD GLN A 290 7447 2.10
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 PRO A 72 85.74 -66.61
REMARK 500 TYR A 125 1.84 -59.69
REMARK 500 ASP A 156 42.13 -149.58
REMARK 500 ASP A 175 77.83 50.17
REMARK 500 ALA A 193 166.59 60.22
REMARK 500 ASP A 210 -158.83 -149.56
REMARK 500 ASP B 156 43.30 -152.19
REMARK 500 ASP B 175 77.51 50.61
REMARK 500 ALA B 193 166.44 60.65
REMARK 500 ALA B 193 165.55 60.65
REMARK 500 MET B 208 54.25 -91.63
REMARK 500 ASP B 210 -158.89 -150.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ATP A 403
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 54E A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 54E A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 54E B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 54E B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 405
DBREF 5CSH A 2 329 UNP P68400 CSK21_HUMAN 2 329
DBREF 5CSH B 2 329 UNP P68400 CSK21_HUMAN 2 329
SEQADV 5CSH GLY A -22 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A -21 UNP P68400 EXPRESSION TAG
SEQADV 5CSH MET A -20 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -19 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ILE A -18 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLU A -17 UNP P68400 EXPRESSION TAG
SEQADV 5CSH PHE A -16 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -15 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -14 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -13 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ALA A -12 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -11 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -10 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP A -9 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY A -8 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A -7 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY A -6 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A -5 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY A -4 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A -3 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY A -2 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A -1 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY A 0 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A 1 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER A 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQADV 5CSH GLY B -22 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B -21 UNP P68400 EXPRESSION TAG
SEQADV 5CSH MET B -20 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -19 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ILE B -18 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLU B -17 UNP P68400 EXPRESSION TAG
SEQADV 5CSH PHE B -16 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -15 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -14 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -13 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ALA B -12 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -11 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -10 UNP P68400 EXPRESSION TAG
SEQADV 5CSH ASP B -9 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY B -8 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B -7 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY B -6 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B -5 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY B -4 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B -3 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY B -2 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B -1 UNP P68400 EXPRESSION TAG
SEQADV 5CSH GLY B 0 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B 1 UNP P68400 EXPRESSION TAG
SEQADV 5CSH SER B 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQRES 1 A 352 GLY SER MET ASP ILE GLU PHE ASP ASP ASP ALA ASP ASP
SEQRES 2 A 352 ASP GLY SER GLY SER GLY SER GLY SER GLY SER SER GLY
SEQRES 3 A 352 PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP VAL ASN
SEQRES 4 A 352 THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU SER HIS
SEQRES 5 A 352 VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN LEU VAL
SEQRES 6 A 352 ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL PHE GLU
SEQRES 7 A 352 ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL VAL LYS
SEQRES 8 A 352 ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE LYS ARG GLU
SEQRES 9 A 352 ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO ASN ILE
SEQRES 10 A 352 ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL SER ARG
SEQRES 11 A 352 THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN THR ASP
SEQRES 12 A 352 PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR ASP ILE
SEQRES 13 A 352 ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU ASP TYR
SEQRES 14 A 352 CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL LYS PRO
SEQRES 15 A 352 HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS LEU ARG
SEQRES 16 A 352 LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS PRO GLY
SEQRES 17 A 352 GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR PHE LYS
SEQRES 18 A 352 GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR ASP TYR
SEQRES 19 A 352 SER LEU ASP MET TRP SER LEU GLY CYS MET LEU ALA SER
SEQRES 20 A 352 MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY HIS ASP
SEQRES 21 A 352 ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL LEU GLY
SEQRES 22 A 352 THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR ASN ILE
SEQRES 23 A 352 GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY ARG HIS
SEQRES 24 A 352 SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER GLU ASN
SEQRES 25 A 352 GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE LEU ASP
SEQRES 26 A 352 LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU THR ALA
SEQRES 27 A 352 ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR VAL VAL
SEQRES 28 A 352 LYS
SEQRES 1 B 352 GLY SER MET ASP ILE GLU PHE ASP ASP ASP ALA ASP ASP
SEQRES 2 B 352 ASP GLY SER GLY SER GLY SER GLY SER GLY SER SER GLY
SEQRES 3 B 352 PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP VAL ASN
SEQRES 4 B 352 THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU SER HIS
SEQRES 5 B 352 VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN LEU VAL
SEQRES 6 B 352 ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL PHE GLU
SEQRES 7 B 352 ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL VAL LYS
SEQRES 8 B 352 ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE LYS ARG GLU
SEQRES 9 B 352 ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO ASN ILE
SEQRES 10 B 352 ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL SER ARG
SEQRES 11 B 352 THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN THR ASP
SEQRES 12 B 352 PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR ASP ILE
SEQRES 13 B 352 ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU ASP TYR
SEQRES 14 B 352 CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL LYS PRO
SEQRES 15 B 352 HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS LEU ARG
SEQRES 16 B 352 LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS PRO GLY
SEQRES 17 B 352 GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR PHE LYS
SEQRES 18 B 352 GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR ASP TYR
SEQRES 19 B 352 SER LEU ASP MET TRP SER LEU GLY CYS MET LEU ALA SER
SEQRES 20 B 352 MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY HIS ASP
SEQRES 21 B 352 ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL LEU GLY
SEQRES 22 B 352 THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR ASN ILE
SEQRES 23 B 352 GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY ARG HIS
SEQRES 24 B 352 SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER GLU ASN
SEQRES 25 B 352 GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE LEU ASP
SEQRES 26 B 352 LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU THR ALA
SEQRES 27 B 352 ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR VAL VAL
SEQRES 28 B 352 LYS
HET 54E A 401 15
HET 54E A 402 15
HET ATP A 403 19
HET ACT B 401 4
HET ACT B 402 4
HET 54E B 403 30
HET 54E B 404 15
HET ATP B 405 31
HETNAM 54E 1-(2-CHLOROBIPHENYL-4-YL)METHANAMINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM ACT ACETATE ION
FORMUL 3 54E 4(C13 H12 CL N)
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 11 HOH *382(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 ASN A 35 ASP A 37 5 3
HELIX 4 AA4 LYS A 74 ARG A 89 1 16
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 HIS A 166 ARG A 169 5 4
HELIX 8 AA8 SER A 194 LYS A 198 5 5
HELIX 9 AA9 GLY A 199 VAL A 204 1 6
HELIX 10 AB1 TYR A 211 ARG A 228 1 18
HELIX 11 AB2 ASP A 237 GLY A 250 1 14
HELIX 12 AB3 GLY A 250 TYR A 261 1 12
HELIX 13 AB4 ASP A 266 ASN A 270 5 5
HELIX 14 AB5 ARG A 280 VAL A 285 5 6
HELIX 15 AB6 ASN A 289 VAL A 293 5 5
HELIX 16 AB7 SER A 294 LYS A 303 1 10
HELIX 17 AB8 ASP A 308 ARG A 312 5 5
HELIX 18 AB9 THR A 314 GLU A 320 1 7
HELIX 19 AC1 HIS A 321 TYR A 325 5 5
HELIX 20 AC2 PRO B 20 ASP B 25 1 6
HELIX 21 AC3 TYR B 26 HIS B 29 5 4
HELIX 22 AC4 LYS B 74 ARG B 89 1 16
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 HIS B 166 ARG B 169 5 4
HELIX 26 AC8 SER B 194 LYS B 198 5 5
HELIX 27 AC9 GLY B 199 VAL B 204 1 6
HELIX 28 AD1 TYR B 211 ARG B 228 1 18
HELIX 29 AD2 ASP B 237 GLY B 250 1 14
HELIX 30 AD3 GLY B 250 ASN B 262 1 13
HELIX 31 AD4 ASP B 266 ASN B 270 5 5
HELIX 32 AD5 ARG B 280 VAL B 285 5 6
HELIX 33 AD6 ASN B 289 VAL B 293 5 5
HELIX 34 AD7 SER B 294 LEU B 305 1 12
HELIX 35 AD8 ASP B 308 ARG B 312 5 5
HELIX 36 AD9 THR B 314 GLU B 320 1 7
HELIX 37 AE1 HIS B 321 TYR B 325 5 5
SHEET 1 AA1 5 TYR A 39 ARG A 47 0
SHEET 2 AA1 5 SER A 51 ASN A 58 -1 O VAL A 53 N LEU A 45
SHEET 3 AA1 5 GLU A 63 LEU A 70 -1 O ILE A 69 N GLU A 52
SHEET 4 AA1 5 THR A 108 GLU A 114 -1 O LEU A 111 N LYS A 68
SHEET 5 AA1 5 LEU A 97 ASP A 103 -1 N ASP A 99 O VAL A 112
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 6 GLY B 34 ASN B 35 0
SHEET 2 AA4 6 LEU B 97 LYS B 102 1 O ILE B 100 N GLY B 34
SHEET 3 AA4 6 PRO B 109 GLU B 114 -1 O VAL B 112 N ASP B 99
SHEET 4 AA4 6 LYS B 64 LEU B 70 -1 N LYS B 68 O LEU B 111
SHEET 5 AA4 6 SER B 51 ASN B 58 -1 N GLU B 52 O ILE B 69
SHEET 6 AA4 6 TYR B 39 ARG B 47 -1 N ARG B 43 O GLU B 55
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 -9.57
CISPEP 2 GLU B 230 PRO B 231 0 -5.05
SITE 1 AC1 10 PHE A 121 TYR A 136 ILE A 140 PRO A 159
SITE 2 AC1 10 VAL A 162 ILE A 164 MET A 221 MET A 225
SITE 3 AC1 10 HOH A 503 HOH A 560
SITE 1 AC2 6 GLN A 36 TYR A 39 ILE A 69 ASP A 103
SITE 2 AC2 6 THR A 108 ALA A 110
SITE 1 AC3 9 LEU A 45 VAL A 53 VAL A 66 ILE A 95
SITE 2 AC3 9 GLU A 114 VAL A 116 ASN A 118 MET A 163
SITE 3 AC3 9 HOH A 581
SITE 1 AC4 4 ARG B 80 ARG B 155 LEU B 178 HOH B 694
SITE 1 AC5 2 ARG B 244 HOH B 507
SITE 1 AC6 11 PHE B 121 LEU B 128 TYR B 136 ILE B 140
SITE 2 AC6 11 PRO B 159 VAL B 162 ILE B 164 MET B 221
SITE 3 AC6 11 MET B 225 HOH B 571 HOH B 574
SITE 1 AC7 8 TRP B 24 GLN B 40 LEU B 41 VAL B 42
SITE 2 AC7 8 HIS B 183 GLN B 186 HOH B 537 HOH B 677
SITE 1 AC8 15 LEU B 45 VAL B 53 VAL B 66 ILE B 95
SITE 2 AC8 15 GLU B 114 VAL B 116 LYS B 158 HIS B 160
SITE 3 AC8 15 MET B 163 ILE B 174 HOH B 505 HOH B 543
SITE 4 AC8 15 HOH B 568 HOH B 573 HOH B 617
CRYST1 64.296 69.150 334.009 90.00 90.00 90.00 C 2 2 21 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 0.015553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002994 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
