HEADER TRANSFERASE 26-JUL-15 5CVF
TITLE CRYSTAL STRUCTURE OF CK2ALPHA WITH COMPOUND 5 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-329;
COMPND 5 SYNONYM: CK II ALPHA;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: PHAT2
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 5CVF 1 REMARK
REVDAT 2 10-MAY-17 5CVF 1 JRNL
REVDAT 1 27-JUL-16 5CVF 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. 1.63 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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 38048
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1906
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 : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.68
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.48
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2794
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2647
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2616
REMARK 3 BIN R VALUE (WORKING SET) : 0.2639
REMARK 3 BIN FREE R VALUE : 0.2766
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 178
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 : 2738
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 213
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34600
REMARK 3 B22 (A**2) : -3.30820
REMARK 3 B33 (A**2) : 2.96220
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.70020
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.226
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.115
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.097
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.113
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.097
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 : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2934 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3987 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1037 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 446 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2934 ; 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 : 354 ; 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 : 3522 ; 0.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.29
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 80.5411 8.8188 131.9012
REMARK 3 T TENSOR
REMARK 3 T11: -0.0780 T22: -0.1284
REMARK 3 T33: -0.1537 T12: 0.0078
REMARK 3 T13: 0.0024 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 0.2302 L22: 0.0796
REMARK 3 L33: 0.5108 L12: -0.0326
REMARK 3 L13: -0.2246 L23: 0.1219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: 0.0611 S13: 0.0154
REMARK 3 S21: 0.1260 S22: 0.0237 S23: -0.0432
REMARK 3 S31: -0.0102 S32: 0.0847 S33: -0.0378
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-13
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
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 0.5.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38063
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 54.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.75200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 3WAR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 112.5MM MES PH 6.5, 35% GLYCEROL
REMARK 280 ETHOXYLATE, 180 MM AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 22.95000
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 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 SER A 2
REMARK 465 ALA A 74
REMARK 465 ALA A 75
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 NE2 HIS A 236 O HOH A 501 0.64
REMARK 500 O HOH A 505 O HOH A 597 1.18
REMARK 500 CE1 HIS A 236 O HOH A 501 1.34
REMARK 500 CD2 HIS A 236 O HOH A 501 1.68
REMARK 500 NH1 ARG A 228 O HOH A 502 2.04
REMARK 500 OD1 ASP A 205 O HOH A 503 2.10
REMARK 500 CA GLN A 126 O HOH A 502 2.15
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 LYS A 44 NH2 ARG A 268 10510 1.95
REMARK 500 OH TYR A 12 CG2 THR A 326 2949 2.09
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 ASP A 205 CB - CG - OD1 ANGL. DEV. = 5.9 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 PRO A 72 91.60 -69.21
REMARK 500 ASP A 156 41.67 -143.17
REMARK 500 ASP A 175 71.77 54.63
REMARK 500 ALA A 193 156.53 61.99
REMARK 500 MET A 208 54.98 -91.37
REMARK 500 HIS A 234 67.50 -101.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 228 0.28 SIDE CHAIN
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 54Z A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 404
DBREF 5CVF A 2 329 UNP P68400 CSK21_HUMAN 2 329
SEQADV 5CVF SER A 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQADV 5CVF ALA A 74 UNP P68400 LYS 74 ENGINEERED MUTATION
SEQADV 5CVF ALA A 75 UNP P68400 LYS 75 ENGINEERED MUTATION
SEQADV 5CVF ALA A 76 UNP P68400 LYS 76 ENGINEERED MUTATION
SEQRES 1 A 328 SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP
SEQRES 2 A 328 VAL ASN THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU
SEQRES 3 A 328 SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN
SEQRES 4 A 328 LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL
SEQRES 5 A 328 PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL
SEQRES 6 A 328 VAL LYS ILE LEU LYS PRO VAL ALA ALA ALA LYS ILE LYS
SEQRES 7 A 328 ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO
SEQRES 8 A 328 ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL
SEQRES 9 A 328 SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN
SEQRES 10 A 328 THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR
SEQRES 11 A 328 ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU
SEQRES 12 A 328 ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL
SEQRES 13 A 328 LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS
SEQRES 14 A 328 LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS
SEQRES 15 A 328 PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR
SEQRES 16 A 328 PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR
SEQRES 17 A 328 ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET LEU
SEQRES 18 A 328 ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY
SEQRES 19 A 328 HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL
SEQRES 20 A 328 LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR
SEQRES 21 A 328 ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY
SEQRES 22 A 328 ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER
SEQRES 23 A 328 GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE
SEQRES 24 A 328 LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU
SEQRES 25 A 328 THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR
SEQRES 26 A 328 VAL VAL LYS
HET 54Z A 401 14
HET ATP A 402 31
HET ACT A 403 4
HET ACT A 404 4
HETNAM 54Z 1-[3-CHLORO-4-(TRIFLUOROMETHOXY)PHENYL]METHANAMINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM ACT ACETATE ION
FORMUL 2 54Z C8 H7 CL F3 N O
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 6 HOH *213(H2 O)
HELIX 1 AA1 ASP A 14 ARG A 19 1 6
HELIX 2 AA2 PRO A 20 ASP A 25 1 6
HELIX 3 AA3 TYR A 26 HIS A 29 5 4
HELIX 4 AA4 ASN A 35 ASP A 37 5 3
HELIX 5 AA5 LYS A 77 ARG A 89 1 13
HELIX 6 AA6 ASP A 120 GLN A 126 1 7
HELIX 7 AA7 THR A 129 MET A 150 1 22
HELIX 8 AA8 LYS A 158 HIS A 160 5 3
HELIX 9 AA9 SER A 194 LYS A 198 5 5
HELIX 10 AB1 GLY A 199 VAL A 204 1 6
HELIX 11 AB2 TYR A 211 ARG A 228 1 18
HELIX 12 AB3 ASP A 237 GLY A 250 1 14
HELIX 13 AB4 GLY A 250 TYR A 261 1 12
HELIX 14 AB5 ASP A 266 ILE A 272 5 7
HELIX 15 AB6 ARG A 280 VAL A 285 5 6
HELIX 16 AB7 ASN A 289 VAL A 293 5 5
HELIX 17 AB8 SER A 294 LEU A 305 1 12
HELIX 18 AB9 ASP A 308 ARG A 312 5 5
HELIX 19 AC1 THR A 314 GLU A 320 1 7
HELIX 20 AC2 HIS A 321 TYR A 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 GLU A 55 N VAL A 42
SHEET 3 AA1 5 GLU A 63 LEU A 70 -1 O VAL A 67 N PHE A 54
SHEET 4 AA1 5 PRO A 109 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 AA1 5 LEU A 97 LYS A 102 -1 N VAL A 101 O ALA A 110
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 ARG A 172 N MET A 163
CISPEP 1 GLU A 230 PRO A 231 0 -1.78
SITE 1 AC1 10 LEU A 124 LEU A 128 TYR A 136 ILE A 140
SITE 2 AC1 10 PRO A 159 VAL A 162 ILE A 164 MET A 221
SITE 3 AC1 10 MET A 225 HOH A 594
SITE 1 AC2 15 GLY A 48 SER A 51 VAL A 53 VAL A 66
SITE 2 AC2 15 LYS A 68 ILE A 95 GLU A 114 VAL A 116
SITE 3 AC2 15 ASN A 161 MET A 163 ILE A 174 ASP A 175
SITE 4 AC2 15 HOH A 506 HOH A 548 HOH A 616
SITE 1 AC3 3 ARG A 80 ARG A 155 HOH A 646
SITE 1 AC4 4 ARG A 191 ALA A 193 LYS A 198 HOH A 520
CRYST1 58.680 45.900 62.900 90.00 111.86 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 0.017042 0.000000 0.006837 0.00000
SCALE2 0.000000 0.021786 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END