HEADER TRANSFERASE 21-AUG-17 5OT6
TITLE THE CRYSTAL STRUCTURE OF CK2ALPHA IN COMPLEX WITH COMPOUND 19
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_VECTOR: 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,J.IEGRE,M.YOSHIDA,S.MITCHELL,M.ROSSMANN,L.CARRO,
AUTHOR 2 H.SORE,M.HYVONEN,D.SPRING
REVDAT 3 17-JAN-24 5OT6 1 REMARK
REVDAT 2 16-MAY-18 5OT6 1 JRNL
REVDAT 1 28-FEB-18 5OT6 0
JRNL AUTH J.IEGRE,P.BREAR,C.DE FUSCO,M.YOSHIDA,S.L.MITCHELL,
JRNL AUTH 2 M.ROSSMANN,L.CARRO,H.F.SORE,M.HYVONEN,D.R.SPRING
JRNL TITL SECOND-GENERATION CK2 ALPHA INHIBITORS TARGETING THE ALPHA D
JRNL TITL 2 POCKET.
JRNL REF CHEM SCI V. 9 3041 2018
JRNL REFN ISSN 2041-6520
JRNL PMID 29732088
JRNL DOI 10.1039/C7SC05122K
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 167.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 55605
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2822
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4041
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2576
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3844
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.88
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 197
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5507
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 234
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.67720
REMARK 3 B22 (A**2) : -13.24580
REMARK 3 B33 (A**2) : 8.56860
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.181
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.150
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.180
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.151
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 : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5764 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7809 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2038 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 144 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 854 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5764 ; 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 : 692 ; 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 : 6570 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.71
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.84
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-15
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) : 0.979490
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55709
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 167.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 12.40
REMARK 200 R MERGE FOR SHELL (I) : 1.48900
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: PHASER
REMARK 200 STARTING MODEL: 5CVH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
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: 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 167.64000
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 167.64000
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 32.41850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.04600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.41850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.04600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 167.64000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.41850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.04600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 167.64000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.41850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 34.04600
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 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 VAL B 328
REMARK 465 LYS B 329
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 A 648 O HOH A 648 4597 1.23
REMARK 500 CZ ARG B 275 O HIS B 291 7447 2.01
REMARK 500 NH2 ARG B 275 O HIS B 291 7447 2.03
REMARK 500 NE ARG B 275 O HIS B 291 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 VAL A 42 -62.71 -100.65
REMARK 500 ASN A 61 4.13 -151.24
REMARK 500 PRO A 72 66.42 -66.84
REMARK 500 ARG A 155 12.51 59.07
REMARK 500 ASP A 156 39.28 -151.42
REMARK 500 ASP A 175 73.56 57.56
REMARK 500 ALA A 193 165.09 62.02
REMARK 500 ALA A 193 163.49 62.02
REMARK 500 ASP A 210 -159.38 -144.57
REMARK 500 VAL B 42 -62.43 -100.20
REMARK 500 ASN B 61 4.52 -151.90
REMARK 500 PRO B 72 40.66 -83.24
REMARK 500 ARG B 155 14.41 58.09
REMARK 500 ASP B 156 37.64 -154.51
REMARK 500 ASP B 175 70.30 56.29
REMARK 500 ALA B 193 161.75 63.36
REMARK 500 ALA B 193 161.74 63.36
REMARK 500 ASP B 210 -159.71 -143.73
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 ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AJK A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 401
DBREF 5OT6 A 2 329 UNP P68400 CSK21_HUMAN 2 329
DBREF 5OT6 B 2 329 UNP P68400 CSK21_HUMAN 2 329
SEQADV 5OT6 GLY A -22 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A -21 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 MET A -20 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -19 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ILE A -18 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLU A -17 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 PHE A -16 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -15 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -14 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -13 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ALA A -12 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -11 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -10 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP A -9 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY A -8 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A -7 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY A -6 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A -5 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY A -4 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A -3 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY A -2 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A -1 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY A 0 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A 1 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER A 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQADV 5OT6 GLY B -22 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B -21 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 MET B -20 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -19 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ILE B -18 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLU B -17 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 PHE B -16 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -15 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -14 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -13 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ALA B -12 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -11 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -10 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 ASP B -9 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY B -8 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B -7 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY B -6 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B -5 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY B -4 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B -3 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY B -2 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B -1 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 GLY B 0 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 SER B 1 UNP P68400 EXPRESSION TAG
SEQADV 5OT6 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 ACT A 401 4
HET ACT A 402 4
HET AJK A 403 22
HET PO4 A 404 5
HET PO4 A 405 5
HET PO4 A 406 5
HET PO4 B 401 5
HETNAM ACT ACETATE ION
HETNAM AJK (3-CHLORANYL-4-PHENYL-PHENYL)METHYL-[2-(1~{H}-PYRROL-2-
HETNAM 2 AJK YL)ETHYL]AZANIUM
HETNAM PO4 PHOSPHATE ION
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 AJK C19 H20 CL N2 1+
FORMUL 6 PO4 4(O4 P 3-)
FORMUL 10 HOH *234(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 LEU A 128 1 9
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 SER A 294 LEU A 305 1 12
HELIX 16 AB7 ASP A 308 ARG A 312 5 5
HELIX 17 AB8 THR A 314 GLU A 320 1 7
HELIX 18 AB9 HIS A 321 TYR A 325 5 5
HELIX 19 AC1 PRO B 20 ASP B 25 1 6
HELIX 20 AC2 TYR B 26 HIS B 29 5 4
HELIX 21 AC3 LYS B 74 ARG B 89 1 16
HELIX 22 AC4 ASP B 120 LEU B 128 1 9
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 ARG B 228 1 18
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 ASP B 266 ASN B 270 5 5
HELIX 31 AD4 ARG B 280 VAL B 285 5 6
HELIX 32 AD5 SER B 294 LEU B 305 1 12
HELIX 33 AD6 ASP B 308 ARG B 312 5 5
HELIX 34 AD7 THR B 314 GLU B 320 1 7
HELIX 35 AD8 HIS B 321 TYR B 325 5 5
SHEET 1 AA1 6 GLY A 34 ASN A 35 0
SHEET 2 AA1 6 LEU A 97 LYS A 102 1 O ILE A 100 N GLY A 34
SHEET 3 AA1 6 PRO A 109 GLU A 114 -1 O VAL A 112 N ALA A 98
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 ARG A 47 -1 N ARG A 43 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 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 ALA B 98
SHEET 4 AA4 6 LYS B 64 LEU B 70 -1 N VAL B 66 O PHE B 113
SHEET 5 AA4 6 SER B 51 ASN B 58 -1 N PHE B 54 O VAL B 67
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 -3.42
CISPEP 2 GLU B 230 PRO B 231 0 -6.48
SITE 1 AC1 6 LYS A 68 ILE A 95 ILE A 174 ASP A 175
SITE 2 AC1 6 HOH A 525 HOH A 630
SITE 1 AC2 3 ARG A 80 ARG A 155 HOH A 580
SITE 1 AC3 8 ASN A 118 PHE A 121 TYR A 136 PRO A 159
SITE 2 AC3 8 HIS A 160 VAL A 162 MET A 221 MET A 225
SITE 1 AC4 5 ARG A 195 TYR A 196 HIS A 234 GLY A 235
SITE 2 AC4 5 HOH A 503
SITE 1 AC5 1 LYS A 247
SITE 1 AC6 3 HIS A 276 SER A 277 LYS A 279
SITE 1 AC7 6 ARG B 195 TYR B 196 HIS B 234 GLY B 235
SITE 2 AC7 6 ARG B 244 LYS B 247
CRYST1 64.837 68.092 335.280 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 0.015423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014686 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002983 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
