HEADER TRANSFERASE 23-JUL-15 5CT0
TITLE CRYSTAL STRUCTURE OF CK2ALPHA WITH 3-(3-CHLORO-4-(PHENYL)BENZYLAMINO)
TITLE 2 PROPAN-1-OL BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP 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: 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 4 10-JAN-24 5CT0 1 REMARK
REVDAT 3 07-JUN-17 5CT0 1 JRNL
REVDAT 2 24-MAY-17 5CT0 1 JRNL
REVDAT 1 30-NOV-16 5CT0 0
JRNL AUTH C.DE FUSCO,P.BREAR,J.IEGRE,K.H.GEORGIOU,H.F.SORE,M.HYVONEN,
JRNL AUTH 2 D.R.SPRING
JRNL TITL A FRAGMENT-BASED APPROACH LEADING TO THE DISCOVERY OF A
JRNL TITL 2 NOVEL BINDING SITE AND THE SELECTIVE CK2 INHIBITOR CAM4066.
JRNL REF BIOORG. MED. CHEM. V. 25 3471 2017
JRNL REFN ESSN 1464-3391
JRNL PMID 28495381
JRNL DOI 10.1016/J.BMC.2017.04.037
REMARK 2
REMARK 2 RESOLUTION. 2.01 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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 49099
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) : 0.200
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2501
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.06
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.53
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) : 3192
REMARK 3 BIN R VALUE (WORKING SET) : 0.2229
REMARK 3 BIN FREE R VALUE : 0.2536
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.25
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 177
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 : 5501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.52810
REMARK 3 B22 (A**2) : -7.74460
REMARK 3 B33 (A**2) : 6.21650
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) : 0.288
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.189
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.150
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.190
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.152
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 : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5727 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7749 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2025 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 144 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 855 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5727 ; 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 : 688 ; 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 : 6513 ; 0.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.90
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.93
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4947 141.6460 357.2890
REMARK 3 T TENSOR
REMARK 3 T11: -0.1656 T22: 0.0360
REMARK 3 T33: -0.0983 T12: -0.0617
REMARK 3 T13: 0.0058 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.3600 L22: 0.6358
REMARK 3 L33: 1.1968 L12: 0.0984
REMARK 3 L13: -0.0099 L23: -0.3297
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: -0.1085 S13: 0.0274
REMARK 3 S21: 0.0639 S22: -0.0947 S23: 0.0203
REMARK 3 S31: -0.0389 S32: 0.0808 S33: -0.0018
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2910 152.7230 398.3460
REMARK 3 T TENSOR
REMARK 3 T11: -0.1014 T22: 0.1162
REMARK 3 T33: -0.2392 T12: -0.0632
REMARK 3 T13: 0.0325 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.9835 L22: 0.8215
REMARK 3 L33: 1.9336 L12: 0.3644
REMARK 3 L13: 0.3692 L23: -0.1423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0786 S12: -0.3494 S13: 0.0192
REMARK 3 S21: -0.2233 S22: 0.0944 S23: -0.0418
REMARK 3 S31: 0.2085 S32: -0.3898 S33: -0.0158
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CT0 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_1000212134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-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 : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9174
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.14
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49184
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.008
REMARK 200 RESOLUTION RANGE LOW (A) : 46.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.93000
REMARK 200 R SYM FOR SHELL (I) : 0.93000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 (%): 44.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
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 167.89750
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 167.89750
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 32.27550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.72450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.27550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.72450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 167.89750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.27550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 33.72450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 167.89750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.27550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 33.72450
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 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 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 O HOH A 501 O HOH A 620 2.17
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 A 636 O HOH A 645 8497 0.74
REMARK 500 OE2 GLU A 264 NH1 ARG A 280 8597 2.06
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 ASP A 156 39.79 -145.08
REMARK 500 ASP A 175 77.87 51.10
REMARK 500 ALA A 193 170.61 62.33
REMARK 500 THR B 127 -7.12 63.22
REMARK 500 ASP B 156 36.00 -148.63
REMARK 500 ASP B 175 78.15 50.98
REMARK 500 ALA B 193 163.54 66.80
REMARK 500 ARG B 195 -36.01 -33.10
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 54P A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 54P B 401
DBREF 5CT0 A 2 329 UNP P68400 CSK21_HUMAN 2 329
DBREF 5CT0 B 2 329 UNP P68400 CSK21_HUMAN 2 329
SEQADV 5CT0 GLY A -22 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A -21 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 MET A -20 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -19 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ILE A -18 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLU A -17 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 PHE A -16 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -15 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -14 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -13 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ALA A -12 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -11 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -10 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP A -9 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY A -8 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A -7 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY A -6 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A -5 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY A -4 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A -3 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY A -2 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A -1 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY A 0 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A 1 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER A 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQADV 5CT0 GLY B -22 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B -21 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 MET B -20 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -19 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ILE B -18 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLU B -17 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 PHE B -16 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -15 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -14 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -13 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ALA B -12 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -11 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -10 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 ASP B -9 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY B -8 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B -7 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY B -6 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B -5 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY B -4 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B -3 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY B -2 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B -1 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 GLY B 0 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 SER B 1 UNP P68400 EXPRESSION TAG
SEQADV 5CT0 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 54P A 403 19
HET 54P B 401 19
HETNAM ACT ACETATE ION
HETNAM 54P 3-{[(2-CHLOROBIPHENYL-4-YL)METHYL]AMINO}PROPAN-1-OL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 54P 2(C16 H18 CL N O)
FORMUL 7 HOH *228(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 ASP A 120 LEU A 128 1 9
HELIX 6 AA6 THR A 129 MET A 150 1 22
HELIX 7 AA7 LYS A 158 HIS A 160 5 3
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 PHE A 227 1 17
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 ASN B 35 ASP B 37 5 3
HELIX 23 AC5 LYS B 74 ARG B 89 1 16
HELIX 24 AC6 THR B 129 MET B 150 1 22
HELIX 25 AC7 LYS B 158 HIS B 160 5 3
HELIX 26 AC8 ASP B 175 ALA B 179 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 TYR B 261 1 12
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 LYS B 303 1 10
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 GLU A 63 N ASN A 58
SHEET 4 AA1 5 THR A 108 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 AA1 5 LEU A 97 ASP A 103 -1 N ALA A 98 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 5 TYR B 39 ARG B 47 0
SHEET 2 AA4 5 SER B 51 ASN B 58 -1 O VAL B 53 N LEU B 45
SHEET 3 AA4 5 GLU B 63 LEU B 70 -1 O GLU B 63 N ASN B 58
SHEET 4 AA4 5 THR B 108 GLU B 114 -1 O PHE B 113 N VAL B 66
SHEET 5 AA4 5 LEU B 97 ASP B 103 -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 -3.46
CISPEP 2 GLU B 230 PRO B 231 0 -5.76
SITE 1 AC1 6 LYS A 68 PHE A 113 ILE A 174 ASP A 175
SITE 2 AC1 6 HOH A 507 HOH A 590
SITE 1 AC2 3 ARG A 80 ARG A 155 HOH A 585
SITE 1 AC3 8 ASN A 118 MET A 137 PRO A 159 VAL A 162
SITE 2 AC3 8 MET A 163 ILE A 164 MET A 221 MET A 225
SITE 1 AC4 12 ASN B 118 PHE B 121 LEU B 124 LEU B 128
SITE 2 AC4 12 ILE B 133 TYR B 136 PRO B 159 HIS B 160
SITE 3 AC4 12 VAL B 162 MET B 163 MET B 221 MET B 225
CRYST1 64.551 67.449 335.795 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 0.015492 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014826 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002978 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
