HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-JUN-12 4FT9
TITLE CRYSTAL STRUCTURE OF THE CHK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHK1 CHECKPOINT HOMOLOG, CELL CYCLE CHECKPOINT KINASE,
COMPND 5 CHECKPOINT KINASE-1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CHEK1, CHK1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,J.A.STUCKEY,P.CHANG,A.J.RUSSELL
REVDAT 4 29-NOV-23 4FT9 1 REMARK
REVDAT 3 15-NOV-17 4FT9 1 AUTHOR REMARK
REVDAT 2 29-MAY-13 4FT9 1 SOURCE
REVDAT 1 22-AUG-12 4FT9 0
JRNL AUTH Y.N.KANG,J.A.STUCKEY,P.CHANG,A.J.RUSSELL
JRNL TITL CRYSTAL STRUCTURE OF THE CHK1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.1
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 16400
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 832
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.35
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.74
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3019
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1723
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2895
REMARK 3 BIN R VALUE (WORKING SET) : 0.1704
REMARK 3 BIN FREE R VALUE : 0.2205
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.11
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 124
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 : 2155
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.30120
REMARK 3 B22 (A**2) : -0.05940
REMARK 3 B33 (A**2) : 1.36070
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04280
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.218
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.217
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2275 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3103 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1052 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 61 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 363 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2275 ; 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 : 285 ; 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 : 2719 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|2 - 18}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9025 -5.0083 -3.0998
REMARK 3 T TENSOR
REMARK 3 T11: 0.0215 T22: 0.0025
REMARK 3 T33: -0.0254 T12: -0.0080
REMARK 3 T13: 0.0133 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.0083 L22: 0.0000
REMARK 3 L33: 0.2709 L12: -0.1427
REMARK 3 L13: -0.0337 L23: 0.2959
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0028 S13: -0.0085
REMARK 3 S21: 0.0254 S22: -0.0118 S23: -0.0031
REMARK 3 S31: 0.0066 S32: -0.0122 S33: 0.0063
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|21 - 33}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1757 -3.4784 -1.9492
REMARK 3 T TENSOR
REMARK 3 T11: 0.0389 T22: 0.0167
REMARK 3 T33: -0.0606 T12: -0.0113
REMARK 3 T13: 0.0117 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: -0.0387 L22: 0.2447
REMARK 3 L33: 0.4452 L12: -0.2815
REMARK 3 L13: 0.2631 L23: 0.7182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0075 S13: -0.0067
REMARK 3 S21: 0.0102 S22: -0.0017 S23: -0.0060
REMARK 3 S31: -0.0004 S32: -0.0036 S33: -0.0014
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|34 - 59}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9946 -7.4442 11.8419
REMARK 3 T TENSOR
REMARK 3 T11: -0.0006 T22: 0.0241
REMARK 3 T33: -0.0312 T12: -0.0943
REMARK 3 T13: -0.0080 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.2005 L22: 0.0952
REMARK 3 L33: 0.0508 L12: 0.3688
REMARK 3 L13: 0.3730 L23: 0.5597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: -0.0016 S13: -0.0162
REMARK 3 S21: -0.0184 S22: -0.0047 S23: 0.0209
REMARK 3 S31: 0.0099 S32: -0.0084 S33: 0.0068
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|60 - 69}
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9222 6.7317 14.6011
REMARK 3 T TENSOR
REMARK 3 T11: -0.0032 T22: 0.0286
REMARK 3 T33: -0.0243 T12: -0.0011
REMARK 3 T13: -0.0471 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: -0.0524 L22: 0.0452
REMARK 3 L33: 0.1787 L12: 0.0194
REMARK 3 L13: 0.3713 L23: -0.3026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: 0.0071 S13: 0.0000
REMARK 3 S21: -0.0033 S22: 0.0018 S23: 0.0040
REMARK 3 S31: -0.0015 S32: -0.0054 S33: -0.0029
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|70 - 76}
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6658 -4.7077 5.2410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0126 T22: 0.0199
REMARK 3 T33: -0.0306 T12: -0.0324
REMARK 3 T13: -0.0149 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: -0.0123 L22: 0.0000
REMARK 3 L33: 0.2578 L12: 0.3178
REMARK 3 L13: 0.0880 L23: -0.1635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0002 S13: -0.0120
REMARK 3 S21: -0.0006 S22: -0.0024 S23: 0.0068
REMARK 3 S31: -0.0020 S32: 0.0027 S33: 0.0026
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|77 - 97}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2144 -4.2741 10.7687
REMARK 3 T TENSOR
REMARK 3 T11: -0.0052 T22: 0.0470
REMARK 3 T33: -0.0557 T12: -0.0315
REMARK 3 T13: 0.0416 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: -0.0299 L22: 0.1766
REMARK 3 L33: 0.6894 L12: -0.5486
REMARK 3 L13: 0.1915 L23: 0.8393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: 0.0214 S13: -0.0259
REMARK 3 S21: -0.0381 S22: 0.0129 S23: -0.0117
REMARK 3 S31: 0.0433 S32: -0.0106 S33: -0.0073
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|98 - 157}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7104 3.1588 21.5553
REMARK 3 T TENSOR
REMARK 3 T11: -0.0270 T22: -0.0503
REMARK 3 T33: -0.0065 T12: 0.0138
REMARK 3 T13: -0.0133 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.6503 L22: 1.3225
REMARK 3 L33: 1.2549 L12: -0.1146
REMARK 3 L13: -0.4394 L23: 0.2328
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0590 S13: -0.0157
REMARK 3 S21: -0.0882 S22: -0.0383 S23: 0.0129
REMARK 3 S31: -0.0181 S32: -0.0527 S33: 0.0431
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|158 - 166}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3252 0.2109 32.5102
REMARK 3 T TENSOR
REMARK 3 T11: -0.0449 T22: 0.0086
REMARK 3 T33: 0.0404 T12: -0.0036
REMARK 3 T13: -0.0025 T23: -0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 0.3152 L22: 0.0697
REMARK 3 L33: 0.0168 L12: 0.1981
REMARK 3 L13: 0.1310 L23: 0.1109
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: -0.0111 S13: 0.0021
REMARK 3 S21: -0.0073 S22: -0.0114 S23: 0.0047
REMARK 3 S31: -0.0077 S32: -0.0072 S33: 0.0136
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {A|167 - 190}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1042 -6.1482 35.0957
REMARK 3 T TENSOR
REMARK 3 T11: -0.0072 T22: -0.0281
REMARK 3 T33: 0.0401 T12: 0.0093
REMARK 3 T13: 0.0287 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.1722 L22: 0.4614
REMARK 3 L33: -0.0488 L12: -0.1544
REMARK 3 L13: -0.3458 L23: -0.3909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: -0.0079 S13: 0.0015
REMARK 3 S21: 0.0203 S22: -0.0111 S23: -0.0020
REMARK 3 S31: 0.0230 S32: -0.0183 S33: 0.0140
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {A|191 - 246}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8683 -2.1941 36.7468
REMARK 3 T TENSOR
REMARK 3 T11: -0.0404 T22: -0.0103
REMARK 3 T33: 0.0313 T12: 0.0252
REMARK 3 T13: -0.0176 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.4017 L22: 0.8289
REMARK 3 L33: 1.0018 L12: 0.1576
REMARK 3 L13: 0.7097 L23: -0.0289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0091 S12: -0.1243 S13: -0.0626
REMARK 3 S21: 0.0260 S22: -0.0143 S23: -0.0314
REMARK 3 S31: 0.0406 S32: 0.0985 S33: 0.0235
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {A|247 - 270}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3792 10.6247 34.2037
REMARK 3 T TENSOR
REMARK 3 T11: -0.0177 T22: -0.0492
REMARK 3 T33: 0.0600 T12: 0.0333
REMARK 3 T13: 0.0316 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.5695 L22: 0.1596
REMARK 3 L33: 0.1514 L12: 0.6381
REMARK 3 L13: 0.2972 L23: -0.1310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.0306 S13: 0.0452
REMARK 3 S21: 0.0036 S22: -0.0099 S23: -0.0086
REMARK 3 S31: -0.0184 S32: -0.0332 S33: 0.0042
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {A|271 - 280}
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0929 21.3544 8.0853
REMARK 3 T TENSOR
REMARK 3 T11: 0.0114 T22: 0.0022
REMARK 3 T33: -0.0072 T12: 0.0024
REMARK 3 T13: 0.0083 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.0551 L22: 0.0361
REMARK 3 L33: 0.0146 L12: -0.1029
REMARK 3 L13: -0.0321 L23: 0.0428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0004 S13: 0.0005
REMARK 3 S21: 0.0017 S22: 0.0006 S23: -0.0007
REMARK 3 S31: 0.0050 S32: 0.0021 S33: 0.0001
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16412
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, ISOPROPANOL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
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 32.90100
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 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 ALA A 19
REMARK 465 TYR A 20
REMARK 465 LYS A 43
REMARK 465 ARG A 44
REMARK 465 ALA A 45
REMARK 465 VAL A 46
REMARK 465 ASP A 47
REMARK 465 CYS A 48
REMARK 465 PRO A 49
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 78 CG OD1 ND2
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 LYS A 232 CG CD CE NZ
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 ARG A 277 CG CD NE CZ NH1 NH2
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 GLU A 76 78.62 -110.12
REMARK 500 ILE A 100 -54.03 -120.86
REMARK 500 ASP A 130 45.36 -148.00
REMARK 500 ASP A 148 98.66 64.17
REMARK 500 LEU A 269 -39.11 -133.28
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 H4K A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FSM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CHK1
REMARK 900 RELATED ID: 4FSN RELATED DB: PDB
REMARK 900 RELATED ID: 4FSQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FSR RELATED DB: PDB
REMARK 900 RELATED ID: 4FST RELATED DB: PDB
REMARK 900 RELATED ID: 4FSU RELATED DB: PDB
REMARK 900 RELATED ID: 4FSW RELATED DB: PDB
REMARK 900 RELATED ID: 4FSY RELATED DB: PDB
REMARK 900 RELATED ID: 4FSZ RELATED DB: PDB
REMARK 900 RELATED ID: 4FT0 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT1 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT3 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT5 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT7 RELATED DB: PDB
REMARK 900 RELATED ID: 4FTA RELATED DB: PDB
REMARK 900 RELATED ID: 4FTC RELATED DB: PDB
REMARK 900 RELATED ID: 4FTI RELATED DB: PDB
REMARK 900 RELATED ID: 4FTJ RELATED DB: PDB
REMARK 900 RELATED ID: 4FTK RELATED DB: PDB
REMARK 900 RELATED ID: 4FTL RELATED DB: PDB
REMARK 900 RELATED ID: 4FTM RELATED DB: PDB
REMARK 900 RELATED ID: 4FTN RELATED DB: PDB
REMARK 900 RELATED ID: 4FTO RELATED DB: PDB
REMARK 900 RELATED ID: 4FTQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FTR RELATED DB: PDB
REMARK 900 RELATED ID: 4FTT RELATED DB: PDB
REMARK 900 RELATED ID: 4FTU RELATED DB: PDB
DBREF 4FT9 A 2 280 UNP O14757 CHK1_HUMAN 2 280
SEQRES 1 A 279 ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN THR
SEQRES 2 A 279 LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA VAL
SEQRES 3 A 279 ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE VAL
SEQRES 4 A 279 ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE LYS
SEQRES 5 A 279 LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU ASN
SEQRES 6 A 279 VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN ILE
SEQRES 7 A 279 GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU LEU
SEQRES 8 A 279 PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU PRO
SEQRES 9 A 279 ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY VAL
SEQRES 10 A 279 VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP ILE
SEQRES 11 A 279 LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN LEU
SEQRES 12 A 279 LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG TYR
SEQRES 13 A 279 ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY THR
SEQRES 14 A 279 LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG GLU
SEQRES 15 A 279 PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY ILE
SEQRES 16 A 279 VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP ASP
SEQRES 17 A 279 GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP LYS
SEQRES 18 A 279 GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE ASP
SEQRES 19 A 279 SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL GLU
SEQRES 20 A 279 ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS LYS
SEQRES 21 A 279 ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA LYS
SEQRES 22 A 279 ARG PRO ARG VAL THR SER
HET H4K A 300 32
HET SO4 A 301 5
HETNAM H4K 1-(5-CYANOPYRAZIN-2-YL)-3-ISOQUINOLIN-3-YLUREA
HETNAM SO4 SULFATE ION
FORMUL 2 H4K C15 H10 N6 O
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *222(H2 O)
HELIX 1 1 ASN A 51 LYS A 60 1 10
HELIX 2 2 PHE A 93 ILE A 96 5 4
HELIX 3 3 PRO A 103 ILE A 124 1 22
HELIX 4 4 LYS A 132 GLU A 134 5 3
HELIX 5 5 THR A 170 VAL A 174 5 5
HELIX 6 6 ALA A 175 ARG A 181 1 7
HELIX 7 7 HIS A 185 GLY A 204 1 20
HELIX 8 8 CYS A 215 GLU A 223 1 9
HELIX 9 9 PRO A 230 ILE A 234 5 5
HELIX 10 10 ASP A 235 LEU A 246 1 12
HELIX 11 11 THR A 255 LYS A 260 1 6
SHEET 1 A 5 TRP A 9 GLY A 16 0
SHEET 2 A 5 GLU A 22 ASN A 28 -1 O VAL A 23 N LEU A 15
SHEET 3 A 5 ALA A 34 ASP A 41 -1 O VAL A 35 N ALA A 26
SHEET 4 A 5 ILE A 79 GLU A 85 -1 O LEU A 84 N ALA A 36
SHEET 5 A 5 PHE A 70 GLU A 76 -1 N TYR A 71 O PHE A 83
SHEET 1 B 3 GLY A 90 GLU A 91 0
SHEET 2 B 3 LEU A 136 LEU A 138 -1 O LEU A 138 N GLY A 90
SHEET 3 B 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 C 2 ILE A 126 THR A 127 0
SHEET 2 C 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 D 2 ARG A 156 TYR A 157 0
SHEET 2 D 2 ARG A 160 GLU A 161 -1 O ARG A 160 N TYR A 157
CISPEP 1 ASN A 229 PRO A 230 0 5.53
SITE 1 AC1 13 LEU A 15 ALA A 36 LYS A 38 VAL A 68
SITE 2 AC1 13 LEU A 84 GLU A 85 TYR A 86 CYS A 87
SITE 3 AC1 13 GLY A 90 LEU A 137 SER A 147 ASP A 148
SITE 4 AC1 13 HOH A 561
SITE 1 AC2 6 LYS A 54 ARG A 129 THR A 153 ARG A 162
SITE 2 AC2 6 LYS A 166 HOH A 417
CRYST1 45.169 65.802 57.959 90.00 93.97 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 0.022139 0.000000 0.001536 0.00000
SCALE2 0.000000 0.015197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017295 0.00000
(ATOM LINES ARE NOT SHOWN.)
END