HEADER TRANSFERASE 09-AUG-17 5OP5
TITLE STRUCTURE OF CHK1 10-PT. MUTANT COMPLEX WITH PYRROLOPYRIMIDINE LRRK2
TITLE 2 INHIBITOR
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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS PARKINSON'S DISEASE, LEUCINE-RICH REPEAT KINASE 2, LRRK2, CHECKPOINT
KEYWDS 2 KINASE 1, CHK1, MUTANT, SURROGATE, KINASE INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.DOKURNO,D.S.WILLIAMSON,P.ACHESON-DOSSANG,I.CHEN,J.B.MURRAY,T.SHAW,
AUTHOR 2 A.E.SURGENOR
REVDAT 3 17-JAN-24 5OP5 1 REMARK
REVDAT 2 22-NOV-17 5OP5 1 JRNL
REVDAT 1 25-OCT-17 5OP5 0
JRNL AUTH D.S.WILLIAMSON,G.P.SMITH,P.ACHESON-DOSSANG,S.T.BEDFORD,
JRNL AUTH 2 V.CHELL,I.J.CHEN,J.C.A.DAECHSEL,Z.DANIELS,L.DAVID,P.DOKURNO,
JRNL AUTH 3 M.HENTZER,M.C.HERZIG,R.E.HUBBARD,J.D.MOORE,J.B.MURRAY,
JRNL AUTH 4 S.NEWLAND,S.C.RAY,T.SHAW,A.E.SURGENOR,L.TERRY,K.THIRSTRUP,
JRNL AUTH 5 Y.WANG,K.V.CHRISTENSEN
JRNL TITL DESIGN OF LEUCINE-RICH REPEAT KINASE 2 (LRRK2) INHIBITORS
JRNL TITL 2 USING A CRYSTALLOGRAPHIC SURROGATE DERIVED FROM CHECKPOINT
JRNL TITL 3 KINASE 1 (CHK1).
JRNL REF J. MED. CHEM. V. 60 8945 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29023112
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01186
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 22915
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1170
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3296
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2083
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.50000
REMARK 3 B22 (A**2) : -0.81000
REMARK 3 B33 (A**2) : 2.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.587
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2160 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2007 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2930 ; 1.915 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4638 ; 1.045 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.455 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;35.133 ;24.400
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 372 ;15.926 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.706 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 317 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2361 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 424 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5OP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-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 : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26984
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 41.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.52800
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: 5OOP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1 M MES BUFFER PH 6.5,
REMARK 280 20% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
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 32.89500
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: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
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 465 GLU A 50
REMARK 465 LYS A 271
REMARK 465 GLY A 272
REMARK 465 ALA A 273
REMARK 465 LYS A 274
REMARK 465 ARG A 275
REMARK 465 PRO A 276
REMARK 465 ARG A 277
REMARK 465 VAL A 278
REMARK 465 THR A 279
REMARK 465 SER A 280
REMARK 465 GLY A 281
REMARK 465 GLY A 282
REMARK 465 VAL A 283
REMARK 465 SER A 284
REMARK 465 GLU A 285
REMARK 465 SER A 286
REMARK 465 PRO A 287
REMARK 465 SER A 288
REMARK 465 GLY A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
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 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 213 CG OD1 OD2
REMARK 470 LYS A 270 CG CD CE NZ
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 428 O HOH A 450 1.32
REMARK 500 O HOH A 460 O HOH A 564 1.79
REMARK 500 O HOH A 490 O HOH A 575 1.79
REMARK 500 O HOH A 570 O HOH A 585 1.91
REMARK 500 O HOH A 525 O HOH A 565 1.96
REMARK 500 O HOH A 468 O HOH A 574 1.98
REMARK 500 O HOH A 582 O HOH A 595 2.00
REMARK 500 O HOH A 497 O HOH A 559 2.08
REMARK 500 O HOH A 572 O HOH A 593 2.08
REMARK 500 O HOH A 537 O HOH A 558 2.15
REMARK 500 O HOH A 432 O HOH A 564 2.15
REMARK 500 O HOH A 544 O HOH A 555 2.16
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 589 O HOH A 614 2555 2.12
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 130 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 181 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 263 NE - CZ - NH1 ANGL. DEV. = 3.2 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 GLU A 7 -124.28 49.88
REMARK 500 VAL A 30 -73.64 -60.04
REMARK 500 GLU A 32 -2.23 73.74
REMARK 500 ASP A 99 -2.30 70.87
REMARK 500 ILE A 100 -50.49 -123.22
REMARK 500 ASP A 130 53.92 -148.83
REMARK 500 ASP A 148 99.79 74.82
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 3FE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5OOP RELATED DB: PDB
REMARK 900 RELATED ID: 5OOR RELATED DB: PDB
REMARK 900 RELATED ID: 5OOT RELATED DB: PDB
REMARK 900 RELATED ID: 5OP2 RELATED DB: PDB
REMARK 900 RELATED ID: 5OP4 RELATED DB: PDB
DBREF 5OP5 A 1 289 UNP O14757 CHK1_HUMAN 1 289
SEQADV 5OP5 LEU A 59 UNP O14757 ASN 59 ENGINEERED MUTATION
SEQADV 5OP5 ILE A 68 UNP O14757 VAL 68 ENGINEERED MUTATION
SEQADV 5OP5 MET A 84 UNP O14757 LEU 84 ENGINEERED MUTATION
SEQADV 5OP5 LEU A 86 UNP O14757 TYR 86 ENGINEERED MUTATION
SEQADV 5OP5 ALA A 87 UNP O14757 CYS 87 ENGINEERED MUTATION
SEQADV 5OP5 SER A 91 UNP O14757 GLU 91 ENGINEERED MUTATION
SEQADV 5OP5 HIS A 134 UNP O14757 GLU 134 ENGINEERED MUTATION
SEQADV 5OP5 ALA A 147 UNP O14757 SER 147 ENGINEERED MUTATION
SEQADV 5OP5 TYR A 149 UNP O14757 PHE 149 ENGINEERED MUTATION
SEQADV 5OP5 SER A 150 UNP O14757 GLY 150 ENGINEERED MUTATION
SEQADV 5OP5 HIS A 290 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 291 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 292 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 293 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 294 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 295 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 296 UNP O14757 EXPRESSION TAG
SEQADV 5OP5 HIS A 297 UNP O14757 EXPRESSION TAG
SEQRES 1 A 297 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 297 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 297 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 297 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 297 LYS LYS GLU ILE CYS ILE LEU LYS MET LEU ASN HIS GLU
SEQRES 6 A 297 ASN VAL ILE LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 297 ILE GLN TYR LEU PHE MET GLU LEU ALA SER GLY GLY SER
SEQRES 8 A 297 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 297 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 297 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 297 ILE LYS PRO HIS ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 297 LEU LYS ILE ALA ASP TYR SER LEU ALA THR VAL PHE ARG
SEQRES 13 A 297 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 297 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 297 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 297 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 297 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 297 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 297 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 297 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 297 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 A 297 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 A 297 PRO SER GLY HIS HIS HIS HIS HIS HIS HIS HIS
HET 3FE A 301 23
HET CL A 302 1
HETNAM 3FE 3-[4-(MORPHOLIN-4-YL)-7H-PYRROLO[2,3-D]PYRIMIDIN-5-
HETNAM 2 3FE YL]BENZONITRILE
HETNAM CL CHLORIDE ION
FORMUL 2 3FE C17 H15 N5 O
FORMUL 3 CL CL 1-
FORMUL 4 HOH *219(H2 O)
HELIX 1 AA1 ILE A 52 LEU A 62 1 11
HELIX 2 AA2 SER A 91 ILE A 96 5 6
HELIX 3 AA3 PRO A 103 ILE A 124 1 22
HELIX 4 AA4 LYS A 132 HIS A 134 5 3
HELIX 5 AA5 THR A 170 VAL A 174 5 5
HELIX 6 AA6 ALA A 175 ARG A 181 1 7
HELIX 7 AA7 HIS A 185 GLY A 204 1 20
HELIX 8 AA8 CYS A 215 GLU A 223 1 9
HELIX 9 AA9 PRO A 230 ILE A 234 5 5
HELIX 10 AB1 ASP A 235 LEU A 246 1 12
HELIX 11 AB2 THR A 255 LYS A 260 1 6
SHEET 1 AA1 6 PHE A 5 VAL A 6 0
SHEET 2 AA1 6 TRP A 9 GLU A 17 -1 O TRP A 9 N VAL A 6
SHEET 3 AA1 6 GLU A 22 ASN A 28 -1 O LEU A 25 N GLN A 13
SHEET 4 AA1 6 ALA A 34 ASP A 41 -1 O ILE A 39 N GLU A 22
SHEET 5 AA1 6 ILE A 79 MET A 84 -1 O MET A 84 N ALA A 36
SHEET 6 AA1 6 PHE A 70 GLU A 76 -1 N GLY A 72 O PHE A 83
SHEET 1 AA2 2 ILE A 126 THR A 127 0
SHEET 2 AA2 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 AA3 2 LEU A 136 LEU A 138 0
SHEET 2 AA3 2 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 AA4 2 ARG A 156 TYR A 157 0
SHEET 2 AA4 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 6.48
SITE 1 AC1 10 GLY A 16 ALA A 36 LYS A 38 MET A 84
SITE 2 AC1 10 GLU A 85 LEU A 86 ALA A 87 LEU A 137
SITE 3 AC1 10 ASP A 148 HOH A 421
SITE 1 AC2 1 HOH A 601
CRYST1 44.940 65.790 54.310 90.00 101.47 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 0.022252 0.000000 0.004515 0.00000
SCALE2 0.000000 0.015200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018788 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
