HEADER TRANSFERASE 06-JUN-11 2YM8
TITLE CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-289;
COMPND 5 SYNONYM: 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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS TRANSFERASE, DNA REPAIR, SERINE/THREONINE KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.READER,T.P.MATTHEWS,S.KLAIR,K.M.J.CHEUNG,J.SCANLON,N.PROISY,
AUTHOR 2 G.ADDISON,J.ELLARD,N.PITON,S.TAYLOR,M.CHERRY,M.FISHER,K.BOXALL,
AUTHOR 3 S.BURNS,M.I.WALTON,I.M.WESTWOOD,A.HAYES,P.EVE,M.VALENTI,A.H.BRANDON,
AUTHOR 4 G.BOX,R.L.M.VANMONTFORT,D.H.WILLIAMS,G.W.AHERNE,F.I.RAYNAUD,
AUTHOR 5 S.A.ECCLES,M.D.GARRETT,I.COLLINS
REVDAT 3 20-DEC-23 2YM8 1 REMARK
REVDAT 2 28-JUN-17 2YM8 1 REMARK
REVDAT 1 11-JAN-12 2YM8 0
JRNL AUTH J.C.READER,T.P.MATTHEWS,S.KLAIR,K.M.J.CHEUNG,J.SCANLON,
JRNL AUTH 2 N.PROISY,G.ADDISON,J.ELLARD,N.PITON,S.TAYLOR,M.CHERRY,
JRNL AUTH 3 M.FISHER,K.BOXALL,S.BURNS,M.I.WALTON,I.M.WESTWOOD,A.HAYES,
JRNL AUTH 4 P.EVE,M.VALENTI,A.DE HAVEN BRANDON,G.BOX,R.L.M.VAN MONTFORT,
JRNL AUTH 5 D.H.WILLIAMS,G.W.AHERNE,F.I.RAYNAUD,S.A.ECCLES,M.D.GARRETT,
JRNL AUTH 6 I.COLLINS
JRNL TITL STRUCTURE-GUIDED EVOLUTION OF POTENT AND SELECTIVE CHK1
JRNL TITL 2 INHIBITORS THROUGH SCAFFOLD MORPHING.
JRNL REF J.MED.CHEM. V. 54 8328 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 22111927
JRNL DOI 10.1021/JM2007326
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.P.MATTHEWS,S.KLAIR,S.BURNS,K.BOXALL,M.CHERRY,M.FISHER,
REMARK 1 AUTH 2 I.M.WESTWOOD,M.I.WALTON,T.MCHARDY,K.J.CHEUNG,R.VAN MONTFORT,
REMARK 1 AUTH 3 D.WILLIAMS,G.W.AHERNE,M.D.GARRETT,J.READER,I.COLLINS
REMARK 1 TITL IDENTIFICATION OF INHIBITORS OF CHECKPOINT KINASE 1 THROUGH
REMARK 1 TITL 2 TEMPLATE SCREENING.
REMARK 1 REF J.MED.CHEM. V. 52 4810 2009
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 19572549
REMARK 1 DOI 10.1021/JM900314J
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.P.MATTHEWS,T.MCHARDY,S.KLAIR,K.BOXALL,M.FISHER,M.CHERRY,
REMARK 1 AUTH 2 C.E.ALLEN,G.J.ADDISON,J.ELLARD,G.W.AHERNE,I.M.WESTWOOD,
REMARK 1 AUTH 3 R.VAN MONTFORT,M.D.GARRETT,J.C.READER,I.COLLINS
REMARK 1 TITL DESIGN AND EVALUATION OF 3,6-DI(HETERO)ARYL
REMARK 1 TITL 2 IMIDAZO[1,2-A]PYRAZINES AS INHIBITORS OF CHECKPOINT AND
REMARK 1 TITL 3 OTHER KINASES.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 20 4045 2010
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 20561787
REMARK 1 DOI 10.1016/J.BMCL.2010.05.096
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.2
REMARK 3 NUMBER OF REFLECTIONS : 31929
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1625
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 15.3077 - 4.6970 0.91 2881 143 0.2150 0.2526
REMARK 3 2 4.6970 - 3.7461 0.88 2766 133 0.1730 0.2193
REMARK 3 3 3.7461 - 3.2779 0.85 2702 133 0.1652 0.1913
REMARK 3 4 3.2779 - 2.9806 0.85 2647 146 0.1599 0.2193
REMARK 3 5 2.9806 - 2.7683 0.82 2576 154 0.1712 0.2065
REMARK 3 6 2.7683 - 2.6059 0.82 2594 131 0.1846 0.2163
REMARK 3 7 2.6059 - 2.4760 0.81 2529 136 0.1955 0.2306
REMARK 3 8 2.4760 - 2.3686 0.79 2525 154 0.2144 0.2792
REMARK 3 9 2.3686 - 2.2777 0.78 2480 107 0.2126 0.2644
REMARK 3 10 2.2777 - 2.1994 0.78 2442 152 0.2159 0.2669
REMARK 3 11 2.1994 - 2.1308 0.76 2335 132 0.2210 0.2711
REMARK 3 12 2.1308 - 2.0700 0.57 1827 104 0.2390 0.2553
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.47
REMARK 3 B_SOL : 71.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.04430
REMARK 3 B22 (A**2) : 0.40070
REMARK 3 B33 (A**2) : 1.64360
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.67780
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 2116
REMARK 3 ANGLE : 0.824 2845
REMARK 3 CHIRALITY : 0.056 305
REMARK 3 PLANARITY : 0.004 358
REMARK 3 DIHEDRAL : 12.649 796
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 8:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8352 -1.8492 0.5998
REMARK 3 T TENSOR
REMARK 3 T11: 0.4916 T22: 0.5303
REMARK 3 T33: 0.0906 T12: 0.0268
REMARK 3 T13: -0.0184 T23: -0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 0.1073 L22: 0.1090
REMARK 3 L33: 0.0860 L12: 0.0213
REMARK 3 L13: -0.0930 L23: 0.0046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0396 S12: 0.1885 S13: -0.0133
REMARK 3 S21: -0.1814 S22: 0.0623 S23: -0.0393
REMARK 3 S31: 0.0082 S32: -0.0018 S33: 0.1832
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 52:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6563 5.3994 14.9068
REMARK 3 T TENSOR
REMARK 3 T11: 0.2344 T22: 0.2795
REMARK 3 T33: 0.1857 T12: -0.0275
REMARK 3 T13: -0.0879 T23: 0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 0.2549 L22: 0.3798
REMARK 3 L33: 0.0670 L12: 0.0673
REMARK 3 L13: 0.0185 L23: 0.1362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: 0.3326 S13: 0.0191
REMARK 3 S21: -0.2203 S22: 0.0057 S23: 0.1923
REMARK 3 S31: -0.0986 S32: -0.0265 S33: 0.0009
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 70:85)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7968 -1.6023 5.3648
REMARK 3 T TENSOR
REMARK 3 T11: 0.4155 T22: 0.5414
REMARK 3 T33: 0.1199 T12: -0.0579
REMARK 3 T13: -0.1448 T23: -0.0908
REMARK 3 L TENSOR
REMARK 3 L11: 0.0546 L22: 0.0099
REMARK 3 L33: 0.0026 L12: 0.0062
REMARK 3 L13: 0.0003 L23: 0.0045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: 0.1073 S13: -0.0162
REMARK 3 S21: -0.1204 S22: -0.0228 S23: 0.0655
REMARK 3 S31: 0.0184 S32: -0.0246 S33: -0.1446
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 86:103)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7616 2.5251 17.4265
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.1888
REMARK 3 T33: 0.0784 T12: 0.0540
REMARK 3 T13: 0.0780 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.1494 L22: 0.4627
REMARK 3 L33: 0.1573 L12: 0.0633
REMARK 3 L13: -0.0331 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0197 S12: 0.2411 S13: -0.0787
REMARK 3 S21: -0.1820 S22: -0.0161 S23: -0.1005
REMARK 3 S31: 0.0466 S32: -0.0062 S33: -0.0074
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 104:143)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0045 8.6809 21.0434
REMARK 3 T TENSOR
REMARK 3 T11: 0.0672 T22: 0.0705
REMARK 3 T33: 0.0637 T12: 0.0078
REMARK 3 T13: -0.0034 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 1.1938 L22: 0.8538
REMARK 3 L33: 0.0079 L12: 0.2428
REMARK 3 L13: -0.0319 L23: 0.0791
REMARK 3 S TENSOR
REMARK 3 S11: -0.0532 S12: 0.2323 S13: -0.0008
REMARK 3 S21: -0.2602 S22: 0.0706 S23: 0.0982
REMARK 3 S31: -0.0214 S32: -0.0377 S33: 0.0473
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 144:161)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2736 5.5705 24.6169
REMARK 3 T TENSOR
REMARK 3 T11: 0.1083 T22: 0.1058
REMARK 3 T33: 0.1928 T12: -0.0072
REMARK 3 T13: -0.0314 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 0.5130 L22: 0.3511
REMARK 3 L33: 0.0768 L12: -0.1454
REMARK 3 L13: -0.0528 L23: 0.0775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: 0.1272 S13: -0.0643
REMARK 3 S21: -0.0551 S22: -0.0350 S23: 0.3246
REMARK 3 S31: -0.0002 S32: -0.0411 S33: -0.0231
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 162:185)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0799 -3.2361 35.0794
REMARK 3 T TENSOR
REMARK 3 T11: 0.1041 T22: 0.1023
REMARK 3 T33: 0.1327 T12: -0.0015
REMARK 3 T13: 0.0121 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.3480 L22: 0.2556
REMARK 3 L33: 0.1482 L12: 0.0896
REMARK 3 L13: -0.0424 L23: -0.0881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: -0.1267 S13: -0.1193
REMARK 3 S21: 0.1292 S22: 0.0159 S23: 0.0621
REMARK 3 S31: 0.0481 S32: -0.1001 S33: 0.0169
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 186:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4233 2.8408 37.0643
REMARK 3 T TENSOR
REMARK 3 T11: 0.0692 T22: 0.0981
REMARK 3 T33: 0.0898 T12: 0.0017
REMARK 3 T13: -0.0172 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 0.5793 L22: 0.6296
REMARK 3 L33: 0.3132 L12: 0.1154
REMARK 3 L13: 0.0208 L23: 0.1206
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: -0.2481 S13: -0.1402
REMARK 3 S21: 0.1391 S22: -0.1085 S23: -0.0294
REMARK 3 S31: 0.0029 S32: 0.0943 S33: -0.4847
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 256:270)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5560 18.5148 30.8734
REMARK 3 T TENSOR
REMARK 3 T11: 0.0796 T22: 0.0283
REMARK 3 T33: 0.1742 T12: -0.0008
REMARK 3 T13: 0.0536 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.0637 L22: 0.1165
REMARK 3 L33: 0.0164 L12: 0.0840
REMARK 3 L13: -0.0152 L23: -0.0278
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: -0.0097 S13: 0.0746
REMARK 3 S21: 0.0583 S22: -0.0273 S23: -0.1031
REMARK 3 S31: -0.0443 S32: 0.0187 S33: -0.0337
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1-7, 17-21, 40-50, 77, 78, 271
REMARK 3 -289 ARE DISORDERED
REMARK 4
REMARK 4 2YM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1290048554.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18722
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 15.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 2WMW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DL-MALIC ACID, PEG 3350.
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 32.73500
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 PRO A 4
REMARK 465 PHE A 5
REMARK 465 VAL A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 TYR A 20
REMARK 465 GLY A 21
REMARK 465 ASP A 41
REMARK 465 MET A 42
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 GLY A 77
REMARK 465 ASN A 78
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 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 99 -4.60 68.25
REMARK 500 ARG A 129 -9.52 83.35
REMARK 500 ASP A 130 48.97 -141.82
REMARK 500 ASP A 148 92.68 69.41
REMARK 500 ASN A 165 -8.34 -143.84
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 YM8 A 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1280
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XF0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2BRB RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2X8D RELATED DB: PDB
REMARK 900 DISCOVERY OF A NOVEL CLASS OF TRIAZOLONES AS CHECKPOINT KINASE
REMARK 900 INHIBITORS - HIT TO LEAD EXPLORATION
REMARK 900 RELATED ID: 2WMR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2CGV RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 2BRN RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2WMX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YER RELATED DB: PDB
REMARK 900 SYNTHESIS AND EVALUATION OF TRIAZOLONES AS CHECKPOINT KINASE 1
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2AYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK1 WITH AN INDOL INHIBITOR
REMARK 900 RELATED ID: 2CGU RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 1NVS RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/SB218078
REMARK 900 RELATED ID: 2BRM RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2YDJ RELATED DB: PDB
REMARK 900 DISCOVERY OF CHECKPOINT KINASE INHIBITOR AZD7762 BY STRUCTURE BASED
REMARK 900 DESIGN AND OPTIMIZATION OF THIOPHENE CARBOXAMIDE UREAS
REMARK 900 RELATED ID: 1NVQ RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/UCN-01
REMARK 900 RELATED ID: 2YDI RELATED DB: PDB
REMARK 900 DISCOVERY OF CHECKPOINT KINASE INHIBITOR AZD7762 BY STRUCTURE BASED
REMARK 900 DESIGN AND OPTIMIZATION OF THIOPHENE CARBOXAMIDE UREAS
REMARK 900 RELATED ID: 2WMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2CGX RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 2C3J RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 2BRO RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2WMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2BRH RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2X8E RELATED DB: PDB
REMARK 900 DISCOVERY OF A NOVEL CLASS OF TRIAZOLONES AS CHECKPOINT KINASE
REMARK 900 INHIBITORS - HIT TO LEAD EXPLORATION
REMARK 900 RELATED ID: 2C3K RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 1NVR RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASECHK1/ STAUROSPORINE
REMARK 900 RELATED ID: 2WMQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 1ZLT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK1 COMPLEXED WITH A HYMENALDISINEANALOG
REMARK 900 RELATED ID: 2CGW RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 2YEX RELATED DB: PDB
REMARK 900 SYNTHESIS AND EVALUATION OF TRIAZOLONES AS CHECKPOINT KINASE 1
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2XEZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 1ZYS RELATED DB: PDB
REMARK 900 CO-CRYSTAL STRUCTURE OF CHECKPOINT KINASE CHK1 WITH APYRROLO-
REMARK 900 PYRIDINE INHIBITOR
REMARK 900 RELATED ID: 1IA8 RELATED DB: PDB
REMARK 900 THE 1.7 A CRYSTAL STRUCTURE OF HUMAN CELL CYCLE CHECKPOINTKINASE
REMARK 900 CHK1
REMARK 900 RELATED ID: 2BR1 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRG RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2YDK RELATED DB: PDB
REMARK 900 DISCOVERY OF CHECKPOINT KINASE INHIBITOR AZD7762 BY STRUCTURE BASED
REMARK 900 DESIGN AND OPTIMIZATION OF THIOPHENE CARBOXAMIDE UREAS
REMARK 900 RELATED ID: 2WMV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2X8I RELATED DB: PDB
REMARK 900 DISCOVERY OF A NOVEL CLASS OF TRIAZOLONES AS CHECKPOINT KINASE
REMARK 900 INHIBITORS - HIT TO LEAD EXPLORATION
REMARK 900 RELATED ID: 2C3L RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 2XEY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YM3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YM5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YM4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YM7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2YM6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
DBREF 2YM8 A 1 289 UNP O14757 CHK1_HUMAN 1 289
SEQRES 1 A 289 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 289 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 289 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 289 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 289 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 A 289 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 289 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 A 289 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 289 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 289 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 289 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 289 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 A 289 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 289 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 289 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 289 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 289 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 289 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 289 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 289 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 289 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 A 289 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 A 289 PRO SER GLY
HET YM8 A1271 27
HET EDO A1272 4
HET EDO A1273 4
HET EDO A1274 4
HET EDO A1275 4
HET EDO A1276 4
HET EDO A1277 4
HET EDO A1278 4
HET EDO A1279 4
HET EDO A1280 4
HETNAM YM8 (R)-5-(8-CHLOROISOQUINOLIN-3-YLAMINO)-3-(1-
HETNAM 2 YM8 (DIMETHYLAMINO)PROPAN-2-YLOXY)PYRAZINE-2-CARBONITRILE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 YM8 C19 H19 CL N6 O
FORMUL 3 EDO 9(C2 H6 O2)
FORMUL 12 HOH *121(H2 O)
HELIX 1 1 ASN A 51 LEU A 62 1 12
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
HELIX 12 12 ARG A 263 LYS A 267 5 5
SHEET 1 AA 5 TRP A 9 THR A 14 0
SHEET 2 AA 5 VAL A 23 ASN A 28 -1 O LEU A 25 N VAL A 12
SHEET 3 AA 5 ALA A 34 VAL A 40 -1 O VAL A 35 N ALA A 26
SHEET 4 AA 5 GLN A 80 GLU A 85 -1 O GLN A 80 N VAL A 40
SHEET 5 AA 5 PHE A 70 ARG A 75 -1 N TYR A 71 O PHE A 83
SHEET 1 AB 3 GLY A 90 GLU A 91 0
SHEET 2 AB 3 LEU A 136 LEU A 138 -1 N LEU A 138 O GLY A 90
SHEET 3 AB 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 AC 2 ILE A 126 THR A 127 0
SHEET 2 AC 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 AD 2 ARG A 156 TYR A 157 0
SHEET 2 AD 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 0.71
SITE 1 AC1 12 ALA A 36 LYS A 38 LEU A 84 GLU A 85
SITE 2 AC1 12 TYR A 86 CYS A 87 GLU A 134 ASN A 135
SITE 3 AC1 12 LEU A 137 SER A 147 ASP A 148 HOH A2054
SITE 1 AC2 2 HIS A 112 ASN A 266
SITE 1 AC3 4 ARG A 129 LEU A 164 ASN A 165 LYS A 166
SITE 1 AC4 5 GLY A 123 ARG A 156 TYR A 157 ASN A 158
SITE 2 AC4 5 ASN A 159
SITE 1 AC5 4 GLN A 108 LYS A 267 PRO A 268 LEU A 269
SITE 1 AC6 3 TRP A 221 LYS A 224 HIS A 243
SITE 1 AC7 3 ARG A 29 ARG A 181 ASN A 249
SITE 1 AC8 5 GLU A 32 VAL A 247 GLU A 248 ASN A 249
SITE 2 AC8 5 ALA A 252
SITE 1 AC9 4 LYS A 132 GLU A 134 HOH A2120 HOH A2121
SITE 1 BC1 3 ALA A 116 LYS A 260 TYR A 265
CRYST1 44.770 65.470 57.930 90.00 95.38 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 0.022336 0.000000 0.002104 0.00000
SCALE2 0.000000 0.015274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
