HEADER TRANSFERASE/TRANSFERASE INHIBITOR 20-DEC-11 3V6S
TITLE DISCOVERY OF POTENT AND SELECTIVE COVALENT INHIBITORS OF JNK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MAP KINASE 10, MAPK 10, MAP KINASE P49 3F12, STRESS-
COMPND 5 ACTIVATED PROTEIN KINASE 1B, SAPK1B, STRESS-ACTIVATED PROTEIN KINASE
COMPND 6 JNK3, C-JUN N-TERMINAL KINASE 3;
COMPND 7 EC: 2.7.11.24;
COMPND 8 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: MAPK10, JNK3, JNK3A, PRKM10, SAPK1B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE FOLD, APOPTOSIS, MAP KINASE, CYS MODIFICATION, JNK,
KEYWDS 2 PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.PARK,J.D.LAUGHLIN,P.V.LOGRASSO
REVDAT 2 25-JUL-12 3V6S 1 JRNL
REVDAT 1 01-FEB-12 3V6S 0
JRNL AUTH T.ZHANG,F.INESTA-VAQUERA,M.NIEPEL,J.ZHANG,S.B.FICARRO,
JRNL AUTH 2 T.MACHLEIDT,T.XIE,J.A.MARTO,N.KIM,T.SIM,J.D.LAUGHLIN,H.PARK,
JRNL AUTH 3 P.V.LOGRASSO,M.PATRICELLI,T.K.NOMANBHOY,P.K.SORGER,
JRNL AUTH 4 D.R.ALESSI,N.S.GRAY
JRNL TITL DISCOVERY OF POTENT AND SELECTIVE COVALENT INHIBITORS OF
JRNL TITL 2 JNK.
JRNL REF CHEM.BIOL. V. 19 140 2012
JRNL REFN ISSN 1074-5521
JRNL PMID 22284361
JRNL DOI 10.1016/J.CHEMBIOL.2011.11.010
REMARK 2
REMARK 2 RESOLUTION. 2.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.2
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) : 2.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16238
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.210
REMARK 3 FREE R VALUE TEST SET COUNT : 1009
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) : 2.97
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2887
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2352
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2691
REMARK 3 BIN R VALUE (WORKING SET) : 0.2321
REMARK 3 BIN FREE R VALUE : 0.2786
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 196
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 : 5478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.99880
REMARK 3 B22 (A**2) : 8.30030
REMARK 3 B33 (A**2) : 2.69850
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) : 0.40
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) : NULL
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 : 0.889
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.845
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5697 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7732 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2598 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 146 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 806 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5611 ; 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 : 734 ; 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 : 6664 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.19
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.06
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.20
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|45 - 96}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2886 -12.4764 -35.6181
REMARK 3 T TENSOR
REMARK 3 T11: -0.0845 T22: -0.0776
REMARK 3 T33: -0.0592 T12: 0.0344
REMARK 3 T13: -0.0193 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.6639 L22: 4.1634
REMARK 3 L33: 6.9611 L12: 0.2470
REMARK 3 L13: -0.6482 L23: -0.1942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: 0.0879 S13: -0.0165
REMARK 3 S21: -0.0145 S22: -0.0705 S23: 0.0803
REMARK 3 S31: -0.0213 S32: -0.1943 S33: 0.1340
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|97 - 111}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8429 -27.0489 -22.2911
REMARK 3 T TENSOR
REMARK 3 T11: 0.0398 T22: -0.0573
REMARK 3 T33: 0.0918 T12: 0.0929
REMARK 3 T13: -0.0920 T23: 0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 1.2827 L22: 3.9151
REMARK 3 L33: 0.0000 L12: -1.5098
REMARK 3 L13: -2.7369 L23: -2.8291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0238 S12: 0.0394 S13: -0.0252
REMARK 3 S21: 0.0021 S22: 0.0293 S23: -0.0343
REMARK 3 S31: 0.1285 S32: 0.1059 S33: -0.0055
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|112 - 199}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9353 -15.3881 -19.9383
REMARK 3 T TENSOR
REMARK 3 T11: -0.0678 T22: -0.0029
REMARK 3 T33: -0.0748 T12: -0.0013
REMARK 3 T13: -0.0129 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.0190 L22: 1.0563
REMARK 3 L33: 1.1819 L12: 0.5842
REMARK 3 L13: 0.8483 L23: -0.1627
REMARK 3 S TENSOR
REMARK 3 S11: -0.1599 S12: 0.0270 S13: 0.1546
REMARK 3 S21: 0.0148 S22: 0.0222 S23: 0.1452
REMARK 3 S31: -0.2307 S32: -0.1294 S33: 0.1377
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|200 - 219}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4201 -22.0599 -14.9371
REMARK 3 T TENSOR
REMARK 3 T11: 0.0003 T22: 0.0005
REMARK 3 T33: -0.0507 T12: 0.0073
REMARK 3 T13: 0.0148 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 3.6788
REMARK 3 L33: 0.4649 L12: 0.6023
REMARK 3 L13: 0.6047 L23: 0.6944
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: -0.1884 S13: -0.1218
REMARK 3 S21: 0.0749 S22: 0.0370 S23: -0.0348
REMARK 3 S31: 0.0082 S32: -0.1612 S33: -0.0259
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|225 - 375}
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0936 -27.3826 -7.4963
REMARK 3 T TENSOR
REMARK 3 T11: -0.0171 T22: -0.0597
REMARK 3 T33: -0.1230 T12: -0.0260
REMARK 3 T13: -0.0210 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.5467 L22: 1.6741
REMARK 3 L33: 0.6446 L12: 0.1279
REMARK 3 L13: -0.1442 L23: 0.3641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: -0.0158 S13: -0.3621
REMARK 3 S21: -0.0491 S22: 0.0257 S23: -0.0685
REMARK 3 S31: 0.2097 S32: 0.0037 S33: -0.0486
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|379 - 401}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5765 -22.4109 -19.4557
REMARK 3 T TENSOR
REMARK 3 T11: -0.0520 T22: 0.0273
REMARK 3 T33: 0.0173 T12: 0.0947
REMARK 3 T13: 0.0260 T23: 0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 1.3175 L12: 0.4409
REMARK 3 L13: -2.8749 L23: -0.4850
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.1279 S13: 0.1263
REMARK 3 S21: 0.0606 S22: -0.0142 S23: -0.0011
REMARK 3 S31: 0.1147 S32: -0.0586 S33: 0.0212
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {B|45 - 92}
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5794 -58.9282 -25.9593
REMARK 3 T TENSOR
REMARK 3 T11: -0.2795 T22: -0.1629
REMARK 3 T33: 0.2874 T12: 0.0168
REMARK 3 T13: 0.1494 T23: -0.0741
REMARK 3 L TENSOR
REMARK 3 L11: 4.9176 L22: 1.5932
REMARK 3 L33: 6.3785 L12: -2.8254
REMARK 3 L13: 0.2412 L23: -0.2349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.1589 S13: 0.0023
REMARK 3 S21: 0.2554 S22: 0.0978 S23: -0.2520
REMARK 3 S31: 0.1635 S32: 0.2768 S33: -0.1129
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {B|93 - 111}
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2082 -71.0345 -31.4416
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: -0.0349
REMARK 3 T33: -0.0257 T12: 0.0175
REMARK 3 T13: 0.0357 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.9421
REMARK 3 L33: 2.3193 L12: -0.2291
REMARK 3 L13: -2.8544 L23: -0.9112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: -0.0095 S13: -0.0764
REMARK 3 S21: 0.0459 S22: -0.0341 S23: 0.0194
REMARK 3 S31: -0.0795 S32: 0.0472 S33: 0.0269
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {B|112 - 187}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5704 -54.9721 -25.0172
REMARK 3 T TENSOR
REMARK 3 T11: -0.1040 T22: -0.1444
REMARK 3 T33: -0.0481 T12: -0.0504
REMARK 3 T13: 0.0720 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.4430 L22: 4.2536
REMARK 3 L33: 1.4281 L12: -0.6308
REMARK 3 L13: 0.2771 L23: 1.9199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: 0.2443 S13: 0.1088
REMARK 3 S21: -0.3756 S22: -0.0223 S23: -0.5418
REMARK 3 S31: 0.1956 S32: 0.0984 S33: 0.0235
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {B|188 - 211}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1491 -55.6793 -21.1128
REMARK 3 T TENSOR
REMARK 3 T11: 0.1145 T22: -0.1113
REMARK 3 T33: -0.0141 T12: -0.0308
REMARK 3 T13: -0.0874 T23: 0.1140
REMARK 3 L TENSOR
REMARK 3 L11: 3.0720 L22: 0.0000
REMARK 3 L33: 1.6156 L12: 1.3985
REMARK 3 L13: -1.5754 L23: 1.1787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.0564 S13: -0.0431
REMARK 3 S21: -0.0840 S22: -0.1150 S23: -0.0230
REMARK 3 S31: 0.0388 S32: -0.0233 S33: 0.1029
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {B|225 - 380}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0515 -57.2888 -12.9731
REMARK 3 T TENSOR
REMARK 3 T11: -0.0225 T22: -0.1233
REMARK 3 T33: -0.1046 T12: 0.0037
REMARK 3 T13: -0.0200 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.6727 L22: 3.0823
REMARK 3 L33: 1.1756 L12: 0.7498
REMARK 3 L13: -0.7022 L23: -1.2720
REMARK 3 S TENSOR
REMARK 3 S11: -0.1124 S12: -0.0036 S13: 0.0353
REMARK 3 S21: 0.1126 S22: 0.0520 S23: 0.1644
REMARK 3 S31: 0.1051 S32: -0.0455 S33: 0.0604
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {B|381 - 401}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9952 -71.2238 -40.7786
REMARK 3 T TENSOR
REMARK 3 T11: 0.2405 T22: -0.0457
REMARK 3 T33: -0.1871 T12: 0.1520
REMARK 3 T13: 0.0563 T23: 0.0917
REMARK 3 L TENSOR
REMARK 3 L11: 0.0633 L22: 2.5207
REMARK 3 L33: 2.1317 L12: -2.7223
REMARK 3 L13: 1.7389 L23: 2.3115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.0945 S13: 0.0784
REMARK 3 S21: -0.1227 S22: 0.0452 S23: 0.0376
REMARK 3 S31: -0.0586 S32: -0.2088 S33: -0.0407
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3V6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-11; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : SSRL; NULL
REMARK 200 BEAMLINE : BL11-1; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945; NULL
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-ROOT I
REMARK 200 -BEAM SINGLE CRYSTAL; ASYMMETRIC
REMARK 200 CUT 4.965 DEGS
REMARK 200 OPTICS : RH COATED FLAT MIRROR; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16326
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 156.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.0, 100 MM NACL, 5%
REMARK 280 GLYCEROL, 5 MM TCEP, 0.4 MM ZWITTERGENT 3-14), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 54.74550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.13100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.74550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.13100
REMARK 290 SMTRY3 4 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 MET A 39
REMARK 465 SER A 40
REMARK 465 LYS A 41
REMARK 465 SER A 42
REMARK 465 LYS A 43
REMARK 465 VAL A 44
REMARK 465 MET A 220
REMARK 465 THR A 221
REMARK 465 PRO A 222
REMARK 465 TYR A 223
REMARK 465 VAL A 224
REMARK 465 TYR A 376
REMARK 465 ASP A 377
REMARK 465 LYS A 378
REMARK 465 GLU A 402
REMARK 465 MET B 39
REMARK 465 SER B 40
REMARK 465 LYS B 41
REMARK 465 SER B 42
REMARK 465 LYS B 43
REMARK 465 VAL B 44
REMARK 465 ARG B 212
REMARK 465 THR B 213
REMARK 465 ALA B 214
REMARK 465 GLY B 215
REMARK 465 THR B 216
REMARK 465 SER B 217
REMARK 465 PHE B 218
REMARK 465 MET B 219
REMARK 465 MET B 220
REMARK 465 THR B 221
REMARK 465 PRO B 222
REMARK 465 TYR B 223
REMARK 465 VAL B 224
REMARK 465 TYR B 376
REMARK 465 ASP B 377
REMARK 465 LYS B 378
REMARK 465 GLU B 402
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 ASP A 45 CG OD1 OD2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 97 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 LYS A 260 CG CD CE NZ
REMARK 470 ARG A 266 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 ARG A 383 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 388 CG CD OE1 OE2
REMARK 470 GLU A 389 CG CD OE1 OE2
REMARK 470 ASP B 45 CG OD1 OD2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 LYS B 260 CG CD CE NZ
REMARK 470 ARG B 266 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 285 CG CD OE1 OE2
REMARK 470 LYS B 289 CG CD CE NZ
REMARK 470 LYS B 326 CG CD CE NZ
REMARK 470 ILE B 375 CG1 CG2 CD1
REMARK 470 GLN B 379 CG CD OE1 NE2
REMARK 470 ARG B 383 CG CD NE CZ NH1 NH2
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 CYS A 154 CA - CB - SG ANGL. DEV. = -14.5 DEGREES
REMARK 500 ARG A 188 CG - CD - NE ANGL. DEV. = -13.8 DEGREES
REMARK 500 ASP A 321 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 CYS B 154 CA - CB - SG ANGL. DEV. = -13.9 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 SER A 72 -117.78 -168.74
REMARK 500 ALA A 74 -45.32 64.15
REMARK 500 GLN A 75 96.00 -161.94
REMARK 500 ARG A 97 70.29 37.23
REMARK 500 GLN A 140 -25.21 -147.08
REMARK 500 ARG A 188 -7.99 73.08
REMARK 500 ALA A 211 -100.99 51.16
REMARK 500 THR A 216 83.29 -55.81
REMARK 500 SER A 322 168.35 75.37
REMARK 500 GLU A 382 7.44 -176.98
REMARK 500 ASN B 46 -56.05 61.61
REMARK 500 ILE B 70 -41.93 -132.20
REMARK 500 ALA B 74 -127.59 59.94
REMARK 500 GLN B 140 -40.40 -142.20
REMARK 500 ARG B 188 -8.47 71.95
REMARK 500 ARG B 227 -3.33 71.18
REMARK 500 SER B 322 151.58 -43.48
REMARK 500 GLU B 369 31.20 -90.41
REMARK 500 GLN B 374 90.91 -62.87
REMARK 500 LEU B 380 -75.52 -111.90
REMARK 500 ASP B 381 -34.46 -154.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 322 GLU A 323 -31.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 643 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH A 667 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 699 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH B 653 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 669 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B 674 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B 687 DISTANCE = 7.71 ANGSTROMS
REMARK 525 HOH B 690 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH B 699 DISTANCE = 5.33 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE ATOMS C33 OF LIGAND 0F0 IS COVALENTLY LINKED TO SG ATOM GROUP
REMARK 600 OF C154. THE STARTING MATERIAL OF LIGAND 0F0 HAS A DOUBLE BOND
REMARK 600 BETWEEN C33 AND C32 ATOM GROUPS ((E)-3-(4-(DIMETHYLAMINO)BUT-2-
REMARK 600 ENAMIDO)-N-(4-((4-(PYRIDIN-3-YL)PYRIMIDIN-2- YL)AMI NO)PHENYL)
REMARK 600 BENZAMIDE ) AND UNDERGOES TO NUCLEOPHILIC ATTACK WITH RESIDUES C154.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0F0 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0F0 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V6R RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE CORRESPONDS TO ISOFORM 3 OF MITOGEN-ACTIVATED PROTEIN
REMARK 999 KINASE 10 UNP ENTRY P53779-3.
DBREF 3V6S A 39 402 UNP P53779 MK10_HUMAN 39 402
DBREF 3V6S B 39 402 UNP P53779 MK10_HUMAN 39 402
SEQRES 1 A 364 MET SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER VAL
SEQRES 2 A 364 GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 A 364 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 A 364 VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN VAL
SEQRES 5 A 364 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 A 364 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 A 364 CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN VAL
SEQRES 8 A 364 PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 A 364 TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES 10 A 364 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 A 364 LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES 12 A 364 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 A 364 ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES 14 A 364 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 A 364 THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 A 364 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE
SEQRES 17 A 364 TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG HIS
SEQRES 18 A 364 LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES 19 A 364 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 A 364 PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL
SEQRES 21 A 364 GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO LYS
SEQRES 22 A 364 LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 A 364 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 A 364 LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER VAL
SEQRES 25 A 364 ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 A 364 ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE TYR
SEQRES 27 A 364 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 A 364 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER GLU
SEQRES 1 B 364 MET SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER VAL
SEQRES 2 B 364 GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 B 364 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 B 364 VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN VAL
SEQRES 5 B 364 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 B 364 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 B 364 CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN VAL
SEQRES 8 B 364 PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 B 364 TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES 10 B 364 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 B 364 LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES 12 B 364 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 B 364 ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES 14 B 364 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 B 364 THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 B 364 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE
SEQRES 17 B 364 TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG HIS
SEQRES 18 B 364 LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES 19 B 364 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 B 364 PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL
SEQRES 21 B 364 GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO LYS
SEQRES 22 B 364 LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 B 364 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 B 364 LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER VAL
SEQRES 25 B 364 ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 B 364 ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE TYR
SEQRES 27 B 364 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 B 364 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER GLU
HET 0F0 A 501 37
HET 0F0 B 501 37
HETNAM 0F0 3-{[4-(DIMETHYLAMINO)BUTANOYL]AMINO}-N-(4-{[4-(PYRIDIN-
HETNAM 2 0F0 3-YL)PYRIMIDIN-2-YL]AMINO}PHENYL)BENZAMIDE
FORMUL 3 0F0 2(C28 H29 N7 O2)
FORMUL 5 HOH *215(H2 O)
HELIX 1 1 ASN A 101 VAL A 118 1 18
HELIX 2 2 LEU A 153 ILE A 157 1 5
HELIX 3 3 ASP A 162 ALA A 183 1 22
HELIX 4 4 LYS A 191 SER A 193 5 3
HELIX 5 5 ALA A 231 LEU A 236 1 6
HELIX 6 6 ASN A 243 HIS A 259 1 17
HELIX 7 7 ASP A 267 GLY A 280 1 14
HELIX 8 8 CYS A 283 LYS A 289 1 7
HELIX 9 9 GLN A 291 ARG A 301 1 11
HELIX 10 10 THR A 308 PHE A 313 1 6
HELIX 11 11 PRO A 314 PHE A 318 5 5
HELIX 12 12 GLU A 323 LEU A 340 1 18
HELIX 13 13 SER A 349 GLN A 355 1 7
HELIX 14 14 ILE A 359 TYR A 363 5 5
HELIX 15 15 ASP A 364 GLU A 369 1 6
HELIX 16 16 THR A 386 ASN A 400 1 15
HELIX 17 17 ASN B 101 VAL B 118 1 18
HELIX 18 19 ASP B 162 ALA B 183 1 22
HELIX 19 20 LYS B 191 SER B 193 5 3
HELIX 20 21 ALA B 231 LEU B 236 1 6
HELIX 21 22 ASN B 243 HIS B 259 1 17
HELIX 22 23 ASP B 267 GLY B 280 1 14
HELIX 23 24 CYS B 283 LYS B 289 1 7
HELIX 24 25 GLN B 291 ARG B 301 1 11
HELIX 25 26 THR B 308 PHE B 313 1 6
HELIX 26 27 PRO B 314 PHE B 318 5 5
HELIX 27 28 SER B 322 LEU B 340 1 19
HELIX 28 29 SER B 349 GLN B 355 1 7
HELIX 29 30 ILE B 359 TYR B 363 5 5
HELIX 30 31 ASP B 364 GLU B 369 1 6
HELIX 31 32 THR B 386 ASN B 400 1 15
SHEET 1 A 2 PHE A 48 VAL A 53 0
SHEET 2 A 2 SER A 56 LEU A 61 -1 O SER A 56 N VAL A 53
SHEET 1 B 5 TYR A 64 PRO A 69 0
SHEET 2 B 5 ILE A 77 ASP A 83 -1 O ALA A 80 N LYS A 68
SHEET 3 B 5 ARG A 88 LYS A 94 -1 O VAL A 90 N ALA A 81
SHEET 4 B 5 TYR A 143 GLU A 147 -1 O MET A 146 N ALA A 91
SHEET 5 B 5 LEU A 126 PHE A 130 -1 N ASN A 128 O VAL A 145
SHEET 1 C 3 ALA A 151 ASN A 152 0
SHEET 2 C 3 ILE A 195 VAL A 197 -1 O VAL A 197 N ALA A 151
SHEET 3 C 3 LEU A 203 ILE A 205 -1 O LYS A 204 N VAL A 196
SHEET 1 D 2 PHE B 48 VAL B 53 0
SHEET 2 D 2 SER B 56 LEU B 61 -1 O SER B 56 N VAL B 53
SHEET 1 E 5 TYR B 64 PRO B 69 0
SHEET 2 E 5 ILE B 77 ASP B 83 -1 O ALA B 80 N LYS B 68
SHEET 3 E 5 ARG B 88 SER B 96 -1 O VAL B 90 N ALA B 81
SHEET 4 E 5 ASP B 141 GLU B 147 -1 O VAL B 142 N LEU B 95
SHEET 5 E 5 LEU B 126 PHE B 130 -1 N ASN B 128 O VAL B 145
SHEET 1 F 3 ALA B 151 ASN B 152 0
SHEET 2 F 3 ILE B 195 VAL B 197 -1 O VAL B 197 N ALA B 151
SHEET 3 F 3 LEU B 203 ILE B 205 -1 O LYS B 204 N VAL B 196
LINK SG CYS B 154 C33 0F0 B 501 1555 1555 1.77
LINK SG CYS A 154 C33 0F0 A 501 1555 1555 1.78
CISPEP 1 GLN A 75 GLY A 76 0 1.15
CISPEP 2 ALA A 320 ASP A 321 0 -12.17
CISPEP 3 GLN A 379 LEU A 380 0 3.29
CISPEP 4 GLY B 73 ALA B 74 0 -2.25
CISPEP 5 ALA B 320 ASP B 321 0 7.87
CISPEP 6 GLN B 379 LEU B 380 0 0.67
SITE 1 AC1 16 GLY A 71 SER A 72 GLN A 75 VAL A 78
SITE 2 AC1 16 ALA A 91 GLU A 147 MET A 149 ASP A 150
SITE 3 AC1 16 ASN A 152 CYS A 154 GLN A 155 VAL A 196
SITE 4 AC1 16 LEU A 206 TYR A 229 ILE A 261 HOH A 613
SITE 1 AC2 14 ILE B 70 VAL B 78 ALA B 91 GLU B 147
SITE 2 AC2 14 MET B 149 ASP B 150 ASN B 152 CYS B 154
SITE 3 AC2 14 GLN B 155 VAL B 196 LEU B 206 TYR B 229
SITE 4 AC2 14 ILE B 261 HOH B 644
CRYST1 109.491 156.262 43.884 90.00 90.00 90.00 P 21 21 2 8
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 0.009133 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022787 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
