HEADER TRANSFERASE/TRANSFERASE INHIBITOR 10-FEB-16 5I3R
TITLE CRYSTAL STRUCTURE OF BMP-2-INDUCIBLE KINASE IN COMPLEX WITH AN
TITLE 2 INDAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BMP-2-INDUCIBLE PROTEIN KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BIKE;
COMPND 5 EC: 2.7.11.1;
COMPND 6 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: BMP2K, BIKE, HRIHFB2017;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS TRANSFERASE, PROTEIN KINASE DOMAIN, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.COUNAGO,F.J.SORRELL,T.KROJER,P.SAVITSKY,J.M.ELKINS,A.AXTMAN,
AUTHOR 2 D.DREWRY,C.WELLS,C.ZHANG,W.ZUERCHER,T.M.WILLSON,C.H.ARROWSMITH,
AUTHOR 3 A.M.EDWARDS,C.BOUNTRA,P.ARRUDA,O.GILEADI,STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (SGC)
REVDAT 5 27-SEP-23 5I3R 1 REMARK
REVDAT 4 01-JAN-20 5I3R 1 REMARK
REVDAT 3 17-APR-19 5I3R 1 REMARK
REVDAT 2 01-NOV-17 5I3R 1 REMARK
REVDAT 1 09-MAR-16 5I3R 0
JRNL AUTH R.M.COUNAGO,F.J.SORRELL,T.KROJER,J.M.ELKINS,O.GILEADI,
JRNL AUTH 2 T.M.WILLSON,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,P.ARRUDA
JRNL TITL CRYSTAL STRUCTURE OF BMP-2-INDUCIBLE KINASE IN COMPLEX WITH
JRNL TITL 2 AN INDAZOLE INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 32097
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830
REMARK 3 FREE R VALUE TEST SET COUNT : 1550
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.48
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2739
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.06
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 146
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4735
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.76310
REMARK 3 B22 (A**2) : -8.76310
REMARK 3 B33 (A**2) : 17.52630
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) : 0.320
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.305
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.221
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.284
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.218
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 : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4910 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6669 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2278 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 124 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 737 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4910 ; 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 : 641 ; 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 : 5590 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.26
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.90
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|42 - 62}
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0757 45.2341 31.4109
REMARK 3 T TENSOR
REMARK 3 T11: -0.0276 T22: 0.2124
REMARK 3 T33: -0.0946 T12: 0.0598
REMARK 3 T13: -0.0275 T23: 0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 5.3367 L22: 1.0144
REMARK 3 L33: 2.2256 L12: 1.7574
REMARK 3 L13: -0.1378 L23: 0.1632
REMARK 3 S TENSOR
REMARK 3 S11: 0.0406 S12: -0.0328 S13: 0.1113
REMARK 3 S21: 0.1130 S22: 0.0917 S23: -0.3290
REMARK 3 S31: -0.0832 S32: 0.3864 S33: -0.1322
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|63 - 85}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6648 47.7552 29.0241
REMARK 3 T TENSOR
REMARK 3 T11: -0.1782 T22: 0.1074
REMARK 3 T33: -0.1683 T12: 0.0204
REMARK 3 T13: -0.0572 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 2.1290 L22: 1.9813
REMARK 3 L33: 4.2335 L12: 1.8373
REMARK 3 L13: -1.0779 L23: 0.8648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: -0.1216 S13: -0.0644
REMARK 3 S21: 0.0972 S22: 0.0192 S23: -0.2534
REMARK 3 S31: 0.1368 S32: 0.4830 S33: -0.0374
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|86 - 131}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4587 54.5426 29.4174
REMARK 3 T TENSOR
REMARK 3 T11: -0.0336 T22: 0.0856
REMARK 3 T33: -0.0779 T12: -0.0317
REMARK 3 T13: 0.0409 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 2.3259 L22: 0.7858
REMARK 3 L33: 3.5043 L12: 0.3319
REMARK 3 L13: -0.2569 L23: -1.2905
REMARK 3 S TENSOR
REMARK 3 S11: 0.2049 S12: -0.3297 S13: 0.4011
REMARK 3 S21: 0.3175 S22: -0.1285 S23: 0.0450
REMARK 3 S31: -0.4711 S32: 0.3848 S33: -0.0764
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|132 - 151}
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4306 41.9003 8.3660
REMARK 3 T TENSOR
REMARK 3 T11: -0.1259 T22: 0.1124
REMARK 3 T33: -0.0435 T12: 0.1520
REMARK 3 T13: -0.0368 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.0231 L22: 4.5010
REMARK 3 L33: 0.0000 L12: -0.1353
REMARK 3 L13: -0.9525 L23: 0.1059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: 0.0867 S13: -0.1961
REMARK 3 S21: 0.1197 S22: 0.0000 S23: -0.2810
REMARK 3 S31: 0.2149 S32: 0.0645 S33: 0.0318
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|152 - 196}
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2235 49.5450 12.1232
REMARK 3 T TENSOR
REMARK 3 T11: -0.0533 T22: 0.0407
REMARK 3 T33: -0.0429 T12: 0.0284
REMARK 3 T13: 0.0006 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 1.7162 L22: 2.6427
REMARK 3 L33: 1.5825 L12: 0.9489
REMARK 3 L13: 0.5443 L23: 0.4448
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: -0.0195 S13: 0.2290
REMARK 3 S21: 0.1796 S22: 0.0296 S23: 0.1506
REMARK 3 S31: -0.0249 S32: -0.0758 S33: -0.0478
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|197 - 224}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5505 69.6074 16.9951
REMARK 3 T TENSOR
REMARK 3 T11: -0.0109 T22: -0.0625
REMARK 3 T33: 0.0809 T12: 0.0479
REMARK 3 T13: -0.0175 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.8526 L22: 2.4492
REMARK 3 L33: 0.4197 L12: 1.4777
REMARK 3 L13: -0.0268 L23: 0.4215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0604 S12: -0.2919 S13: 0.4683
REMARK 3 S21: 0.1340 S22: -0.0381 S23: 0.2892
REMARK 3 S31: -0.2715 S32: 0.0885 S33: 0.0985
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|225 - 343}
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4180 57.7681 0.4319
REMARK 3 T TENSOR
REMARK 3 T11: -0.0842 T22: -0.0218
REMARK 3 T33: -0.0403 T12: 0.0477
REMARK 3 T13: -0.0851 T23: 0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 2.1334 L22: 2.2470
REMARK 3 L33: 1.6001 L12: 1.1644
REMARK 3 L13: 0.1953 L23: 0.5097
REMARK 3 S TENSOR
REMARK 3 S11: -0.2481 S12: 0.3120 S13: 0.4235
REMARK 3 S21: -0.2381 S22: 0.0950 S23: 0.3874
REMARK 3 S31: -0.2563 S32: -0.0496 S33: 0.1532
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {B|42 - 85}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5688 68.4400 0.0669
REMARK 3 T TENSOR
REMARK 3 T11: 0.0044 T22: -0.0200
REMARK 3 T33: -0.0877 T12: -0.0701
REMARK 3 T13: -0.0811 T23: 0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 2.5811 L22: 1.0574
REMARK 3 L33: 1.8655 L12: 1.4527
REMARK 3 L13: -0.1911 L23: -1.3727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0617 S12: 0.2198 S13: -0.3909
REMARK 3 S21: -0.4145 S22: 0.2860 S23: 0.1304
REMARK 3 S31: 0.2216 S32: -0.4466 S33: -0.2243
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {B|86 - 102}
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9644 85.8479 1.6193
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.0021
REMARK 3 T33: -0.0210 T12: 0.1063
REMARK 3 T13: -0.0547 T23: 0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 1.8962 L22: 0.7565
REMARK 3 L33: 0.0000 L12: -0.7833
REMARK 3 L13: 0.4903 L23: -1.2185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0127 S12: -0.0409 S13: 0.1495
REMARK 3 S21: -0.1192 S22: 0.1748 S23: 0.1649
REMARK 3 S31: -0.1879 S32: -0.1413 S33: -0.1875
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {B|103 - 131}
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6674 77.4760 0.2666
REMARK 3 T TENSOR
REMARK 3 T11: 0.0334 T22: -0.0001
REMARK 3 T33: -0.0986 T12: -0.0293
REMARK 3 T13: -0.0370 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.4244 L22: 2.2277
REMARK 3 L33: 3.1527 L12: 0.9168
REMARK 3 L13: -1.7070 L23: 0.8595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: 0.3120 S13: 0.1278
REMARK 3 S21: -0.1740 S22: 0.1384 S23: 0.3473
REMARK 3 S31: -0.1286 S32: -0.3153 S33: -0.1261
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {B|132 - 151}
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8602 66.5903 22.7088
REMARK 3 T TENSOR
REMARK 3 T11: 0.0253 T22: 0.0260
REMARK 3 T33: -0.0948 T12: -0.0294
REMARK 3 T13: -0.0953 T23: 0.1032
REMARK 3 L TENSOR
REMARK 3 L11: 0.7312 L22: 0.0000
REMARK 3 L33: 0.4812 L12: -1.4210
REMARK 3 L13: 0.1274 L23: 2.6211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: -0.0499 S13: -0.2495
REMARK 3 S21: -0.0372 S22: 0.0346 S23: 0.1170
REMARK 3 S31: 0.0181 S32: -0.0862 S33: -0.0232
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {B|152 - 196}
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3587 81.0763 19.1351
REMARK 3 T TENSOR
REMARK 3 T11: 0.0591 T22: -0.0021
REMARK 3 T33: -0.1378 T12: 0.0370
REMARK 3 T13: 0.0113 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 1.3676 L22: 1.9349
REMARK 3 L33: 3.5320 L12: -1.0059
REMARK 3 L13: 2.4185 L23: -2.2428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: 0.0772 S13: 0.0769
REMARK 3 S21: -0.1007 S22: 0.0530 S23: -0.1286
REMARK 3 S31: -0.5436 S32: -0.1605 S33: -0.0299
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {B|197 - 224}
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3313 94.0676 12.7376
REMARK 3 T TENSOR
REMARK 3 T11: 0.1352 T22: 0.0855
REMARK 3 T33: -0.1769 T12: 0.1520
REMARK 3 T13: -0.0733 T23: 0.1060
REMARK 3 L TENSOR
REMARK 3 L11: 3.2531 L22: 0.6500
REMARK 3 L33: 0.0000 L12: -0.3924
REMARK 3 L13: 0.6714 L23: -1.5615
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.1077 S13: 0.2114
REMARK 3 S21: -0.1300 S22: -0.0419 S23: 0.0646
REMARK 3 S31: -0.2806 S32: -0.2104 S33: 0.0831
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {B|225 - 261}
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4409 89.0807 24.6535
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: -0.0349
REMARK 3 T33: -0.0903 T12: 0.1520
REMARK 3 T13: -0.0265 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.9983 L22: 0.0000
REMARK 3 L33: 1.3118 L12: 1.3961
REMARK 3 L13: -0.2089 L23: -0.8671
REMARK 3 S TENSOR
REMARK 3 S11: -0.0532 S12: 0.0415 S13: 0.2526
REMARK 3 S21: -0.0295 S22: 0.0782 S23: 0.2559
REMARK 3 S31: -0.2944 S32: -0.3152 S33: -0.0250
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {B|262 - 343}
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0650 87.3155 32.8430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0822 T22: -0.0774
REMARK 3 T33: -0.1540 T12: 0.0813
REMARK 3 T13: -0.0019 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 2.5276 L22: 1.7455
REMARK 3 L33: 3.3402 L12: 0.1464
REMARK 3 L13: 0.1573 L23: -0.3488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: -0.3300 S13: 0.3967
REMARK 3 S21: 0.1603 S22: 0.0569 S23: 0.2618
REMARK 3 S31: -0.5442 S32: -0.4394 S33: 0.0152
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5I3R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 0.976250
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32194
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4W9W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000; 0.2 M AMMONIUM CHLORIDE;
REMARK 280 10% ETHYLENEGLYCOL; 0.1M MES PH 6.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 127.61050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.21650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.21650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 191.41575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.21650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.21650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 63.80525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.21650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.21650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 191.41575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.21650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.21650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.80525
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 127.61050
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 300 REMARK: MONOMER ACCORDING TO GEL FILTRATION
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 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 PHE A 62 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 118 OG
REMARK 470 ILE A 119 CG1 CG2 CD1
REMARK 470 SER A 120 OG
REMARK 470 ASP A 121 CG OD1 OD2
REMARK 470 ASN A 122 CG OD1 ND2
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS B 173 CG CD CE NZ
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 54 -60.34 -101.28
REMARK 500 PHE A 62 -60.94 80.61
REMARK 500 ASN A 122 -6.88 67.54
REMARK 500 ASP A 180 49.41 -148.24
REMARK 500 THR A 244 -168.32 -115.96
REMARK 500 ASN A 283 33.02 -94.10
REMARK 500 GLU B 54 -61.12 -103.48
REMARK 500 PHE B 62 -29.51 75.49
REMARK 500 ASN B 122 -6.03 66.66
REMARK 500 ASP B 180 49.68 -147.02
REMARK 500 THR B 244 -166.79 -116.06
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 612 DISTANCE = 9.96 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IDK A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IDK B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I3O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BMP-2-INDUCIBLE KINASE IN COMPLEX WITH AN
REMARK 900 INDAZOLE INHIBITOR
REMARK 900 RELATED ID: 4W9W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BMP-2-INDUCIBLE KINASE IN COMPLEX WITH SMALL
REMARK 900 MOLECULE AZD-7762
REMARK 900 RELATED ID: 4W9X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BMP-2-INDUCIBLE KINASE IN COMPLEX WITH
REMARK 900 BARICITINIB
DBREF 5I3R A 42 343 UNP Q9NSY1 BMP2K_HUMAN 42 343
DBREF 5I3R B 42 343 UNP Q9NSY1 BMP2K_HUMAN 42 343
SEQADV 5I3R ALA A 320 UNP Q9NSY1 LYS 320 ENGINEERED MUTATION
SEQADV 5I3R ALA A 321 UNP Q9NSY1 LYS 321 ENGINEERED MUTATION
SEQADV 5I3R ALA B 320 UNP Q9NSY1 LYS 320 ENGINEERED MUTATION
SEQADV 5I3R ALA B 321 UNP Q9NSY1 LYS 321 ENGINEERED MUTATION
SEQRES 1 A 302 ARG VAL PHE ALA VAL GLY ARG HIS GLN VAL THR LEU GLU
SEQRES 2 A 302 GLU SER LEU ALA GLU GLY GLY PHE SER THR VAL PHE LEU
SEQRES 3 A 302 VAL ARG THR HIS GLY GLY ILE ARG CYS ALA LEU LYS ARG
SEQRES 4 A 302 MET TYR VAL ASN ASN MET PRO ASP LEU ASN VAL CYS LYS
SEQRES 5 A 302 ARG GLU ILE THR ILE MET LYS GLU LEU SER GLY HIS LYS
SEQRES 6 A 302 ASN ILE VAL GLY TYR LEU ASP CYS ALA VAL ASN SER ILE
SEQRES 7 A 302 SER ASP ASN VAL TRP GLU VAL LEU ILE LEU MET GLU TYR
SEQRES 8 A 302 CYS ARG ALA GLY GLN VAL VAL ASN GLN MET ASN LYS LYS
SEQRES 9 A 302 LEU GLN THR GLY PHE THR GLU PRO GLU VAL LEU GLN ILE
SEQRES 10 A 302 PHE CYS ASP THR CYS GLU ALA VAL ALA ARG LEU HIS GLN
SEQRES 11 A 302 CYS LYS THR PRO ILE ILE HIS ARG ASP LEU LYS VAL GLU
SEQRES 12 A 302 ASN ILE LEU LEU ASN ASP GLY GLY ASN TYR VAL LEU CYS
SEQRES 13 A 302 ASP PHE GLY SER ALA THR ASN LYS PHE LEU ASN PRO GLN
SEQRES 14 A 302 LYS ASP GLY VAL ASN VAL VAL GLU GLU GLU ILE LYS LYS
SEQRES 15 A 302 TYR THR THR LEU SER TYR ARG ALA PRO GLU MET ILE ASN
SEQRES 16 A 302 LEU TYR GLY GLY LYS PRO ILE THR THR LYS ALA ASP ILE
SEQRES 17 A 302 TRP ALA LEU GLY CYS LEU LEU TYR LYS LEU CYS PHE PHE
SEQRES 18 A 302 THR LEU PRO PHE GLY GLU SER GLN VAL ALA ILE CYS ASP
SEQRES 19 A 302 GLY ASN PHE THR ILE PRO ASP ASN SER ARG TYR SER ARG
SEQRES 20 A 302 ASN ILE HIS CYS LEU ILE ARG PHE MET LEU GLU PRO ASP
SEQRES 21 A 302 PRO GLU HIS ARG PRO ASP ILE PHE GLN VAL SER TYR PHE
SEQRES 22 A 302 ALA PHE LYS PHE ALA ALA ALA ASP CYS PRO VAL SER ASN
SEQRES 23 A 302 ILE ASN ASN SER SER ILE PRO SER ALA LEU PRO GLU PRO
SEQRES 24 A 302 MET THR ALA
SEQRES 1 B 302 ARG VAL PHE ALA VAL GLY ARG HIS GLN VAL THR LEU GLU
SEQRES 2 B 302 GLU SER LEU ALA GLU GLY GLY PHE SER THR VAL PHE LEU
SEQRES 3 B 302 VAL ARG THR HIS GLY GLY ILE ARG CYS ALA LEU LYS ARG
SEQRES 4 B 302 MET TYR VAL ASN ASN MET PRO ASP LEU ASN VAL CYS LYS
SEQRES 5 B 302 ARG GLU ILE THR ILE MET LYS GLU LEU SER GLY HIS LYS
SEQRES 6 B 302 ASN ILE VAL GLY TYR LEU ASP CYS ALA VAL ASN SER ILE
SEQRES 7 B 302 SER ASP ASN VAL TRP GLU VAL LEU ILE LEU MET GLU TYR
SEQRES 8 B 302 CYS ARG ALA GLY GLN VAL VAL ASN GLN MET ASN LYS LYS
SEQRES 9 B 302 LEU GLN THR GLY PHE THR GLU PRO GLU VAL LEU GLN ILE
SEQRES 10 B 302 PHE CYS ASP THR CYS GLU ALA VAL ALA ARG LEU HIS GLN
SEQRES 11 B 302 CYS LYS THR PRO ILE ILE HIS ARG ASP LEU LYS VAL GLU
SEQRES 12 B 302 ASN ILE LEU LEU ASN ASP GLY GLY ASN TYR VAL LEU CYS
SEQRES 13 B 302 ASP PHE GLY SER ALA THR ASN LYS PHE LEU ASN PRO GLN
SEQRES 14 B 302 LYS ASP GLY VAL ASN VAL VAL GLU GLU GLU ILE LYS LYS
SEQRES 15 B 302 TYR THR THR LEU SER TYR ARG ALA PRO GLU MET ILE ASN
SEQRES 16 B 302 LEU TYR GLY GLY LYS PRO ILE THR THR LYS ALA ASP ILE
SEQRES 17 B 302 TRP ALA LEU GLY CYS LEU LEU TYR LYS LEU CYS PHE PHE
SEQRES 18 B 302 THR LEU PRO PHE GLY GLU SER GLN VAL ALA ILE CYS ASP
SEQRES 19 B 302 GLY ASN PHE THR ILE PRO ASP ASN SER ARG TYR SER ARG
SEQRES 20 B 302 ASN ILE HIS CYS LEU ILE ARG PHE MET LEU GLU PRO ASP
SEQRES 21 B 302 PRO GLU HIS ARG PRO ASP ILE PHE GLN VAL SER TYR PHE
SEQRES 22 B 302 ALA PHE LYS PHE ALA ALA ALA ASP CYS PRO VAL SER ASN
SEQRES 23 B 302 ILE ASN ASN SER SER ILE PRO SER ALA LEU PRO GLU PRO
SEQRES 24 B 302 MET THR ALA
HET IDK A 401 29
HET PO4 A 402 5
HET IDK B 401 29
HET PO4 B 402 5
HETNAM IDK N-[6-(3-{[(CYCLOPROPYLMETHYL)SULFONYL]AMINO}PHENYL)-1H-
HETNAM 2 IDK INDAZOL-3-YL]CYCLOPROPANECARBOXAMIDE
HETNAM PO4 PHOSPHATE ION
FORMUL 3 IDK 2(C21 H22 N4 O3 S)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 7 HOH *192(H2 O)
HELIX 1 AA1 ASN A 85 SER A 103 1 19
HELIX 2 AA2 GLN A 137 LYS A 144 1 8
HELIX 3 AA3 THR A 151 GLN A 171 1 21
HELIX 4 AA4 LYS A 182 GLU A 184 5 3
HELIX 5 AA5 ASN A 208 GLY A 213 1 6
HELIX 6 AA6 GLY A 213 THR A 225 1 13
HELIX 7 AA7 THR A 226 ARG A 230 5 5
HELIX 8 AA8 ALA A 231 ASN A 236 1 6
HELIX 9 AA9 THR A 245 PHE A 262 1 18
HELIX 10 AB1 SER A 269 GLY A 276 1 8
HELIX 11 AB2 SER A 287 LEU A 298 1 12
HELIX 12 AB3 ASP A 307 ALA A 320 1 14
HELIX 13 AB4 ASN B 85 SER B 103 1 19
HELIX 14 AB5 GLN B 137 LYS B 145 1 9
HELIX 15 AB6 THR B 151 GLN B 171 1 21
HELIX 16 AB7 LYS B 182 GLU B 184 5 3
HELIX 17 AB8 ASN B 208 GLY B 213 1 6
HELIX 18 AB9 GLY B 213 THR B 225 1 13
HELIX 19 AC1 THR B 226 ARG B 230 5 5
HELIX 20 AC2 ALA B 231 ILE B 235 5 5
HELIX 21 AC3 THR B 245 PHE B 262 1 18
HELIX 22 AC4 SER B 269 GLY B 276 1 8
HELIX 23 AC5 SER B 287 LEU B 298 1 12
HELIX 24 AC6 ASP B 307 ALA B 320 1 14
SHEET 1 AA1 6 VAL A 43 VAL A 46 0
SHEET 2 AA1 6 HIS A 49 GLU A 59 -1 O VAL A 51 N PHE A 44
SHEET 3 AA1 6 SER A 63 THR A 70 -1 O LEU A 67 N GLU A 55
SHEET 4 AA1 6 ARG A 75 VAL A 83 -1 O ARG A 80 N THR A 64
SHEET 5 AA1 6 TRP A 124 GLU A 131 -1 O VAL A 126 N MET A 81
SHEET 6 AA1 6 TYR A 111 SER A 118 -1 N ASP A 113 O LEU A 129
SHEET 1 AA2 2 ILE A 186 LEU A 188 0
SHEET 2 AA2 2 TYR A 194 LEU A 196 -1 O VAL A 195 N LEU A 187
SHEET 1 AA3 2 THR A 279 ILE A 280 0
SHEET 2 AA3 2 MET A 341 THR A 342 1 O MET A 341 N ILE A 280
SHEET 1 AA4 6 VAL B 43 VAL B 46 0
SHEET 2 AA4 6 HIS B 49 GLU B 59 -1 O VAL B 51 N PHE B 44
SHEET 3 AA4 6 SER B 63 THR B 70 -1 O LEU B 67 N GLU B 55
SHEET 4 AA4 6 ARG B 75 VAL B 83 -1 O ARG B 80 N THR B 64
SHEET 5 AA4 6 TRP B 124 GLU B 131 -1 O MET B 130 N ALA B 77
SHEET 6 AA4 6 TYR B 111 SER B 118 -1 N ASP B 113 O LEU B 129
SHEET 1 AA5 2 ILE B 186 LEU B 188 0
SHEET 2 AA5 2 TYR B 194 LEU B 196 -1 O VAL B 195 N LEU B 187
SHEET 1 AA6 2 THR B 279 ILE B 280 0
SHEET 2 AA6 2 MET B 341 THR B 342 1 O MET B 341 N ILE B 280
CISPEP 1 GLY A 61 PHE A 62 0 0.28
CISPEP 2 GLY B 61 PHE B 62 0 -0.86
SITE 1 AC1 16 GLY A 60 SER A 63 VAL A 65 ALA A 77
SITE 2 AC1 16 MET A 130 GLU A 131 TYR A 132 CYS A 133
SITE 3 AC1 16 ARG A 134 GLY A 136 GLN A 137 GLU A 184
SITE 4 AC1 16 ASN A 185 CYS A 197 ASP A 198 HOH A 519
SITE 1 AC2 6 ALA A 321 ASP A 322 HOH A 526 HIS B 49
SITE 2 AC2 6 GLN B 50 THR B 70
SITE 1 AC3 18 LEU B 57 ALA B 58 GLU B 59 SER B 63
SITE 2 AC3 18 VAL B 65 ALA B 77 MET B 130 GLU B 131
SITE 3 AC3 18 TYR B 132 CYS B 133 ARG B 134 GLY B 136
SITE 4 AC3 18 GLN B 137 GLU B 184 ASN B 185 LEU B 187
SITE 5 AC3 18 CYS B 197 ASP B 198
SITE 1 AC4 5 HIS A 49 GLN A 50 THR A 70 ALA B 321
SITE 2 AC4 5 ASP B 322
CRYST1 78.433 78.433 255.221 90.00 90.00 90.00 P 43 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012750 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012750 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003918 0.00000
(ATOM LINES ARE NOT SHOWN.)
END