HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-MAR-17 5VAL
TITLE BRAF IN COMPLEX WITH N-(3-(TERT-BUTYL)PHENYL)-4-METHYL-3-(6-
TITLE 2 MORPHOLINOPYRIMIDIN-4-YL)BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 445-723;
COMPND 5 SYNONYM: PROTO-ONCOGENE B-RAF,P94,V-RAF MURINE SARCOMA VIRAL ONCOGENE
COMPND 6 HOMOLOG B1;
COMPND 7 EC: 2.7.11.1;
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: BRAF, BRAF1, RAFB1;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS BRAF SERINE/THREONINE-PROTEIN KINASE B-RAF, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAMO,B.A.APPLETON
REVDAT 3 06-MAR-24 5VAL 1 REMARK
REVDAT 2 05-JUL-17 5VAL 1 JRNL
REVDAT 1 28-JUN-17 5VAL 0
JRNL AUTH G.A.NISHIGUCHI,A.RICO,H.TANNER,R.J.AVERSA,B.R.TAFT,
JRNL AUTH 2 S.SUBRAMANIAN,L.SETTI,M.T.BURGER,L.WAN,V.TAMEZ,A.SMITH,
JRNL AUTH 3 Y.LOU,P.A.BARSANTI,B.A.APPLETON,M.MAMO,L.TANDESKE,I.DIX,
JRNL AUTH 4 J.E.TELLEW,S.HUANG,L.A.MATHEWS GRINER,V.G.COOKE,
JRNL AUTH 5 A.VAN ABBEMA,H.MERRITT,S.MA,K.GAMPA,F.FENG,J.YUAN,Y.WANG,
JRNL AUTH 6 J.R.HALING,S.VAZIRI,M.HEKMAT-NEJAD,J.M.JANSEN,V.POLYAKOV,
JRNL AUTH 7 R.ZANG,V.SETHURAMAN,P.AMIRI,M.SINGH,E.LEES,W.SHAO,
JRNL AUTH 8 D.D.STUART,M.P.DILLON,S.RAMURTHY
JRNL TITL DESIGN AND DISCOVERY OF
JRNL TITL 2 N-(2-METHYL-5'-MORPHOLINO-6'-((TETRAHYDRO-2H-PYRAN-4-YL)OXY)
JRNL TITL 3 -[3,3'-BIPYRIDIN]-5-YL)-3-(TRIFLUOROMETHYL)BENZAMIDE
JRNL TITL 4 (RAF709): A POTENT, SELECTIVE, AND EFFICACIOUS RAF INHIBITOR
JRNL TITL 5 TARGETING RAS MUTANT CANCERS.
JRNL REF J. MED. CHEM. V. 60 4869 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28557458
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01862
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 33658
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1724
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3013
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1980
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2847
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE : 0.2320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.51
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
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 : 4035
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.48410
REMARK 3 B22 (A**2) : -1.48410
REMARK 3 B33 (A**2) : 2.96810
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) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.230
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.183
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.215
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.179
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 : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4191 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5664 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1462 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 91 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 645 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4191 ; 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 : 538 ; 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 : 4990 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.25
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.62
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|449 - A|491 }
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1134 46.4119 -15.6343
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: -0.0423
REMARK 3 T33: -0.0463 T12: -0.0094
REMARK 3 T13: -0.0352 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 3.2000 L22: 0.6060
REMARK 3 L33: 1.4462 L12: 0.7447
REMARK 3 L13: -0.0129 L23: 1.2253
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: 0.3005 S13: 0.1000
REMARK 3 S21: -0.1847 S22: -0.0823 S23: 0.2366
REMARK 3 S31: -0.2341 S32: -0.0825 S33: 0.1503
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|492 - A|507 }
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4085 53.5913 -4.7506
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: -0.0960
REMARK 3 T33: -0.0406 T12: -0.0492
REMARK 3 T13: 0.0327 T23: -0.0777
REMARK 3 L TENSOR
REMARK 3 L11: 0.9056 L22: 1.7940
REMARK 3 L33: 0.4913 L12: 1.7532
REMARK 3 L13: 0.3580 L23: 0.0958
REMARK 3 S TENSOR
REMARK 3 S11: -0.0273 S12: -0.2106 S13: 0.2869
REMARK 3 S21: -0.0442 S22: -0.0874 S23: 0.0669
REMARK 3 S31: -0.3766 S32: -0.0074 S33: 0.1147
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|508 - A|596 }
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2844 37.7841 -0.2292
REMARK 3 T TENSOR
REMARK 3 T11: -0.0811 T22: -0.0574
REMARK 3 T33: 0.0095 T12: -0.0071
REMARK 3 T13: 0.0285 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.2473 L22: 1.0105
REMARK 3 L33: 2.3378 L12: -0.3882
REMARK 3 L13: -1.6861 L23: 0.3910
REMARK 3 S TENSOR
REMARK 3 S11: -0.3169 S12: 0.1229 S13: -0.2222
REMARK 3 S21: -0.0007 S22: 0.1136 S23: 0.2752
REMARK 3 S31: 0.1798 S32: -0.1338 S33: 0.2033
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|616 - A|621 }
REMARK 3 ORIGIN FOR THE GROUP (A): -35.3782 48.6803 8.7661
REMARK 3 T TENSOR
REMARK 3 T11: -0.0357 T22: -0.0386
REMARK 3 T33: 0.0283 T12: 0.0523
REMARK 3 T13: 0.0837 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.7677 L22: 0.0000
REMARK 3 L33: 0.0737 L12: -0.1569
REMARK 3 L13: -0.0366 L23: -0.2087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: 0.0693 S13: 0.1499
REMARK 3 S21: 0.0192 S22: -0.0136 S23: 0.0092
REMARK 3 S31: -0.0246 S32: -0.0395 S33: 0.0240
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|622 - A|706 }
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6931 44.6616 15.7746
REMARK 3 T TENSOR
REMARK 3 T11: -0.0322 T22: -0.0527
REMARK 3 T33: -0.0372 T12: 0.0467
REMARK 3 T13: 0.0916 T23: 0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 4.6364 L22: 0.8809
REMARK 3 L33: 1.1428 L12: -2.2682
REMARK 3 L13: -2.3690 L23: 0.8001
REMARK 3 S TENSOR
REMARK 3 S11: -0.3395 S12: -0.3573 S13: -0.2406
REMARK 3 S21: 0.2860 S22: 0.1614 S23: 0.2510
REMARK 3 S31: 0.1501 S32: 0.1194 S33: 0.1781
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { A|707 - A|720 }
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8784 30.1223 17.4999
REMARK 3 T TENSOR
REMARK 3 T11: 0.0576 T22: -0.0032
REMARK 3 T33: -0.0622 T12: 0.1520
REMARK 3 T13: 0.1520 T23: 0.0863
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0855
REMARK 3 L33: 0.0059 L12: -2.8907
REMARK 3 L13: 0.7159 L23: -2.1701
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: -0.0656 S13: -0.3042
REMARK 3 S21: 0.1399 S22: 0.0357 S23: -0.0490
REMARK 3 S31: 0.1721 S32: -0.0145 S33: -0.0044
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { B|449 - B|475 }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5940 27.3071 7.6008
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.0032
REMARK 3 T33: -0.0709 T12: 0.1127
REMARK 3 T13: 0.0320 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 1.8554 L22: 1.5229
REMARK 3 L33: 1.1393 L12: -0.5429
REMARK 3 L13: 1.0333 L23: 1.1265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0285 S12: -0.3218 S13: -0.2885
REMARK 3 S21: 0.0736 S22: -0.0631 S23: -0.0608
REMARK 3 S31: 0.3614 S32: 0.4617 S33: 0.0915
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { B|476 - B|491 }
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6966 28.1008 7.8549
REMARK 3 T TENSOR
REMARK 3 T11: -0.0596 T22: 0.0480
REMARK 3 T33: -0.0566 T12: 0.0745
REMARK 3 T13: -0.0177 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.1731 L22: 1.4073
REMARK 3 L33: 1.9209 L12: -0.7726
REMARK 3 L13: -0.5571 L23: -1.6874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: -0.0522 S13: -0.0559
REMARK 3 S21: 0.3347 S22: -0.1658 S23: -0.0142
REMARK 3 S31: 0.2648 S32: 0.4049 S33: 0.1635
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { B|492 - B|507 }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2919 33.0595 -2.4333
REMARK 3 T TENSOR
REMARK 3 T11: -0.0924 T22: 0.2191
REMARK 3 T33: -0.1516 T12: 0.0160
REMARK 3 T13: 0.0455 T23: -0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.6703 L22: 1.4749
REMARK 3 L33: 0.2887 L12: 2.2094
REMARK 3 L13: 0.7654 L23: -1.5236
REMARK 3 S TENSOR
REMARK 3 S11: -0.0235 S12: -0.1151 S13: 0.0456
REMARK 3 S21: -0.1495 S22: -0.0228 S23: -0.1474
REMARK 3 S31: 0.1197 S32: 0.4161 S33: 0.0462
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { B|508 - B|587 }
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3291 23.2064 -8.4778
REMARK 3 T TENSOR
REMARK 3 T11: -0.0487 T22: -0.0393
REMARK 3 T33: 0.0024 T12: 0.0068
REMARK 3 T13: 0.0567 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.9497 L22: 1.7538
REMARK 3 L33: 1.6948 L12: -0.0140
REMARK 3 L13: -0.4652 L23: 1.0694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0494 S12: -0.0403 S13: -0.1962
REMARK 3 S21: 0.0911 S22: -0.0534 S23: 0.0965
REMARK 3 S31: 0.1627 S32: -0.0443 S33: 0.1028
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { B|588 - B|597 }
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4342 21.9451 -7.0397
REMARK 3 T TENSOR
REMARK 3 T11: 0.0096 T22: -0.0532
REMARK 3 T33: -0.0021 T12: 0.0203
REMARK 3 T13: 0.0249 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 3.4476
REMARK 3 L33: 3.2034 L12: 0.8015
REMARK 3 L13: 0.1967 L23: 0.3451
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0266 S13: -0.0428
REMARK 3 S21: 0.2426 S22: 0.0655 S23: -0.0306
REMARK 3 S31: 0.2554 S32: 0.0062 S33: -0.0684
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { B|615 - B|706 }
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1775 13.4001 -23.6134
REMARK 3 T TENSOR
REMARK 3 T11: -0.0587 T22: -0.0176
REMARK 3 T33: -0.0329 T12: -0.0127
REMARK 3 T13: 0.0362 T23: -0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 1.6839 L22: 3.8467
REMARK 3 L33: 0.8724 L12: -1.9292
REMARK 3 L13: -0.4514 L23: 0.9787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: 0.1039 S13: -0.1582
REMARK 3 S21: -0.1454 S22: -0.1149 S23: 0.1275
REMARK 3 S31: -0.0098 S32: -0.0871 S33: 0.0797
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { B|707 - B|721 }
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5210 25.1103 -26.5782
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: -0.0274
REMARK 3 T33: -0.0413 T12: 0.0421
REMARK 3 T13: -0.0169 T23: -0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 0.5493 L22: 0.0000
REMARK 3 L33: 2.1638 L12: -2.5406
REMARK 3 L13: 2.4816 L23: -2.2724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: 0.1250 S13: 0.0400
REMARK 3 S21: -0.0616 S22: 0.0384 S23: 0.3077
REMARK 3 S31: -0.1095 S32: -0.0876 S33: -0.0499
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { A|801 - A|801 }
REMARK 3 ORIGIN FOR THE GROUP (A): -23.0911 43.6048 -5.0350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0468 T22: -0.0161
REMARK 3 T33: -0.0269 T12: -0.0253
REMARK 3 T13: -0.0147 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.1427 L22: 0.7216
REMARK 3 L33: 0.3734 L12: -1.1638
REMARK 3 L13: 0.4453 L23: -0.4784
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: -0.0248 S13: -0.0301
REMARK 3 S21: -0.0245 S22: 0.0229 S23: 0.0359
REMARK 3 S31: 0.0080 S32: -0.0179 S33: -0.0317
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { B|801 - B|801 }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6952 25.0539 -3.1275
REMARK 3 T TENSOR
REMARK 3 T11: 0.0102 T22: -0.0082
REMARK 3 T33: -0.0007 T12: 0.0286
REMARK 3 T13: -0.0207 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.7819 L22: 0.7306
REMARK 3 L33: 0.5875 L12: -1.1526
REMARK 3 L13: 0.9887 L23: -0.2205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0139 S13: -0.0638
REMARK 3 S21: -0.0224 S22: 0.0731 S23: 0.0024
REMARK 3 S31: -0.0021 S32: 0.0556 S33: -0.0664
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227112.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33857
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 47.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.90
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.4, 12% PEG8000, AND
REMARK 280 100MM NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 81.76850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.06050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.06050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.88425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.06050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.06050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 122.65275
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.06050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.06050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.88425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.06050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.06050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 122.65275
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 81.76850
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A 443
REMARK 465 SER A 444
REMARK 465 ASP A 445
REMARK 465 LEU A 597
REMARK 465 ALA A 598
REMARK 465 THR A 599
REMARK 465 VAL A 600
REMARK 465 LYS A 601
REMARK 465 SER A 602
REMARK 465 ARG A 603
REMARK 465 TRP A 604
REMARK 465 SER A 605
REMARK 465 GLY A 606
REMARK 465 SER A 607
REMARK 465 HIS A 608
REMARK 465 GLN A 609
REMARK 465 PHE A 610
REMARK 465 GLU A 611
REMARK 465 GLN A 612
REMARK 465 LEU A 613
REMARK 465 SER A 614
REMARK 465 GLY A 615
REMARK 465 GLN A 628
REMARK 465 ASP A 629
REMARK 465 LEU A 721
REMARK 465 PRO A 722
REMARK 465 LYS A 723
REMARK 465 GLY B 443
REMARK 465 SER B 444
REMARK 465 ASP B 445
REMARK 465 SER B 446
REMARK 465 SER B 447
REMARK 465 ALA B 598
REMARK 465 THR B 599
REMARK 465 VAL B 600
REMARK 465 LYS B 601
REMARK 465 SER B 602
REMARK 465 ARG B 603
REMARK 465 TRP B 604
REMARK 465 SER B 605
REMARK 465 GLY B 606
REMARK 465 SER B 607
REMARK 465 HIS B 608
REMARK 465 GLN B 609
REMARK 465 PHE B 610
REMARK 465 GLU B 611
REMARK 465 GLN B 612
REMARK 465 LEU B 613
REMARK 465 SER B 614
REMARK 465 GLN B 628
REMARK 465 ASP B 629
REMARK 465 LYS B 630
REMARK 465 PRO B 722
REMARK 465 LYS B 723
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 449 CG OD1 OD2
REMARK 470 MET A 627 CG SD CE
REMARK 470 LYS A 630 CG CD CE NZ
REMARK 470 LYS A 687 CG CD CE NZ
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 ASN B 631 CG OD1 ND2
REMARK 470 LYS B 687 CG CD CE NZ
REMARK 470 ARG B 691 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 467 -109.84 45.30
REMARK 500 TRP A 476 93.09 -173.60
REMARK 500 ARG A 575 -12.33 80.65
REMARK 500 ASP A 576 39.29 -147.67
REMARK 500 LEU A 588 -57.26 -131.26
REMARK 500 ARG A 682 152.53 -48.00
REMARK 500 TRP B 476 93.33 -173.66
REMARK 500 ARG B 575 -12.76 81.08
REMARK 500 ASP B 576 40.00 -148.12
REMARK 500 LEU B 588 -57.37 -131.02
REMARK 500 ARG B 682 152.55 -48.48
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 92D A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 92D B 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VAM RELATED DB: PDB
DBREF 5VAL A 445 723 UNP P15056 BRAF_HUMAN 445 723
DBREF 5VAL B 445 723 UNP P15056 BRAF_HUMAN 445 723
SEQADV 5VAL GLY A 443 UNP P15056 EXPRESSION TAG
SEQADV 5VAL SER A 444 UNP P15056 EXPRESSION TAG
SEQADV 5VAL GLY B 443 UNP P15056 EXPRESSION TAG
SEQADV 5VAL SER B 444 UNP P15056 EXPRESSION TAG
SEQRES 1 A 281 GLY SER ASP SER SER ASP ASP TRP GLU ILE PRO ASP GLY
SEQRES 2 A 281 GLN ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE
SEQRES 3 A 281 GLY THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA
SEQRES 4 A 281 VAL LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN
SEQRES 5 A 281 LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS
SEQRES 6 A 281 THR ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER
SEQRES 7 A 281 THR LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU
SEQRES 8 A 281 GLY SER SER LEU TYR HIS HIS LEU HIS ILE ILE GLU THR
SEQRES 9 A 281 LYS PHE GLU MET ILE LYS LEU ILE ASP ILE ALA ARG GLN
SEQRES 10 A 281 THR ALA GLN GLY MET ASP TYR LEU HIS ALA LYS SER ILE
SEQRES 11 A 281 ILE HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS
SEQRES 12 A 281 GLU ASP LEU THR VAL LYS ILE GLY ASP PHE GLY LEU ALA
SEQRES 13 A 281 THR VAL LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU
SEQRES 14 A 281 GLN LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL
SEQRES 15 A 281 ILE ARG MET GLN ASP LYS ASN PRO TYR SER PHE GLN SER
SEQRES 16 A 281 ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET
SEQRES 17 A 281 THR GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP
SEQRES 18 A 281 GLN ILE ILE PHE MET VAL GLY ARG GLY TYR LEU SER PRO
SEQRES 19 A 281 ASP LEU SER LYS VAL ARG SER ASN CYS PRO LYS ALA MET
SEQRES 20 A 281 LYS ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP
SEQRES 21 A 281 GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA SER ILE GLU
SEQRES 22 A 281 LEU LEU ALA ARG SER LEU PRO LYS
SEQRES 1 B 281 GLY SER ASP SER SER ASP ASP TRP GLU ILE PRO ASP GLY
SEQRES 2 B 281 GLN ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE
SEQRES 3 B 281 GLY THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA
SEQRES 4 B 281 VAL LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN
SEQRES 5 B 281 LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS
SEQRES 6 B 281 THR ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER
SEQRES 7 B 281 THR LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU
SEQRES 8 B 281 GLY SER SER LEU TYR HIS HIS LEU HIS ILE ILE GLU THR
SEQRES 9 B 281 LYS PHE GLU MET ILE LYS LEU ILE ASP ILE ALA ARG GLN
SEQRES 10 B 281 THR ALA GLN GLY MET ASP TYR LEU HIS ALA LYS SER ILE
SEQRES 11 B 281 ILE HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS
SEQRES 12 B 281 GLU ASP LEU THR VAL LYS ILE GLY ASP PHE GLY LEU ALA
SEQRES 13 B 281 THR VAL LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU
SEQRES 14 B 281 GLN LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL
SEQRES 15 B 281 ILE ARG MET GLN ASP LYS ASN PRO TYR SER PHE GLN SER
SEQRES 16 B 281 ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET
SEQRES 17 B 281 THR GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP
SEQRES 18 B 281 GLN ILE ILE PHE MET VAL GLY ARG GLY TYR LEU SER PRO
SEQRES 19 B 281 ASP LEU SER LYS VAL ARG SER ASN CYS PRO LYS ALA MET
SEQRES 20 B 281 LYS ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP
SEQRES 21 B 281 GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA SER ILE GLU
SEQRES 22 B 281 LEU LEU ALA ARG SER LEU PRO LYS
HET 92D A 801 32
HET 92D B 801 32
HETNAM 92D N-(3-TERT-BUTYLPHENYL)-4-METHYL-3-[6-(MORPHOLIN-4-YL)
HETNAM 2 92D PYRIMIDIN-4-YL]BENZAMIDE
FORMUL 3 92D 2(C26 H30 N4 O2)
FORMUL 5 HOH *272(H2 O)
HELIX 1 AA1 THR A 491 ARG A 506 1 16
HELIX 2 AA2 LEU A 537 ILE A 543 1 7
HELIX 3 AA3 GLU A 549 LYS A 570 1 22
HELIX 4 AA4 SER A 616 MET A 620 5 5
HELIX 5 AA5 ALA A 621 MET A 627 1 7
HELIX 6 AA6 SER A 634 GLY A 652 1 19
HELIX 7 AA7 ASN A 661 ARG A 671 1 11
HELIX 8 AA8 ASP A 677 VAL A 681 5 5
HELIX 9 AA9 PRO A 686 LEU A 697 1 12
HELIX 10 AB1 LYS A 700 ARG A 704 5 5
HELIX 11 AB2 LEU A 706 ARG A 719 1 14
HELIX 12 AB3 THR B 491 ARG B 506 1 16
HELIX 13 AB4 LEU B 537 ILE B 543 1 7
HELIX 14 AB5 GLU B 549 LYS B 570 1 22
HELIX 15 AB6 SER B 616 MET B 620 5 5
HELIX 16 AB7 ALA B 621 MET B 627 1 7
HELIX 17 AB8 SER B 634 GLY B 652 1 19
HELIX 18 AB9 ASN B 661 ARG B 671 1 11
HELIX 19 AC1 ASP B 677 VAL B 681 5 5
HELIX 20 AC2 PRO B 686 LEU B 697 1 12
HELIX 21 AC3 LYS B 700 ARG B 704 5 5
HELIX 22 AC4 LEU B 706 ARG B 719 1 14
SHEET 1 AA1 5 THR A 458 GLY A 466 0
SHEET 2 AA1 5 GLY A 469 LYS A 475 -1 O LYS A 473 N GLY A 460
SHEET 3 AA1 5 ASP A 479 MET A 484 -1 O VAL A 480 N GLY A 474
SHEET 4 AA1 5 ALA A 526 GLN A 530 -1 O ILE A 527 N LYS A 483
SHEET 5 AA1 5 PHE A 516 SER A 520 -1 N MET A 517 O VAL A 528
SHEET 1 AA2 3 GLY A 534 SER A 536 0
SHEET 2 AA2 3 ILE A 582 HIS A 585 -1 O LEU A 584 N SER A 535
SHEET 3 AA2 3 THR A 589 ILE A 592 -1 O LYS A 591 N PHE A 583
SHEET 1 AA3 5 THR B 458 SER B 465 0
SHEET 2 AA3 5 THR B 470 LYS B 475 -1 O LYS B 473 N GLY B 460
SHEET 3 AA3 5 ASP B 479 MET B 484 -1 O VAL B 480 N GLY B 474
SHEET 4 AA3 5 ALA B 526 GLN B 530 -1 O ILE B 527 N LYS B 483
SHEET 5 AA3 5 PHE B 516 SER B 520 -1 N MET B 517 O VAL B 528
SHEET 1 AA4 3 GLY B 534 SER B 536 0
SHEET 2 AA4 3 ILE B 582 HIS B 585 -1 O LEU B 584 N SER B 535
SHEET 3 AA4 3 THR B 589 ILE B 592 -1 O LYS B 591 N PHE B 583
CISPEP 1 LYS A 522 PRO A 523 0 2.66
CISPEP 2 LYS B 522 PRO B 523 0 2.80
SITE 1 AC1 16 VAL A 471 ALA A 481 LYS A 483 GLU A 501
SITE 2 AC1 16 VAL A 504 LEU A 505 LEU A 514 THR A 529
SITE 3 AC1 16 GLN A 530 TRP A 531 CYS A 532 HIS A 574
SITE 4 AC1 16 GLY A 593 ASP A 594 PHE A 595 HOH A 969
SITE 1 AC2 13 VAL B 471 ALA B 481 LYS B 483 GLU B 501
SITE 2 AC2 13 LEU B 514 THR B 529 GLN B 530 TRP B 531
SITE 3 AC2 13 CYS B 532 GLY B 593 ASP B 594 PHE B 595
SITE 4 AC2 13 HOH B 994
CRYST1 94.121 94.121 163.537 90.00 90.00 90.00 P 41 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 0.010625 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010625 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006115 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
