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HEADER TRANSFERASE 03-JUL-17 5OCJ
TITLE CRYSTAL STRUCTURE OF AG85C BOUND TO CYCLOPHOSTIN 8BETA INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DGAT,ACYL-COA:DIACYLGLYCEROL ACYLTRANSFERASE,ANTIGEN 85
COMPND 5 COMPLEX C,AG85C,FIBRONECTIN-BINDING PROTEIN C,FBPS C;
COMPND 6 EC: 2.3.1.122,2.3.1.20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: FBPC, MPT45, RV0129C, MTCI5.03C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS AG85C, MYCOLICATE, MYCOMEMBRANE, TMM, TDM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VILJOEN,M.RICHARD,P.C.NGUYEN,C.D.SPILLING,S.CANAAN,J.F.CAVALIER,
AUTHOR 2 M.BLAISE,L.KREMER
REVDAT 1 24-JAN-18 5OCJ 0
JRNL AUTH A.VILJOEN,M.RICHARD,P.C.NGUYEN,P.FOURQUET,L.CAMOIN,
JRNL AUTH 2 R.R.PAUDAL,G.R.GNAWALI,C.D.SPILLING,J.F.CAVALIER,S.CANAAN,
JRNL AUTH 3 M.BLAISE,L.KREMER
JRNL TITL CYCLIPOSTINS AND CYCLOPHOSTIN ANALOGS INHIBIT THE ANTIGEN
JRNL TITL 2 85C FROM MYCOBACTERIUM TUBERCULOSIS BOTH IN VITRO AND IN
JRNL TITL 3 VIVO.
JRNL REF J. BIOL. CHEM. 2018
JRNL REFN ESSN 1083-351X
JRNL PMID 29301937
JRNL DOI 10.1074/JBC.RA117.000760
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 65862
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 48.1118 - 4.3373 1.00 4843 152 0.1466 0.1640
REMARK 3 2 4.3373 - 3.4429 1.00 4634 145 0.1247 0.1350
REMARK 3 3 3.4429 - 3.0078 1.00 4606 144 0.1434 0.1591
REMARK 3 4 3.0078 - 2.7328 1.00 4575 143 0.1544 0.1737
REMARK 3 5 2.7328 - 2.5370 1.00 4553 143 0.1597 0.2042
REMARK 3 6 2.5370 - 2.3874 1.00 4572 143 0.1590 0.1956
REMARK 3 7 2.3874 - 2.2678 1.00 4518 141 0.1485 0.1911
REMARK 3 8 2.2678 - 2.1691 1.00 4516 142 0.1476 0.1803
REMARK 3 9 2.1691 - 2.0856 1.00 4544 142 0.1482 0.1888
REMARK 3 10 2.0856 - 2.0136 1.00 4502 141 0.1562 0.1911
REMARK 3 11 2.0136 - 1.9507 1.00 4496 141 0.1743 0.2123
REMARK 3 12 1.9507 - 1.8949 1.00 4521 142 0.1886 0.2240
REMARK 3 13 1.8949 - 1.8450 1.00 4475 140 0.2058 0.2195
REMARK 3 14 1.8450 - 1.8000 1.00 4507 141 0.2377 0.2682
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.006 4501
REMARK 3 ANGLE : 0.821 6152
REMARK 3 CHIRALITY : 0.056 613
REMARK 3 PLANARITY : 0.006 815
REMARK 3 DIHEDRAL : 13.521 2562
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 27 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9519 -21.9193 -5.2548
REMARK 3 T TENSOR
REMARK 3 T11: 0.1681 T22: 0.2258
REMARK 3 T33: 0.2013 T12: -0.0156
REMARK 3 T13: -0.0092 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 8.9472 L22: 5.6984
REMARK 3 L33: 2.9563 L12: -6.6736
REMARK 3 L13: -2.9004 L23: 3.4784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: -0.0152 S13: 0.3330
REMARK 3 S21: -0.0651 S22: 0.2498 S23: -0.5407
REMARK 3 S31: 0.0590 S32: 0.1932 S33: -0.2354
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4075 -20.4450 -7.8332
REMARK 3 T TENSOR
REMARK 3 T11: 0.1495 T22: 0.1312
REMARK 3 T33: 0.2256 T12: 0.0399
REMARK 3 T13: -0.0133 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 3.1330 L22: 3.0029
REMARK 3 L33: 4.1370 L12: 1.2315
REMARK 3 L13: 0.7046 L23: 0.3077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: 0.1886 S13: 0.0988
REMARK 3 S21: -0.2531 S22: 0.0492 S23: -0.1648
REMARK 3 S31: 0.0086 S32: -0.0956 S33: 0.0098
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1291 -18.2431 -6.6376
REMARK 3 T TENSOR
REMARK 3 T11: 0.1406 T22: 0.1537
REMARK 3 T33: 0.1699 T12: 0.0004
REMARK 3 T13: -0.0028 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.7287 L22: 1.1692
REMARK 3 L33: 2.0595 L12: 0.1110
REMARK 3 L13: -0.0066 L23: -0.2724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: -0.0756 S13: 0.1414
REMARK 3 S21: -0.0541 S22: -0.0610 S23: 0.0252
REMARK 3 S31: -0.1538 S32: -0.0754 S33: 0.0075
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3318 -31.2097 -6.1054
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.1565
REMARK 3 T33: 0.1919 T12: 0.0081
REMARK 3 T13: 0.0001 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 1.5583 L22: 2.8800
REMARK 3 L33: 7.4150 L12: -0.3245
REMARK 3 L13: -0.3565 L23: 3.6668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: 0.0386 S13: -0.0875
REMARK 3 S21: -0.0962 S22: 0.0900 S23: -0.1810
REMARK 3 S31: 0.0123 S32: 0.3646 S33: -0.1274
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0366 -34.8008 -13.2240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1752 T22: 0.1719
REMARK 3 T33: 0.1723 T12: -0.0189
REMARK 3 T13: -0.0074 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.1700 L22: 1.2014
REMARK 3 L33: 2.3840 L12: -0.2205
REMARK 3 L13: -0.4666 L23: 0.6448
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0851 S13: -0.0648
REMARK 3 S21: -0.0744 S22: -0.0150 S23: 0.0337
REMARK 3 S31: 0.1890 S32: -0.1202 S33: 0.0120
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 193 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4908 -26.1120 -8.8183
REMARK 3 T TENSOR
REMARK 3 T11: 0.1121 T22: 0.1895
REMARK 3 T33: 0.1807 T12: -0.0076
REMARK 3 T13: -0.0060 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 1.6630 L22: 2.3471
REMARK 3 L33: 3.7295 L12: -0.0669
REMARK 3 L13: -0.0105 L23: -0.9709
REMARK 3 S TENSOR
REMARK 3 S11: -0.1166 S12: 0.0292 S13: 0.0645
REMARK 3 S21: -0.0583 S22: 0.0088 S23: -0.0162
REMARK 3 S31: -0.1168 S32: -0.3633 S33: 0.1066
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8197 -29.0769 -15.8083
REMARK 3 T TENSOR
REMARK 3 T11: 0.2233 T22: 0.3378
REMARK 3 T33: 0.2792 T12: -0.0049
REMARK 3 T13: -0.0121 T23: -0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 1.9265 L22: 5.4511
REMARK 3 L33: 6.4847 L12: 3.4181
REMARK 3 L13: -3.6257 L23: -5.8088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0933 S12: 0.1230 S13: 0.0780
REMARK 3 S21: -0.3094 S22: 0.1608 S23: 0.5625
REMARK 3 S31: 0.2948 S32: -0.5234 S33: -0.3076
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 245 THROUGH 282 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8640 -20.5549 -4.9489
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.1894
REMARK 3 T33: 0.1710 T12: 0.0263
REMARK 3 T13: -0.0044 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 2.4015 L22: 1.7568
REMARK 3 L33: 3.0152 L12: 0.2823
REMARK 3 L13: -0.5356 L23: 0.0983
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.2158 S13: 0.0561
REMARK 3 S21: 0.1056 S22: -0.0060 S23: 0.1176
REMARK 3 S31: -0.0856 S32: -0.2968 S33: 0.0260
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 27 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7458 -12.8358 -53.8066
REMARK 3 T TENSOR
REMARK 3 T11: 0.3227 T22: 0.2115
REMARK 3 T33: 0.2440 T12: 0.0330
REMARK 3 T13: -0.1131 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 8.8908 L22: 5.2854
REMARK 3 L33: 4.3142 L12: 3.9155
REMARK 3 L13: -3.7827 L23: -1.9411
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: 0.3062 S13: 0.5760
REMARK 3 S21: -0.3446 S22: 0.2024 S23: 0.4498
REMARK 3 S31: -0.2050 S32: -0.1684 S33: -0.2487
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 28 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9350 -18.6992 -50.2300
REMARK 3 T TENSOR
REMARK 3 T11: 0.1864 T22: 0.1441
REMARK 3 T33: 0.1771 T12: -0.0214
REMARK 3 T13: -0.0460 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 2.4848 L22: 5.3385
REMARK 3 L33: 1.8330 L12: 0.0733
REMARK 3 L13: -1.1959 L23: -0.7412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: 0.0366 S13: 0.0963
REMARK 3 S21: -0.2978 S22: -0.0143 S23: 0.0669
REMARK 3 S31: -0.0815 S32: -0.1229 S33: 0.0071
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0906 -19.4009 -51.7653
REMARK 3 T TENSOR
REMARK 3 T11: 0.2567 T22: 0.1484
REMARK 3 T33: 0.1651 T12: 0.0123
REMARK 3 T13: -0.0080 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 2.2121 L22: 2.7133
REMARK 3 L33: 1.7643 L12: 0.1693
REMARK 3 L13: 0.5733 L23: 0.1945
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.1582 S13: 0.0800
REMARK 3 S21: -0.4560 S22: -0.0943 S23: -0.1268
REMARK 3 S31: -0.0522 S32: 0.1498 S33: 0.1264
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2413 -21.0345 -49.3159
REMARK 3 T TENSOR
REMARK 3 T11: 0.2071 T22: 0.1966
REMARK 3 T33: 0.3270 T12: 0.0114
REMARK 3 T13: -0.1014 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 2.7958 L22: 2.7042
REMARK 3 L33: 6.3326 L12: -0.1341
REMARK 3 L13: -0.5724 L23: -0.3960
REMARK 3 S TENSOR
REMARK 3 S11: -0.1134 S12: -0.0294 S13: 0.1089
REMARK 3 S21: -0.2147 S22: -0.1650 S23: 0.5110
REMARK 3 S31: -0.3036 S32: -0.3733 S33: 0.2305
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2173 -31.4495 -40.2740
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.2039
REMARK 3 T33: 0.2215 T12: -0.0104
REMARK 3 T13: -0.0062 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.7104 L22: 2.4858
REMARK 3 L33: 3.2273 L12: -0.3043
REMARK 3 L13: -0.4559 L23: 0.5291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0500 S12: -0.1894 S13: -0.0760
REMARK 3 S21: 0.1139 S22: -0.0789 S23: 0.2120
REMARK 3 S31: 0.0999 S32: -0.1131 S33: 0.1404
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1773 -34.7831 -46.1887
REMARK 3 T TENSOR
REMARK 3 T11: 0.2102 T22: 0.1801
REMARK 3 T33: 0.2293 T12: 0.0416
REMARK 3 T13: 0.0265 T23: 0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 2.7552 L22: 3.8710
REMARK 3 L33: 3.2381 L12: 1.3684
REMARK 3 L13: 1.3052 L23: 1.6100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0463 S12: 0.0828 S13: -0.0250
REMARK 3 S21: -0.1339 S22: -0.0044 S23: -0.2014
REMARK 3 S31: 0.0009 S32: 0.2842 S33: 0.0372
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2737 -37.2429 -38.3368
REMARK 3 T TENSOR
REMARK 3 T11: 0.2390 T22: 0.2304
REMARK 3 T33: 0.1949 T12: 0.0173
REMARK 3 T13: 0.0268 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 7.5866 L22: 2.1534
REMARK 3 L33: 5.1285 L12: 3.8268
REMARK 3 L13: 5.8503 L23: 2.4738
REMARK 3 S TENSOR
REMARK 3 S11: 0.1296 S12: -0.3515 S13: -0.2918
REMARK 3 S21: 0.1446 S22: -0.0912 S23: -0.2754
REMARK 3 S31: 0.2369 S32: -0.1161 S33: -0.0531
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 245 THROUGH 282 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1338 -31.8668 -51.4845
REMARK 3 T TENSOR
REMARK 3 T11: 0.2124 T22: 0.2209
REMARK 3 T33: 0.2308 T12: 0.0370
REMARK 3 T13: 0.0518 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 1.0203 L22: 4.2297
REMARK 3 L33: 1.8271 L12: 0.0789
REMARK 3 L13: -0.1674 L23: 0.9081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: 0.1380 S13: -0.0904
REMARK 3 S21: -0.4331 S22: -0.0688 S23: -0.4126
REMARK 3 S31: 0.0391 S32: 0.1893 S33: 0.0310
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65871
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.095
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.240
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: 3HRH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M SODIUM CITRATE TRIBASIC DIHYDRATE PH 5 AND 10% W/V
REMARK 280 POLYETHYLENE GLYCOL 20000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 33.69500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.66000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.66000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.69500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.88500
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 0
REMARK 465 PHE A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 283
REMARK 465 THR A 284
REMARK 465 PRO A 285
REMARK 465 PRO A 286
REMARK 465 ALA A 287
REMARK 465 ALA A 288
REMARK 465 PRO A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 ALA A 294
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 0
REMARK 465 PHE B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 GLY B 5
REMARK 465 ALA B 283
REMARK 465 THR B 284
REMARK 465 PRO B 285
REMARK 465 PRO B 286
REMARK 465 ALA B 287
REMARK 465 ALA B 288
REMARK 465 PRO B 289
REMARK 465 ALA B 290
REMARK 465 ALA B 291
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 ALA B 294
REMARK 465 LEU B 295
REMARK 465 GLU B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 689 O HOH A 693 1.94
REMARK 500 O07 9SW B 401 O HOH B 501 2.06
REMARK 500 O07 9SW A 401 O HOH A 501 2.07
REMARK 500 O HOH A 660 O HOH A 717 2.08
REMARK 500 O HOH A 694 O HOH A 704 2.10
REMARK 500 O HOH B 714 O HOH B 728 2.11
REMARK 500 O HOH A 679 O HOH A 740 2.16
REMARK 500 O HOH A 666 O HOH A 729 2.17
REMARK 500 O HOH A 615 O HOH A 711 2.18
REMARK 500 O HOH B 646 O HOH B 676 2.18
REMARK 500 O HOH A 647 O HOH A 711 2.19
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 PRO A 54 38.37 -90.47
REMARK 500 PHE A 76 17.91 55.79
REMARK 500 ARG A 101 -59.24 -126.76
REMARK 500 SER A 124 -124.30 50.30
REMARK 500 SER A 169 73.64 -101.32
REMARK 500 SER A 215 -168.74 -108.09
REMARK 500 ARG A 248 17.79 -142.00
REMARK 500 PRO A 256 47.15 -80.16
REMARK 500 ARG B 41 35.47 -93.22
REMARK 500 PRO B 54 41.64 -91.98
REMARK 500 PHE B 76 18.32 57.12
REMARK 500 ARG B 101 -58.92 -128.73
REMARK 500 SER B 124 -124.00 50.96
REMARK 500 SER B 169 75.90 -100.28
REMARK 500 SER B 215 -162.32 -103.73
REMARK 500 ARG B 248 14.06 -142.51
REMARK 500 PRO B 256 35.14 -79.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 9SW A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SW A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SW B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 402
DBREF 5OCJ A 1 294 UNP P9WQN9 A85C_MYCTU 47 340
DBREF 5OCJ B 1 294 UNP P9WQN9 A85C_MYCTU 47 340
SEQADV 5OCJ MET A 0 UNP P9WQN9 INITIATING METHIONINE
SEQADV 5OCJ LEU A 295 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ GLU A 296 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 297 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 298 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 299 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 300 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 301 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS A 302 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ MET B 0 UNP P9WQN9 INITIATING METHIONINE
SEQADV 5OCJ LEU B 295 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ GLU B 296 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 297 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 298 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 299 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 300 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 301 UNP P9WQN9 EXPRESSION TAG
SEQADV 5OCJ HIS B 302 UNP P9WQN9 EXPRESSION TAG
SEQRES 1 A 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 A 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 A 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 A 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 A 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 A 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 A 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 A 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 A 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 A 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 A 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 A 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 A 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 A 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 A 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 A 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 A 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 A 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 A 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 A 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 A 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 A 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 A 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 B 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 B 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 B 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 B 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 B 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 B 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 B 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 B 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 B 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 B 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 B 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 B 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 B 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 B 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 B 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 B 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 B 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 B 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 B 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 B 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 B 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 B 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET 9SW A 401 18
HET DMS A 402 4
HET 9SW B 401 28
HET DMS B 402 4
HETNAM 9SW METHOXY-[(3~{R})-3-[(2~{R})-1-METHOXY-1,3-
HETNAM 2 9SW BIS(OXIDANYLIDENE)BUTAN-2-YL]PENTADECYL]PHOSPHINIC
HETNAM 3 9SW ACID
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 9SW 2(C21 H41 O6 P)
FORMUL 4 DMS 2(C2 H6 O S)
FORMUL 7 HOH *533(H2 O)
HELIX 1 AA1 ASN A 47 THR A 53 1 7
HELIX 2 AA2 PRO A 54 TYR A 60 1 7
HELIX 3 AA3 LYS A 94 ARG A 101 1 8
HELIX 4 AA4 ARG A 101 GLY A 112 1 12
HELIX 5 AA5 SER A 124 TYR A 137 1 14
HELIX 6 AA6 TRP A 157 SER A 169 1 13
HELIX 7 AA7 ASN A 173 GLY A 179 1 7
HELIX 8 AA8 PRO A 184 ASN A 189 1 6
HELIX 9 AA9 GLN A 194 ASN A 201 1 8
HELIX 10 AB1 ASN A 221 ASP A 245 1 25
HELIX 11 AB2 SER A 261 MET A 272 1 12
HELIX 12 AB3 MET A 272 GLY A 282 1 11
HELIX 13 AB4 ASN B 47 THR B 53 1 7
HELIX 14 AB5 PRO B 54 TYR B 60 1 7
HELIX 15 AB6 LYS B 94 ARG B 101 1 8
HELIX 16 AB7 ARG B 101 GLY B 112 1 12
HELIX 17 AB8 SER B 124 TYR B 137 1 14
HELIX 18 AB9 TRP B 157 SER B 169 1 13
HELIX 19 AC1 ASN B 173 GLY B 179 1 7
HELIX 20 AC2 ASP B 183 ASN B 189 1 7
HELIX 21 AC3 GLN B 194 ASN B 202 1 9
HELIX 22 AC4 ASN B 221 ASP B 245 1 25
HELIX 23 AC5 SER B 261 MET B 272 1 12
HELIX 24 AC6 MET B 272 GLY B 282 1 11
SHEET 1 AA1 8 GLU A 9 SER A 15 0
SHEET 2 AA1 8 ARG A 20 GLN A 27 -1 O VAL A 24 N LEU A 11
SHEET 3 AA1 8 SER A 65 PRO A 69 -1 O MET A 68 N GLN A 25
SHEET 4 AA1 8 ALA A 33 LEU A 36 1 N LEU A 36 O ILE A 67
SHEET 5 AA1 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 AA1 8 TYR A 143 LEU A 147 1 O ALA A 145 N ALA A 120
SHEET 7 AA1 8 ARG A 204 TYR A 208 1 O TRP A 206 N SER A 146
SHEET 8 AA1 8 GLY A 250 ASN A 253 1 O VAL A 251 N VAL A 207
SHEET 1 AA2 8 VAL B 8 SER B 15 0
SHEET 2 AA2 8 ARG B 20 GLN B 27 -1 O ILE B 22 N VAL B 13
SHEET 3 AA2 8 SER B 65 PRO B 69 -1 O MET B 68 N GLN B 25
SHEET 4 AA2 8 ALA B 33 LEU B 36 1 N LEU B 36 O ILE B 67
SHEET 5 AA2 8 ALA B 119 LEU B 123 1 O ALA B 119 N TYR B 35
SHEET 6 AA2 8 TYR B 143 LEU B 147 1 O ALA B 145 N ALA B 120
SHEET 7 AA2 8 ARG B 204 TYR B 208 1 O ARG B 204 N ALA B 144
SHEET 8 AA2 8 GLY B 250 ASN B 253 1 O VAL B 251 N VAL B 207
SITE 1 AC1 9 GLY A 39 LEU A 40 SER A 124 PRO A 223
SITE 2 AC1 9 LEU A 227 HIS A 260 TRP A 265 HOH A 501
SITE 3 AC1 9 9SW B 401
SITE 1 AC2 6 PHE A 26 GLY A 29 GLY A 30 SER A 65
SITE 2 AC2 6 LYS A 111 GLY A 112
SITE 1 AC3 16 ALA A 165 ILE A 222 PRO A 223 PHE A 226
SITE 2 AC3 16 9SW A 401 GLY B 39 LEU B 40 ARG B 41
SITE 3 AC3 16 SER B 124 ILE B 222 PRO B 223 PHE B 226
SITE 4 AC3 16 LEU B 227 HIS B 260 TRP B 265 HOH B 501
SITE 1 AC4 4 ASP B 79 TYR B 81 MET B 177 HOH B 656
CRYST1 67.390 75.770 137.320 90.00 90.00 90.00 P 21 21 21 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 0.014839 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013198 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007282 0.00000
TER 2145 GLY A 282
TER 4310 GLY B 282
MASTER 588 0 4 24 16 0 10 6 4884 2 54 48
END |