HEADER DNA BINDING PROTEIN 03-JUL-09 3I59
TITLE CRYSTAL STRUCTURE OF MTBCRP IN COMPLEX WITH N6-CAMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, CRP/FNR FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TRANSCRIPTIONAL REGULATOR, CRP/FNR FAMILY;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MT3777, RV3676;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 12 ORGANISM_TAXID: 1773;
SOURCE 13 GENE: MT3777, RV3676;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS MYCOBACTERIUM TUBERCULOSIS, CAMP RECEPTOR PROTEIN, CRP, ALLOSTERIC
KEYWDS 2 MECHANISM, DNA BINDING, INHIBITION, N6-CAMP, STRUCTURAL GENOMICS, TB
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, TBSGC, DNA-BINDING, TRANSCRIPTION,
KEYWDS 4 TRANSCRIPTION REGULATION, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.REDDY,S.K.PALANINATHAN,J.B.BRUNING,C.THURMAN,D.SMITH,
AUTHOR 2 J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 5 22-NOV-23 3I59 1 REMARK
REVDAT 4 06-SEP-23 3I59 1 REMARK SEQADV HETSYN LINK
REVDAT 3 01-NOV-17 3I59 1 REMARK
REVDAT 2 29-DEC-09 3I59 1 JRNL
REVDAT 1 08-SEP-09 3I59 0
JRNL AUTH M.C.REDDY,S.K.PALANINATHAN,J.B.BRUNING,C.THURMAN,D.SMITH,
JRNL AUTH 2 J.C.SACCHETTINI
JRNL TITL STRUCTURAL INSIGHTS INTO THE MECHANISM OF THE ALLOSTERIC
JRNL TITL 2 TRANSITIONS OF MYCOBACTERIUM TUBERCULOSIS CAMP RECEPTOR
JRNL TITL 3 PROTEIN.
JRNL REF J.BIOL.CHEM. V. 284 36581 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19740754
JRNL DOI 10.1074/JBC.M109.041343
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 22393
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1149
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 18.9610 - 7.7790 0.67 383 0 0.2090 0.0000
REMARK 3 2 7.7790 - 6.2470 0.93 517 0 0.2240 0.0000
REMARK 3 3 6.2470 - 5.4790 0.96 529 0 0.2450 0.0000
REMARK 3 4 5.4790 - 4.9880 0.94 518 0 0.2150 0.0000
REMARK 3 5 4.9880 - 4.6360 0.93 508 0 0.2010 0.0000
REMARK 3 6 4.6360 - 4.3660 0.93 512 0 0.1610 0.0000
REMARK 3 7 4.3660 - 4.1500 0.95 513 0 0.1790 0.0000
REMARK 3 8 4.1500 - 3.9710 0.94 498 0 0.1800 0.0000
REMARK 3 9 3.9710 - 3.8200 0.94 523 0 0.2180 0.0000
REMARK 3 10 3.8200 - 3.6890 0.95 518 0 0.2160 0.0000
REMARK 3 11 3.6890 - 3.5740 0.95 506 0 0.2220 0.0000
REMARK 3 12 3.5740 - 3.4730 0.96 544 0 0.2230 0.0000
REMARK 3 13 3.4730 - 3.3820 0.96 505 0 0.2400 0.0000
REMARK 3 14 3.3820 - 3.3000 0.95 513 0 0.2450 0.0000
REMARK 3 15 3.3000 - 3.2250 0.94 508 0 0.2760 0.0000
REMARK 3 16 3.2250 - 3.1570 0.95 505 0 0.2480 0.0000
REMARK 3 17 3.1570 - 3.0940 0.96 523 0 0.2420 0.0000
REMARK 3 18 3.0940 - 3.0360 0.95 514 0 0.2710 0.0000
REMARK 3 19 3.0360 - 2.9820 0.96 516 0 0.2660 0.0000
REMARK 3 20 2.9820 - 2.9310 0.95 531 0 0.2870 0.0000
REMARK 3 21 2.9310 - 2.8840 0.95 489 0 0.2920 0.0000
REMARK 3 22 2.8840 - 2.8400 0.96 536 0 0.2730 0.0000
REMARK 3 23 2.8400 - 2.7980 0.96 493 0 0.2720 0.0000
REMARK 3 24 2.7980 - 2.7590 0.96 534 0 0.2770 0.0000
REMARK 3 25 2.7590 - 2.7220 0.94 506 0 0.2850 0.0000
REMARK 3 26 2.7220 - 2.6870 0.94 515 0 0.3180 0.0000
REMARK 3 27 2.6870 - 2.6530 0.94 487 0 0.2640 0.0000
REMARK 3 28 2.6530 - 2.6210 0.96 536 0 0.2640 0.0000
REMARK 3 29 2.6210 - 2.5910 0.96 509 0 0.2870 0.0000
REMARK 3 30 2.5910 - 2.5620 0.95 516 0 0.2900 0.0000
REMARK 3 31 2.5620 - 2.5340 0.96 479 0 0.2830 0.0000
REMARK 3 32 2.5340 - 2.5070 0.97 567 0 0.2760 0.0000
REMARK 3 33 2.5070 - 2.4820 0.93 497 0 0.2770 0.0000
REMARK 3 34 2.4820 - 2.4570 0.92 473 0 0.2740 0.0000
REMARK 3 35 2.4570 - 2.4340 0.95 526 0 0.3010 0.0000
REMARK 3 36 2.4340 - 2.4110 0.96 516 0 0.3300 0.0000
REMARK 3 37 2.4110 - 2.3890 0.94 526 0 0.2930 0.0000
REMARK 3 38 2.3890 - 2.3680 0.92 453 0 0.3260 0.0000
REMARK 3 39 2.3680 - 2.3480 0.92 515 0 0.3010 0.0000
REMARK 3 40 2.3480 - 2.3280 0.90 495 0 0.3200 0.0000
REMARK 3 41 2.3280 - 2.3090 0.89 462 0 0.3150 0.0000
REMARK 3 42 2.3090 - 2.2900 0.79 430 0 0.3380 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 56.74
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.70100
REMARK 3 B22 (A**2) : 1.51100
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.33800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 NULL
REMARK 3 ANGLE : 0.802 NULL
REMARK 3 CHIRALITY : 0.056 NULL
REMARK 3 PLANARITY : 0.003 NULL
REMARK 3 DIHEDRAL : 11.848 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 0:12)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0241 11.9152 -50.7918
REMARK 3 T TENSOR
REMARK 3 T11: 0.6504 T22: 0.6943
REMARK 3 T33: 0.5926 T12: 0.1195
REMARK 3 T13: 0.1642 T23: 0.2821
REMARK 3 L TENSOR
REMARK 3 L11: 5.5126 L22: 5.6058
REMARK 3 L33: 2.0784 L12: 1.5505
REMARK 3 L13: -6.4702 L23: -5.3128
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: -0.5753 S13: 0.5108
REMARK 3 S21: -0.2676 S22: -0.7960 S23: -1.0721
REMARK 3 S31: -0.3873 S32: 1.8339 S33: 0.7575
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 13:27)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2329 4.6379 -52.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.9812 T22: 1.5236
REMARK 3 T33: 1.0914 T12: 0.4360
REMARK 3 T13: 0.1624 T23: -0.0752
REMARK 3 L TENSOR
REMARK 3 L11: -0.2656 L22: 0.1503
REMARK 3 L33: 2.8738 L12: -0.5975
REMARK 3 L13: -4.3254 L23: 2.4249
REMARK 3 S TENSOR
REMARK 3 S11: 0.4869 S12: 0.8846 S13: 0.5875
REMARK 3 S21: 0.9458 S22: 0.1728 S23: 0.7244
REMARK 3 S31: 0.5700 S32: 0.7579 S33: -0.7156
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 28:109)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8584 21.1113 -45.2351
REMARK 3 T TENSOR
REMARK 3 T11: 0.5286 T22: 0.4156
REMARK 3 T33: 0.4990 T12: 0.0629
REMARK 3 T13: 0.0154 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 2.6062 L22: 2.3603
REMARK 3 L33: 2.5207 L12: -1.2959
REMARK 3 L13: 0.3113 L23: -0.2291
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.1492 S13: 0.4429
REMARK 3 S21: -0.0456 S22: -0.1659 S23: -0.1685
REMARK 3 S31: 0.0239 S32: -0.5206 S33: 0.1052
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 110:140)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8531 12.0441 -36.2982
REMARK 3 T TENSOR
REMARK 3 T11: 0.3921 T22: 0.3728
REMARK 3 T33: 0.3545 T12: -0.0771
REMARK 3 T13: 0.0524 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 3.7270 L22: 4.2639
REMARK 3 L33: 3.0965 L12: 1.6416
REMARK 3 L13: 0.1515 L23: 3.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.2456 S12: 0.2708 S13: 0.0330
REMARK 3 S21: -0.5173 S22: 0.6133 S23: -0.2071
REMARK 3 S31: -0.2729 S32: 0.7216 S33: -0.1919
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 141:150)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9979 40.7917 -34.2210
REMARK 3 T TENSOR
REMARK 3 T11: 0.6455 T22: 0.6301
REMARK 3 T33: 1.9258 T12: -0.1946
REMARK 3 T13: -0.0491 T23: 0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 7.1976 L22: 9.3790
REMARK 3 L33: 4.0528 L12: 0.8180
REMARK 3 L13: -0.9479 L23: 0.9035
REMARK 3 S TENSOR
REMARK 3 S11: 1.5635 S12: -0.9653 S13: 0.7272
REMARK 3 S21: -0.6337 S22: -0.7775 S23: -0.4798
REMARK 3 S31: -1.3051 S32: 0.3206 S33: -0.2842
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 151:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5720 38.4108 -45.9601
REMARK 3 T TENSOR
REMARK 3 T11: 0.5043 T22: 0.4945
REMARK 3 T33: 1.1553 T12: 0.0479
REMARK 3 T13: -0.0041 T23: 0.2979
REMARK 3 L TENSOR
REMARK 3 L11: 1.6985 L22: -0.8105
REMARK 3 L33: 3.0368 L12: 3.6707
REMARK 3 L13: 1.6732 L23: -3.2760
REMARK 3 S TENSOR
REMARK 3 S11: -0.1161 S12: 0.4746 S13: 0.8144
REMARK 3 S21: 0.2043 S22: -0.0961 S23: 0.4062
REMARK 3 S31: -0.4124 S32: 0.3700 S33: 0.2883
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 0:15)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3805 -0.2951 -18.9136
REMARK 3 T TENSOR
REMARK 3 T11: 1.2697 T22: 0.6580
REMARK 3 T33: 0.8451 T12: -0.0369
REMARK 3 T13: 0.0225 T23: 0.1084
REMARK 3 L TENSOR
REMARK 3 L11: 0.5923 L22: 3.9365
REMARK 3 L33: 2.1303 L12: 2.8591
REMARK 3 L13: 0.4208 L23: 5.6612
REMARK 3 S TENSOR
REMARK 3 S11: 0.1840 S12: 0.3930 S13: -0.0788
REMARK 3 S21: 1.1255 S22: -0.3920 S23: 0.2976
REMARK 3 S31: 3.1838 S32: -0.5839 S33: -0.0359
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 16:31)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0818 -1.9270 -12.3173
REMARK 3 T TENSOR
REMARK 3 T11: 0.6667 T22: 0.5333
REMARK 3 T33: 0.6943 T12: 0.0591
REMARK 3 T13: 0.0436 T23: 0.1007
REMARK 3 L TENSOR
REMARK 3 L11: 5.2991 L22: 0.8232
REMARK 3 L33: 5.2796 L12: -0.2081
REMARK 3 L13: -0.6378 L23: 0.3883
REMARK 3 S TENSOR
REMARK 3 S11: -1.0854 S12: -0.5463 S13: -0.5826
REMARK 3 S21: 0.1184 S22: 0.4639 S23: 0.4344
REMARK 3 S31: 0.2705 S32: 1.2607 S33: 0.4993
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 32:97)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0733 13.9807 -17.0940
REMARK 3 T TENSOR
REMARK 3 T11: 0.3634 T22: 0.5287
REMARK 3 T33: 0.3583 T12: -0.0490
REMARK 3 T13: -0.0270 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.6570 L22: 1.1781
REMARK 3 L33: 1.4569 L12: 0.0243
REMARK 3 L13: -1.1356 L23: -0.1010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: 0.3133 S13: -0.0872
REMARK 3 S21: 0.0933 S22: -0.0760 S23: -0.1692
REMARK 3 S31: 0.0036 S32: 0.3300 S33: 0.0732
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 98:116)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0997 -0.3123 -22.5469
REMARK 3 T TENSOR
REMARK 3 T11: 0.3777 T22: 0.5630
REMARK 3 T33: 0.4564 T12: 0.1542
REMARK 3 T13: -0.0418 T23: -0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 2.1723 L22: 2.9253
REMARK 3 L33: 4.6937 L12: 1.1664
REMARK 3 L13: 0.9752 L23: 1.3164
REMARK 3 S TENSOR
REMARK 3 S11: 0.3730 S12: 0.2441 S13: -0.4280
REMARK 3 S21: 0.1441 S22: 0.1932 S23: -0.6080
REMARK 3 S31: -0.3854 S32: 0.5969 S33: -0.6014
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 117:138)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1327 12.9565 -29.6170
REMARK 3 T TENSOR
REMARK 3 T11: 0.4722 T22: 0.5516
REMARK 3 T33: 0.3931 T12: 0.0043
REMARK 3 T13: 0.0232 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.2559 L22: 2.9388
REMARK 3 L33: 1.0006 L12: -0.1501
REMARK 3 L13: 0.9639 L23: 0.1449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0746 S12: -0.0917 S13: 0.1294
REMARK 3 S21: 0.8194 S22: 0.2336 S23: 0.2383
REMARK 3 S31: 0.1258 S32: -0.6223 S33: -0.2263
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 139:223)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5584 27.1116 -11.0905
REMARK 3 T TENSOR
REMARK 3 T11: 0.5276 T22: 0.4847
REMARK 3 T33: 0.4916 T12: 0.0188
REMARK 3 T13: 0.0104 T23: 0.1045
REMARK 3 L TENSOR
REMARK 3 L11: 3.0930 L22: 3.7766
REMARK 3 L33: 1.8107 L12: -1.1317
REMARK 3 L13: -0.4602 L23: -0.8230
REMARK 3 S TENSOR
REMARK 3 S11: -0.1672 S12: 0.1553 S13: 0.2275
REMARK 3 S21: 0.2299 S22: 0.3522 S23: 0.3663
REMARK 3 S31: -0.3561 S32: -0.1134 S33: -0.1483
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 3I59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS: ADJUSTABLE FOCUS K-B
REMARK 200 PAIR SI PLUS PT, RH COATINGS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22400
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
REMARK 200 R SYM FOR SHELL (I) : 0.41900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3I54
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MICROLITERS OF PROTEIN + 2
REMARK 280 MICROLITERS OF WELL SOLUTION. WELL SOLUTION WAS 0.4M NAH2PO4/
REMARK 280 1.6M K2HPO4, 0.1M IMIDAZOLE PH 8.0, 0.2M NACL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 56.86600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.85800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.86600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.85800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 270 LIES ON A SPECIAL POSITION.
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 -24
REMARK 465 GLY A -23
REMARK 465 SER A -22
REMARK 465 SER A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 SER A -1
REMARK 465 ALA A 18
REMARK 465 ILE A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 LEU A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 GLY A 64
REMARK 465 ARG A 65
REMARK 465 ARG A 224
REMARK 465 MET B -24
REMARK 465 GLY B -23
REMARK 465 SER B -22
REMARK 465 SER B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 PRO B 16
REMARK 465 SER B 17
REMARK 465 ALA B 18
REMARK 465 ILE B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 LEU B 22
REMARK 465 ILE B 142
REMARK 465 PHE B 143
REMARK 465 THR B 144
REMARK 465 GLN B 164
REMARK 465 GLU B 165
REMARK 465 GLY B 166
REMARK 465 GLY B 167
REMARK 465 ALA B 168
REMARK 465 SER B 216
REMARK 465 GLU B 217
REMARK 465 ARG B 218
REMARK 465 LEU B 219
REMARK 465 ALA B 220
REMARK 465 ARG B 221
REMARK 465 ARG B 222
REMARK 465 ALA B 223
REMARK 465 ARG B 224
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 SER A 17 OG
REMARK 470 GLN A 25 CG CD OE1 NE2
REMARK 470 LEU A 26 CG CD1 CD2
REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 45 CG OD1 OD2
REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 ARG A 116 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 136 CG OD1 ND2
REMARK 470 GLN A 159 CD OE1 NE2
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 189 CG CD OE1 OE2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 SER B -1 OG
REMARK 470 ASP B 2 CG OD1 OD2
REMARK 470 GLU B 15 CG CD OE1 OE2
REMARK 470 THR B 23 OG1 CG2
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 GLN B 25 CG CD OE1 NE2
REMARK 470 GLN B 27 CG CD OE1 NE2
REMARK 470 ARG B 33 CD NE CZ NH1 NH2
REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 116 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 137 CG OD1 ND2
REMARK 470 LEU B 138 CG CD1 CD2
REMARK 470 LEU B 141 CG CD1 CD2
REMARK 470 ASP B 145 CG OD1 OD2
REMARK 470 VAL B 146 CG1 CG2
REMARK 470 GLN B 156 CG CD OE1 NE2
REMARK 470 ARG B 170 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 177 CG CD OE1 NE2
REMARK 470 GLU B 178 CG CD OE1 OE2
REMARK 470 GLU B 189 CG CD OE1 OE2
REMARK 470 LYS B 193 CG CD CE NZ
REMARK 470 ASP B 197 CG OD1 OD2
REMARK 470 HIS B 200 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 201 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 204 CG1 CG2 CD1
REMARK 470 ARG B 205 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 206 CG CD1 CD2
REMARK 470 GLU B 207 CG CD OE1 OE2
REMARK 470 LYS B 209 CG CD CE NZ
REMARK 470 LEU B 212 CG CD1 CD2
REMARK 470 ILE B 213 CG1 CG2 CD1
REMARK 470 SER B 214 OG
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 16 62.57 -54.29
REMARK 500 SER A 75 -18.77 91.42
REMARK 500 GLN B 12 88.06 -52.69
REMARK 500 LYS B 24 60.89 73.27
REMARK 500 LEU B 26 -76.13 -120.36
REMARK 500 GLN B 27 111.11 154.25
REMARK 500 ASP B 45 29.98 -145.77
REMARK 500 SER B 75 -16.42 88.95
REMARK 500 PRO B 86 116.70 -39.16
REMARK 500 ASN B 137 58.71 -106.62
REMARK 500 VAL B 146 -51.36 108.88
REMARK 500 ASP B 174 25.71 48.44
REMARK 500 SER B 187 150.23 -48.43
REMARK 500 GLU B 189 -71.97 -60.86
REMARK 500 TRP B 203 -80.14 -63.06
REMARK 500 LYS B 209 30.44 -79.90
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 N6R A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N6S B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I54 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MTBCRP IN COMPLEX WITH CAMP
REMARK 900 RELATED ID: RV3676 RELATED DB: TARGETDB
DBREF 3I59 A 1 224 UNP O69644 O69644_MYCTU 1 224
DBREF 3I59 B 1 224 UNP O69644 O69644_MYCTU 1 224
SEQADV 3I59 MET A -24 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY A -23 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER A -22 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER A -21 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -20 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -19 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -18 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -17 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -16 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A -15 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER A -14 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER A -13 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY A -12 UNP O69644 EXPRESSION TAG
SEQADV 3I59 LEU A -11 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY A -10 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY A -9 UNP O69644 EXPRESSION TAG
SEQADV 3I59 THR A -8 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLU A -7 UNP O69644 EXPRESSION TAG
SEQADV 3I59 ASN A -6 UNP O69644 EXPRESSION TAG
SEQADV 3I59 LEU A -5 UNP O69644 EXPRESSION TAG
SEQADV 3I59 TYR A -4 UNP O69644 EXPRESSION TAG
SEQADV 3I59 PHE A -3 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLN A -2 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER A -1 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS A 0 UNP O69644 EXPRESSION TAG
SEQADV 3I59 MET B -24 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY B -23 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER B -22 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER B -21 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -20 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -19 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -18 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -17 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -16 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B -15 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER B -14 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER B -13 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY B -12 UNP O69644 EXPRESSION TAG
SEQADV 3I59 LEU B -11 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY B -10 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLY B -9 UNP O69644 EXPRESSION TAG
SEQADV 3I59 THR B -8 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLU B -7 UNP O69644 EXPRESSION TAG
SEQADV 3I59 ASN B -6 UNP O69644 EXPRESSION TAG
SEQADV 3I59 LEU B -5 UNP O69644 EXPRESSION TAG
SEQADV 3I59 TYR B -4 UNP O69644 EXPRESSION TAG
SEQADV 3I59 PHE B -3 UNP O69644 EXPRESSION TAG
SEQADV 3I59 GLN B -2 UNP O69644 EXPRESSION TAG
SEQADV 3I59 SER B -1 UNP O69644 EXPRESSION TAG
SEQADV 3I59 HIS B 0 UNP O69644 EXPRESSION TAG
SEQRES 1 A 249 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 249 LEU GLY GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 A 249 ASP GLU ILE LEU ALA ARG ALA GLY ILE PHE GLN GLY VAL
SEQRES 4 A 249 GLU PRO SER ALA ILE ALA ALA LEU THR LYS GLN LEU GLN
SEQRES 5 A 249 PRO VAL ASP PHE PRO ARG GLY HIS THR VAL PHE ALA GLU
SEQRES 6 A 249 GLY GLU PRO GLY ASP ARG LEU TYR ILE ILE ILE SER GLY
SEQRES 7 A 249 LYS VAL LYS ILE GLY ARG ARG ALA PRO ASP GLY ARG GLU
SEQRES 8 A 249 ASN LEU LEU THR ILE MSE GLY PRO SER ASP MET PHE GLY
SEQRES 9 A 249 GLU LEU SER ILE PHE ASP PRO GLY PRO ARG THR SER SER
SEQRES 10 A 249 ALA THR THR ILE THR GLU VAL ARG ALA VAL SER MET ASP
SEQRES 11 A 249 ARG ASP ALA LEU ARG SER TRP ILE ALA ASP ARG PRO GLU
SEQRES 12 A 249 ILE SER GLU GLN LEU LEU ARG VAL LEU ALA ARG ARG LEU
SEQRES 13 A 249 ARG ARG THR ASN ASN ASN LEU ALA ASP LEU ILE PHE THR
SEQRES 14 A 249 ASP VAL PRO GLY ARG VAL ALA LYS GLN LEU LEU GLN LEU
SEQRES 15 A 249 ALA GLN ARG PHE GLY THR GLN GLU GLY GLY ALA LEU ARG
SEQRES 16 A 249 VAL THR HIS ASP LEU THR GLN GLU GLU ILE ALA GLN LEU
SEQRES 17 A 249 VAL GLY ALA SER ARG GLU THR VAL ASN LYS ALA LEU ALA
SEQRES 18 A 249 ASP PHE ALA HIS ARG GLY TRP ILE ARG LEU GLU GLY LYS
SEQRES 19 A 249 SER VAL LEU ILE SER ASP SER GLU ARG LEU ALA ARG ARG
SEQRES 20 A 249 ALA ARG
SEQRES 1 B 249 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 249 LEU GLY GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 B 249 ASP GLU ILE LEU ALA ARG ALA GLY ILE PHE GLN GLY VAL
SEQRES 4 B 249 GLU PRO SER ALA ILE ALA ALA LEU THR LYS GLN LEU GLN
SEQRES 5 B 249 PRO VAL ASP PHE PRO ARG GLY HIS THR VAL PHE ALA GLU
SEQRES 6 B 249 GLY GLU PRO GLY ASP ARG LEU TYR ILE ILE ILE SER GLY
SEQRES 7 B 249 LYS VAL LYS ILE GLY ARG ARG ALA PRO ASP GLY ARG GLU
SEQRES 8 B 249 ASN LEU LEU THR ILE MET GLY PRO SER ASP MET PHE GLY
SEQRES 9 B 249 GLU LEU SER ILE PHE ASP PRO GLY PRO ARG THR SER SER
SEQRES 10 B 249 ALA THR THR ILE THR GLU VAL ARG ALA VAL SER MET ASP
SEQRES 11 B 249 ARG ASP ALA LEU ARG SER TRP ILE ALA ASP ARG PRO GLU
SEQRES 12 B 249 ILE SER GLU GLN LEU LEU ARG VAL LEU ALA ARG ARG LEU
SEQRES 13 B 249 ARG ARG THR ASN ASN ASN LEU ALA ASP LEU ILE PHE THR
SEQRES 14 B 249 ASP VAL PRO GLY ARG VAL ALA LYS GLN LEU LEU GLN LEU
SEQRES 15 B 249 ALA GLN ARG PHE GLY THR GLN GLU GLY GLY ALA LEU ARG
SEQRES 16 B 249 VAL THR HIS ASP LEU THR GLN GLU GLU ILE ALA GLN LEU
SEQRES 17 B 249 VAL GLY ALA SER ARG GLU THR VAL ASN LYS ALA LEU ALA
SEQRES 18 B 249 ASP PHE ALA HIS ARG GLY TRP ILE ARG LEU GLU GLY LYS
SEQRES 19 B 249 SER VAL LEU ILE SER ASP SER GLU ARG LEU ALA ARG ARG
SEQRES 20 B 249 ALA ARG
MODRES 3I59 MSE A 72 MET SELENOMETHIONINE
HET MSE A 72 8
HET N6R A 301 31
HET CL A 302 1
HET N6S B 301 31
HETNAM MSE SELENOMETHIONINE
HETNAM N6R (2R)-N6-(1-METHYL-2-PHENYLETHYL)ADENOSINE-3',5'-CYCLIC
HETNAM 2 N6R MONOPHOSPHATE
HETNAM CL CHLORIDE ION
HETNAM N6S (2S)-N6-(1-METHYL-2-PHENYLETHYL)ADENOSINE-3',5'-CYCLIC
HETNAM 2 N6S MONOPHOSPHATE
HETSYN N6R (2R,4AS,6R,7R,7AR)-6-(6-{[(1R)-1-METHYL-2-
HETSYN 2 N6R PHENYLETHYL]AMINO}-9H-PURIN-9-YL)TETRAHYDRO-4H-FURO[3,
HETSYN 3 N6R 2-D][1,3,2]DIOXAPHOSPHININE-2,7-DIOL 2-OXIDE
HETSYN N6S (2S,4AS,6R,7R,7AR)-6-(6-{[(1S)-1-METHYL-2-
HETSYN 2 N6S PHENYLETHYL]AMINO}-9H-PURIN-9-YL)TETRAHYDRO-4H-FURO[3,
HETSYN 3 N6S 2-D][1,3,2]DIOXAPHOSPHI NINE-2,7-DIOL 2-OXIDE
FORMUL 1 MSE C5 H11 N O2 SE
FORMUL 3 N6R C19 H22 N5 O6 P
FORMUL 4 CL CL 1-
FORMUL 5 N6S C19 H22 N5 O6 P
FORMUL 6 HOH *92(H2 O)
HELIX 1 1 HIS A 0 ALA A 6 1 7
HELIX 2 2 ARG A 7 GLN A 12 5 6
HELIX 3 3 GLU A 80 ASP A 85 1 6
HELIX 4 4 ARG A 106 ARG A 116 1 11
HELIX 5 5 ARG A 116 THR A 144 1 29
HELIX 6 6 ASP A 145 GLY A 162 1 18
HELIX 7 7 THR A 176 GLY A 185 1 10
HELIX 8 8 SER A 187 ARG A 201 1 15
HELIX 9 9 ASP A 215 ALA A 223 1 9
HELIX 10 10 HIS B 0 ARG B 7 1 8
HELIX 11 11 ALA B 8 GLN B 12 5 5
HELIX 12 12 GLU B 80 ASP B 85 1 6
HELIX 13 13 ASP B 105 ARG B 116 1 12
HELIX 14 14 PRO B 117 ASN B 137 1 21
HELIX 15 15 VAL B 146 GLY B 162 1 17
HELIX 16 16 THR B 176 GLY B 185 1 10
HELIX 17 17 SER B 187 ARG B 201 1 15
SHEET 1 A 4 VAL A 29 PHE A 31 0
SHEET 2 A 4 VAL A 99 ASP A 105 -1 O VAL A 99 N PHE A 31
SHEET 3 A 4 ARG A 46 SER A 52 -1 N ILE A 49 O VAL A 102
SHEET 4 A 4 MET A 77 PHE A 78 -1 O PHE A 78 N TYR A 48
SHEET 1 B 4 THR A 36 PHE A 38 0
SHEET 2 B 4 SER A 92 THR A 95 -1 O ALA A 93 N VAL A 37
SHEET 3 B 4 VAL A 55 ARG A 59 -1 N LYS A 56 O THR A 94
SHEET 4 B 4 ASN A 67 MSE A 72 -1 O MSE A 72 N VAL A 55
SHEET 1 C 4 THR A 163 GLN A 164 0
SHEET 2 C 4 LEU A 169 THR A 172 -1 O ARG A 170 N THR A 163
SHEET 3 C 4 SER A 210 ILE A 213 -1 O ILE A 213 N LEU A 169
SHEET 4 C 4 ILE A 204 GLU A 207 -1 N ARG A 205 O LEU A 212
SHEET 1 D 4 PRO B 28 PHE B 31 0
SHEET 2 D 4 VAL B 99 MET B 104 -1 O VAL B 99 N PHE B 31
SHEET 3 D 4 LEU B 47 SER B 52 -1 N ILE B 51 O ARG B 100
SHEET 4 D 4 MET B 77 PHE B 78 -1 O PHE B 78 N TYR B 48
SHEET 1 E 4 THR B 36 PHE B 38 0
SHEET 2 E 4 SER B 92 THR B 95 -1 O ALA B 93 N PHE B 38
SHEET 3 E 4 VAL B 55 ARG B 60 -1 N LYS B 56 O THR B 94
SHEET 4 E 4 GLU B 66 MET B 72 -1 O LEU B 69 N ILE B 57
LINK C ILE A 71 N MSE A 72 1555 1555 1.32
LINK C MSE A 72 N GLY A 73 1555 1555 1.33
SITE 1 AC1 16 PHE A 38 ILE A 57 LEU A 69 PHE A 78
SITE 2 AC1 16 GLY A 79 GLU A 80 LEU A 81 SER A 82
SITE 3 AC1 16 ARG A 89 THR A 90 SER A 91 ARG A 130
SITE 4 AC1 16 THR A 134 ASN A 137 LEU A 141 ASN B 135
SITE 1 AC2 4 ARG A 129 ARG A 130 ARG A 133 ARG A 160
SITE 1 AC3 15 ASN A 135 LEU A 138 PHE B 38 ILE B 57
SITE 2 AC3 15 LEU B 69 THR B 70 PHE B 78 GLY B 79
SITE 3 AC3 15 GLU B 80 LEU B 81 SER B 82 ARG B 89
SITE 4 AC3 15 THR B 90 SER B 91 THR B 134
CRYST1 113.732 75.716 63.639 90.00 110.91 90.00 C 1 2 1 4
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 0.008793 0.000000 0.003359 0.00000
SCALE2 0.000000 0.013207 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016821 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
