HEADER RNA/IMMUNE SYSTEM 10-JUN-24 9C75 TITLE THE CRYSTAL STRUCTURE OF HIV-1 REV RESPONSE ELEMENT STEM-LOOP II G34U TITLE 2 MUTANT IN COMPLEX WITH A FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BL3-6 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BL3-6 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: REV RESPONSE ELEMENT; COMPND 11 CHAIN: R; COMPND 12 FRAGMENT: STEM-LOOP II; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 14 ORGANISM_TAXID: 11676 KEYWDS HIV-1, REPLICATION, FAB, CHAPERONE, REV RESPONSE ELEMENT, RNA, RNA- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.OJHA,D.KOIRALA REVDAT 1 28-MAY-25 9C75 0 JRNL AUTH M.OJHA,D.KOIRALA JRNL TITL THE CRYSTAL STRUCTURE OF HIV-1 REV RESPONSE ELEMENT JRNL TITL 2 STEM-LOOP II G34U MUTANT IN COMPLEX WITH A FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.04 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 17488 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850 REMARK 3 FREE R VALUE TEST SET COUNT : 849 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 34.6400 - 5.5200 0.99 2855 176 0.1708 0.2212 REMARK 3 2 5.5200 - 4.3900 1.00 2820 117 0.1716 0.1966 REMARK 3 3 4.3900 - 3.8300 1.00 2767 140 0.1960 0.2401 REMARK 3 4 3.8300 - 3.4800 1.00 2738 148 0.2404 0.3219 REMARK 3 5 3.4800 - 3.2300 1.00 2737 123 0.2914 0.3297 REMARK 3 6 3.2300 - 3.0400 1.00 2722 145 0.3862 0.4813 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.660 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.806 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 135.2 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 : 0.009 5126 REMARK 3 ANGLE : 1.226 7308 REMARK 3 CHIRALITY : 0.059 879 REMARK 3 PLANARITY : 0.011 663 REMARK 3 DIHEDRAL : 16.682 1339 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.1033 -1.0385 33.2888 REMARK 3 T TENSOR REMARK 3 T11: 0.7348 T22: 0.9999 REMARK 3 T33: 0.8809 T12: -0.1785 REMARK 3 T13: 0.0308 T23: -0.0511 REMARK 3 L TENSOR REMARK 3 L11: 2.0029 L22: 1.5084 REMARK 3 L33: 5.0152 L12: -1.2053 REMARK 3 L13: 1.9077 L23: -2.1964 REMARK 3 S TENSOR REMARK 3 S11: 0.3227 S12: -0.3848 S13: -0.4253 REMARK 3 S21: 0.1229 S22: 0.3343 S23: 0.0558 REMARK 3 S31: -0.2376 S32: 0.3470 S33: -0.5436 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 144 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.4134 -13.2477 48.9528 REMARK 3 T TENSOR REMARK 3 T11: 0.8318 T22: 1.1453 REMARK 3 T33: 1.0154 T12: -0.2696 REMARK 3 T13: -0.1156 T23: 0.1713 REMARK 3 L TENSOR REMARK 3 L11: 2.6975 L22: 3.2875 REMARK 3 L33: 1.6373 L12: 0.9510 REMARK 3 L13: 1.1449 L23: 0.4688 REMARK 3 S TENSOR REMARK 3 S11: 0.1215 S12: -0.4192 S13: 0.1533 REMARK 3 S21: 0.2432 S22: -0.4374 S23: 0.7997 REMARK 3 S31: 0.0256 S32: 0.3950 S33: 0.1440 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 198 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.5723 -20.3107 52.6825 REMARK 3 T TENSOR REMARK 3 T11: 0.8239 T22: 1.1203 REMARK 3 T33: 1.3269 T12: -0.3790 REMARK 3 T13: -0.2924 T23: 0.5816 REMARK 3 L TENSOR REMARK 3 L11: 1.4233 L22: 3.1499 REMARK 3 L33: 2.3022 L12: -0.2429 REMARK 3 L13: -0.6053 L23: 2.8144 REMARK 3 S TENSOR REMARK 3 S11: -0.2815 S12: -0.7620 S13: -0.6538 REMARK 3 S21: 0.2527 S22: -0.1811 S23: -0.5824 REMARK 3 S31: 0.4215 S32: 2.6173 S33: 0.1037 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 19 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.3276 -1.0920 29.1503 REMARK 3 T TENSOR REMARK 3 T11: 0.8701 T22: 1.1840 REMARK 3 T33: 0.9333 T12: -0.0827 REMARK 3 T13: 0.0333 T23: -0.1665 REMARK 3 L TENSOR REMARK 3 L11: 4.4024 L22: 2.4103 REMARK 3 L33: 4.7566 L12: -1.2838 REMARK 3 L13: -0.3646 L23: 0.9436 REMARK 3 S TENSOR REMARK 3 S11: 0.5885 S12: -1.1626 S13: 0.2706 REMARK 3 S21: 0.2852 S22: -0.4265 S23: 0.8862 REMARK 3 S31: -0.3149 S32: -0.2671 S33: -0.1458 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 20 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.0188 -1.7406 21.7073 REMARK 3 T TENSOR REMARK 3 T11: 0.6788 T22: 0.6497 REMARK 3 T33: 0.7515 T12: -0.0328 REMARK 3 T13: -0.0360 T23: -0.1007 REMARK 3 L TENSOR REMARK 3 L11: 5.8686 L22: 3.3124 REMARK 3 L33: 3.2455 L12: 1.9199 REMARK 3 L13: -1.8815 L23: 0.1972 REMARK 3 S TENSOR REMARK 3 S11: 0.2669 S12: -0.3133 S13: -0.2550 REMARK 3 S21: -0.1946 S22: -0.0107 S23: -0.0167 REMARK 3 S31: 0.0792 S32: 0.1760 S33: -0.2166 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 104 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5203 -16.5213 42.7010 REMARK 3 T TENSOR REMARK 3 T11: 0.8596 T22: 1.5935 REMARK 3 T33: 1.0785 T12: -0.3901 REMARK 3 T13: -0.0148 T23: 0.2746 REMARK 3 L TENSOR REMARK 3 L11: 0.9360 L22: 2.0526 REMARK 3 L33: 4.1473 L12: -1.3117 REMARK 3 L13: 0.9122 L23: -0.3100 REMARK 3 S TENSOR REMARK 3 S11: 0.4560 S12: -1.8464 S13: -0.7776 REMARK 3 S21: 0.7858 S22: -0.1518 S23: 0.2346 REMARK 3 S31: 0.1205 S32: -0.5473 S33: -0.2445 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 117 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3410 -11.7952 58.0892 REMARK 3 T TENSOR REMARK 3 T11: 1.3028 T22: 1.7665 REMARK 3 T33: 1.1523 T12: -0.2340 REMARK 3 T13: 0.0426 T23: 0.2040 REMARK 3 L TENSOR REMARK 3 L11: 1.6232 L22: 3.0502 REMARK 3 L33: 2.8467 L12: 2.1209 REMARK 3 L13: 0.6522 L23: -0.4512 REMARK 3 S TENSOR REMARK 3 S11: 0.5444 S12: -1.1729 S13: -0.4962 REMARK 3 S21: 1.2800 S22: -0.2733 S23: 0.1768 REMARK 3 S31: -0.3512 S32: -0.1238 S33: -0.0284 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.1889 -11.2037 59.8537 REMARK 3 T TENSOR REMARK 3 T11: 1.2572 T22: 1.8182 REMARK 3 T33: 1.1102 T12: -0.1959 REMARK 3 T13: 0.1696 T23: 0.1993 REMARK 3 L TENSOR REMARK 3 L11: 3.0383 L22: 3.3983 REMARK 3 L33: 3.0840 L12: -0.0258 REMARK 3 L13: 2.4824 L23: 0.3404 REMARK 3 S TENSOR REMARK 3 S11: 0.2364 S12: -1.5191 S13: 0.0031 REMARK 3 S21: 0.9121 S22: 0.0845 S23: 0.5862 REMARK 3 S31: -0.2113 S32: -1.9412 S33: -0.3844 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.7823 38.6904 -18.1965 REMARK 3 T TENSOR REMARK 3 T11: 3.4158 T22: 1.4494 REMARK 3 T33: 1.3878 T12: -0.1121 REMARK 3 T13: 0.7061 T23: -0.5753 REMARK 3 L TENSOR REMARK 3 L11: 3.5356 L22: 3.2538 REMARK 3 L33: 2.0048 L12: 3.6630 REMARK 3 L13: 0.4108 L23: -0.2134 REMARK 3 S TENSOR REMARK 3 S11: -3.3134 S12: 2.1767 S13: -1.5701 REMARK 3 S21: 1.9198 S22: 1.1456 S23: -0.8669 REMARK 3 S31: -0.3865 S32: 0.5266 S33: 0.4012 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 16 THROUGH 35 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.7258 34.1048 -19.6756 REMARK 3 T TENSOR REMARK 3 T11: 2.7998 T22: 2.1593 REMARK 3 T33: 3.0349 T12: -0.4723 REMARK 3 T13: 1.0639 T23: -0.4713 REMARK 3 L TENSOR REMARK 3 L11: 2.3051 L22: 6.1891 REMARK 3 L33: 2.6959 L12: -1.6650 REMARK 3 L13: -2.1415 L23: 1.4438 REMARK 3 S TENSOR REMARK 3 S11: -0.3570 S12: -2.3038 S13: 0.6316 REMARK 3 S21: -2.8504 S22: 1.6575 S23: -2.6096 REMARK 3 S31: 0.2603 S32: 0.2228 S33: -0.6491 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 36 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4322 25.6980 -23.5685 REMARK 3 T TENSOR REMARK 3 T11: 3.4099 T22: 1.6918 REMARK 3 T33: 1.8197 T12: -0.1421 REMARK 3 T13: 0.5707 T23: -0.1505 REMARK 3 L TENSOR REMARK 3 L11: 2.0830 L22: 0.0328 REMARK 3 L33: 0.7246 L12: 0.0945 REMARK 3 L13: -1.2098 L23: -0.0801 REMARK 3 S TENSOR REMARK 3 S11: -1.2530 S12: 1.1377 S13: 0.2982 REMARK 3 S21: -1.9796 S22: 0.8699 S23: 1.2811 REMARK 3 S31: -1.5436 S32: -1.2123 S33: 0.1417 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 41 THROUGH 65 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.6591 19.8038 -2.8229 REMARK 3 T TENSOR REMARK 3 T11: 1.1982 T22: 0.8926 REMARK 3 T33: 1.0987 T12: -0.1733 REMARK 3 T13: 0.2249 T23: -0.2058 REMARK 3 L TENSOR REMARK 3 L11: -0.4477 L22: 2.3355 REMARK 3 L33: 1.4519 L12: 0.7001 REMARK 3 L13: -0.0526 L23: -1.7480 REMARK 3 S TENSOR REMARK 3 S11: 0.4559 S12: 0.1719 S13: -0.0166 REMARK 3 S21: 0.9034 S22: -0.6006 S23: 1.0084 REMARK 3 S31: -1.3500 S32: 1.0926 S33: 0.1528 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 66 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5098 50.3647 -9.8292 REMARK 3 T TENSOR REMARK 3 T11: 2.6604 T22: 0.9284 REMARK 3 T33: 1.7416 T12: -0.1509 REMARK 3 T13: 0.2066 T23: 0.2690 REMARK 3 L TENSOR REMARK 3 L11: 0.0317 L22: 0.2567 REMARK 3 L33: 1.1727 L12: 0.1616 REMARK 3 L13: -0.1982 L23: -0.2619 REMARK 3 S TENSOR REMARK 3 S11: 0.1025 S12: -0.1738 S13: -0.1551 REMARK 3 S21: 1.5065 S22: -0.1557 S23: 0.2057 REMARK 3 S31: -1.9198 S32: -1.8286 S33: -0.6207 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.2118 2.9603 27.1531 REMARK 3 T TENSOR REMARK 3 T11: 0.7803 T22: 1.0293 REMARK 3 T33: 0.8409 T12: -0.0982 REMARK 3 T13: -0.0652 T23: -0.1264 REMARK 3 L TENSOR REMARK 3 L11: 2.8367 L22: 2.6378 REMARK 3 L33: 7.2986 L12: -0.4189 REMARK 3 L13: -0.6557 L23: 1.0435 REMARK 3 S TENSOR REMARK 3 S11: 0.3330 S12: 0.6094 S13: -0.1621 REMARK 3 S21: 0.3241 S22: 0.6664 S23: -1.3741 REMARK 3 S31: 0.1542 S32: 2.0357 S33: -0.5718 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 27 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.4639 7.0832 19.4718 REMARK 3 T TENSOR REMARK 3 T11: 0.7631 T22: 0.9193 REMARK 3 T33: 0.7960 T12: -0.1036 REMARK 3 T13: 0.0318 T23: -0.2148 REMARK 3 L TENSOR REMARK 3 L11: 4.1081 L22: 1.7564 REMARK 3 L33: 3.1017 L12: 0.3387 REMARK 3 L13: 0.9398 L23: -1.7959 REMARK 3 S TENSOR REMARK 3 S11: 0.2571 S12: 0.3470 S13: -0.2110 REMARK 3 S21: 0.0840 S22: -0.5650 S23: 0.0281 REMARK 3 S31: -0.5782 S32: 0.8884 S33: 0.2739 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 64 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.7454 11.6399 22.6664 REMARK 3 T TENSOR REMARK 3 T11: 0.9036 T22: 1.2393 REMARK 3 T33: 0.8635 T12: -0.3161 REMARK 3 T13: 0.0609 T23: -0.1395 REMARK 3 L TENSOR REMARK 3 L11: 3.0842 L22: 3.2449 REMARK 3 L33: 4.9227 L12: 0.0397 REMARK 3 L13: -1.1946 L23: -0.6961 REMARK 3 S TENSOR REMARK 3 S11: 0.5371 S12: 0.0519 S13: 0.1593 REMARK 3 S21: 0.4985 S22: -0.6374 S23: 0.3096 REMARK 3 S31: -0.0785 S32: -0.0393 S33: -0.0232 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 9C75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284931. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7-8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97936 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17512 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.040 REMARK 200 RESOLUTION RANGE LOW (A) : 34.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.18300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.90 REMARK 200 R MERGE FOR SHELL (I) : 2.51800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, 0.1M TRIS PH 8.0, 12.5% REMARK 280 POLYVINYLPYRROLIDONE, 10% PEG 4000, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.43900 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.50700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.30150 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.43900 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.50700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.30150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.43900 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.50700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.30150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.43900 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.50700 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.30150 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, R 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 GLU H 1 REMARK 465 ILE H 2 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 THR H 233 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 A R 51 O4' - C1' - N9 ANGL. DEV. = -5.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR H 57 -61.79 69.55 REMARK 500 LYS H 68 83.05 -68.34 REMARK 500 SER H 88 58.37 34.91 REMARK 500 SER H 108 17.57 -144.77 REMARK 500 PRO H 159 -158.61 -79.28 REMARK 500 ASN H 167 51.38 37.32 REMARK 500 GLU H 224 143.56 -177.16 REMARK 500 SER H 227 -164.55 59.68 REMARK 500 LEU L 12 119.94 -161.14 REMARK 500 SER L 31 -128.21 50.03 REMARK 500 ALA L 52 -19.92 70.99 REMARK 500 SER L 53 -15.47 -144.37 REMARK 500 TYR L 56 -176.88 -66.33 REMARK 500 ASP L 83 52.61 -97.79 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C75 H 1 233 PDB 9C75 9C75 1 233 DBREF 9C75 L 1 215 PDB 9C75 9C75 1 215 DBREF 9C75 R 2 71 GB 902798 U26942.1 7175 7240 SEQADV 9C75 G R 1 GB 902798 INSERTION SEQADV 9C75 U R 34 GB 902798 G 7207 ENGINEERED MUTATION SEQADV 9C75 G R 49 GB 902798 U 7222 CONFLICT SEQADV 9C75 A R 50 GB 902798 U 7223 CONFLICT SEQADV 9C75 A R 52 GB 902798 INSERTION SEQADV 9C75 C R 53 GB 902798 INSERTION SEQADV 9C75 A R 54 GB 902798 INSERTION SEQADV 9C75 C R 55 GB 902798 INSERTION SEQADV 9C75 C R 72 GB 902798 INSERTION SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE TYR ILE SER TYR SER SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE SER PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR SEQRES 9 H 233 ARG ARG ARG SER GLY ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 10 H 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER TYR SER PHE PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 R 72 G G C A C U A U G G G C G SEQRES 2 R 72 C A G C G U C A A U G A C SEQRES 3 R 72 G C U G A C G U U A C A G SEQRES 4 R 72 G C C A G A C A A G A A A SEQRES 5 R 72 C A C U U G U C U G A U A SEQRES 6 R 72 U A G U G C C HELIX 1 AA1 TYR H 31 SER H 35 5 5 HELIX 2 AA2 ARG H 90 THR H 94 5 5 HELIX 3 AA3 TYR H 104 GLY H 109 1 6 HELIX 4 AA4 SER H 199 GLN H 204 1 6 HELIX 5 AA5 SER L 122 SER L 128 1 7 HELIX 6 AA6 LYS L 184 LYS L 189 1 6 SHEET 1 AA1 4 GLU H 9 SER H 10 0 SHEET 2 AA1 4 LEU H 21 ALA H 26 -1 O SER H 24 N SER H 10 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N SER H 74 O TYR H 83 SHEET 1 AA2 6 LEU H 14 VAL H 15 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AA2 6 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AA2 6 SER H 36 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA2 6 GLU H 49 ILE H 54 -1 O GLU H 49 N ARG H 41 SHEET 6 AA2 6 THR H 61 TYR H 63 -1 O TYR H 62 N SER H 53 SHEET 1 AA3 4 LEU H 14 VAL H 15 0 SHEET 2 AA3 4 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AA3 4 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AA3 4 PHE H 112 TRP H 115 -1 O TYR H 114 N ARG H 101 SHEET 1 AA4 4 SER H 132 LEU H 136 0 SHEET 2 AA4 4 THR H 147 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA4 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA5 4 SER H 132 LEU H 136 0 SHEET 2 AA5 4 THR H 147 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AA5 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA5 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AA6 3 THR H 163 TRP H 166 0 SHEET 2 AA6 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AA6 3 THR H 217 VAL H 223 -1 O VAL H 223 N TYR H 206 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 SER L 11 ALA L 14 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA8 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA8 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AA8 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 SER L 11 ALA L 14 0 SHEET 2 AA9 4 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA9 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB2 3 LYS L 146 VAL L 151 0 SHEET 2 AB2 3 TYR L 193 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 3 AB2 3 VAL L 206 PHE L 210 -1 O LYS L 208 N CYS L 195 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.04 SSBOND 2 CYS H 152 CYS H 208 1555 1555 2.02 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.06 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.04 CISPEP 1 PHE H 158 PRO H 159 0 -19.90 CISPEP 2 GLU H 160 PRO H 161 0 15.87 CISPEP 3 SER L 8 PRO L 9 0 5.15 CISPEP 4 PHE L 95 PRO L 96 0 0.72 CISPEP 5 TYR L 141 PRO L 142 0 9.20 CRYST1 90.878 105.014 186.603 90.00 90.00 90.00 I 2 2 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011004 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009523 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005359 0.00000