HEADER RNA 01-NOV-24 9E7G TITLE CRYSTAL STRUCTURE OF HIV-1 RRE SLII G34C MUTANT IN COMPLEX WITH FAB TITLE 2 BL3-6 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 SLII; COMPND 11 CHAIN: R; COMPND 12 ENGINEERED: YES; COMPND 13 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 EXPDTA X-RAY DIFFRACTION AUTHOR M.OJHA,D.KOIRALA REVDAT 1 28-MAY-25 9E7G 0 JRNL AUTH M.OJHA,D.KOIRALA JRNL TITL CRYSTAL STRUCTURE OF HIV-1 RRE SLII G34C MUTANT IN COMPLEX JRNL TITL 2 WITH FAB BL3-6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 35117 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.970 REMARK 3 FREE R VALUE TEST SET COUNT : 3502 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 38.7700 - 8.7300 1.00 1286 136 0.1382 0.1833 REMARK 3 2 8.7200 - 6.9400 1.00 1265 140 0.1825 0.2158 REMARK 3 3 6.9400 - 6.0700 1.00 1277 145 0.1914 0.2177 REMARK 3 4 6.0600 - 5.5100 1.00 1275 136 0.1870 0.2378 REMARK 3 5 5.5100 - 5.1200 1.00 1271 134 0.1595 0.1968 REMARK 3 6 5.1200 - 4.8200 1.00 1277 137 0.1540 0.2058 REMARK 3 7 4.8200 - 4.5800 1.00 1280 145 0.1445 0.2196 REMARK 3 8 4.5800 - 4.3800 1.00 1285 144 0.1587 0.2015 REMARK 3 9 4.3800 - 4.2100 1.00 1267 137 0.1541 0.1992 REMARK 3 10 4.2100 - 4.0600 1.00 1262 139 0.1775 0.2348 REMARK 3 11 4.0600 - 3.9400 1.00 1263 145 0.1792 0.2275 REMARK 3 12 3.9400 - 3.8200 1.00 1276 144 0.1940 0.2561 REMARK 3 13 3.8200 - 3.7200 1.00 1277 145 0.2020 0.2279 REMARK 3 14 3.7200 - 3.6300 1.00 1261 132 0.2096 0.2415 REMARK 3 15 3.6300 - 3.5500 1.00 1252 137 0.2364 0.2679 REMARK 3 16 3.5500 - 3.4800 0.99 1269 143 0.2401 0.3044 REMARK 3 17 3.4800 - 3.4100 0.99 1241 135 0.2310 0.2367 REMARK 3 18 3.4100 - 3.3400 0.99 1253 143 0.2533 0.2855 REMARK 3 19 3.3400 - 3.2800 0.99 1313 143 0.2357 0.3007 REMARK 3 20 3.2800 - 3.2300 0.99 1242 140 0.2685 0.3195 REMARK 3 21 3.2300 - 3.1700 0.99 1248 144 0.2881 0.3005 REMARK 3 22 3.1700 - 3.1300 0.99 1273 142 0.3357 0.3309 REMARK 3 23 3.1300 - 3.0800 0.99 1234 140 0.3708 0.4463 REMARK 3 24 3.0800 - 3.0400 0.99 1287 143 0.3918 0.4060 REMARK 3 25 3.0400 - 3.0000 0.95 1181 133 0.4476 0.5615 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) : 0.505 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.627 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 84.16 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.4 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 : 0.008 5126 REMARK 3 ANGLE : 1.152 7308 REMARK 3 CHIRALITY : 0.056 879 REMARK 3 PLANARITY : 0.010 663 REMARK 3 DIHEDRAL : 18.322 1339 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 10 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3581 10.6306 -13.8193 REMARK 3 T TENSOR REMARK 3 T11: 2.7656 T22: 1.5754 REMARK 3 T33: 1.3572 T12: 0.0163 REMARK 3 T13: 0.1395 T23: 0.2340 REMARK 3 L TENSOR REMARK 3 L11: 6.6037 L22: 8.1258 REMARK 3 L33: 3.2775 L12: 1.5568 REMARK 3 L13: 0.1578 L23: 5.1276 REMARK 3 S TENSOR REMARK 3 S11: 0.8341 S12: 1.3512 S13: 1.0425 REMARK 3 S21: 2.1820 S22: -2.5021 S23: -1.7484 REMARK 3 S31: 0.1136 S32: 2.8287 S33: 1.3500 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 11 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7535 20.0788 -24.5181 REMARK 3 T TENSOR REMARK 3 T11: 3.7988 T22: 2.9832 REMARK 3 T33: 5.1244 T12: 0.3112 REMARK 3 T13: -0.9321 T23: -0.3419 REMARK 3 L TENSOR REMARK 3 L11: 3.4678 L22: 7.4505 REMARK 3 L33: 9.4504 L12: 2.0476 REMARK 3 L13: 3.3805 L23: 0.3493 REMARK 3 S TENSOR REMARK 3 S11: -0.4694 S12: 0.6328 S13: 1.1471 REMARK 3 S21: 0.2789 S22: 0.0665 S23: 5.3437 REMARK 3 S31: -0.5281 S32: -3.3128 S33: 0.5194 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 26 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0853 19.4784 -23.7576 REMARK 3 T TENSOR REMARK 3 T11: 3.1368 T22: 2.0404 REMARK 3 T33: 2.4212 T12: -0.1939 REMARK 3 T13: -0.2484 T23: -0.2482 REMARK 3 L TENSOR REMARK 3 L11: 3.2706 L22: 4.5040 REMARK 3 L33: 4.9026 L12: 0.6691 REMARK 3 L13: 3.7525 L23: 1.2440 REMARK 3 S TENSOR REMARK 3 S11: -0.6981 S12: 1.1961 S13: 0.1949 REMARK 3 S21: -1.6534 S22: 0.4117 S23: 2.0352 REMARK 3 S31: 0.2866 S32: 0.5137 S33: 0.2135 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 41 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4201 36.4033 -1.2599 REMARK 3 T TENSOR REMARK 3 T11: 1.0377 T22: 0.7291 REMARK 3 T33: 1.1744 T12: -0.1451 REMARK 3 T13: -0.0973 T23: 0.0696 REMARK 3 L TENSOR REMARK 3 L11: 0.4910 L22: 0.1363 REMARK 3 L33: 4.4012 L12: 0.2369 REMARK 3 L13: -1.9070 L23: -0.5570 REMARK 3 S TENSOR REMARK 3 S11: 0.0264 S12: -0.0751 S13: -0.3995 REMARK 3 S21: 0.5087 S22: -0.5260 S23: 0.0363 REMARK 3 S31: 0.9655 S32: -0.1742 S33: 0.4268 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 61 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5121 10.8330 -9.1120 REMARK 3 T TENSOR REMARK 3 T11: 2.5060 T22: 1.1365 REMARK 3 T33: 1.8551 T12: 0.0890 REMARK 3 T13: 0.0468 T23: 0.1411 REMARK 3 L TENSOR REMARK 3 L11: 0.5226 L22: 3.7750 REMARK 3 L33: 1.0760 L12: -0.6341 REMARK 3 L13: 1.2433 L23: -0.6321 REMARK 3 S TENSOR REMARK 3 S11: 1.2032 S12: 0.2789 S13: -0.9526 REMARK 3 S21: 1.0835 S22: -0.7298 S23: -0.1860 REMARK 3 S31: 2.3998 S32: 0.0565 S33: 0.1018 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.8365 51.4448 27.9334 REMARK 3 T TENSOR REMARK 3 T11: 0.8147 T22: 1.2563 REMARK 3 T33: 1.0010 T12: -0.2499 REMARK 3 T13: -0.0393 T23: 0.0190 REMARK 3 L TENSOR REMARK 3 L11: 3.6793 L22: 2.4903 REMARK 3 L33: 2.9317 L12: -1.7526 REMARK 3 L13: -0.6694 L23: -0.5240 REMARK 3 S TENSOR REMARK 3 S11: 0.3434 S12: 0.2540 S13: 0.2038 REMARK 3 S21: 0.1799 S22: 0.9307 S23: 1.0129 REMARK 3 S31: 0.1535 S32: -2.3179 S33: -0.9636 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 21 THROUGH 42 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5471 49.3932 18.8741 REMARK 3 T TENSOR REMARK 3 T11: 0.6784 T22: 0.9668 REMARK 3 T33: 0.9462 T12: -0.2263 REMARK 3 T13: 0.0132 T23: 0.0686 REMARK 3 L TENSOR REMARK 3 L11: 4.0789 L22: 2.1097 REMARK 3 L33: 6.3401 L12: -0.7653 REMARK 3 L13: -0.0145 L23: 0.8202 REMARK 3 S TENSOR REMARK 3 S11: 0.4619 S12: -0.1329 S13: -0.0709 REMARK 3 S21: 0.0656 S22: 0.0807 S23: 0.4344 REMARK 3 S31: 0.2157 S32: -1.3663 S33: -0.1817 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 43 THROUGH 54 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.4164 46.4521 28.5291 REMARK 3 T TENSOR REMARK 3 T11: 0.8261 T22: 0.8410 REMARK 3 T33: 1.1103 T12: -0.2259 REMARK 3 T13: -0.0177 T23: 0.1041 REMARK 3 L TENSOR REMARK 3 L11: 5.6297 L22: 3.2885 REMARK 3 L33: 5.1096 L12: -0.0837 REMARK 3 L13: -1.5234 L23: 1.4043 REMARK 3 S TENSOR REMARK 3 S11: 0.4341 S12: -1.3773 S13: -0.2329 REMARK 3 S21: 0.4190 S22: 0.0888 S23: -0.5488 REMARK 3 S31: 0.9646 S32: 0.7740 S33: -0.2953 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 55 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6297 38.4756 17.9796 REMARK 3 T TENSOR REMARK 3 T11: 0.9181 T22: 0.8073 REMARK 3 T33: 1.1524 T12: -0.2624 REMARK 3 T13: -0.0410 T23: 0.1361 REMARK 3 L TENSOR REMARK 3 L11: 3.4678 L22: 0.6897 REMARK 3 L33: 9.7453 L12: 0.2749 REMARK 3 L13: -0.2017 L23: 0.3107 REMARK 3 S TENSOR REMARK 3 S11: 0.6516 S12: 0.4670 S13: -1.6082 REMARK 3 S21: 0.0361 S22: 0.5658 S23: 0.1638 REMARK 3 S31: 1.5177 S32: 0.8984 S33: -0.0970 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 68 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7394 42.6864 21.5330 REMARK 3 T TENSOR REMARK 3 T11: 0.8140 T22: 1.1104 REMARK 3 T33: 0.9682 T12: -0.3172 REMARK 3 T13: -0.0097 T23: 0.1375 REMARK 3 L TENSOR REMARK 3 L11: 4.8224 L22: 3.3944 REMARK 3 L33: 6.8279 L12: 0.1564 REMARK 3 L13: -0.1238 L23: -0.6240 REMARK 3 S TENSOR REMARK 3 S11: 0.2869 S12: 0.1197 S13: -0.3942 REMARK 3 S21: 0.2564 S22: -0.3874 S23: -0.1261 REMARK 3 S31: 0.7322 S32: -0.9593 S33: -0.0816 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.5137 45.8272 29.9269 REMARK 3 T TENSOR REMARK 3 T11: 0.8128 T22: 1.1424 REMARK 3 T33: 0.9875 T12: -0.3033 REMARK 3 T13: 0.0402 T23: 0.1419 REMARK 3 L TENSOR REMARK 3 L11: 5.4759 L22: 1.8883 REMARK 3 L33: 7.2375 L12: -0.2212 REMARK 3 L13: -0.9828 L23: 1.7090 REMARK 3 S TENSOR REMARK 3 S11: 0.2360 S12: -1.0417 S13: -0.3418 REMARK 3 S21: 0.8619 S22: -0.3283 S23: -0.1822 REMARK 3 S31: 0.5064 S32: -0.6885 S33: -0.1592 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 103 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8735 54.1951 29.8557 REMARK 3 T TENSOR REMARK 3 T11: 0.7831 T22: 1.0405 REMARK 3 T33: 0.9838 T12: -0.2691 REMARK 3 T13: -0.0362 T23: 0.0045 REMARK 3 L TENSOR REMARK 3 L11: 2.9576 L22: 1.4232 REMARK 3 L33: 2.9272 L12: -1.0366 REMARK 3 L13: -0.4158 L23: 0.9702 REMARK 3 S TENSOR REMARK 3 S11: 0.3241 S12: -0.4451 S13: 0.4018 REMARK 3 S21: 0.0012 S22: 0.0636 S23: -0.0910 REMARK 3 S31: -0.2105 S32: -0.7716 S33: -0.1305 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 137 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8617 71.0333 50.5664 REMARK 3 T TENSOR REMARK 3 T11: 0.8577 T22: 1.4223 REMARK 3 T33: 1.2934 T12: -0.1929 REMARK 3 T13: 0.0912 T23: -0.4484 REMARK 3 L TENSOR REMARK 3 L11: 3.7054 L22: 4.2895 REMARK 3 L33: 7.6525 L12: 2.1968 REMARK 3 L13: -2.7396 L23: -2.0350 REMARK 3 S TENSOR REMARK 3 S11: 0.2871 S12: -0.8609 S13: 1.1068 REMARK 3 S21: 0.3178 S22: -0.0434 S23: -0.3236 REMARK 3 S31: -0.8738 S32: -0.7591 S33: -0.4003 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 178 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.7350 68.4882 51.8223 REMARK 3 T TENSOR REMARK 3 T11: 1.0512 T22: 1.5124 REMARK 3 T33: 1.1514 T12: -0.2244 REMARK 3 T13: 0.0031 T23: -0.4421 REMARK 3 L TENSOR REMARK 3 L11: 3.1373 L22: 5.2661 REMARK 3 L33: 3.9641 L12: 1.0182 REMARK 3 L13: -1.6110 L23: -0.9579 REMARK 3 S TENSOR REMARK 3 S11: -0.0727 S12: -1.2346 S13: 0.2972 REMARK 3 S21: 0.6128 S22: 0.2446 S23: -0.8169 REMARK 3 S31: -0.5839 S32: -0.4847 S33: -0.1346 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 206 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9906 70.0826 52.1009 REMARK 3 T TENSOR REMARK 3 T11: 1.0831 T22: 1.9878 REMARK 3 T33: 1.3502 T12: -0.1283 REMARK 3 T13: 0.2141 T23: -0.5860 REMARK 3 L TENSOR REMARK 3 L11: 1.6685 L22: 3.0876 REMARK 3 L33: 6.5463 L12: -0.9049 REMARK 3 L13: -0.1463 L23: -1.3802 REMARK 3 S TENSOR REMARK 3 S11: -0.0594 S12: -0.5062 S13: 0.7937 REMARK 3 S21: -0.3758 S22: 0.1955 S23: 0.3527 REMARK 3 S31: -1.6384 S32: -1.4309 S33: -0.1483 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.2280 55.1209 22.5118 REMARK 3 T TENSOR REMARK 3 T11: 0.6567 T22: 0.5566 REMARK 3 T33: 0.8541 T12: -0.2114 REMARK 3 T13: 0.0355 T23: 0.0825 REMARK 3 L TENSOR REMARK 3 L11: 7.6886 L22: 3.3701 REMARK 3 L33: 6.1125 L12: -1.1133 REMARK 3 L13: 0.4536 L23: 2.4011 REMARK 3 S TENSOR REMARK 3 S11: 0.1994 S12: -0.8010 S13: 0.1816 REMARK 3 S21: -0.0091 S22: -0.0991 S23: -0.1777 REMARK 3 S31: -0.1029 S32: 0.1442 S33: -0.1302 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 77 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3409 61.0733 38.6357 REMARK 3 T TENSOR REMARK 3 T11: 0.6682 T22: 0.9687 REMARK 3 T33: 0.9174 T12: -0.1497 REMARK 3 T13: -0.0685 T23: -0.0921 REMARK 3 L TENSOR REMARK 3 L11: 4.1745 L22: 1.6596 REMARK 3 L33: 5.8994 L12: -1.1078 REMARK 3 L13: -2.4134 L23: 1.0858 REMARK 3 S TENSOR REMARK 3 S11: 0.3543 S12: -1.2935 S13: 0.5176 REMARK 3 S21: 0.3671 S22: -0.0777 S23: -0.2064 REMARK 3 S31: -0.2715 S32: -0.2045 S33: -0.3140 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.6985 64.5906 58.8760 REMARK 3 T TENSOR REMARK 3 T11: 1.0533 T22: 1.7783 REMARK 3 T33: 1.1406 T12: -0.1515 REMARK 3 T13: -0.0976 T23: -0.3338 REMARK 3 L TENSOR REMARK 3 L11: 3.0415 L22: 3.4329 REMARK 3 L33: 5.6573 L12: 0.2949 REMARK 3 L13: -2.7706 L23: -0.1174 REMARK 3 S TENSOR REMARK 3 S11: 0.1671 S12: -1.2346 S13: 0.0898 REMARK 3 S21: 0.7262 S22: -0.0589 S23: -0.5314 REMARK 3 S31: 0.1242 S32: 0.5763 S33: -0.1600 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 9E7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289692. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.8 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) : 0.97934 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 : 35117 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 46.830 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 13.60 REMARK 200 R MERGE (I) : 0.11500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.67100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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 (%): 61.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M CITRIC ACID, 0.08 M BIS-TRIS REMARK 280 PROPANE PH 8.8, 16% PEG 3350 AND 0.3% ETHANOL, VAPOR DIFFUSION, REMARK 280 SITTING 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 45.39250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.31500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.66550 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.39250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.31500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.66550 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.39250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.31500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.66550 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.39250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.31500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.66550 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 C8 - N9 - C4 ANGL. DEV. = 2.8 DEGREES REMARK 500 A R 52 C2 - N3 - C4 ANGL. DEV. = -3.1 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 -21.34 73.94 REMARK 500 SER H 108 26.45 -141.20 REMARK 500 SER H 139 -164.84 -77.25 REMARK 500 SER H 140 -9.90 -51.70 REMARK 500 THR H 143 70.42 51.97 REMARK 500 ASP H 156 69.39 60.28 REMARK 500 ASN H 167 58.65 39.21 REMARK 500 SER H 227 -169.54 54.50 REMARK 500 SER L 15 -167.77 -100.54 REMARK 500 SER L 31 -133.21 49.34 REMARK 500 ALA L 52 -22.96 69.65 REMARK 500 SER L 64 136.68 -172.25 REMARK 500 ASN L 139 61.56 60.35 REMARK 500 ASN L 159 34.90 -95.69 REMARK 500 TYR L 174 -169.06 -115.46 REMARK 500 ASN L 211 -75.32 -100.32 REMARK 500 ARG L 212 -71.51 -129.23 REMARK 500 GLU L 214 47.14 35.60 REMARK 500 REMARK 500 REMARK: NULL DBREF 9E7G H 1 233 PDB 9E7G 9E7G 1 233 DBREF 9E7G L 1 215 PDB 9E7G 9E7G 1 215 DBREF 9E7G R 1 72 GB 902798 U26942.1 7174 7241 SEQADV 9E7G G R 1 GB 902798 A 7174 CONFLICT SEQADV 9E7G C R 34 GB 902798 G 7207 ENGINEERED MUTATION SEQADV 9E7G G R 49 GB 902798 U 7222 CONFLICT SEQADV 9E7G A R 50 GB 902798 U 7223 CONFLICT SEQADV 9E7G A R 52 GB 902798 INSERTION SEQADV 9E7G C R 53 GB 902798 INSERTION SEQADV 9E7G A R 54 GB 902798 INSERTION SEQADV 9E7G C R 55 GB 902798 INSERTION SEQADV 9E7G C R 72 GB 902798 A 7241 CONFLICT 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 C 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 ASP H 65 LYS H 68 5 4 HELIX 3 AA3 ARG H 90 THR H 94 5 5 HELIX 4 AA4 TYR H 104 GLY H 109 1 6 HELIX 5 AA5 LYS H 213 ASN H 216 5 4 HELIX 6 AA6 GLN L 80 PHE L 84 5 5 HELIX 7 AA7 SER L 122 LYS L 127 1 6 HELIX 8 AA8 LYS L 184 LYS L 189 1 6 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O SER H 28 N GLN H 6 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O ALA H 82 N CYS H 25 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N SER H 74 O TYR H 83 SHEET 1 AA2 6 GLY H 13 VAL H 15 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 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 LEU H 48 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 GLY H 13 VAL H 15 0 SHEET 2 AA3 4 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 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 GLY H 151 N LEU H 136 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O SER H 192 N CYS H 152 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 GLY H 151 N LEU H 136 SHEET 3 AA5 4 TYR H 188 PRO H 197 -1 O SER H 192 N CYS H 152 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 THR H 217 N HIS H 212 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O ARG L 25 N THR L 6 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O ILE L 76 N VAL L 20 SHEET 4 AA7 4 GLY L 65 SER L 68 -1 N SER L 68 O ASP L 71 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 TYR L 37 O TYR L 88 SHEET 5 AA8 6 PRO L 45 TYR L 50 -1 O LYS L 46 N GLN L 38 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 ASN L 138 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 SER L 175 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 ALA L 145 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 TYR L 193 HIS L 199 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 VAL L 206 PHE L 210 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.06 SSBOND 2 CYS H 152 CYS H 208 1555 1555 2.03 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.08 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.04 CISPEP 1 PHE H 158 PRO H 159 0 -12.98 CISPEP 2 GLU H 160 PRO H 161 0 5.05 CISPEP 3 SER L 8 PRO L 9 0 3.21 CISPEP 4 PHE L 95 PRO L 96 0 -3.56 CISPEP 5 TYR L 141 PRO L 142 0 3.21 CRYST1 90.785 106.630 187.331 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 0.011015 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009378 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005338 0.00000