HEADER IMMUNE SYSTEM/RNA 26-MAY-20 6X5N TITLE CRYSTAL STRUCTURE OF A STABILIZED PAN ENE BIMOLECULAR TRIPLEX WITH A TITLE 2 GC-CLAMPED POLYA TAIL COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN FAB BL-3 6; COMPND 3 CHAIN: l, L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN FAB BL-3 6; COMPND 7 CHAIN: h, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GGPAN RNA (39-MER); COMPND 11 CHAIN: R, r; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: GGCA9 RNA (12-MER); COMPND 15 CHAIN: A, a; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 14 ORGANISM_TAXID: 32630; SOURCE 15 MOL_ID: 4; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 18 ORGANISM_TAXID: 32630 KEYWDS VIRAL ENCODED RNA, RNA THERAPEUTICS, STRUCTURE-FUNCTION STUDIES, KEYWDS 2 SMALL MOLECULES BINDING, PAN TRIPLEX, GGENE, GGCA9, RNA, IMMUNE KEYWDS 3 SYSTEM-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.SWAIN,M.LI,A.WOLDAWER,S.F.J.LEGRICE REVDAT 1 01-JUL-20 6X5N 0 JRNL AUTH M.SWAIN,M.LI,A.AGEELI,W.KASPRZAK,J.T.MILLER, JRNL AUTH 2 J.SZTUBA-SOLINSKA,T.KENDERDINE,A.FRABONI,J.SCHNEEKLOTH, JRNL AUTH 3 J.PICCIRRILI,R.P.MURELLI,D.FABRIS,A.WLODAWER,B.SHAPIRO, JRNL AUTH 4 N.BAIRD,S.F.J.LE GRICE JRNL TITL TARGETING THE NUCLEAR EXPRESSION ELEMENT (ENE) TRIPLE HELIX JRNL TITL 2 OF KAPOSI SARCOMA HERPESVIRUS POLYADENYLATED NUCLEAR RNA, JRNL TITL 3 PAN. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.16_3549 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) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.180 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8 REMARK 3 NUMBER OF REFLECTIONS : 18300 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.183 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.350 REMARK 3 FREE R VALUE TEST SET COUNT : 613 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 37.9900 - 5.2400 0.94 4609 126 0.1542 0.2336 REMARK 3 2 5.2400 - 4.1600 0.93 4527 190 0.1711 0.2523 REMARK 3 3 4.1600 - 3.6300 0.95 4615 168 0.2207 0.3390 REMARK 3 4 3.6300 - 3.3000 0.81 3936 129 0.2270 0.2979 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) : 0.459 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.012 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 82.53 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 113.8 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 : 0.010 9215 REMARK 3 ANGLE : 1.308 12988 REMARK 3 CHIRALITY : 0.062 1545 REMARK 3 PLANARITY : 0.009 1282 REMARK 3 DIHEDRAL : 11.681 5265 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 41 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.3939 48.5167 98.3742 REMARK 3 T TENSOR REMARK 3 T11: 0.8417 T22: 0.7175 REMARK 3 T33: 0.9321 T12: -0.0799 REMARK 3 T13: 0.1673 T23: -0.2924 REMARK 3 L TENSOR REMARK 3 L11: 6.0904 L22: 7.5639 REMARK 3 L33: 2.8523 L12: 0.7417 REMARK 3 L13: -1.9100 L23: -4.2409 REMARK 3 S TENSOR REMARK 3 S11: -0.2292 S12: -0.9793 S13: 1.0800 REMARK 3 S21: 0.2296 S22: 0.4130 S23: 0.3657 REMARK 3 S31: -0.5140 S32: 0.4828 S33: -0.2322 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 27 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.3598 42.4496 96.8670 REMARK 3 T TENSOR REMARK 3 T11: 0.5534 T22: 0.5186 REMARK 3 T33: 0.6056 T12: -0.2485 REMARK 3 T13: 0.1239 T23: -0.1289 REMARK 3 L TENSOR REMARK 3 L11: 3.8625 L22: 8.7829 REMARK 3 L33: 4.3253 L12: -0.7351 REMARK 3 L13: 1.3796 L23: -2.4464 REMARK 3 S TENSOR REMARK 3 S11: -0.2505 S12: -0.1336 S13: 0.5029 REMARK 3 S21: 0.1266 S22: 0.1947 S23: -0.3340 REMARK 3 S31: -0.8050 S32: 0.4329 S33: 0.1108 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.4394 53.0648 74.3995 REMARK 3 T TENSOR REMARK 3 T11: 1.2098 T22: 0.8286 REMARK 3 T33: 0.9694 T12: -0.2576 REMARK 3 T13: -0.3139 T23: 0.2398 REMARK 3 L TENSOR REMARK 3 L11: 6.5290 L22: 1.1078 REMARK 3 L33: 3.4697 L12: 2.7083 REMARK 3 L13: 4.7643 L23: 1.9628 REMARK 3 S TENSOR REMARK 3 S11: -1.0301 S12: 1.1793 S13: 1.5724 REMARK 3 S21: -1.3858 S22: 0.8676 S23: 1.3935 REMARK 3 S31: -0.6345 S32: -0.3600 S33: 0.4026 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 120 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.3106 45.3722 65.7074 REMARK 3 T TENSOR REMARK 3 T11: 1.3617 T22: 1.2427 REMARK 3 T33: 1.0431 T12: -0.3359 REMARK 3 T13: -0.1935 T23: 0.4904 REMARK 3 L TENSOR REMARK 3 L11: 6.0790 L22: 5.1929 REMARK 3 L33: 9.7764 L12: 3.7482 REMARK 3 L13: 6.7046 L23: 6.0256 REMARK 3 S TENSOR REMARK 3 S11: -0.9961 S12: 1.0123 S13: 0.6314 REMARK 3 S21: -1.5308 S22: 1.0885 S23: 1.0811 REMARK 3 S31: -1.2392 S32: -0.4174 S33: -0.1294 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.7141 47.4752 69.1765 REMARK 3 T TENSOR REMARK 3 T11: 1.5111 T22: 0.8196 REMARK 3 T33: 1.1892 T12: 0.2114 REMARK 3 T13: -0.1105 T23: 0.4045 REMARK 3 L TENSOR REMARK 3 L11: 3.1499 L22: 1.2917 REMARK 3 L33: 2.1841 L12: -0.6792 REMARK 3 L13: -2.2047 L23: 1.3349 REMARK 3 S TENSOR REMARK 3 S11: -0.2359 S12: 1.9787 S13: 1.2529 REMARK 3 S21: -0.9014 S22: -0.2847 S23: 0.3008 REMARK 3 S31: -0.7712 S32: -0.3599 S33: 0.6370 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 192 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.0333 45.0267 66.9613 REMARK 3 T TENSOR REMARK 3 T11: 1.2526 T22: 1.0472 REMARK 3 T33: 0.9069 T12: -0.2424 REMARK 3 T13: -0.3654 T23: 0.4679 REMARK 3 L TENSOR REMARK 3 L11: 0.3953 L22: 3.5224 REMARK 3 L33: 3.3536 L12: -1.1302 REMARK 3 L13: -0.0304 L23: -0.8340 REMARK 3 S TENSOR REMARK 3 S11: -0.0939 S12: 0.6733 S13: 0.0844 REMARK 3 S21: -1.0094 S22: 0.3690 S23: 0.8236 REMARK 3 S31: 0.0353 S32: -0.2964 S33: -0.1250 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 193 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.7645 54.2467 61.5256 REMARK 3 T TENSOR REMARK 3 T11: 1.9276 T22: 1.2632 REMARK 3 T33: 1.1277 T12: -0.4708 REMARK 3 T13: -0.5990 T23: 0.6800 REMARK 3 L TENSOR REMARK 3 L11: 3.8607 L22: 0.6158 REMARK 3 L33: 1.0005 L12: 0.5308 REMARK 3 L13: 1.5240 L23: 0.0186 REMARK 3 S TENSOR REMARK 3 S11: -0.2815 S12: 0.6853 S13: 0.2856 REMARK 3 S21: -1.6544 S22: 0.6490 S23: 0.8832 REMARK 3 S31: -0.1172 S32: -0.2760 S33: -0.0843 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 4 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.4440 21.1076 85.3894 REMARK 3 T TENSOR REMARK 3 T11: 0.5165 T22: 0.4030 REMARK 3 T33: 0.3731 T12: -0.1225 REMARK 3 T13: 0.0713 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 5.5552 L22: 4.3831 REMARK 3 L33: 5.9219 L12: -2.9671 REMARK 3 L13: 1.0718 L23: 1.2355 REMARK 3 S TENSOR REMARK 3 S11: 0.1529 S12: 1.1318 S13: -0.2415 REMARK 3 S21: -0.6963 S22: -0.1823 S23: -0.0669 REMARK 3 S31: 0.3746 S32: 0.0808 S33: -0.0163 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 21 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.2512 23.3889 95.6028 REMARK 3 T TENSOR REMARK 3 T11: 0.3095 T22: 0.5569 REMARK 3 T33: 0.3905 T12: -0.1049 REMARK 3 T13: 0.0576 T23: 0.0933 REMARK 3 L TENSOR REMARK 3 L11: 3.5751 L22: 1.7962 REMARK 3 L33: 3.2340 L12: -0.1499 REMARK 3 L13: 2.4381 L23: 0.4028 REMARK 3 S TENSOR REMARK 3 S11: 0.3493 S12: -0.0217 S13: -0.1484 REMARK 3 S21: 0.0742 S22: -0.0933 S23: 0.3883 REMARK 3 S31: 0.2276 S32: 0.2493 S33: -0.3079 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 64 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.2257 17.1602 95.6896 REMARK 3 T TENSOR REMARK 3 T11: 0.4862 T22: 0.6701 REMARK 3 T33: 0.6337 T12: -0.0538 REMARK 3 T13: 0.0070 T23: -0.0268 REMARK 3 L TENSOR REMARK 3 L11: 4.5147 L22: 9.1631 REMARK 3 L33: 3.7162 L12: -4.3845 REMARK 3 L13: -3.7246 L23: 1.8645 REMARK 3 S TENSOR REMARK 3 S11: -0.0358 S12: -1.0670 S13: -1.2616 REMARK 3 S21: 0.3290 S22: 0.0035 S23: 0.8855 REMARK 3 S31: 0.4957 S32: 0.0377 S33: 0.0618 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.1204 28.1896 94.7634 REMARK 3 T TENSOR REMARK 3 T11: 0.5863 T22: 0.3863 REMARK 3 T33: 0.3632 T12: -0.1104 REMARK 3 T13: 0.0360 T23: -0.0539 REMARK 3 L TENSOR REMARK 3 L11: 4.3067 L22: 2.6717 REMARK 3 L33: 7.3039 L12: 0.8050 REMARK 3 L13: 4.1796 L23: -0.4790 REMARK 3 S TENSOR REMARK 3 S11: -0.1571 S12: -0.1410 S13: 0.0174 REMARK 3 S21: 0.1045 S22: 0.1534 S23: 0.0928 REMARK 3 S31: -0.3453 S32: 0.2064 S33: 0.0092 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 116 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.4966 33.3680 67.8489 REMARK 3 T TENSOR REMARK 3 T11: 1.2248 T22: 0.8968 REMARK 3 T33: 0.5553 T12: -0.3305 REMARK 3 T13: 0.0647 T23: 0.0349 REMARK 3 L TENSOR REMARK 3 L11: 3.7666 L22: 4.5350 REMARK 3 L33: 4.9769 L12: -0.3191 REMARK 3 L13: -1.5804 L23: -3.2995 REMARK 3 S TENSOR REMARK 3 S11: -0.2872 S12: 1.4445 S13: 0.0991 REMARK 3 S21: -1.3274 S22: 0.7379 S23: -0.0377 REMARK 3 S31: -0.4876 S32: -0.6620 S33: -0.4274 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 166 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.7591 37.1122 64.7102 REMARK 3 T TENSOR REMARK 3 T11: 1.1251 T22: 1.0489 REMARK 3 T33: 0.7702 T12: -0.3375 REMARK 3 T13: 0.2193 T23: -0.0765 REMARK 3 L TENSOR REMARK 3 L11: 3.1329 L22: 4.5675 REMARK 3 L33: 7.7398 L12: -3.0820 REMARK 3 L13: -0.2415 L23: -0.7765 REMARK 3 S TENSOR REMARK 3 S11: -0.5924 S12: 1.5925 S13: -0.0803 REMARK 3 S21: -1.5376 S22: 0.2171 S23: -0.6165 REMARK 3 S31: 0.0567 S32: 0.5291 S33: 0.4450 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 213 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.3992 29.8437 59.3593 REMARK 3 T TENSOR REMARK 3 T11: 1.7860 T22: 0.9501 REMARK 3 T33: 0.7908 T12: -0.5471 REMARK 3 T13: -0.0489 T23: -0.2165 REMARK 3 L TENSOR REMARK 3 L11: 5.8964 L22: 5.4771 REMARK 3 L33: 6.7403 L12: 1.3298 REMARK 3 L13: -1.3201 L23: -5.6588 REMARK 3 S TENSOR REMARK 3 S11: -0.4758 S12: 1.3309 S13: -0.1043 REMARK 3 S21: -1.0328 S22: 0.5209 S23: -0.1043 REMARK 3 S31: -1.7118 S32: 0.7821 S33: -0.0926 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 4 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.8065 44.4907 2.5650 REMARK 3 T TENSOR REMARK 3 T11: 0.6947 T22: 1.1106 REMARK 3 T33: 0.6238 T12: 0.3627 REMARK 3 T13: -0.1335 T23: -0.2094 REMARK 3 L TENSOR REMARK 3 L11: 1.4979 L22: 2.0114 REMARK 3 L33: 3.6772 L12: -1.0416 REMARK 3 L13: -1.2091 L23: -0.9560 REMARK 3 S TENSOR REMARK 3 S11: 0.9241 S12: 0.4244 S13: -0.4499 REMARK 3 S21: -0.3295 S22: -0.5531 S23: 0.1531 REMARK 3 S31: 0.4049 S32: 1.2070 S33: -0.2416 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 64 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.8986 49.8376 -0.0922 REMARK 3 T TENSOR REMARK 3 T11: 0.4794 T22: 0.8999 REMARK 3 T33: 0.5653 T12: 0.1342 REMARK 3 T13: 0.0256 T23: -0.0728 REMARK 3 L TENSOR REMARK 3 L11: 8.6521 L22: 9.1082 REMARK 3 L33: 5.9609 L12: 0.4006 REMARK 3 L13: 2.5010 L23: -0.6851 REMARK 3 S TENSOR REMARK 3 S11: 0.3799 S12: 1.5509 S13: -0.7035 REMARK 3 S21: -0.6775 S22: 0.0189 S23: 0.0786 REMARK 3 S31: 0.0781 S32: 0.8470 S33: -0.3512 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.8037 39.6847 2.7749 REMARK 3 T TENSOR REMARK 3 T11: 0.7092 T22: 1.2025 REMARK 3 T33: 0.7033 T12: 0.4246 REMARK 3 T13: -0.2028 T23: -0.4139 REMARK 3 L TENSOR REMARK 3 L11: 6.9657 L22: 5.5251 REMARK 3 L33: 2.5409 L12: -4.3316 REMARK 3 L13: -3.6548 L23: 0.9787 REMARK 3 S TENSOR REMARK 3 S11: 0.4252 S12: 0.4470 S13: -0.3571 REMARK 3 S21: -0.1478 S22: 0.0763 S23: -0.1769 REMARK 3 S31: 0.7150 S32: 1.1994 S33: -0.0616 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 124 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.7278 30.5853 32.3429 REMARK 3 T TENSOR REMARK 3 T11: 1.3471 T22: 1.5977 REMARK 3 T33: 1.1135 T12: 0.4008 REMARK 3 T13: 0.0310 T23: 0.3981 REMARK 3 L TENSOR REMARK 3 L11: 1.9655 L22: 5.0409 REMARK 3 L33: 2.5943 L12: 0.3042 REMARK 3 L13: -0.5296 L23: 2.4473 REMARK 3 S TENSOR REMARK 3 S11: -0.3438 S12: -1.6489 S13: -1.2272 REMARK 3 S21: 1.5467 S22: 1.4068 S23: 1.4242 REMARK 3 S31: 1.4471 S32: -0.6142 S33: -0.8915 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 158 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9732 32.5427 25.1186 REMARK 3 T TENSOR REMARK 3 T11: 0.8789 T22: 1.0987 REMARK 3 T33: 1.0273 T12: 0.2894 REMARK 3 T13: -0.2874 T23: -0.1800 REMARK 3 L TENSOR REMARK 3 L11: 5.0553 L22: 5.0763 REMARK 3 L33: 7.4186 L12: -3.2609 REMARK 3 L13: 0.4902 L23: -3.7688 REMARK 3 S TENSOR REMARK 3 S11: -0.0291 S12: -0.6657 S13: -0.4457 REMARK 3 S21: 0.7738 S22: 0.5447 S23: -0.0225 REMARK 3 S31: 0.5402 S32: 1.2398 S33: -0.4210 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 188 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.7383 25.7740 32.5888 REMARK 3 T TENSOR REMARK 3 T11: 1.5571 T22: 1.0417 REMARK 3 T33: 1.7368 T12: 0.4619 REMARK 3 T13: -0.4942 T23: 0.1308 REMARK 3 L TENSOR REMARK 3 L11: 8.9604 L22: 8.7274 REMARK 3 L33: 6.3306 L12: -3.8858 REMARK 3 L13: 0.6465 L23: -6.5883 REMARK 3 S TENSOR REMARK 3 S11: -0.6122 S12: -1.5771 S13: -0.8714 REMARK 3 S21: 1.7674 S22: 0.8764 S23: 0.3463 REMARK 3 S31: 0.2755 S32: 0.5259 S33: -0.2177 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 201 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.7197 35.3621 36.6130 REMARK 3 T TENSOR REMARK 3 T11: 1.5267 T22: 1.1754 REMARK 3 T33: 0.9164 T12: 0.4267 REMARK 3 T13: -0.1754 T23: 0.0756 REMARK 3 L TENSOR REMARK 3 L11: 9.2731 L22: 4.1043 REMARK 3 L33: 5.7652 L12: 2.8698 REMARK 3 L13: -0.7852 L23: 0.2675 REMARK 3 S TENSOR REMARK 3 S11: 0.4244 S12: -2.1993 S13: -1.0233 REMARK 3 S21: 1.7650 S22: 0.5149 S23: -0.0038 REMARK 3 S31: 0.6314 S32: 0.5828 S33: -0.8093 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6261 18.8238 -2.8214 REMARK 3 T TENSOR REMARK 3 T11: 2.3986 T22: 1.3937 REMARK 3 T33: 1.6009 T12: 0.8948 REMARK 3 T13: -1.1839 T23: -0.7656 REMARK 3 L TENSOR REMARK 3 L11: 0.2535 L22: 0.2260 REMARK 3 L33: 1.3492 L12: 0.1151 REMARK 3 L13: 0.0429 L23: 0.3591 REMARK 3 S TENSOR REMARK 3 S11: 0.1527 S12: 0.1563 S13: -0.2776 REMARK 3 S21: 0.1772 S22: -0.0777 S23: -0.1317 REMARK 3 S31: -0.0401 S32: -0.1157 S33: 0.0058 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 27 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5505 24.9055 -1.9696 REMARK 3 T TENSOR REMARK 3 T11: 1.7328 T22: 1.2611 REMARK 3 T33: 0.9330 T12: 1.7754 REMARK 3 T13: -0.4202 T23: -0.6837 REMARK 3 L TENSOR REMARK 3 L11: 0.3446 L22: 0.0420 REMARK 3 L33: -0.0039 L12: -0.0868 REMARK 3 L13: -0.0017 L23: 0.0027 REMARK 3 S TENSOR REMARK 3 S11: 0.1214 S12: 0.3958 S13: -0.3515 REMARK 3 S21: -0.1165 S22: -0.1186 S23: 0.0153 REMARK 3 S31: 0.7577 S32: 0.4700 S33: -0.2093 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 77 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7912 25.8003 0.2132 REMARK 3 T TENSOR REMARK 3 T11: 1.6390 T22: 1.0776 REMARK 3 T33: 1.0459 T12: 1.0392 REMARK 3 T13: -0.7150 T23: -0.4309 REMARK 3 L TENSOR REMARK 3 L11: 1.7644 L22: 2.2291 REMARK 3 L33: 1.9997 L12: -1.2305 REMARK 3 L13: 0.5202 L23: -1.0746 REMARK 3 S TENSOR REMARK 3 S11: 0.2066 S12: 0.5132 S13: -0.1973 REMARK 3 S21: -0.3980 S22: -0.3117 S23: 0.1014 REMARK 3 S31: 0.0349 S32: 0.1847 S33: 0.1403 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1010 13.9000 20.9330 REMARK 3 T TENSOR REMARK 3 T11: 2.0357 T22: 1.1727 REMARK 3 T33: 1.4157 T12: 0.5523 REMARK 3 T13: -0.3933 T23: -0.1039 REMARK 3 L TENSOR REMARK 3 L11: 2.5603 L22: 4.4915 REMARK 3 L33: 6.5055 L12: 1.3341 REMARK 3 L13: 0.8442 L23: -3.5570 REMARK 3 S TENSOR REMARK 3 S11: 1.1748 S12: 0.0701 S13: -1.2555 REMARK 3 S21: -0.1347 S22: 0.8266 S23: 1.0924 REMARK 3 S31: 1.3714 S32: -0.3440 S33: -1.9847 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 120 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4741 31.2454 37.1771 REMARK 3 T TENSOR REMARK 3 T11: 1.5819 T22: 1.5100 REMARK 3 T33: 1.7379 T12: 0.5334 REMARK 3 T13: 0.5304 T23: 0.6338 REMARK 3 L TENSOR REMARK 3 L11: 9.0872 L22: 2.0454 REMARK 3 L33: 8.8172 L12: -1.7708 REMARK 3 L13: 6.1984 L23: -4.0010 REMARK 3 S TENSOR REMARK 3 S11: -0.5077 S12: -1.2523 S13: -1.2694 REMARK 3 S21: 1.1541 S22: 1.0196 S23: 0.9925 REMARK 3 S31: 0.5516 S32: -0.6760 S33: -0.5218 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 134 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.6799 14.6533 22.8090 REMARK 3 T TENSOR REMARK 3 T11: 2.0151 T22: 0.8401 REMARK 3 T33: 1.9934 T12: 0.1668 REMARK 3 T13: -0.5739 T23: 0.2543 REMARK 3 L TENSOR REMARK 3 L11: 7.4151 L22: 6.4457 REMARK 3 L33: 1.7996 L12: -1.9710 REMARK 3 L13: 2.2680 L23: 1.9436 REMARK 3 S TENSOR REMARK 3 S11: 0.2500 S12: -0.2506 S13: -1.6633 REMARK 3 S21: 0.3392 S22: 0.9146 S23: 1.4442 REMARK 3 S31: 0.7130 S32: -0.5076 S33: -1.1424 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 147 THROUGH 159 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.9811 16.0550 28.8274 REMARK 3 T TENSOR REMARK 3 T11: 1.6019 T22: 1.5423 REMARK 3 T33: 2.2272 T12: -0.3474 REMARK 3 T13: 0.0644 T23: 0.7220 REMARK 3 L TENSOR REMARK 3 L11: 1.3021 L22: 0.9368 REMARK 3 L33: 6.4203 L12: 1.1055 REMARK 3 L13: 2.8921 L23: 2.4540 REMARK 3 S TENSOR REMARK 3 S11: -0.0528 S12: -1.4473 S13: -2.2139 REMARK 3 S21: 0.6062 S22: 0.5011 S23: 1.0194 REMARK 3 S31: 1.9799 S32: -2.5828 S33: -0.4374 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 160 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.8961 19.4647 19.9891 REMARK 3 T TENSOR REMARK 3 T11: 1.5666 T22: 0.9532 REMARK 3 T33: 2.2748 T12: 0.2180 REMARK 3 T13: -0.8037 T23: -0.0224 REMARK 3 L TENSOR REMARK 3 L11: 2.9295 L22: 4.5635 REMARK 3 L33: 7.0871 L12: -3.6300 REMARK 3 L13: -0.2920 L23: -0.3003 REMARK 3 S TENSOR REMARK 3 S11: 0.6185 S12: -0.0508 S13: -0.7522 REMARK 3 S21: 0.7613 S22: 0.7898 S23: 0.0180 REMARK 3 S31: 0.9165 S32: 0.1456 S33: -1.2775 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 176 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5101 21.3357 34.0455 REMARK 3 T TENSOR REMARK 3 T11: 1.6991 T22: 1.4440 REMARK 3 T33: 1.8104 T12: -0.1489 REMARK 3 T13: 0.1109 T23: 0.3998 REMARK 3 L TENSOR REMARK 3 L11: 0.1950 L22: 0.4179 REMARK 3 L33: 0.0161 L12: 0.2857 REMARK 3 L13: -0.0072 L23: -0.0032 REMARK 3 S TENSOR REMARK 3 S11: -0.4352 S12: -0.6846 S13: -0.6208 REMARK 3 S21: 0.6410 S22: 0.3084 S23: -0.6452 REMARK 3 S31: 1.3294 S32: -0.9531 S33: 0.0807 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 198 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.5898 11.8013 34.0824 REMARK 3 T TENSOR REMARK 3 T11: 1.8767 T22: 1.1118 REMARK 3 T33: 1.6097 T12: -0.1965 REMARK 3 T13: 0.1561 T23: 0.3776 REMARK 3 L TENSOR REMARK 3 L11: 7.3836 L22: 2.1696 REMARK 3 L33: 4.8494 L12: 2.3532 REMARK 3 L13: 3.7581 L23: -0.8234 REMARK 3 S TENSOR REMARK 3 S11: 1.0729 S12: -0.9062 S13: -1.0857 REMARK 3 S21: 1.3455 S22: 0.2036 S23: -0.3894 REMARK 3 S31: 0.3643 S32: -0.9696 S33: -1.3332 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 5 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.7730 40.7377 -45.2450 REMARK 3 T TENSOR REMARK 3 T11: 2.0130 T22: 2.2539 REMARK 3 T33: 1.0001 T12: 0.1184 REMARK 3 T13: -0.1591 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 9.0906 L22: 5.6822 REMARK 3 L33: 7.3722 L12: -5.6343 REMARK 3 L13: -2.1099 L23: -0.0768 REMARK 3 S TENSOR REMARK 3 S11: 0.9352 S12: 1.6216 S13: -0.8031 REMARK 3 S21: -2.2195 S22: -0.3519 S23: 0.6057 REMARK 3 S31: 1.0064 S32: 0.5260 S33: -0.6622 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 6 THROUGH 10 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.6236 43.9461 -30.4930 REMARK 3 T TENSOR REMARK 3 T11: 1.2286 T22: 1.4427 REMARK 3 T33: 1.2289 T12: -0.0151 REMARK 3 T13: 0.2198 T23: 0.0607 REMARK 3 L TENSOR REMARK 3 L11: 2.3717 L22: 9.0812 REMARK 3 L33: 9.9027 L12: -4.4663 REMARK 3 L13: 2.6147 L23: -2.7667 REMARK 3 S TENSOR REMARK 3 S11: 0.6126 S12: 0.7760 S13: -0.1506 REMARK 3 S21: -0.3342 S22: -0.1333 S23: 1.2033 REMARK 3 S31: -0.6431 S32: 0.0377 S33: -0.4850 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 11 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.3552 43.2553 -16.5622 REMARK 3 T TENSOR REMARK 3 T11: 0.9903 T22: 1.5796 REMARK 3 T33: 0.8804 T12: 0.5433 REMARK 3 T13: 0.1219 T23: 0.0434 REMARK 3 L TENSOR REMARK 3 L11: 1.6950 L22: 5.4404 REMARK 3 L33: 8.4545 L12: 1.7424 REMARK 3 L13: -2.4407 L23: 1.7568 REMARK 3 S TENSOR REMARK 3 S11: -0.9420 S12: -0.9492 S13: -0.9051 REMARK 3 S21: -0.6927 S22: 0.7955 S23: -0.0668 REMARK 3 S31: -0.4802 S32: -0.0146 S33: 0.1406 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 26 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.7250 36.1016 -39.3486 REMARK 3 T TENSOR REMARK 3 T11: 2.3884 T22: 1.3899 REMARK 3 T33: 1.3880 T12: -0.2943 REMARK 3 T13: -0.0378 T23: -0.3024 REMARK 3 L TENSOR REMARK 3 L11: 6.5320 L22: 6.5525 REMARK 3 L33: 5.0485 L12: 0.6968 REMARK 3 L13: -3.1186 L23: -0.2329 REMARK 3 S TENSOR REMARK 3 S11: 0.3946 S12: 2.2503 S13: -2.0476 REMARK 3 S21: -3.3293 S22: 0.0120 S23: 0.6801 REMARK 3 S31: 2.4930 S32: -1.1614 S33: -0.3124 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 31 THROUGH 35 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.8426 45.9509 -51.7197 REMARK 3 T TENSOR REMARK 3 T11: 2.3046 T22: 1.6091 REMARK 3 T33: 1.3674 T12: 0.3371 REMARK 3 T13: -0.0280 T23: 0.2172 REMARK 3 L TENSOR REMARK 3 L11: 6.5727 L22: 3.1192 REMARK 3 L33: 4.6320 L12: -1.1916 REMARK 3 L13: 4.9198 L23: -2.5526 REMARK 3 S TENSOR REMARK 3 S11: 0.2891 S12: 0.3681 S13: -0.9533 REMARK 3 S21: -0.3552 S22: -0.2118 S23: 0.9373 REMARK 3 S31: 1.6080 S32: 0.0104 S33: -0.0297 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 36 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.9126 46.6383 -60.3937 REMARK 3 T TENSOR REMARK 3 T11: 1.9776 T22: 2.0055 REMARK 3 T33: 1.7612 T12: -0.0274 REMARK 3 T13: 0.6012 T23: -0.0018 REMARK 3 L TENSOR REMARK 3 L11: 8.8581 L22: 2.6217 REMARK 3 L33: 4.6660 L12: 4.5379 REMARK 3 L13: -6.4002 L23: -3.1683 REMARK 3 S TENSOR REMARK 3 S11: 0.6217 S12: 3.4949 S13: 1.5736 REMARK 3 S21: -1.0504 S22: 2.3335 S23: -0.8977 REMARK 3 S31: -1.2592 S32: 0.1497 S33: -3.1324 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 12 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.6776 44.5854 -46.5283 REMARK 3 T TENSOR REMARK 3 T11: 1.8865 T22: 2.1146 REMARK 3 T33: 1.0704 T12: 0.1455 REMARK 3 T13: -0.0227 T23: -0.0199 REMARK 3 L TENSOR REMARK 3 L11: 8.8405 L22: 3.1606 REMARK 3 L33: 3.5246 L12: -1.6684 REMARK 3 L13: -5.5510 L23: 1.2136 REMARK 3 S TENSOR REMARK 3 S11: 1.1485 S12: 0.4033 S13: 0.1887 REMARK 3 S21: -1.0148 S22: -0.0594 S23: -0.0522 REMARK 3 S31: -0.7344 S32: 0.1313 S33: -1.0484 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.1354 25.2343 125.9197 REMARK 3 T TENSOR REMARK 3 T11: 1.5302 T22: 1.1345 REMARK 3 T33: 0.6652 T12: -0.1981 REMARK 3 T13: 0.1367 T23: 0.0810 REMARK 3 L TENSOR REMARK 3 L11: 2.0861 L22: 0.3317 REMARK 3 L33: 6.0285 L12: -0.4032 REMARK 3 L13: -1.4281 L23: -0.8579 REMARK 3 S TENSOR REMARK 3 S11: 0.3748 S12: -0.3180 S13: 0.0245 REMARK 3 S21: 0.8393 S22: 0.6764 S23: 0.2730 REMARK 3 S31: -1.2461 S32: -0.8971 S33: -0.8871 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 16 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.2963 23.2747 132.2939 REMARK 3 T TENSOR REMARK 3 T11: 1.8659 T22: 1.2760 REMARK 3 T33: 0.8864 T12: -0.0816 REMARK 3 T13: -0.0127 T23: 0.0747 REMARK 3 L TENSOR REMARK 3 L11: 2.4766 L22: 0.3724 REMARK 3 L33: 3.0520 L12: 0.1277 REMARK 3 L13: 1.9872 L23: 0.4141 REMARK 3 S TENSOR REMARK 3 S11: -0.0187 S12: -0.7200 S13: -0.5618 REMARK 3 S21: 1.6253 S22: 0.6134 S23: -0.0184 REMARK 3 S31: -1.6682 S32: 1.0184 S33: -0.4719 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 12 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.3764 21.2652 142.2519 REMARK 3 T TENSOR REMARK 3 T11: 1.8683 T22: 1.3894 REMARK 3 T33: 1.0476 T12: 0.1826 REMARK 3 T13: -0.2059 T23: -0.0564 REMARK 3 L TENSOR REMARK 3 L11: 3.2238 L22: 2.5853 REMARK 3 L33: 4.6611 L12: 0.5723 REMARK 3 L13: 1.1456 L23: -0.0877 REMARK 3 S TENSOR REMARK 3 S11: -0.0972 S12: -0.6446 S13: -0.4669 REMARK 3 S21: 0.5196 S22: 0.4789 S23: -0.3829 REMARK 3 S31: 0.4672 S32: -0.5896 S33: -0.4335 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 4 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'A' REMARK 3 SELECTION : CHAIN 'A' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'H' REMARK 3 SELECTION : CHAIN 'H' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'L' REMARK 3 SELECTION : CHAIN 'L' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN 'R' AND (RESID 1 THROUGH 30 OR REMARK 3 RESID 33 OR (RESID 34 AND (NAME P OR NAME REMARK 3 OP1 OR NAME OP2 OR NAME O5' OR NAME C5' REMARK 3 OR NAME C4' OR NAME O4' OR NAME C3' OR REMARK 3 NAME O3' OR NAME C2' OR NAME O2' OR NAME REMARK 3 C1' OR NAME C2 OR NAME O2 OR NAME N3 OR REMARK 3 NAME C4 OR NAME N4 OR NAME C5 OR NAME C6 ) REMARK 3 ) OR RESID 35 THROUGH 39)) REMARK 3 SELECTION : (CHAIN 'R' AND (RESID 1 THROUGH 30 OR REMARK 3 RESID 33 THROUGH 39)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6X5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1000249075. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-FEB-20 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 : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18323 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 72.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04500 REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.10800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 6B14 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL, 0.2 M LI2SO4, 22% PEG REMARK 280 3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: l, h, r, 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, R, 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 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 G R 40 REMARK 465 G R 41 REMARK 465 G R 42 REMARK 465 U R 43 REMARK 465 U R 44 REMARK 465 U R 45 REMARK 465 U R 46 REMARK 465 U R 47 REMARK 465 C R 48 REMARK 465 C R 49 REMARK 465 U R 50 REMARK 465 U R 51 REMARK 465 C R 52 REMARK 465 G R 53 REMARK 465 A R 54 REMARK 465 A R 55 REMARK 465 A R 56 REMARK 465 C R 57 REMARK 465 A R 58 REMARK 465 C R 59 REMARK 465 G R 60 REMARK 465 A R 61 REMARK 465 A R 62 REMARK 465 G R 63 REMARK 465 G R 64 REMARK 465 U R 65 REMARK 465 U R 66 REMARK 465 U R 67 REMARK 465 U R 68 REMARK 465 U R 69 REMARK 465 A R 70 REMARK 465 U R 71 REMARK 465 C R 72 REMARK 465 C R 73 REMARK 465 C R 74 REMARK 465 U R 75 REMARK 465 G R 76 REMARK 465 C R 77 REMARK 465 C R 78 REMARK 465 G r 40 REMARK 465 G r 41 REMARK 465 G r 42 REMARK 465 U r 43 REMARK 465 U r 44 REMARK 465 U r 45 REMARK 465 U r 46 REMARK 465 U r 47 REMARK 465 C r 48 REMARK 465 C r 49 REMARK 465 U r 50 REMARK 465 U r 51 REMARK 465 C r 52 REMARK 465 G r 53 REMARK 465 A r 54 REMARK 465 A r 55 REMARK 465 A r 56 REMARK 465 C r 57 REMARK 465 A r 58 REMARK 465 C r 59 REMARK 465 G r 60 REMARK 465 A r 61 REMARK 465 A r 62 REMARK 465 G r 63 REMARK 465 G r 64 REMARK 465 U r 65 REMARK 465 U r 66 REMARK 465 U r 67 REMARK 465 U r 68 REMARK 465 U r 69 REMARK 465 A r 70 REMARK 465 U r 71 REMARK 465 C r 72 REMARK 465 C r 73 REMARK 465 C r 74 REMARK 465 U r 75 REMARK 465 G r 76 REMARK 465 C r 77 REMARK 465 C r 78 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 C r 34 N1 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 GLN l 91 O HOH l 401 1.86 REMARK 500 OP2 A r 16 O HOH r 101 1.90 REMARK 500 NH2 ARG H 105 OP2 G R 14 2.05 REMARK 500 O SER l 53 O HOH l 402 2.09 REMARK 500 O LEU l 126 NZ LYS l 184 2.09 REMARK 500 NH2 ARG L 62 OD2 ASP L 83 2.09 REMARK 500 O ALA L 52 O HOH L 401 2.10 REMARK 500 O GLY h 13 O HOH h 301 2.12 REMARK 500 O6 G R 3 N4 C R 33 2.12 REMARK 500 OE2 GLU h 9 N GLY h 118 2.14 REMARK 500 O ARG l 25 O HOH l 403 2.15 REMARK 500 O6 G R 37 N4 C A 3 2.15 REMARK 500 OD2 ASP h 156 O HOH h 302 2.15 REMARK 500 O2 C R 20 O HOH R 101 2.17 REMARK 500 OE1 GLU L 214 O HOH L 402 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 LEU L 12 CA - CB - CG ANGL. DEV. = 16.4 DEGREES REMARK 500 G R 3 N7 - C8 - N9 ANGL. DEV. = 3.1 DEGREES REMARK 500 U R 11 O5' - P - OP1 ANGL. DEV. = -5.9 DEGREES REMARK 500 A R 17 C8 - N9 - C4 ANGL. DEV. = 2.5 DEGREES REMARK 500 U R 29 O5' - P - OP1 ANGL. DEV. = -9.1 DEGREES REMARK 500 A r 17 N9 - C4 - C5 ANGL. DEV. = 2.7 DEGREES REMARK 500 A r 17 N1 - C6 - N6 ANGL. DEV. = -4.5 DEGREES REMARK 500 U r 26 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES REMARK 500 U r 29 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES REMARK 500 U r 30 C6 - N1 - C1' ANGL. DEV. = -9.2 DEGREES REMARK 500 U r 30 C2 - N1 - C1' ANGL. DEV. = 9.3 DEGREES REMARK 500 C r 34 C2 - N3 - C4 ANGL. DEV. = 5.2 DEGREES REMARK 500 C r 34 N3 - C4 - C5 ANGL. DEV. = 6.7 DEGREES REMARK 500 C r 34 C4 - C5 - C6 ANGL. DEV. = 7.8 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 SER l 31 -137.34 58.54 REMARK 500 ALA l 52 -33.08 62.28 REMARK 500 SER l 53 -20.61 -141.38 REMARK 500 GLU l 82 -8.31 -51.92 REMARK 500 ALA l 85 -169.41 -160.40 REMARK 500 ASN l 139 82.53 51.83 REMARK 500 ASN l 153 -0.04 65.12 REMARK 500 LYS l 170 -62.37 -103.28 REMARK 500 SER l 209 -169.50 -167.07 REMARK 500 LYS h 46 -164.12 -100.95 REMARK 500 VAL h 51 -52.38 -121.81 REMARK 500 TYR h 57 -52.33 63.49 REMARK 500 SER h 108 14.38 -176.19 REMARK 500 SER h 142 -151.47 -142.69 REMARK 500 SER h 144 55.94 -115.74 REMARK 500 ASP h 156 84.25 61.78 REMARK 500 LYS h 226 -149.84 -95.58 REMARK 500 LYS H 46 -166.01 -101.57 REMARK 500 VAL H 51 -50.38 -123.70 REMARK 500 TYR H 57 -49.61 61.13 REMARK 500 SER H 108 -1.57 -163.62 REMARK 500 SER H 140 31.25 -61.74 REMARK 500 SER H 144 54.03 -101.93 REMARK 500 ASP H 156 84.00 58.25 REMARK 500 LYS H 226 -158.34 -96.07 REMARK 500 SER L 31 -134.83 56.44 REMARK 500 ALA L 52 -31.53 61.66 REMARK 500 PRO L 60 169.15 -49.48 REMARK 500 SER L 77 -80.66 -60.48 REMARK 500 ALA L 85 -166.85 -160.38 REMARK 500 ASN L 139 84.61 52.67 REMARK 500 ASN L 153 -0.39 62.79 REMARK 500 ASP L 186 1.19 -66.85 REMARK 500 ARG L 212 -101.38 -85.00 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 SO4 l 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301 DBREF 6X5N l 1 215 PDB 6X5N 6X5N 1 215 DBREF 6X5N h 4 228 PDB 6X5N 6X5N 4 228 DBREF 6X5N H 4 228 PDB 6X5N 6X5N 4 228 DBREF 6X5N L 1 215 PDB 6X5N 6X5N 1 215 DBREF 6X5N R 1 78 PDB 6X5N 6X5N 1 78 DBREF 6X5N A 1 12 PDB 6X5N 6X5N 1 12 DBREF 6X5N r 1 78 PDB 6X5N 6X5N 1 78 DBREF 6X5N a 1 12 PDB 6X5N 6X5N 1 12 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 h 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 h 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 h 225 PHE TYR ILE SER TYR SER SER ILE HIS TRP VAL ARG GLN SEQRES 4 h 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 h 225 PRO TYR SER GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 h 225 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 h 225 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 h 225 ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR ARG ARG ARG SEQRES 9 h 225 SER GLY ARG GLY PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 h 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 h 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 h 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 h 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 h 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 h 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 h 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 h 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 h 225 PRO LYS SER CYS SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 225 PHE TYR ILE SER TYR SER SER ILE HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 225 PRO TYR SER GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 225 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 H 225 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR ARG ARG ARG SEQRES 9 H 225 SER GLY ARG GLY PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS 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 78 G G G U U U U U C C U U C SEQRES 2 R 78 G A A A C A C G A A G G U SEQRES 3 R 78 U U U U A U C C C U G C C SEQRES 4 R 78 G G G U U U U U C C U U C SEQRES 5 R 78 G A A A C A C G A A G G U SEQRES 6 R 78 U U U U A U C C C U G C C SEQRES 1 A 12 G G C A A A A A A A A A SEQRES 1 r 78 G G G U U U U U C C U U C SEQRES 2 r 78 G A A A C A C G A A G G U SEQRES 3 r 78 U U U U A U C C C U G C C SEQRES 4 r 78 G G G U U U U U C C U U C SEQRES 5 r 78 G A A A C A C G A A G G U SEQRES 6 r 78 U U U U A U C C C U G C C SEQRES 1 a 12 G G C A A A A A A A A A HET SO4 l 301 5 HET SO4 L 301 5 HETNAM SO4 SULFATE ION FORMUL 9 SO4 2(O4 S 2-) FORMUL 11 HOH *63(H2 O) HELIX 1 AA1 GLN l 80 PHE l 84 5 5 HELIX 2 AA2 SER l 122 LYS l 127 1 6 HELIX 3 AA3 LYS l 184 HIS l 190 1 7 HELIX 4 AA4 TYR h 31 SER h 35 5 5 HELIX 5 AA5 ARG h 90 THR h 94 5 5 HELIX 6 AA6 TYR h 104 GLY h 109 1 6 HELIX 7 AA7 SER h 168 ALA h 170 5 3 HELIX 8 AA8 SER h 199 LEU h 201 5 3 HELIX 9 AA9 TYR H 31 SER H 35 5 5 HELIX 10 AB1 ARG H 90 THR H 94 5 5 HELIX 11 AB2 SER H 168 ALA H 170 5 3 HELIX 12 AB3 SER H 199 LEU H 201 5 3 HELIX 13 AB4 GLN L 80 PHE L 84 5 5 HELIX 14 AB5 SER L 122 LYS L 127 1 6 HELIX 15 AB6 LYS L 184 GLU L 188 5 5 SHEET 1 AA1 4 MET l 5 SER l 8 0 SHEET 2 AA1 4 VAL l 20 ALA l 26 -1 O THR l 23 N SER l 8 SHEET 3 AA1 4 ASP l 71 ILE l 76 -1 O PHE l 72 N CYS l 24 SHEET 4 AA1 4 PHE l 63 SER l 68 -1 N SER l 68 O ASP l 71 SHEET 1 AA2 6 SER l 11 SER l 15 0 SHEET 2 AA2 6 THR l 103 LYS l 108 1 O GLU l 106 N LEU l 12 SHEET 3 AA2 6 ALA l 85 GLN l 91 -1 N TYR l 87 O THR l 103 SHEET 4 AA2 6 VAL l 34 GLN l 39 -1 N ALA l 35 O GLN l 90 SHEET 5 AA2 6 LYS l 46 TYR l 50 -1 O LEU l 48 N TRP l 36 SHEET 6 AA2 6 SER l 54 LEU l 55 -1 O SER l 54 N TYR l 50 SHEET 1 AA3 4 SER l 11 SER l 15 0 SHEET 2 AA3 4 THR l 103 LYS l 108 1 O GLU l 106 N LEU l 12 SHEET 3 AA3 4 ALA l 85 GLN l 91 -1 N TYR l 87 O THR l 103 SHEET 4 AA3 4 THR l 98 PHE l 99 -1 O THR l 98 N GLN l 91 SHEET 1 AA4 4 SER l 115 PHE l 119 0 SHEET 2 AA4 4 THR l 130 PHE l 140 -1 O LEU l 136 N PHE l 117 SHEET 3 AA4 4 TYR l 174 SER l 183 -1 O SER l 178 N CYS l 135 SHEET 4 AA4 4 SER l 160 VAL l 164 -1 N SER l 163 O SER l 177 SHEET 1 AA5 4 ALA l 154 GLN l 156 0 SHEET 2 AA5 4 LYS l 146 VAL l 151 -1 N TRP l 149 O GLN l 156 SHEET 3 AA5 4 TYR l 193 THR l 198 -1 O GLU l 196 N GLN l 148 SHEET 4 AA5 4 VAL l 206 LYS l 208 -1 O VAL l 206 N VAL l 197 SHEET 1 AA6 4 GLN h 6 SER h 10 0 SHEET 2 AA6 4 LEU h 21 SER h 28 -1 O ALA h 26 N VAL h 8 SHEET 3 AA6 4 THR h 81 MET h 86 -1 O MET h 86 N LEU h 21 SHEET 4 AA6 4 PHE h 71 ASP h 76 -1 N ASP h 76 O THR h 81 SHEET 1 AA7 6 LEU h 14 VAL h 15 0 SHEET 2 AA7 6 THR h 119 VAL h 123 1 O THR h 122 N VAL h 15 SHEET 3 AA7 6 ALA h 95 GLN h 102 -1 N ALA h 95 O VAL h 121 SHEET 4 AA7 6 ILE h 37 GLN h 42 -1 N VAL h 40 O TYR h 98 SHEET 5 AA7 6 LEU h 48 ILE h 54 -1 O GLU h 49 N ARG h 41 SHEET 6 AA7 6 THR h 61 TYR h 63 -1 O TYR h 62 N SER h 53 SHEET 1 AA8 4 LEU h 14 VAL h 15 0 SHEET 2 AA8 4 THR h 119 VAL h 123 1 O THR h 122 N VAL h 15 SHEET 3 AA8 4 ALA h 95 GLN h 102 -1 N ALA h 95 O VAL h 121 SHEET 4 AA8 4 PHE h 112 TRP h 115 -1 O TYR h 114 N ARG h 101 SHEET 1 AA9 4 SER h 132 LEU h 136 0 SHEET 2 AA9 4 THR h 147 TYR h 157 -1 O GLY h 151 N LEU h 136 SHEET 3 AA9 4 TYR h 188 PRO h 197 -1 O TYR h 188 N TYR h 157 SHEET 4 AA9 4 VAL h 175 THR h 177 -1 N HIS h 176 O VAL h 193 SHEET 1 AB1 4 SER h 132 LEU h 136 0 SHEET 2 AB1 4 THR h 147 TYR h 157 -1 O GLY h 151 N LEU h 136 SHEET 3 AB1 4 TYR h 188 PRO h 197 -1 O TYR h 188 N TYR h 157 SHEET 4 AB1 4 VAL h 181 LEU h 182 -1 N VAL h 181 O SER h 189 SHEET 1 AB2 3 THR h 163 TRP h 166 0 SHEET 2 AB2 3 TYR h 206 HIS h 212 -1 O ASN h 209 N SER h 165 SHEET 3 AB2 3 THR h 217 VAL h 223 -1 O THR h 217 N HIS h 212 SHEET 1 AB3 4 GLN H 6 SER H 10 0 SHEET 2 AB3 4 LEU H 21 SER H 28 -1 O SER H 24 N SER H 10 SHEET 3 AB3 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AB3 4 PHE H 71 ASP H 76 -1 N ASP H 76 O THR H 81 SHEET 1 AB4 6 LEU H 14 VAL H 15 0 SHEET 2 AB4 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AB4 6 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AB4 6 ILE H 37 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AB4 6 LEU H 48 ILE H 54 -1 O ALA H 52 N TRP H 39 SHEET 6 AB4 6 THR H 61 TYR H 63 -1 O TYR H 62 N SER H 53 SHEET 1 AB5 4 LEU H 14 VAL H 15 0 SHEET 2 AB5 4 THR H 119 VAL H 123 1 O THR H 122 N VAL H 15 SHEET 3 AB5 4 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AB5 4 PHE H 112 TRP H 115 -1 O TYR H 114 N ARG H 101 SHEET 1 AB6 4 SER H 132 LEU H 136 0 SHEET 2 AB6 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136 SHEET 3 AB6 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AB6 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AB7 4 SER H 132 LEU H 136 0 SHEET 2 AB7 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136 SHEET 3 AB7 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AB7 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AB8 3 THR H 163 TRP H 166 0 SHEET 2 AB8 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AB8 3 THR H 217 VAL H 223 -1 O VAL H 219 N VAL H 210 SHEET 1 AB9 4 MET L 5 SER L 8 0 SHEET 2 AB9 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AB9 4 ASP L 71 ILE L 76 -1 O LEU L 74 N ILE L 22 SHEET 4 AB9 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AC1 6 SER L 11 ALA L 14 0 SHEET 2 AC1 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AC1 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AC1 6 VAL L 34 GLN L 39 -1 N ALA L 35 O GLN L 90 SHEET 5 AC1 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AC1 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AC2 4 SER L 115 PHE L 119 0 SHEET 2 AC2 4 VAL L 133 PHE L 140 -1 O ASN L 138 N SER L 115 SHEET 3 AC2 4 TYR L 174 LEU L 180 -1 O TYR L 174 N PHE L 140 SHEET 4 AC2 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AC3 4 ALA L 154 LEU L 155 0 SHEET 2 AC3 4 VAL L 147 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AC3 4 TYR L 193 VAL L 197 -1 O GLU L 196 N GLN L 148 SHEET 4 AC3 4 VAL L 206 LYS L 208 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS l 24 CYS l 89 1555 1555 2.01 SSBOND 2 CYS l 135 CYS l 195 1555 1555 2.06 SSBOND 3 CYS h 25 CYS h 99 1555 1555 2.05 SSBOND 4 CYS h 152 CYS h 208 1555 1555 2.05 SSBOND 5 CYS H 25 CYS H 99 1555 1555 2.06 SSBOND 6 CYS H 152 CYS H 208 1555 1555 2.05 SSBOND 7 CYS L 24 CYS L 89 1555 1555 2.05 SSBOND 8 CYS L 135 CYS L 195 1555 1555 2.03 CISPEP 1 SER l 8 PRO l 9 0 0.77 CISPEP 2 PHE l 95 PRO l 96 0 -4.80 CISPEP 3 TYR l 141 PRO l 142 0 -3.96 CISPEP 4 PHE h 158 PRO h 159 0 -8.19 CISPEP 5 GLU h 160 PRO h 161 0 -0.53 CISPEP 6 PHE H 158 PRO H 159 0 -10.18 CISPEP 7 GLU H 160 PRO H 161 0 2.60 CISPEP 8 SER L 8 PRO L 9 0 1.15 CISPEP 9 PHE L 95 PRO L 96 0 -5.45 CISPEP 10 TYR L 141 PRO L 142 0 -4.07 SITE 1 AC1 3 SER l 31 SER l 32 ARG l 67 SITE 1 AC2 2 SER L 31 ARG L 67 CRYST1 43.299 76.182 110.523 72.22 88.58 86.57 P 1 2 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 0.023095 -0.001385 -0.000157 0.00000 SCALE2 0.000000 0.013150 -0.004203 0.00000 SCALE3 0.000000 0.000000 0.009502 0.00000