HEADER IMMUNE SYSTEM 15-AUG-19 6U12 TITLE VHH R303 C33A/C102A IN COMPLEX WITHTHE LRR DOMAIN OF INLB COMPND MOL_ID: 1; COMPND 2 MOLECULE: INLB; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VHH R303 C33A/C102A MUTANT; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES; SOURCE 3 ORGANISM_TAXID: 1639; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 8 ORGANISM_TAXID: 9838; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, VHH, INTERNALIN, LISTERIA, DISULFIDE BOND, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.N.MENDOZA,M.JIAN,M.TORIDE KING,C.L.BROOKS REVDAT 1 12-FEB-20 6U12 0 JRNL AUTH M.N.MENDOZA,M.JIAN,M.T.KING,C.L.BROOKS JRNL TITL ROLE OF A NON-CANONICAL DISULFIDE BOND IN THE STABILITY, JRNL TITL 2 AFFINITY AND FLEXIBILITY OF A VHH SPECIFIC FOR THE LISTERIA JRNL TITL 3 VIRULENCE FACTOR INLB. JRNL REF PROTEIN SCI. 2020 JRNL REFN ESSN 1469-896X JRNL PMID 31981247 JRNL DOI 10.1002/PRO.3831 REMARK 2 REMARK 2 RESOLUTION. 1.56 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.19 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 62672 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.176 REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.199 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3134 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 51.1900 - 4.3701 1.00 2783 169 0.1572 0.1932 REMARK 3 2 4.3701 - 3.4689 1.00 2747 170 0.1437 0.1531 REMARK 3 3 3.4689 - 3.0304 1.00 2735 137 0.1620 0.2088 REMARK 3 4 3.0304 - 2.7534 1.00 2738 155 0.1639 0.2188 REMARK 3 5 2.7534 - 2.5560 1.00 2715 161 0.1670 0.1792 REMARK 3 6 2.5560 - 2.4054 1.00 2710 151 0.1657 0.1561 REMARK 3 7 2.4054 - 2.2849 1.00 2779 117 0.1717 0.2111 REMARK 3 8 2.2849 - 2.1854 1.00 2710 140 0.1689 0.1973 REMARK 3 9 2.1854 - 2.1013 1.00 2744 112 0.1740 0.1700 REMARK 3 10 2.1013 - 2.0288 1.00 2715 134 0.1729 0.1953 REMARK 3 11 2.0288 - 1.9653 1.00 2748 146 0.1896 0.2106 REMARK 3 12 1.9653 - 1.9092 1.00 2702 144 0.2015 0.2262 REMARK 3 13 1.9092 - 1.8589 1.00 2696 147 0.1993 0.2429 REMARK 3 14 1.8589 - 1.8135 1.00 2746 131 0.2037 0.2739 REMARK 3 15 1.8135 - 1.7723 1.00 2704 152 0.2119 0.2233 REMARK 3 16 1.7723 - 1.7346 1.00 2680 167 0.2230 0.2711 REMARK 3 17 1.7346 - 1.6999 1.00 2773 101 0.2338 0.2629 REMARK 3 18 1.6999 - 1.6678 1.00 2691 149 0.2450 0.2647 REMARK 3 19 1.6678 - 1.6380 0.99 2694 152 0.2562 0.2846 REMARK 3 20 1.6380 - 1.6103 0.99 2720 125 0.2760 0.3108 REMARK 3 21 1.6103 - 1.5843 0.96 2596 129 0.2869 0.2465 REMARK 3 22 1.5843 - 1.5600 0.90 2412 145 0.2915 0.3004 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.120 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.12 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.0455 -9.8584 -9.5617 REMARK 3 T TENSOR REMARK 3 T11: 0.2306 T22: 0.3820 REMARK 3 T33: 0.4514 T12: -0.0270 REMARK 3 T13: -0.1325 T23: -0.0273 REMARK 3 L TENSOR REMARK 3 L11: 1.2786 L22: 4.7784 REMARK 3 L33: 2.1374 L12: -0.4969 REMARK 3 L13: 1.4571 L23: 0.6808 REMARK 3 S TENSOR REMARK 3 S11: 0.4385 S12: 0.2698 S13: -0.6404 REMARK 3 S21: -0.3599 S22: -0.0960 S23: 0.5256 REMARK 3 S31: 0.5856 S32: -0.1608 S33: -0.3465 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.4211 -0.8587 -5.9642 REMARK 3 T TENSOR REMARK 3 T11: 0.1583 T22: 0.2942 REMARK 3 T33: 0.3549 T12: -0.0012 REMARK 3 T13: -0.0244 T23: 0.0175 REMARK 3 L TENSOR REMARK 3 L11: 3.2287 L22: 1.3781 REMARK 3 L33: 2.3897 L12: 0.6054 REMARK 3 L13: 1.4655 L23: 0.1406 REMARK 3 S TENSOR REMARK 3 S11: 0.1036 S12: -0.1942 S13: -0.2379 REMARK 3 S21: -0.0474 S22: 0.0187 S23: 0.5962 REMARK 3 S31: 0.0797 S32: -0.3645 S33: -0.1296 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.4222 -5.5044 4.4768 REMARK 3 T TENSOR REMARK 3 T11: 0.1745 T22: 0.2721 REMARK 3 T33: 0.2926 T12: -0.0459 REMARK 3 T13: -0.0151 T23: 0.0904 REMARK 3 L TENSOR REMARK 3 L11: 4.5067 L22: 9.1000 REMARK 3 L33: 7.8097 L12: 1.1349 REMARK 3 L13: 2.2410 L23: 6.3515 REMARK 3 S TENSOR REMARK 3 S11: 0.2831 S12: -0.4350 S13: -0.5258 REMARK 3 S21: 0.4604 S22: -0.0902 S23: 0.2328 REMARK 3 S31: 0.4213 S32: -0.5375 S33: -0.1145 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.2556 -4.2642 -3.6575 REMARK 3 T TENSOR REMARK 3 T11: 0.1043 T22: 0.2436 REMARK 3 T33: 0.2589 T12: 0.0074 REMARK 3 T13: -0.0390 T23: -0.0477 REMARK 3 L TENSOR REMARK 3 L11: 2.1162 L22: 3.8482 REMARK 3 L33: 4.0164 L12: 0.3490 REMARK 3 L13: 1.5824 L23: -0.3718 REMARK 3 S TENSOR REMARK 3 S11: 0.1746 S12: 0.1774 S13: -0.4833 REMARK 3 S21: -0.1663 S22: 0.0295 S23: 0.1146 REMARK 3 S31: 0.3037 S32: -0.0029 S33: -0.1913 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.9201 -2.6796 4.1492 REMARK 3 T TENSOR REMARK 3 T11: 0.1167 T22: 0.2256 REMARK 3 T33: 0.1993 T12: -0.0235 REMARK 3 T13: -0.0594 T23: -0.0265 REMARK 3 L TENSOR REMARK 3 L11: 5.3526 L22: 6.1919 REMARK 3 L33: 4.9351 L12: 0.2414 REMARK 3 L13: -2.1290 L23: 0.0925 REMARK 3 S TENSOR REMARK 3 S11: 0.1460 S12: -0.1968 S13: -0.4753 REMARK 3 S21: 0.2437 S22: 0.1587 S23: 0.0233 REMARK 3 S31: 0.1563 S32: -0.1960 S33: -0.2709 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 158 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.8457 -4.0845 1.1836 REMARK 3 T TENSOR REMARK 3 T11: 0.1297 T22: 0.1709 REMARK 3 T33: 0.2397 T12: -0.0326 REMARK 3 T13: -0.0279 T23: -0.0425 REMARK 3 L TENSOR REMARK 3 L11: 3.0003 L22: 4.4128 REMARK 3 L33: 3.5361 L12: -1.5955 REMARK 3 L13: 1.4196 L23: -1.2187 REMARK 3 S TENSOR REMARK 3 S11: 0.1453 S12: 0.1789 S13: -0.4474 REMARK 3 S21: -0.2294 S22: -0.0003 S23: 0.0297 REMARK 3 S31: 0.2408 S32: -0.1035 S33: -0.1510 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.7194 -0.5684 2.3929 REMARK 3 T TENSOR REMARK 3 T11: 0.1287 T22: 0.1650 REMARK 3 T33: 0.1646 T12: 0.0109 REMARK 3 T13: -0.0268 T23: -0.0655 REMARK 3 L TENSOR REMARK 3 L11: 2.7041 L22: 2.3303 REMARK 3 L33: 2.0733 L12: -0.8927 REMARK 3 L13: -0.1435 L23: 0.4083 REMARK 3 S TENSOR REMARK 3 S11: 0.0929 S12: 0.1340 S13: -0.2451 REMARK 3 S21: -0.1286 S22: 0.0240 S23: -0.1285 REMARK 3 S31: 0.0846 S32: 0.0292 S33: -0.1049 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.2296 2.9999 8.0745 REMARK 3 T TENSOR REMARK 3 T11: 0.1610 T22: 0.1727 REMARK 3 T33: 0.1716 T12: -0.0021 REMARK 3 T13: -0.0627 T23: -0.0741 REMARK 3 L TENSOR REMARK 3 L11: 5.2798 L22: 4.5201 REMARK 3 L33: 2.1694 L12: -0.0487 REMARK 3 L13: -1.3416 L23: -1.1767 REMARK 3 S TENSOR REMARK 3 S11: -0.0012 S12: -0.0273 S13: -0.1748 REMARK 3 S21: -0.0350 S22: 0.0310 S23: -0.1846 REMARK 3 S31: 0.0962 S32: 0.0423 S33: -0.0261 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.2602 5.0083 14.8197 REMARK 3 T TENSOR REMARK 3 T11: 0.1972 T22: 0.1863 REMARK 3 T33: 0.1715 T12: 0.0155 REMARK 3 T13: -0.0434 T23: -0.0396 REMARK 3 L TENSOR REMARK 3 L11: 3.2547 L22: 2.5537 REMARK 3 L33: 2.4244 L12: -1.0146 REMARK 3 L13: 1.4233 L23: -1.0096 REMARK 3 S TENSOR REMARK 3 S11: -0.0368 S12: -0.2297 S13: -0.1702 REMARK 3 S21: 0.1439 S22: 0.1143 S23: -0.0802 REMARK 3 S31: -0.1338 S32: -0.0356 S33: -0.0667 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 243 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.1279 9.7905 11.8966 REMARK 3 T TENSOR REMARK 3 T11: 0.2428 T22: 0.1635 REMARK 3 T33: 0.1968 T12: -0.0169 REMARK 3 T13: -0.0796 T23: -0.0633 REMARK 3 L TENSOR REMARK 3 L11: 2.7315 L22: 2.4879 REMARK 3 L33: 4.4092 L12: -0.7692 REMARK 3 L13: 0.5669 L23: -1.9628 REMARK 3 S TENSOR REMARK 3 S11: -0.1139 S12: -0.1021 S13: 0.0751 REMARK 3 S21: 0.0901 S22: 0.1081 S23: -0.1492 REMARK 3 S31: -0.0422 S32: -0.1542 S33: 0.0210 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.3345 23.4142 14.9072 REMARK 3 T TENSOR REMARK 3 T11: 0.7522 T22: 0.3589 REMARK 3 T33: 0.2332 T12: 0.2869 REMARK 3 T13: 0.1731 T23: -0.0192 REMARK 3 L TENSOR REMARK 3 L11: 4.5560 L22: 4.1620 REMARK 3 L33: 1.6917 L12: -0.0913 REMARK 3 L13: -0.6188 L23: -2.2176 REMARK 3 S TENSOR REMARK 3 S11: 0.1286 S12: 0.0487 S13: -0.2307 REMARK 3 S21: 0.9086 S22: -0.0642 S23: 0.3261 REMARK 3 S31: -0.2340 S32: -0.1918 S33: 0.0500 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.0141 40.3041 -0.0167 REMARK 3 T TENSOR REMARK 3 T11: 0.4931 T22: 0.3235 REMARK 3 T33: 0.3656 T12: 0.1996 REMARK 3 T13: 0.1521 T23: 0.1221 REMARK 3 L TENSOR REMARK 3 L11: 3.4179 L22: 2.1081 REMARK 3 L33: 3.1981 L12: 2.4883 REMARK 3 L13: -0.4607 L23: -1.2744 REMARK 3 S TENSOR REMARK 3 S11: -0.7797 S12: -0.4421 S13: -0.1610 REMARK 3 S21: 1.1638 S22: 0.9004 S23: 0.7120 REMARK 3 S31: -0.5046 S32: -0.6288 S33: -0.2894 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.3135 30.1825 10.7352 REMARK 3 T TENSOR REMARK 3 T11: 0.7526 T22: 0.2763 REMARK 3 T33: 0.2305 T12: 0.1634 REMARK 3 T13: -0.0608 T23: -0.0773 REMARK 3 L TENSOR REMARK 3 L11: 1.6869 L22: 3.2609 REMARK 3 L33: 5.1478 L12: -1.1197 REMARK 3 L13: 1.4559 L23: -4.1056 REMARK 3 S TENSOR REMARK 3 S11: -0.3339 S12: 0.0147 S13: 0.4152 REMARK 3 S21: 1.4114 S22: 0.0116 S23: -0.3067 REMARK 3 S31: -0.9271 S32: -0.2172 S33: 0.1104 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.1016 20.0374 9.5454 REMARK 3 T TENSOR REMARK 3 T11: 0.2838 T22: 0.2118 REMARK 3 T33: 0.1606 T12: 0.0922 REMARK 3 T13: 0.0128 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: 3.2059 L22: 2.7720 REMARK 3 L33: 2.7968 L12: 0.2850 REMARK 3 L13: -0.6893 L23: -0.3522 REMARK 3 S TENSOR REMARK 3 S11: -0.4538 S12: -0.6128 S13: -0.0754 REMARK 3 S21: 0.7696 S22: 0.5335 S23: 0.2317 REMARK 3 S31: -0.4184 S32: -0.4168 S33: -0.1828 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.7459 21.2612 1.1799 REMARK 3 T TENSOR REMARK 3 T11: 0.1996 T22: 0.2436 REMARK 3 T33: 0.1742 T12: -0.0187 REMARK 3 T13: 0.0047 T23: -0.0054 REMARK 3 L TENSOR REMARK 3 L11: 4.4023 L22: 7.0564 REMARK 3 L33: 4.3725 L12: -1.2046 REMARK 3 L13: 4.3783 L23: -1.1120 REMARK 3 S TENSOR REMARK 3 S11: 0.2932 S12: -0.0748 S13: -0.2630 REMARK 3 S21: -0.2805 S22: -0.0059 S23: 0.4298 REMARK 3 S31: 0.4943 S32: -0.2610 S33: -0.3209 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.7031 28.0608 4.0777 REMARK 3 T TENSOR REMARK 3 T11: 0.3189 T22: 0.1631 REMARK 3 T33: 0.2175 T12: 0.0344 REMARK 3 T13: -0.0717 T23: -0.0268 REMARK 3 L TENSOR REMARK 3 L11: 3.8326 L22: 3.0190 REMARK 3 L33: 2.3443 L12: -0.7918 REMARK 3 L13: 1.4188 L23: -0.5466 REMARK 3 S TENSOR REMARK 3 S11: -0.2754 S12: -0.0020 S13: 0.4420 REMARK 3 S21: 0.6461 S22: 0.1367 S23: -0.6400 REMARK 3 S31: -0.2432 S32: 0.1204 S33: 0.1267 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.7491 35.3462 -5.6776 REMARK 3 T TENSOR REMARK 3 T11: 0.3429 T22: 0.2680 REMARK 3 T33: 0.3461 T12: -0.0232 REMARK 3 T13: -0.0687 T23: 0.0812 REMARK 3 L TENSOR REMARK 3 L11: 1.8196 L22: 3.0397 REMARK 3 L33: 3.1721 L12: 0.8155 REMARK 3 L13: 0.0618 L23: 2.8343 REMARK 3 S TENSOR REMARK 3 S11: -0.2766 S12: 0.4931 S13: 0.7913 REMARK 3 S21: -0.7483 S22: 0.3339 S23: 0.4554 REMARK 3 S31: -0.5005 S32: -0.1302 S33: -0.0928 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.3834 20.8847 4.1865 REMARK 3 T TENSOR REMARK 3 T11: 0.2042 T22: 0.2155 REMARK 3 T33: 0.2307 T12: 0.0581 REMARK 3 T13: 0.0384 T23: 0.0488 REMARK 3 L TENSOR REMARK 3 L11: 1.1028 L22: 3.8771 REMARK 3 L33: 1.5835 L12: -0.1888 REMARK 3 L13: -0.3867 L23: -1.5696 REMARK 3 S TENSOR REMARK 3 S11: -0.1689 S12: 0.1187 S13: 0.2250 REMARK 3 S21: 0.5064 S22: 0.3856 S23: 0.5017 REMARK 3 S31: -0.2842 S32: -0.2270 S33: -0.1566 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 6U12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-19. REMARK 100 THE DEPOSITION ID IS D_1000243719. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.1 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62702 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560 REMARK 200 RESOLUTION RANGE LOW (A) : 64.920 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : 0.06300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.61300 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: 6DBF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.49 M SODIUM PHOSPHATE MONOBASIC REMARK 280 MONOHYDRATE, 0.91 M POTASSIUM PHOSPHATE DIBASIC PH 6.8., VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y,X,Z+3/4 REMARK 290 4555 Y,-X,Z+1/4 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 32.46500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.69750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.23250 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 21 REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 HIS A 24 REMARK 465 HIS A 25 REMARK 465 HIS A 26 REMARK 465 HIS A 27 REMARK 465 HIS A 28 REMARK 465 HIS A 29 REMARK 465 GLU A 30 REMARK 465 ASN A 31 REMARK 465 LEU A 32 REMARK 465 TYR A 33 REMARK 465 PHE A 34 REMARK 465 GLN A 35 REMARK 465 GLY A 36 REMARK 465 LEU A 244 REMARK 465 ASN A 245 REMARK 465 LYS A 246 REMARK 465 PRO A 247 REMARK 465 ILE A 248 REMARK 465 ASN A 249 REMARK 465 PRO B 41 REMARK 465 GLY B 42 REMARK 465 LYS B 43 REMARK 465 GLY B 124 REMARK 465 SER B 125 REMARK 465 GLU B 126 REMARK 465 GLN B 127 REMARK 465 LYS B 128 REMARK 465 LEU B 129 REMARK 465 ILE B 130 REMARK 465 SER B 131 REMARK 465 GLU B 132 REMARK 465 GLU B 133 REMARK 465 ASP B 134 REMARK 465 LEU B 135 REMARK 465 ASN B 136 REMARK 465 HIS B 137 REMARK 465 HIS B 138 REMARK 465 HIS B 139 REMARK 465 HIS B 140 REMARK 465 HIS B 141 REMARK 465 HIS B 142 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 LYS A 46 CG CD CE NZ REMARK 470 LYS A 63 CE NZ REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 LYS A 132 NZ REMARK 470 LYS A 144 NZ REMARK 470 LYS A 146 CE NZ REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 LYS B 3 CG CD CE NZ REMARK 470 GLU B 5 CG CD OE1 OE2 REMARK 470 VAL B 40 CG1 CG2 REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 66 CG OD1 OD2 REMARK 470 LYS B 76 CG CD CE NZ REMARK 470 GLU B 89 CG CD OE1 OE2 REMARK 470 GLN B 115 CG CD OE1 NE2 REMARK 470 THR B 117 CG2 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 ALA A 84 48.28 -142.71 REMARK 500 LEU A 98 73.26 -113.56 REMARK 500 ASN A 109 -163.84 -128.31 REMARK 500 ASN A 131 -161.81 -117.69 REMARK 500 LEU A 164 53.31 -117.54 REMARK 500 ASN A 175 -156.06 -128.56 REMARK 500 ASP A 196 62.29 60.03 REMARK 500 ASN A 197 -154.25 -135.36 REMARK 500 ASN A 219 -153.13 -126.69 REMARK 500 REMARK 500 REMARK: NULL DBREF 6U12 A 37 249 UNP Q45GD4 Q45GD4_LISMN 36 248 DBREF 6U12 B 1 142 PDB 6U12 6U12 1 142 SEQADV 6U12 MET A 21 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 GLY A 22 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 SER A 23 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 24 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 25 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 26 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 27 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 28 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 HIS A 29 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 GLU A 30 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 ASN A 31 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 LEU A 32 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 TYR A 33 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 PHE A 34 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 GLN A 35 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 GLY A 36 UNP Q45GD4 EXPRESSION TAG SEQADV 6U12 VAL A 118 UNP Q45GD4 THR 117 ENGINEERED MUTATION SEQADV 6U12 ALA A 243 UNP Q45GD4 CYS 242 ENGINEERED MUTATION SEQRES 1 A 229 MET GLY SER HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 A 229 PHE GLN GLY GLU THR ILE THR VAL SER THR PRO ILE LYS SEQRES 3 A 229 GLN ILE PHE PRO ASP ASP ALA PHE ALA GLU THR ILE LYS SEQRES 4 A 229 ASP ASN LEU LYS LYS LYS SER VAL THR ASP ALA VAL THR SEQRES 5 A 229 GLN ASN GLU LEU ASN SER ILE ASP GLN ILE ILE ALA ASN SEQRES 6 A 229 ASN SER ASP ILE LYS SER VAL GLN GLY ILE GLN TYR LEU SEQRES 7 A 229 PRO ASN VAL THR LYS LEU PHE LEU ASN GLY ASN LYS LEU SEQRES 8 A 229 THR ASP ILE LYS PRO LEU VAL ASN LEU LYS ASN LEU GLY SEQRES 9 A 229 TRP LEU PHE LEU ASP GLU ASN LYS ILE LYS ASP LEU SER SEQRES 10 A 229 SER LEU LYS ASP LEU LYS LYS LEU LYS SER LEU SER LEU SEQRES 11 A 229 GLU HIS ASN GLY ILE SER ASP ILE ASN GLY LEU VAL HIS SEQRES 12 A 229 LEU PRO GLN LEU GLU SER LEU TYR LEU GLY ASN ASN LYS SEQRES 13 A 229 ILE THR ASP ILE THR VAL LEU SER ARG LEU THR LYS LEU SEQRES 14 A 229 ASP THR LEU SER LEU GLU ASP ASN GLN ILE SER ASP ILE SEQRES 15 A 229 VAL PRO LEU ALA GLY LEU THR LYS LEU GLN ASN LEU TYR SEQRES 16 A 229 LEU SER LYS ASN HIS ILE SER ASP LEU ARG ALA LEU ALA SEQRES 17 A 229 GLY LEU LYS ASN LEU ASP VAL LEU GLU LEU PHE SER GLN SEQRES 18 A 229 GLU ALA LEU ASN LYS PRO ILE ASN SEQRES 1 B 142 GLN VAL LYS LEU GLU GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 B 142 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 142 HIS THR TYR SER THR TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 B 142 VAL PRO GLY LYS GLU ARG GLU GLY VAL ALA ARG ILE ASN SEQRES 5 B 142 VAL GLY GLY SER SER THR TRP TYR ALA ASP SER VAL ARG SEQRES 6 B 142 ASP ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 B 142 VAL TYR LEU GLN MET ASN SER LEU LYS LEU GLU ASP THR SEQRES 8 B 142 ALA ILE TYR TYR CYS THR LEU HIS ARG PHE ALA ASN THR SEQRES 9 B 142 TRP SER LEU GLY THR LEU ASN VAL TRP GLY GLN GLY THR SEQRES 10 B 142 GLN VAL THR VAL SER SER GLY SER GLU GLN LYS LEU ILE SEQRES 11 B 142 SER GLU GLU ASP LEU ASN HIS HIS HIS HIS HIS HIS FORMUL 3 HOH *404(H2 O) HELIX 1 AA1 ILE A 45 PHE A 49 1 5 HELIX 2 AA2 ASP A 51 LEU A 62 1 12 HELIX 3 AA3 THR A 72 SER A 78 1 7 HELIX 4 AA4 GLY A 94 LEU A 98 5 5 HELIX 5 AA5 ILE A 114 VAL A 118 5 5 HELIX 6 AA6 LEU A 136 LYS A 140 5 5 HELIX 7 AA7 ILE A 158 LEU A 164 5 7 HELIX 8 AA8 ILE A 180 LEU A 186 5 7 HELIX 9 AA9 ILE A 202 ALA A 206 5 5 HELIX 10 AB1 LEU A 224 ALA A 228 5 5 HELIX 11 AB2 LYS B 87 THR B 91 5 5 HELIX 12 AB3 PHE B 101 SER B 106 1 6 SHEET 1 AA1 2 THR A 43 PRO A 44 0 SHEET 2 AA1 2 ALA A 70 VAL A 71 -1 O VAL A 71 N THR A 43 SHEET 1 AA2 8 GLN A 81 ILE A 83 0 SHEET 2 AA2 8 LYS A 103 PHE A 105 1 O PHE A 105 N ILE A 82 SHEET 3 AA2 8 TRP A 125 PHE A 127 1 O PHE A 127 N LEU A 104 SHEET 4 AA2 8 SER A 147 SER A 149 1 O SER A 147 N LEU A 126 SHEET 5 AA2 8 SER A 169 TYR A 171 1 O TYR A 171 N LEU A 148 SHEET 6 AA2 8 THR A 191 SER A 193 1 O SER A 193 N LEU A 170 SHEET 7 AA2 8 ASN A 213 TYR A 215 1 O ASN A 213 N LEU A 192 SHEET 8 AA2 8 VAL A 235 GLU A 237 1 O VAL A 235 N LEU A 214 SHEET 1 AA3 4 LYS B 3 SER B 7 0 SHEET 2 AA3 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA3 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA3 4 PHE B 68 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA4 6 GLY B 10 GLN B 13 0 SHEET 2 AA4 6 THR B 117 SER B 122 1 O THR B 120 N VAL B 12 SHEET 3 AA4 6 ALA B 92 HIS B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AA4 6 TYR B 32 GLN B 39 -1 N ALA B 33 O HIS B 99 SHEET 5 AA4 6 GLU B 46 VAL B 53 -1 O GLU B 46 N ARG B 38 SHEET 6 AA4 6 THR B 58 TYR B 60 -1 O TRP B 59 N ARG B 50 SHEET 1 AA5 4 GLY B 10 GLN B 13 0 SHEET 2 AA5 4 THR B 117 SER B 122 1 O THR B 120 N VAL B 12 SHEET 3 AA5 4 ALA B 92 HIS B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AA5 4 VAL B 112 TRP B 113 -1 O VAL B 112 N LEU B 98 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.00 CRYST1 83.210 83.210 64.930 90.00 90.00 90.00 P 43 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012018 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012018 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015401 0.00000