HEADER BIOSYNTHETIC PROTEIN 24-NOV-24 9HI6 TITLE STRUCTURE OF SCAFFOLD FI6-FOCUSED DESIGN_04 IN COMPLEX WITH FI6-FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: FI6 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FI6-FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FI6-FOCUSED DESIGN_04; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: BACTEROIDES UNIFORMIS ATCC 8492; SOURCE 15 ORGANISM_TAXID: 411479; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS SCAFFOLD, INFLUENZA, BIOSYNTHETIC PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.T.CRAMER,T.KREY REVDAT 1 03-DEC-25 9HI6 0 JRNL AUTH J.T.CRAMER,T.KREY JRNL TITL STRUCTURE OF SCAFFOLD FI6-FOCUSED DESIGN_04 IN COMPLEX WITH JRNL TITL 2 FI6-FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.50 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) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.40 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 110467 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5523 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 43.4000 - 4.6600 1.00 3677 194 0.1621 0.1694 REMARK 3 2 4.6600 - 3.7000 1.00 3569 188 0.1385 0.1622 REMARK 3 3 3.7000 - 3.2300 1.00 3567 188 0.1587 0.1933 REMARK 3 4 3.2300 - 2.9400 1.00 3552 187 0.1786 0.1901 REMARK 3 5 2.9400 - 2.7300 1.00 3545 186 0.1730 0.1907 REMARK 3 6 2.7300 - 2.5700 1.00 3526 186 0.1803 0.2037 REMARK 3 7 2.5700 - 2.4400 1.00 3496 184 0.1742 0.2209 REMARK 3 8 2.4400 - 2.3300 1.00 3544 187 0.1766 0.1940 REMARK 3 9 2.3300 - 2.2400 1.00 3503 184 0.1692 0.2250 REMARK 3 10 2.2400 - 2.1700 1.00 3503 184 0.1688 0.1967 REMARK 3 11 2.1700 - 2.1000 1.00 3508 185 0.1695 0.2238 REMARK 3 12 2.1000 - 2.0400 1.00 3537 185 0.1796 0.2021 REMARK 3 13 2.0400 - 1.9800 1.00 3470 183 0.1937 0.2301 REMARK 3 14 1.9800 - 1.9400 1.00 3550 187 0.1888 0.2192 REMARK 3 15 1.9400 - 1.8900 1.00 3457 182 0.1816 0.2072 REMARK 3 16 1.8900 - 1.8500 1.00 3518 186 0.1818 0.1987 REMARK 3 17 1.8500 - 1.8100 1.00 3487 183 0.1814 0.2238 REMARK 3 18 1.8100 - 1.7800 1.00 3447 182 0.1849 0.2078 REMARK 3 19 1.7800 - 1.7500 0.99 3497 183 0.1924 0.2214 REMARK 3 20 1.7500 - 1.7200 1.00 3516 185 0.2089 0.2347 REMARK 3 21 1.7200 - 1.6900 0.99 3455 182 0.2324 0.2703 REMARK 3 22 1.6900 - 1.6600 1.00 3490 184 0.2486 0.3081 REMARK 3 23 1.6600 - 1.6400 0.99 3476 182 0.2780 0.3419 REMARK 3 24 1.6400 - 1.6200 0.99 3434 181 0.2718 0.2926 REMARK 3 25 1.6200 - 1.6000 1.00 3484 183 0.2264 0.2585 REMARK 3 26 1.6000 - 1.5700 0.98 3463 182 0.2360 0.2880 REMARK 3 27 1.5700 - 1.5600 0.99 3433 180 0.2414 0.2596 REMARK 3 28 1.5600 - 1.5400 0.98 3453 183 0.2521 0.2489 REMARK 3 29 1.5400 - 1.5200 0.99 3426 180 0.2565 0.2569 REMARK 3 30 1.5200 - 1.5000 0.97 3361 177 0.2801 0.3200 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) : 0.179 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.217 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.74 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.97 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 5141 REMARK 3 ANGLE : 0.962 7015 REMARK 3 CHIRALITY : 0.064 785 REMARK 3 PLANARITY : 0.008 910 REMARK 3 DIHEDRAL : 10.205 728 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3401 11.6443 -31.2722 REMARK 3 T TENSOR REMARK 3 T11: 0.1158 T22: 0.0994 REMARK 3 T33: 0.1308 T12: 0.0198 REMARK 3 T13: -0.0256 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: 5.0565 L22: 3.1826 REMARK 3 L33: 7.5175 L12: 2.1982 REMARK 3 L13: -3.8567 L23: -1.7867 REMARK 3 S TENSOR REMARK 3 S11: 0.1134 S12: -0.3784 S13: 0.1770 REMARK 3 S21: 0.1528 S22: -0.0136 S23: -0.1680 REMARK 3 S31: -0.2249 S32: 0.6077 S33: -0.1547 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7814 7.3084 -44.5558 REMARK 3 T TENSOR REMARK 3 T11: 0.1173 T22: 0.1081 REMARK 3 T33: 0.1331 T12: 0.0138 REMARK 3 T13: -0.0038 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 0.8366 L22: 0.6425 REMARK 3 L33: 2.1807 L12: -0.0165 REMARK 3 L13: -0.0957 L23: 0.6851 REMARK 3 S TENSOR REMARK 3 S11: -0.0375 S12: 0.0029 S13: 0.0456 REMARK 3 S21: -0.0302 S22: 0.0565 S23: 0.0054 REMARK 3 S31: -0.0080 S32: 0.1494 S33: -0.0147 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 135 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.7138 7.7847 -22.7992 REMARK 3 T TENSOR REMARK 3 T11: 0.2006 T22: 0.2747 REMARK 3 T33: 0.1894 T12: 0.0986 REMARK 3 T13: -0.0316 T23: -0.1089 REMARK 3 L TENSOR REMARK 3 L11: 1.7972 L22: 0.6572 REMARK 3 L33: 2.1727 L12: 0.4377 REMARK 3 L13: 1.9220 L23: 0.4154 REMARK 3 S TENSOR REMARK 3 S11: -0.0522 S12: -0.5579 S13: 0.4734 REMARK 3 S21: 0.1903 S22: 0.2503 S23: -0.1618 REMARK 3 S31: 0.0376 S32: 0.0186 S33: -0.0595 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 136 THROUGH 161 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.8127 -0.0721 -9.1973 REMARK 3 T TENSOR REMARK 3 T11: 0.1802 T22: 0.4295 REMARK 3 T33: 0.2261 T12: 0.0760 REMARK 3 T13: -0.0178 T23: -0.1079 REMARK 3 L TENSOR REMARK 3 L11: 3.9409 L22: 5.0431 REMARK 3 L33: 3.6518 L12: -1.9549 REMARK 3 L13: -0.5848 L23: 0.8014 REMARK 3 S TENSOR REMARK 3 S11: -0.3955 S12: -1.2851 S13: 0.4212 REMARK 3 S21: 0.2917 S22: 0.3007 S23: -0.1932 REMARK 3 S31: -0.1357 S32: -0.1725 S33: 0.0955 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 162 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6321 1.8574 -15.7345 REMARK 3 T TENSOR REMARK 3 T11: 0.1789 T22: 0.2574 REMARK 3 T33: 0.1270 T12: 0.0502 REMARK 3 T13: -0.0051 T23: -0.0462 REMARK 3 L TENSOR REMARK 3 L11: 8.1866 L22: 2.4075 REMARK 3 L33: 2.0206 L12: 0.6286 REMARK 3 L13: 2.1313 L23: -0.0843 REMARK 3 S TENSOR REMARK 3 S11: -0.2398 S12: -0.4443 S13: 0.3046 REMARK 3 S21: -0.0340 S22: 0.0693 S23: -0.1900 REMARK 3 S31: -0.2241 S32: 0.1372 S33: 0.1499 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 210 THROUGH 230 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.5466 9.2139 -11.2971 REMARK 3 T TENSOR REMARK 3 T11: 0.3035 T22: 0.3949 REMARK 3 T33: 0.5488 T12: 0.0751 REMARK 3 T13: -0.1189 T23: -0.2036 REMARK 3 L TENSOR REMARK 3 L11: 4.2866 L22: 2.3839 REMARK 3 L33: 3.9324 L12: -3.0089 REMARK 3 L13: 3.7252 L23: -2.8325 REMARK 3 S TENSOR REMARK 3 S11: -0.4076 S12: -1.1631 S13: 0.6623 REMARK 3 S21: 0.2079 S22: 0.0572 S23: 0.4110 REMARK 3 S31: -0.5435 S32: -0.2793 S33: 0.2626 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.0509 -6.9780 -47.7443 REMARK 3 T TENSOR REMARK 3 T11: 0.2018 T22: 0.4079 REMARK 3 T33: 0.2284 T12: 0.1260 REMARK 3 T13: -0.0239 T23: -0.0697 REMARK 3 L TENSOR REMARK 3 L11: 4.5039 L22: 1.9748 REMARK 3 L33: 1.2396 L12: -1.3333 REMARK 3 L13: -0.0014 L23: 0.0766 REMARK 3 S TENSOR REMARK 3 S11: -0.0412 S12: -0.1775 S13: -0.1575 REMARK 3 S21: 0.1693 S22: 0.1896 S23: -0.2023 REMARK 3 S31: 0.2714 S32: 0.5544 S33: -0.1291 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 95 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7693 -10.0711 -39.2808 REMARK 3 T TENSOR REMARK 3 T11: 0.2108 T22: 0.2427 REMARK 3 T33: 0.1885 T12: 0.0815 REMARK 3 T13: -0.0262 T23: -0.0452 REMARK 3 L TENSOR REMARK 3 L11: 7.7443 L22: 0.9968 REMARK 3 L33: 7.3383 L12: -3.2603 REMARK 3 L13: 7.9617 L23: -3.5770 REMARK 3 S TENSOR REMARK 3 S11: 0.1321 S12: 0.2710 S13: -0.2962 REMARK 3 S21: 0.0159 S22: -0.0251 S23: 0.0775 REMARK 3 S31: 0.1190 S32: 0.3669 S33: -0.1112 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 117 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.3513 -12.5323 -11.0088 REMARK 3 T TENSOR REMARK 3 T11: 0.2328 T22: 0.4714 REMARK 3 T33: 0.2337 T12: -0.0430 REMARK 3 T13: 0.0850 T23: 0.0449 REMARK 3 L TENSOR REMARK 3 L11: 4.4759 L22: 2.4487 REMARK 3 L33: 4.1431 L12: -0.8256 REMARK 3 L13: -1.3592 L23: 1.4134 REMARK 3 S TENSOR REMARK 3 S11: -0.1160 S12: -0.5170 S13: -0.3738 REMARK 3 S21: 0.3682 S22: -0.1794 S23: 0.3313 REMARK 3 S31: 0.4964 S32: -0.7088 S33: 0.2275 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8165 7.9473 -89.0745 REMARK 3 T TENSOR REMARK 3 T11: 0.2636 T22: 0.2165 REMARK 3 T33: 0.1394 T12: -0.0664 REMARK 3 T13: -0.0397 T23: -0.0273 REMARK 3 L TENSOR REMARK 3 L11: 3.5181 L22: 2.5542 REMARK 3 L33: 3.9356 L12: -0.8879 REMARK 3 L13: -1.1559 L23: 0.6633 REMARK 3 S TENSOR REMARK 3 S11: -0.0817 S12: 0.6054 S13: -0.1167 REMARK 3 S21: -0.5337 S22: 0.0485 S23: 0.1528 REMARK 3 S31: 0.0446 S32: -0.1151 S33: 0.0442 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.2290 2.8416 -83.2655 REMARK 3 T TENSOR REMARK 3 T11: 0.2024 T22: 0.1471 REMARK 3 T33: 0.1610 T12: -0.0373 REMARK 3 T13: 0.0348 T23: -0.0471 REMARK 3 L TENSOR REMARK 3 L11: 1.7960 L22: 4.2981 REMARK 3 L33: 3.2159 L12: -1.0639 REMARK 3 L13: 0.2630 L23: -1.1356 REMARK 3 S TENSOR REMARK 3 S11: -0.0998 S12: 0.1971 S13: -0.2303 REMARK 3 S21: -0.3454 S22: -0.0121 S23: -0.0676 REMARK 3 S31: 0.4790 S32: 0.0160 S33: 0.1037 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2834 7.4109 -77.8787 REMARK 3 T TENSOR REMARK 3 T11: 0.1563 T22: 0.1768 REMARK 3 T33: 0.1247 T12: -0.0193 REMARK 3 T13: 0.0226 T23: -0.0252 REMARK 3 L TENSOR REMARK 3 L11: 6.5062 L22: 5.0246 REMARK 3 L33: 8.7956 L12: 0.3359 REMARK 3 L13: 0.1079 L23: -6.6020 REMARK 3 S TENSOR REMARK 3 S11: -0.0337 S12: 0.1437 S13: -0.0546 REMARK 3 S21: 0.0397 S22: -0.2027 S23: -0.1757 REMARK 3 S31: -0.0009 S32: 0.4480 S33: 0.2300 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.7592 7.2472 -70.1769 REMARK 3 T TENSOR REMARK 3 T11: 0.1245 T22: 0.0974 REMARK 3 T33: 0.1200 T12: -0.0068 REMARK 3 T13: 0.0091 T23: -0.0209 REMARK 3 L TENSOR REMARK 3 L11: 1.2744 L22: 1.5158 REMARK 3 L33: 1.3774 L12: 0.1675 REMARK 3 L13: 0.1373 L23: -0.6470 REMARK 3 S TENSOR REMARK 3 S11: 0.0296 S12: -0.0181 S13: 0.0608 REMARK 3 S21: -0.0019 S22: 0.0126 S23: 0.1448 REMARK 3 S31: -0.0340 S32: 0.0372 S33: -0.0481 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 9HI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1292143239. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JUN-20 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 : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03674 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 : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110619 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 43.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 6.863 REMARK 200 R MERGE (I) : 0.09500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : 6.83 REMARK 200 R MERGE FOR SHELL (I) : 1.19300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.430 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: 3ZTJ, 4IYJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG3350, 200MM (NH4)2HCITRATE REMARK 280 PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.93450 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 SER H 144 REMARK 465 LYS H 145 REMARK 465 SER H 146 REMARK 465 THR H 147 REMARK 465 SER H 148 REMARK 465 GLY H 149 REMARK 465 SER H 231 REMARK 465 CYS H 232 REMARK 465 ASP H 233 REMARK 465 LYS H 234 REMARK 465 GLY H 235 REMARK 465 ASP L 9 REMARK 465 SER L 10 REMARK 465 LEU L 11 REMARK 465 GLU L 216 REMARK 465 CYS L 217 REMARK 465 GLY A 1 REMARK 465 SER A 2 REMARK 465 ASP A 3 REMARK 465 ALA A 4 REMARK 465 GLU A 5 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 GLN H 1 CG CD OE1 NE2 REMARK 470 ARG H 16 CZ NH1 NH2 REMARK 470 LYS H 76 CE NZ REMARK 470 GLN H 208 CG CD OE1 NE2 REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 ASN H 220 CG OD1 ND2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 LYS H 226 CG CD CE NZ REMARK 470 GLU H 228 CG CD OE1 OE2 REMARK 470 LYS H 230 CG CD CE NZ REMARK 470 ARG L 18 NH1 NH2 REMARK 470 LYS L 24 CG CD CE NZ REMARK 470 LYS L 34 CG CD CE NZ REMARK 470 LYS L 49 CG CD CE NZ REMARK 470 LYS L 129 CG CD CE NZ REMARK 470 SER L 130 OG REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 GLN L 150 CG CD OE1 NE2 REMARK 470 LYS L 152 CG CD CE NZ REMARK 470 LYS L 186 CE NZ REMARK 470 LYS L 191 CG CD CE NZ REMARK 470 LYS L 193 CG CD CE NZ REMARK 470 LYS A 6 CG CD CE NZ REMARK 470 GLN A 7 CG CD OE1 NE2 REMARK 470 LYS A 13 CG CD CE NZ REMARK 470 GLU A 21 CG CD OE1 OE2 REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 25 CG CD CE NZ REMARK 470 LYS A 27 CG CD CE NZ REMARK 470 GLN A 28 CG CD OE1 NE2 REMARK 470 LYS A 29 CG CD CE NZ REMARK 470 GLU A 52 CG CD OE1 OE2 REMARK 470 LYS A 81 NZ 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 LEU H 106 58.95 -95.39 REMARK 500 ALA L 55 -36.70 69.43 REMARK 500 ASN A 37 -138.95 -106.69 REMARK 500 VAL A 77 -64.48 -124.47 REMARK 500 LYS A 81 54.22 39.37 REMARK 500 ASN A 138 -60.23 -94.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 568 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH H 569 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH A 699 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH A 700 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH A 701 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH A 702 DISTANCE = 6.32 ANGSTROMS REMARK 525 HOH A 703 DISTANCE = 6.59 ANGSTROMS DBREF 9HI6 H 1 235 PDB 9HI6 9HI6 1 235 DBREF 9HI6 L 1 217 PDB 9HI6 9HI6 1 217 DBREF 9HI6 A 1 220 PDB 9HI6 9HI6 1 220 SEQRES 1 H 235 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 235 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 235 PHE THR PHE SER THR TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 H 235 TYR ASP ALA ASN TYR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 235 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA LYS ASP SER GLN LEU ARG SER SEQRES 9 H 235 LEU LEU TYR PHE GLU TRP LEU SER GLN GLY TYR PHE ASP SEQRES 10 H 235 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 11 H 235 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 235 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 235 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 235 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 235 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 235 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 235 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 235 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS SEQRES 19 H 235 GLY SEQRES 1 L 217 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 217 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 L 217 GLN SER VAL THR PHE ASN TYR LYS ASN TYR LEU ALA TRP SEQRES 4 L 217 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 217 TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO ASP ARG SEQRES 6 L 217 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 7 L 217 ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL TYR TYR SEQRES 8 L 217 CYS GLN GLN HIS TYR ARG THR PRO PRO THR PHE GLY GLN SEQRES 9 L 217 GLY THR VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 220 GLY SER ASP ALA GLU LYS GLN ASP PRO ALA ASN LYS LYS SEQRES 2 A 220 ARG TYR ALA GLU ALA ASN LYS GLU LEU VAL ARG LYS GLY SEQRES 3 A 220 LYS GLN LYS ASN ARG VAL VAL PHE MET GLY ASN SER ILE SEQRES 4 A 220 THR GLU GLY TRP VAL ALA ASN ASP PRO ALA PHE PHE GLU SEQRES 5 A 220 ASP ASN GLY TYR VAL GLY ARG GLY ILE SER GLY GLN THR SEQRES 6 A 220 SER SER HIS MET LEU GLU ARG PHE GLU GLU ASP VAL ILE SEQRES 7 A 220 LYS LEU LYS PRO ALA VAL VAL VAL ILE MET ALA GLY THR SEQRES 8 A 220 ASN ASP ILE ALA GLU ASN ALA GLY PRO TYR ASN GLU GLU SEQRES 9 A 220 GLN THR PHE GLY ASN ILE VAL LYS MET VAL GLU LEU ALA SEQRES 10 A 220 ARG ALA ALA LYS ILE LYS VAL ILE LEU THR SER VAL LEU SEQRES 11 A 220 PRO HIS ALA ALA ALA PRO TRP ASN GLU SER GLN LYS GLU SEQRES 12 A 220 ALA THR GLN ALA ILE ILE ASN LEU ASN THR ARG ILE ILE SEQRES 13 A 220 ASN TYR ALA ILE GLU ASN LYS ILE PRO PHE VAL ASP TYR SEQRES 14 A 220 PHE VAL GLU MET ALA GLN SER PRO ASN GLY ASP LEU ASN SEQRES 15 A 220 SER SER TYR THR ARG ASP GLY VAL HIS PRO ASN LEU GLU SEQRES 16 A 220 GLY TYR LYS VAL MET GLU ALA LEU ILE LYS LYS ALA ILE SEQRES 17 A 220 ASP LYS VAL LEU LEU GLU HIS HIS HIS HIS HIS HIS HET CIT A 301 13 HET CIT A 302 13 HET PEG A 303 7 HET PEG A 304 7 HETNAM CIT CITRIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 4 CIT 2(C6 H8 O7) FORMUL 6 PEG 2(C4 H10 O3) FORMUL 8 HOH *743(H2 O) HELIX 1 AA1 THR H 28 SER H 30 5 3 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 SER H 172 ALA H 174 5 3 HELIX 4 AA4 SER H 203 GLY H 206 5 4 HELIX 5 AA5 LYS H 217 ASN H 220 5 4 HELIX 6 AA6 GLN L 83 VAL L 87 5 5 HELIX 7 AA7 SER L 124 LYS L 129 1 6 HELIX 8 AA8 LYS L 186 LYS L 191 1 6 HELIX 9 AA9 LYS A 12 GLY A 26 1 15 HELIX 10 AB1 ASN A 37 ASP A 47 1 11 HELIX 11 AB2 ASP A 47 GLY A 55 1 9 HELIX 12 AB3 THR A 65 ARG A 72 1 8 HELIX 13 AB4 ARG A 72 VAL A 77 1 6 HELIX 14 AB5 ILE A 78 LYS A 81 5 4 HELIX 15 AB6 GLY A 90 GLU A 96 1 7 HELIX 16 AB7 ASN A 102 ALA A 120 1 19 HELIX 17 AB8 SER A 140 LYS A 163 1 24 HELIX 18 AB9 ASP A 168 MET A 173 1 6 HELIX 19 AC1 SER A 183 THR A 186 5 4 HELIX 20 AC2 ASN A 193 GLU A 214 1 22 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 123 VAL H 127 1 O THR H 126 N VAL H 12 SHEET 3 AA2 6 ALA H 92 LEU H 102 -1 N TYR H 94 O THR H 123 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N VAL H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 123 VAL H 127 1 O THR H 126 N VAL H 12 SHEET 3 AA3 4 ALA H 92 LEU H 102 -1 N TYR H 94 O THR H 123 SHEET 4 AA3 4 PHE H 116 TRP H 119 -1 O TYR H 118 N LYS H 98 SHEET 1 AA4 4 SER H 136 LEU H 140 0 SHEET 2 AA4 4 THR H 151 TYR H 161 -1 O GLY H 155 N LEU H 140 SHEET 3 AA4 4 TYR H 192 PRO H 201 -1 O VAL H 200 N ALA H 152 SHEET 4 AA4 4 VAL H 179 THR H 181 -1 N HIS H 180 O VAL H 197 SHEET 1 AA5 4 SER H 136 LEU H 140 0 SHEET 2 AA5 4 THR H 151 TYR H 161 -1 O GLY H 155 N LEU H 140 SHEET 3 AA5 4 TYR H 192 PRO H 201 -1 O VAL H 200 N ALA H 152 SHEET 4 AA5 4 VAL H 185 LEU H 186 -1 N VAL H 185 O SER H 193 SHEET 1 AA6 3 THR H 167 TRP H 170 0 SHEET 2 AA6 3 TYR H 210 HIS H 216 -1 O ASN H 213 N SER H 169 SHEET 3 AA6 3 THR H 221 VAL H 227 -1 O VAL H 223 N VAL H 214 SHEET 1 AA7 4 MET L 4 THR L 5 0 SHEET 2 AA7 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA7 4 ASP L 74 ILE L 79 -1 O ILE L 79 N ALA L 19 SHEET 4 AA7 4 PHE L 66 SER L 71 -1 N SER L 67 O THR L 78 SHEET 1 AA8 2 THR L 30 PHE L 31 0 SHEET 2 AA8 2 LYS L 34 ASN L 35 -1 O LYS L 34 N PHE L 31 SHEET 1 AA9 5 THR L 57 ARG L 58 0 SHEET 2 AA9 5 LYS L 49 TYR L 53 -1 N TYR L 53 O THR L 57 SHEET 3 AA9 5 LEU L 37 GLN L 42 -1 N TRP L 39 O LEU L 51 SHEET 4 AA9 5 ALA L 88 GLN L 94 -1 O GLN L 93 N ALA L 38 SHEET 5 AA9 5 THR L 101 VAL L 107 -1 O GLY L 103 N CYS L 92 SHEET 1 AB1 4 SER L 117 PHE L 121 0 SHEET 2 AB1 4 THR L 132 PHE L 142 -1 O ASN L 140 N SER L 117 SHEET 3 AB1 4 TYR L 176 SER L 185 -1 O LEU L 182 N VAL L 135 SHEET 4 AB1 4 SER L 162 VAL L 166 -1 N SER L 165 O SER L 179 SHEET 1 AB2 4 ALA L 156 LEU L 157 0 SHEET 2 AB2 4 LYS L 148 VAL L 153 -1 N VAL L 153 O ALA L 156 SHEET 3 AB2 4 VAL L 194 THR L 200 -1 O GLU L 198 N GLN L 150 SHEET 4 AB2 4 VAL L 208 ASN L 213 -1 O VAL L 208 N VAL L 199 SHEET 1 AB3 5 TYR A 56 GLY A 60 0 SHEET 2 AB3 5 VAL A 32 GLY A 36 1 N VAL A 32 O VAL A 57 SHEET 3 AB3 5 VAL A 84 MET A 88 1 O MET A 88 N MET A 35 SHEET 4 AB3 5 LYS A 123 THR A 127 1 O LYS A 123 N VAL A 85 SHEET 5 AB3 5 PHE A 166 VAL A 167 1 O VAL A 167 N LEU A 126 SHEET 1 AB4 2 ALA A 174 GLN A 175 0 SHEET 2 AB4 2 ASP A 180 LEU A 181 -1 O ASP A 180 N GLN A 175 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.10 SSBOND 2 CYS H 156 CYS H 212 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 92 1555 1555 2.08 SSBOND 4 CYS L 137 CYS L 197 1555 1555 2.05 CISPEP 1 PHE H 162 PRO H 163 0 -3.06 CISPEP 2 GLU H 164 PRO H 165 0 2.42 CISPEP 3 THR L 98 PRO L 99 0 3.30 CISPEP 4 TYR L 143 PRO L 144 0 2.66 CISPEP 5 SER A 176 PRO A 177 0 5.65 CRYST1 71.213 47.869 107.093 90.00 106.13 90.00 P 1 21 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 0.014042 0.000000 0.004061 0.00000 SCALE2 0.000000 0.020890 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009720 0.00000