HEADER SIGNALING PROTEIN 10-JUL-25 9PI9 TITLE SACITUZUMAB FAB BOUND TO TROP2 DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: SACITUZUMAB HEAVY CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SACITUZUMAB LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TUMOR-ASSOCIATED CALCIUM SIGNAL TRANSDUCER 2; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: CELL SURFACE GLYCOPROTEIN TROP-2,MEMBRANE COMPONENT COMPND 13 CHROMOSOME 1 SURFACE MARKER 1,PANCREATIC CARCINOMA MARKER PROTEIN COMPND 14 GA733-1; COMPND 15 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: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: TACSTD2, GA733-1, M1S1, TROP2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS ANTIBODY DRUG CONJUGATE, IMMUNE COMPLEX, DIMER, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.F.FERRAO,E.B.LANSDON REVDAT 1 10-DEC-25 9PI9 0 JRNL AUTH R.FERRAO,J.ZHANG,C.C.CHOU,A.NIETO,D.LANGESLAY,M.CHATTERJEE, JRNL AUTH 2 D.JIN,M.HUNG,I.SCOTT,M.NAGEL,W.XING,S.LETARTE,J.WANG, JRNL AUTH 3 A.AMBROGELLY,E.B.LANSDON JRNL TITL THE THERAPEUTIC ANTIBODY SACITUZUMAB INDUCES TROPHOBLAST JRNL TITL 2 CELL-SURFACE ANTIGEN-2 CONFORMATIONAL REARRANGEMENT. JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 JRNL PMID 41314216 JRNL DOI 10.1016/J.STR.2025.11.002 REMARK 2 REMARK 2 RESOLUTION. 1.56 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 1.56 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.34 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 220899 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.181 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.211 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.910 REMARK 3 FREE R VALUE TEST SET COUNT : 2005 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 47.3400 - 3.7600 1.00 15766 139 0.1525 0.1726 REMARK 3 2 3.7600 - 2.9800 0.99 15614 145 0.1653 0.1867 REMARK 3 3 2.9800 - 2.6100 0.99 15626 144 0.1768 0.2090 REMARK 3 4 2.6100 - 2.3700 1.00 15696 146 0.1792 0.2222 REMARK 3 5 2.3700 - 2.2000 1.00 15635 148 0.1748 0.2043 REMARK 3 6 2.2000 - 2.0700 1.00 15665 141 0.1738 0.2031 REMARK 3 7 2.0700 - 1.9600 1.00 15671 145 0.1899 0.2263 REMARK 3 8 1.9600 - 1.8800 1.00 15607 141 0.2110 0.2510 REMARK 3 9 1.8800 - 1.8100 1.00 15706 144 0.2037 0.2499 REMARK 3 10 1.8100 - 1.7400 1.00 15618 155 0.2113 0.2776 REMARK 3 11 1.7400 - 1.6900 1.00 15664 128 0.2336 0.2436 REMARK 3 12 1.6900 - 1.6400 1.00 15683 149 0.2688 0.3375 REMARK 3 13 1.6400 - 1.6000 1.00 15642 151 0.2995 0.3302 REMARK 3 14 1.6000 - 1.5600 0.98 15301 129 0.3418 0.3495 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) : 0.217 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.841 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.52 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 : 0.011 10427 REMARK 3 ANGLE : 1.151 14147 REMARK 3 CHIRALITY : 0.078 1584 REMARK 3 PLANARITY : 0.011 1819 REMARK 3 DIHEDRAL : 13.466 3811 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 39 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.1122 44.4356 4.5881 REMARK 3 T TENSOR REMARK 3 T11: 0.1475 T22: 0.1153 REMARK 3 T33: 0.1407 T12: 0.0146 REMARK 3 T13: -0.0281 T23: 0.0231 REMARK 3 L TENSOR REMARK 3 L11: 9.4975 L22: 7.8109 REMARK 3 L33: 6.4702 L12: 6.4749 REMARK 3 L13: 6.1692 L23: 5.7087 REMARK 3 S TENSOR REMARK 3 S11: 0.5244 S12: -0.5748 S13: -0.2078 REMARK 3 S21: 0.6486 S22: -0.4256 S23: -0.1435 REMARK 3 S31: 0.4533 S32: -0.2708 S33: -0.1212 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.6358 42.6714 -7.7172 REMARK 3 T TENSOR REMARK 3 T11: 0.0621 T22: 0.1326 REMARK 3 T33: 0.1478 T12: 0.0072 REMARK 3 T13: 0.0152 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 0.5749 L22: 8.1300 REMARK 3 L33: 2.7980 L12: 0.7677 REMARK 3 L13: 0.8883 L23: 2.9188 REMARK 3 S TENSOR REMARK 3 S11: 0.0804 S12: -0.0125 S13: -0.0752 REMARK 3 S21: -0.1203 S22: -0.0319 S23: -0.1253 REMARK 3 S31: 0.0720 S32: 0.0677 S33: -0.0520 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.7705 45.9287 -9.1731 REMARK 3 T TENSOR REMARK 3 T11: 0.1189 T22: 0.1896 REMARK 3 T33: 0.2162 T12: -0.0137 REMARK 3 T13: 0.0261 T23: -0.0366 REMARK 3 L TENSOR REMARK 3 L11: 2.7391 L22: 5.6578 REMARK 3 L33: 3.4082 L12: -3.1207 REMARK 3 L13: 2.0733 L23: -0.9994 REMARK 3 S TENSOR REMARK 3 S11: -0.1591 S12: 0.1049 S13: 0.2845 REMARK 3 S21: -0.1912 S22: 0.0379 S23: -0.5854 REMARK 3 S31: -0.1729 S32: 0.4208 S33: 0.1097 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.3480 44.0202 -1.9988 REMARK 3 T TENSOR REMARK 3 T11: 0.1357 T22: 0.1522 REMARK 3 T33: 0.3321 T12: 0.0223 REMARK 3 T13: -0.0260 T23: -0.0259 REMARK 3 L TENSOR REMARK 3 L11: 4.7956 L22: 2.0972 REMARK 3 L33: 3.3782 L12: 7.9987 REMARK 3 L13: 3.7006 L23: 6.3148 REMARK 3 S TENSOR REMARK 3 S11: 0.0180 S12: -0.0080 S13: -0.2993 REMARK 3 S21: -0.0398 S22: 0.0815 S23: -0.7990 REMARK 3 S31: 0.0805 S32: 0.1892 S33: -0.1233 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.9451 47.7692 -3.9597 REMARK 3 T TENSOR REMARK 3 T11: 0.0697 T22: 0.0946 REMARK 3 T33: 0.1440 T12: 0.0155 REMARK 3 T13: 0.0119 T23: -0.0002 REMARK 3 L TENSOR REMARK 3 L11: 1.7034 L22: 2.4584 REMARK 3 L33: 7.1205 L12: 0.9860 REMARK 3 L13: 2.8737 L23: 3.2238 REMARK 3 S TENSOR REMARK 3 S11: -0.0267 S12: -0.0408 S13: 0.0184 REMARK 3 S21: 0.0024 S22: 0.0269 S23: -0.0643 REMARK 3 S31: 0.0012 S32: 0.0105 S33: -0.0082 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2078 71.8732 25.8706 REMARK 3 T TENSOR REMARK 3 T11: 0.4641 T22: 0.2024 REMARK 3 T33: 0.1897 T12: 0.0392 REMARK 3 T13: -0.0076 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 6.2893 L22: 4.8401 REMARK 3 L33: 4.9022 L12: -3.1111 REMARK 3 L13: -0.6855 L23: 1.1784 REMARK 3 S TENSOR REMARK 3 S11: -0.3321 S12: -0.7348 S13: 0.3973 REMARK 3 S21: 0.9837 S22: 0.4102 S23: -0.1885 REMARK 3 S31: -0.1067 S32: -0.0402 S33: -0.0296 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4636 65.8833 23.2159 REMARK 3 T TENSOR REMARK 3 T11: 0.3798 T22: 0.1712 REMARK 3 T33: 0.1878 T12: 0.0357 REMARK 3 T13: 0.0580 T23: 0.0405 REMARK 3 L TENSOR REMARK 3 L11: 4.5174 L22: 2.3780 REMARK 3 L33: 3.7102 L12: -0.8868 REMARK 3 L13: -1.0268 L23: 0.7488 REMARK 3 S TENSOR REMARK 3 S11: -0.1560 S12: -0.4188 S13: -0.2577 REMARK 3 S21: 0.7385 S22: 0.1291 S23: 0.1577 REMARK 3 S31: 0.2398 S32: -0.0572 S33: 0.0501 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.8021 59.9490 28.7303 REMARK 3 T TENSOR REMARK 3 T11: 0.6416 T22: 0.3583 REMARK 3 T33: 0.3015 T12: 0.0995 REMARK 3 T13: -0.0873 T23: 0.1049 REMARK 3 L TENSOR REMARK 3 L11: 8.0184 L22: 3.7731 REMARK 3 L33: 4.7984 L12: -3.3392 REMARK 3 L13: -3.8598 L23: 0.8229 REMARK 3 S TENSOR REMARK 3 S11: -0.4503 S12: -1.1047 S13: -0.6062 REMARK 3 S21: 1.1853 S22: 0.5770 S23: -0.0575 REMARK 3 S31: 0.3614 S32: 0.3264 S33: -0.1022 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.0926 54.8736 -10.6595 REMARK 3 T TENSOR REMARK 3 T11: 0.0942 T22: 0.1213 REMARK 3 T33: 0.1405 T12: 0.0088 REMARK 3 T13: -0.0135 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 2.0101 L22: 2.0466 REMARK 3 L33: 2.3305 L12: -0.3720 REMARK 3 L13: -0.7695 L23: 0.7224 REMARK 3 S TENSOR REMARK 3 S11: 0.0567 S12: 0.0240 S13: 0.1027 REMARK 3 S21: -0.1319 S22: -0.0787 S23: 0.2294 REMARK 3 S31: -0.0595 S32: -0.1631 S33: 0.0121 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9279 68.8002 4.9172 REMARK 3 T TENSOR REMARK 3 T11: 0.1426 T22: 0.1992 REMARK 3 T33: 0.2201 T12: -0.0247 REMARK 3 T13: 0.0347 T23: -0.0273 REMARK 3 L TENSOR REMARK 3 L11: 2.8503 L22: 9.8467 REMARK 3 L33: 5.4910 L12: -5.3028 REMARK 3 L13: -4.0732 L23: 7.3728 REMARK 3 S TENSOR REMARK 3 S11: -0.0791 S12: 0.1829 S13: -0.2551 REMARK 3 S21: 0.2353 S22: -0.2299 S23: 0.5915 REMARK 3 S31: 0.1716 S32: -0.3246 S33: 0.3431 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4074 77.9377 24.4919 REMARK 3 T TENSOR REMARK 3 T11: 0.3816 T22: 0.2179 REMARK 3 T33: 0.2227 T12: 0.0528 REMARK 3 T13: -0.1001 T23: -0.0151 REMARK 3 L TENSOR REMARK 3 L11: 8.7960 L22: 4.7886 REMARK 3 L33: 8.3916 L12: -0.1776 REMARK 3 L13: 5.7902 L23: 0.2130 REMARK 3 S TENSOR REMARK 3 S11: -0.2598 S12: -0.5392 S13: -0.0790 REMARK 3 S21: 0.8410 S22: 0.2561 S23: -0.7328 REMARK 3 S31: 0.1224 S32: 0.3950 S33: 0.0264 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.0052 77.6173 11.8638 REMARK 3 T TENSOR REMARK 3 T11: 0.1320 T22: 0.1594 REMARK 3 T33: 0.1576 T12: 0.0358 REMARK 3 T13: 0.0361 T23: 0.0168 REMARK 3 L TENSOR REMARK 3 L11: 6.3807 L22: 5.7999 REMARK 3 L33: 4.6013 L12: 5.8654 REMARK 3 L13: 4.7129 L23: 3.6917 REMARK 3 S TENSOR REMARK 3 S11: -0.1317 S12: 0.2302 S13: 0.0838 REMARK 3 S21: -0.0766 S22: 0.1178 S23: 0.0716 REMARK 3 S31: -0.0459 S32: 0.1689 S33: -0.0263 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.4142 73.2845 10.8364 REMARK 3 T TENSOR REMARK 3 T11: 0.1915 T22: 0.1524 REMARK 3 T33: 0.0518 T12: 0.0017 REMARK 3 T13: 0.0306 T23: 0.0260 REMARK 3 L TENSOR REMARK 3 L11: 7.2974 L22: 8.4679 REMARK 3 L33: 0.9218 L12: 5.1199 REMARK 3 L13: 2.1790 L23: 2.3758 REMARK 3 S TENSOR REMARK 3 S11: 0.1993 S12: -0.1438 S13: -0.3427 REMARK 3 S21: 0.1964 S22: -0.1661 S23: -0.1569 REMARK 3 S31: 0.1191 S32: -0.0507 S33: -0.0269 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7296 84.1893 15.9159 REMARK 3 T TENSOR REMARK 3 T11: 0.1801 T22: 0.1512 REMARK 3 T33: 0.1223 T12: -0.0069 REMARK 3 T13: 0.0044 T23: 0.0539 REMARK 3 L TENSOR REMARK 3 L11: 7.8322 L22: 5.9690 REMARK 3 L33: 3.4989 L12: 2.7914 REMARK 3 L13: 4.0688 L23: 2.6070 REMARK 3 S TENSOR REMARK 3 S11: -0.3389 S12: 0.1620 S13: 0.4751 REMARK 3 S21: 0.2130 S22: 0.1289 S23: -0.2848 REMARK 3 S31: -0.1315 S32: 0.2211 S33: 0.2149 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4825 8.4341 6.0243 REMARK 3 T TENSOR REMARK 3 T11: 0.1733 T22: 0.1582 REMARK 3 T33: 0.1584 T12: -0.0016 REMARK 3 T13: 0.0011 T23: -0.0286 REMARK 3 L TENSOR REMARK 3 L11: 9.7675 L22: 8.2693 REMARK 3 L33: 8.9429 L12: 7.6147 REMARK 3 L13: -8.3330 L23: -7.7976 REMARK 3 S TENSOR REMARK 3 S11: 0.5374 S12: -0.4883 S13: 0.1509 REMARK 3 S21: 0.6896 S22: -0.4012 S23: -0.0272 REMARK 3 S31: -0.6103 S32: 0.3737 S33: -0.1508 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4476 10.4481 -6.6605 REMARK 3 T TENSOR REMARK 3 T11: 0.0827 T22: 0.1355 REMARK 3 T33: 0.1358 T12: -0.0033 REMARK 3 T13: 0.0140 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 1.4177 L22: 6.8206 REMARK 3 L33: 2.9405 L12: 0.7583 REMARK 3 L13: -0.4788 L23: -2.6892 REMARK 3 S TENSOR REMARK 3 S11: 0.0685 S12: -0.0223 S13: 0.0843 REMARK 3 S21: -0.0858 S22: 0.0799 S23: 0.3219 REMARK 3 S31: -0.0962 S32: -0.1626 S33: -0.1494 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 60 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.6618 6.9715 -6.6309 REMARK 3 T TENSOR REMARK 3 T11: 0.1484 T22: 0.2041 REMARK 3 T33: 0.1367 T12: -0.0228 REMARK 3 T13: -0.0171 T23: 0.0459 REMARK 3 L TENSOR REMARK 3 L11: 6.3837 L22: 9.6623 REMARK 3 L33: 5.5682 L12: -0.4999 REMARK 3 L13: -1.6821 L23: 0.6803 REMARK 3 S TENSOR REMARK 3 S11: -0.1070 S12: 0.2331 S13: -0.2042 REMARK 3 S21: -0.3442 S22: 0.1834 S23: 0.4687 REMARK 3 S31: 0.3734 S32: -0.4700 S33: -0.0660 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 76 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.8747 8.7809 0.5179 REMARK 3 T TENSOR REMARK 3 T11: 0.1388 T22: 0.1855 REMARK 3 T33: 0.3096 T12: -0.0093 REMARK 3 T13: 0.0087 T23: 0.0176 REMARK 3 L TENSOR REMARK 3 L11: 5.3279 L22: 2.0439 REMARK 3 L33: 5.0784 L12: 7.5695 REMARK 3 L13: -4.0896 L23: -5.6879 REMARK 3 S TENSOR REMARK 3 S11: 0.2630 S12: -0.1181 S13: 0.4318 REMARK 3 S21: 0.0699 S22: -0.0052 S23: 0.8145 REMARK 3 S31: -0.1130 S32: -0.2642 S33: -0.2094 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 88 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9606 5.3351 -3.2892 REMARK 3 T TENSOR REMARK 3 T11: 0.0922 T22: 0.1252 REMARK 3 T33: 0.1256 T12: 0.0056 REMARK 3 T13: -0.0056 T23: -0.0098 REMARK 3 L TENSOR REMARK 3 L11: 1.4196 L22: 3.7442 REMARK 3 L33: 3.5194 L12: 1.2261 REMARK 3 L13: -1.1430 L23: -2.8678 REMARK 3 S TENSOR REMARK 3 S11: 0.0904 S12: -0.1566 S13: -0.0571 REMARK 3 S21: 0.1275 S22: -0.1160 S23: -0.0521 REMARK 3 S31: -0.1933 S32: 0.0445 S33: -0.0658 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 124 THROUGH 192 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.3458 -12.8475 21.4121 REMARK 3 T TENSOR REMARK 3 T11: 0.3232 T22: 0.1821 REMARK 3 T33: 0.1652 T12: 0.0564 REMARK 3 T13: -0.0701 T23: -0.0407 REMARK 3 L TENSOR REMARK 3 L11: 5.3722 L22: 1.8728 REMARK 3 L33: 2.1132 L12: -1.6571 REMARK 3 L13: 0.8796 L23: -0.3607 REMARK 3 S TENSOR REMARK 3 S11: -0.2581 S12: -0.3796 S13: 0.0681 REMARK 3 S21: 0.5994 S22: 0.2814 S23: -0.2116 REMARK 3 S31: 0.0219 S32: 0.0537 S33: -0.0204 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 193 THROUGH 207 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4856 -14.7937 30.7784 REMARK 3 T TENSOR REMARK 3 T11: 0.6590 T22: 0.4990 REMARK 3 T33: 0.3574 T12: 0.1845 REMARK 3 T13: -0.2237 T23: -0.1019 REMARK 3 L TENSOR REMARK 3 L11: 3.5650 L22: 1.0290 REMARK 3 L33: 4.8259 L12: 1.9148 REMARK 3 L13: 1.2877 L23: 0.5861 REMARK 3 S TENSOR REMARK 3 S11: -0.6702 S12: -1.1615 S13: 0.2966 REMARK 3 S21: 1.3307 S22: 0.4902 S23: -0.6776 REMARK 3 S31: 0.2370 S32: 0.3453 S33: 0.1612 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 208 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.1893 -5.7334 29.1446 REMARK 3 T TENSOR REMARK 3 T11: 0.6634 T22: 0.5208 REMARK 3 T33: 0.2540 T12: 0.2292 REMARK 3 T13: -0.0975 T23: -0.0831 REMARK 3 L TENSOR REMARK 3 L11: 9.5506 L22: 9.0689 REMARK 3 L33: 5.3486 L12: -7.8032 REMARK 3 L13: 6.5288 L23: -6.7932 REMARK 3 S TENSOR REMARK 3 S11: -0.5961 S12: -1.3294 S13: 0.6868 REMARK 3 S21: 1.3723 S22: 0.5317 S23: -0.4921 REMARK 3 S31: -0.0430 S32: 0.1090 S33: 0.1334 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.2349 -1.0230 -12.5215 REMARK 3 T TENSOR REMARK 3 T11: 0.1242 T22: 0.1110 REMARK 3 T33: 0.1235 T12: 0.0001 REMARK 3 T13: 0.0038 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 2.8218 L22: 1.5805 REMARK 3 L33: 2.0678 L12: -0.3958 REMARK 3 L13: 0.8993 L23: -0.6197 REMARK 3 S TENSOR REMARK 3 S11: 0.0807 S12: 0.0195 S13: -0.1677 REMARK 3 S21: -0.1674 S22: -0.0540 S23: -0.1125 REMARK 3 S31: 0.0446 S32: 0.1129 S33: -0.0360 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 102 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.9474 -14.4960 1.7898 REMARK 3 T TENSOR REMARK 3 T11: 0.2236 T22: 0.2261 REMARK 3 T33: 0.2007 T12: 0.0254 REMARK 3 T13: -0.0143 T23: 0.0111 REMARK 3 L TENSOR REMARK 3 L11: 6.7124 L22: 8.6165 REMARK 3 L33: 2.1815 L12: -7.6468 REMARK 3 L13: 8.0881 L23: -9.1653 REMARK 3 S TENSOR REMARK 3 S11: 0.0512 S12: 0.4742 S13: 0.2679 REMARK 3 S21: 0.0178 S22: -0.2904 S23: -0.1942 REMARK 3 S31: 0.0681 S32: 0.2500 S33: 0.2263 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 114 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.1970 -24.4941 24.8565 REMARK 3 T TENSOR REMARK 3 T11: 0.5344 T22: 0.2505 REMARK 3 T33: 0.1991 T12: 0.1419 REMARK 3 T13: 0.1156 T23: 0.0249 REMARK 3 L TENSOR REMARK 3 L11: 9.5241 L22: 2.9243 REMARK 3 L33: 8.6467 L12: -1.3322 REMARK 3 L13: -6.5135 L23: 1.2568 REMARK 3 S TENSOR REMARK 3 S11: -0.2879 S12: -0.5820 S13: 0.3550 REMARK 3 S21: 1.1392 S22: 0.3441 S23: 0.3121 REMARK 3 S31: -0.2621 S32: -0.1886 S33: -0.0619 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.0382 -24.0817 10.9024 REMARK 3 T TENSOR REMARK 3 T11: 0.1134 T22: 0.1654 REMARK 3 T33: 0.1552 T12: 0.0284 REMARK 3 T13: -0.0267 T23: -0.0177 REMARK 3 L TENSOR REMARK 3 L11: 7.2903 L22: 7.0330 REMARK 3 L33: 6.1323 L12: 6.8558 REMARK 3 L13: -5.9974 L23: -5.6837 REMARK 3 S TENSOR REMARK 3 S11: -0.2028 S12: 0.3658 S13: -0.0798 REMARK 3 S21: -0.1535 S22: 0.2613 S23: -0.0902 REMARK 3 S31: 0.0537 S32: -0.3885 S33: -0.0610 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.9340 -19.7765 9.8545 REMARK 3 T TENSOR REMARK 3 T11: 0.1619 T22: 0.1479 REMARK 3 T33: 0.0853 T12: 0.0130 REMARK 3 T13: -0.0329 T23: -0.0356 REMARK 3 L TENSOR REMARK 3 L11: 7.4349 L22: 6.5471 REMARK 3 L33: 2.2749 L12: 5.2320 REMARK 3 L13: -3.5081 L23: -3.6102 REMARK 3 S TENSOR REMARK 3 S11: 0.1753 S12: -0.0585 S13: 0.3265 REMARK 3 S21: 0.2349 S22: -0.0864 S23: 0.1464 REMARK 3 S31: -0.1666 S32: 0.0240 S33: -0.0794 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 175 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4780 -30.1254 17.3518 REMARK 3 T TENSOR REMARK 3 T11: 0.1682 T22: 0.1959 REMARK 3 T33: 0.1967 T12: -0.0104 REMARK 3 T13: 0.0445 T23: -0.0317 REMARK 3 L TENSOR REMARK 3 L11: 1.6402 L22: 7.1100 REMARK 3 L33: 2.8218 L12: -0.0927 REMARK 3 L13: 1.2161 L23: -1.3840 REMARK 3 S TENSOR REMARK 3 S11: -0.1344 S12: 0.0488 S13: -0.2171 REMARK 3 S21: 0.4370 S22: 0.2362 S23: 0.6241 REMARK 3 S31: -0.0293 S32: -0.4116 S33: -0.0784 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 198 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.1958 -32.2910 14.2780 REMARK 3 T TENSOR REMARK 3 T11: 0.1997 T22: 0.1477 REMARK 3 T33: 0.1793 T12: -0.0069 REMARK 3 T13: 0.0145 T23: -0.0397 REMARK 3 L TENSOR REMARK 3 L11: 8.6944 L22: 8.1874 REMARK 3 L33: 9.6016 L12: 4.2988 REMARK 3 L13: -7.9683 L23: -5.5756 REMARK 3 S TENSOR REMARK 3 S11: -0.8350 S12: -0.2100 S13: -0.8975 REMARK 3 S21: -0.1547 S22: -0.1319 S23: -0.6816 REMARK 3 S31: 0.8904 S32: 0.2236 S33: 0.9086 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 33 THROUGH 71 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4146 54.4909 -36.1482 REMARK 3 T TENSOR REMARK 3 T11: 0.7665 T22: 0.4434 REMARK 3 T33: 0.5648 T12: 0.0395 REMARK 3 T13: 0.3218 T23: 0.1520 REMARK 3 L TENSOR REMARK 3 L11: 3.0146 L22: 2.8158 REMARK 3 L33: 2.6721 L12: -0.8534 REMARK 3 L13: -1.1139 L23: -1.8792 REMARK 3 S TENSOR REMARK 3 S11: 0.6776 S12: 0.6152 S13: 0.9563 REMARK 3 S21: -1.4949 S22: -0.6037 S23: -1.1280 REMARK 3 S31: -0.7165 S32: 0.6372 S33: -0.0237 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 72 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.5361 39.1698 -41.3729 REMARK 3 T TENSOR REMARK 3 T11: 0.4836 T22: 0.4574 REMARK 3 T33: 0.3600 T12: 0.0647 REMARK 3 T13: 0.0474 T23: 0.0695 REMARK 3 L TENSOR REMARK 3 L11: 7.4316 L22: 8.9068 REMARK 3 L33: 4.1819 L12: -8.2330 REMARK 3 L13: 5.6621 L23: -6.2324 REMARK 3 S TENSOR REMARK 3 S11: 0.1574 S12: 0.5740 S13: 1.0505 REMARK 3 S21: -0.1093 S22: -0.5698 S23: -1.0942 REMARK 3 S31: -0.2041 S32: 0.4644 S33: 0.4971 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 90 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.0341 31.5039 -49.3256 REMARK 3 T TENSOR REMARK 3 T11: 0.6900 T22: 0.5253 REMARK 3 T33: 0.3720 T12: 0.0455 REMARK 3 T13: 0.1149 T23: 0.0853 REMARK 3 L TENSOR REMARK 3 L11: 1.1904 L22: 7.1684 REMARK 3 L33: 3.2343 L12: -2.4864 REMARK 3 L13: 1.9358 L23: -4.3694 REMARK 3 S TENSOR REMARK 3 S11: 0.4294 S12: 0.4726 S13: 0.1181 REMARK 3 S21: -1.0263 S22: -0.1470 S23: 0.1098 REMARK 3 S31: 0.0415 S32: -0.0461 S33: -0.2920 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 110 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.2665 37.4095 -38.3046 REMARK 3 T TENSOR REMARK 3 T11: 0.3486 T22: 0.2763 REMARK 3 T33: 0.1884 T12: 0.0632 REMARK 3 T13: -0.0713 T23: -0.0214 REMARK 3 L TENSOR REMARK 3 L11: 2.3788 L22: 2.5563 REMARK 3 L33: 3.2517 L12: -0.0798 REMARK 3 L13: -0.2655 L23: -0.2555 REMARK 3 S TENSOR REMARK 3 S11: 0.0714 S12: 0.4391 S13: 0.0802 REMARK 3 S21: -0.6875 S22: -0.0298 S23: 0.2363 REMARK 3 S31: -0.1139 S32: -0.2698 S33: -0.0297 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 219 THROUGH 268 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.3482 35.1977 -33.8624 REMARK 3 T TENSOR REMARK 3 T11: 0.2663 T22: 0.2183 REMARK 3 T33: 0.1701 T12: 0.0636 REMARK 3 T13: -0.0070 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: 2.7716 L22: 2.7049 REMARK 3 L33: 4.7408 L12: 0.4838 REMARK 3 L13: 1.4827 L23: 1.5385 REMARK 3 S TENSOR REMARK 3 S11: 0.1068 S12: 0.4137 S13: -0.1991 REMARK 3 S21: -0.4669 S22: -0.0573 S23: 0.0605 REMARK 3 S31: 0.2299 S32: 0.0627 S33: -0.0765 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 33 THROUGH 71 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.8882 -2.0679 -33.3051 REMARK 3 T TENSOR REMARK 3 T11: 0.3891 T22: 0.2961 REMARK 3 T33: 0.4321 T12: -0.0091 REMARK 3 T13: -0.1606 T23: -0.0802 REMARK 3 L TENSOR REMARK 3 L11: 5.7590 L22: 6.1459 REMARK 3 L33: 6.5749 L12: 0.0028 REMARK 3 L13: 2.2689 L23: 2.8446 REMARK 3 S TENSOR REMARK 3 S11: 0.4873 S12: -0.0260 S13: -0.9671 REMARK 3 S21: -0.5870 S22: -0.4475 S23: 1.0083 REMARK 3 S31: 0.6460 S32: -0.7505 S33: -0.0512 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 72 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3437 14.3891 -38.4821 REMARK 3 T TENSOR REMARK 3 T11: 0.4454 T22: 0.4074 REMARK 3 T33: 0.3747 T12: 0.0617 REMARK 3 T13: -0.1340 T23: -0.0813 REMARK 3 L TENSOR REMARK 3 L11: 6.4175 L22: 8.9856 REMARK 3 L33: 7.0660 L12: -7.7793 REMARK 3 L13: -6.7450 L23: 7.9390 REMARK 3 S TENSOR REMARK 3 S11: 0.3743 S12: 0.4944 S13: -0.6647 REMARK 3 S21: -0.0355 S22: -0.6208 S23: 0.8127 REMARK 3 S31: 0.3534 S32: -0.6501 S33: 0.1771 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 92 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9763 16.8314 -47.7844 REMARK 3 T TENSOR REMARK 3 T11: 0.5844 T22: 0.5886 REMARK 3 T33: 0.5024 T12: 0.0188 REMARK 3 T13: -0.1227 T23: -0.2037 REMARK 3 L TENSOR REMARK 3 L11: 4.0040 L22: 6.3630 REMARK 3 L33: 1.6742 L12: -5.0840 REMARK 3 L13: -1.6301 L23: 2.1931 REMARK 3 S TENSOR REMARK 3 S11: 0.5174 S12: 0.3204 S13: -0.2423 REMARK 3 S21: -1.0874 S22: -0.3370 S23: 0.2340 REMARK 3 S31: -0.1006 S32: -0.2361 S33: -0.1755 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 112 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.5615 12.1544 -54.7726 REMARK 3 T TENSOR REMARK 3 T11: 0.9719 T22: 0.8029 REMARK 3 T33: 0.3318 T12: 0.0836 REMARK 3 T13: -0.2536 T23: -0.0114 REMARK 3 L TENSOR REMARK 3 L11: 5.2449 L22: 1.8621 REMARK 3 L33: 4.3184 L12: 1.9472 REMARK 3 L13: -0.1334 L23: 0.1195 REMARK 3 S TENSOR REMARK 3 S11: 0.0005 S12: 2.1914 S13: 0.0476 REMARK 3 S21: -1.6896 S22: 0.1951 S23: 0.3789 REMARK 3 S31: 0.1787 S32: 0.1624 S33: -0.1945 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 151 THROUGH 268 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.4518 16.4256 -33.4921 REMARK 3 T TENSOR REMARK 3 T11: 0.2847 T22: 0.1878 REMARK 3 T33: 0.1352 T12: 0.0517 REMARK 3 T13: 0.0196 T23: -0.0055 REMARK 3 L TENSOR REMARK 3 L11: 2.0040 L22: 2.5530 REMARK 3 L33: 1.6493 L12: 0.1961 REMARK 3 L13: -0.1014 L23: -0.0500 REMARK 3 S TENSOR REMARK 3 S11: 0.0730 S12: 0.2654 S13: 0.0564 REMARK 3 S21: -0.5707 S22: -0.0390 S23: -0.1139 REMARK 3 S31: -0.0763 S32: 0.1053 S33: -0.0351 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 9PI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000297877. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-MAR-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.9 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.977410 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 426530 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.559 REMARK 200 RESOLUTION RANGE LOW (A) : 47.340 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 1.800 REMARK 200 R MERGE (I) : 0.04403 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3900 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 (%) : 97.7 REMARK 200 DATA REDUNDANCY IN SHELL : 1.70 REMARK 200 R MERGE FOR SHELL (I) : 0.97620 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.760 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACITRATE, 18% PEG3350, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.15K 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 105.30000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 19870 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 56230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G 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 A 138 REMARK 465 THR A 139 REMARK 465 SER A 140 REMARK 465 GLY A 141 REMARK 465 SER A 223 REMARK 465 CYS A 224 REMARK 465 ASP A 225 REMARK 465 LYS A 226 REMARK 465 CYS B 214 REMARK 465 LYS C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 SER C 223 REMARK 465 CYS C 224 REMARK 465 ASP C 225 REMARK 465 LYS C 226 REMARK 465 CYS D 214 REMARK 465 GLN E 120 REMARK 465 GLN E 121 REMARK 465 THR E 122 REMARK 465 LEU E 141 REMARK 465 SER E 142 REMARK 465 LEU E 143 REMARK 465 ARG E 144 REMARK 465 SER E 269 REMARK 465 MET E 270 REMARK 465 LYS E 271 REMARK 465 ARG E 272 REMARK 465 LEU E 273 REMARK 465 THR E 274 REMARK 465 HIS E 275 REMARK 465 HIS E 276 REMARK 465 HIS E 277 REMARK 465 HIS E 278 REMARK 465 HIS E 279 REMARK 465 HIS E 280 REMARK 465 PCA F 31 REMARK 465 GLY F 50 REMARK 465 GLY F 51 REMARK 465 PRO F 83 REMARK 465 LYS F 84 REMARK 465 ASN F 85 REMARK 465 GLN F 120 REMARK 465 GLN F 121 REMARK 465 THR F 122 REMARK 465 GLY F 139 REMARK 465 ASP F 140 REMARK 465 LEU F 141 REMARK 465 SER F 142 REMARK 465 LEU F 143 REMARK 465 ARG F 144 REMARK 465 SER F 269 REMARK 465 MET F 270 REMARK 465 LYS F 271 REMARK 465 ARG F 272 REMARK 465 LEU F 273 REMARK 465 THR F 274 REMARK 465 HIS F 275 REMARK 465 HIS F 276 REMARK 465 HIS F 277 REMARK 465 HIS F 278 REMARK 465 HIS F 279 REMARK 465 HIS F 280 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 137 CG CD CE NZ REMARK 470 LYS A 222 CG CD CE NZ REMARK 470 GLU B 213 CG CD OE1 OE2 REMARK 470 LYS C 222 CG CD CE NZ REMARK 470 LYS D 45 CE NZ REMARK 470 ASN E 33 CG OD1 ND2 REMARK 470 ASP E 47 CG OD1 OD2 REMARK 470 ARG E 52 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 84 CG CD CE NZ REMARK 470 ASN E 85 CG OD1 ND2 REMARK 470 ARG E 91 CG CD NE CZ NH1 NH2 REMARK 470 ASN E 100 CG OD1 ND2 REMARK 470 LEU E 103 CG CD1 CD2 REMARK 470 SER E 123 OG REMARK 470 VAL E 124 CG1 CG2 REMARK 470 ASP E 140 CG OD1 OD2 REMARK 470 ARG E 247 CG CD NE CZ NH1 NH2 REMARK 470 ASP F 32 CG OD1 OD2 REMARK 470 GLN F 54 CG CD OE1 NE2 REMARK 470 ASP F 99 CG OD1 OD2 REMARK 470 ASP F 101 CG OD1 OD2 REMARK 470 LEU F 103 CG CD1 CD2 REMARK 470 SER F 123 OG REMARK 470 VAL F 124 CG1 CG2 REMARK 470 LYS F 267 CG CD CE NZ REMARK 470 PHE F 268 CG CD1 CD2 CE1 CE2 CZ 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 CYS B 134 CA - CB - SG ANGL. DEV. = 7.3 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 TRP A 106 46.00 -98.50 REMARK 500 ASP A 152 59.75 73.34 REMARK 500 SER B 30 -135.45 60.90 REMARK 500 ALA B 51 -34.78 75.13 REMARK 500 ASP C 152 64.24 67.78 REMARK 500 SER D 30 -126.76 53.02 REMARK 500 ALA D 51 -37.95 73.10 REMARK 500 ALA D 84 -178.77 -175.73 REMARK 500 ASN E 39 98.37 -160.80 REMARK 500 PRO E 46 35.06 -79.76 REMARK 500 ARG E 87 -120.81 50.61 REMARK 500 GLN E 207 107.45 -164.18 REMARK 500 ARG E 247 35.71 90.94 REMARK 500 LYS E 267 73.95 -115.03 REMARK 500 ASN F 39 98.86 -162.20 REMARK 500 SER F 60 -35.30 -142.88 REMARK 500 ARG F 87 -120.15 57.69 REMARK 500 ASP F 99 35.60 -92.44 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 A 633 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH A 634 DISTANCE = 6.08 ANGSTROMS DBREF 9PI9 A 1 226 PDB 9PI9 9PI9 1 226 DBREF 9PI9 B 1 214 PDB 9PI9 9PI9 1 214 DBREF 9PI9 C 1 226 PDB 9PI9 9PI9 1 226 DBREF 9PI9 D 1 214 PDB 9PI9 9PI9 1 214 DBREF 9PI9 E 31 274 UNP P09758 TACD2_HUMAN 31 274 DBREF 9PI9 F 31 274 UNP P09758 TACD2_HUMAN 31 274 SEQADV 9PI9 GLN E 120 UNP P09758 ASN 120 CONFLICT SEQADV 9PI9 GLN E 208 UNP P09758 ASN 208 CONFLICT SEQADV 9PI9 HIS E 275 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS E 276 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS E 277 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS E 278 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS E 279 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS E 280 UNP P09758 EXPRESSION TAG SEQADV 9PI9 GLN F 120 UNP P09758 ASN 120 CONFLICT SEQADV 9PI9 GLN F 208 UNP P09758 ASN 208 CONFLICT SEQADV 9PI9 HIS F 275 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS F 276 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS F 277 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS F 278 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS F 279 UNP P09758 EXPRESSION TAG SEQADV 9PI9 HIS F 280 UNP P09758 EXPRESSION TAG SEQRES 1 A 226 GLN VAL GLN LEU GLN GLN SER GLY SER GLU LEU LYS LYS SEQRES 2 A 226 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 226 TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 A 226 ALA PRO GLY GLN GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 A 226 THR TYR THR GLY GLU PRO THR TYR THR ASP ASP PHE LYS SEQRES 6 A 226 GLY ARG PHE ALA PHE SER LEU ASP THR SER VAL SER THR SEQRES 7 A 226 ALA TYR LEU GLN ILE SER SER LEU LYS ALA ASP ASP THR SEQRES 8 A 226 ALA VAL TYR PHE CYS ALA ARG GLY GLY PHE GLY SER SER SEQRES 9 A 226 TYR TRP TYR PHE ASP VAL TRP GLY GLN GLY SER LEU VAL SEQRES 10 A 226 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 226 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 226 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 226 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 226 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 226 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 226 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 226 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 A 226 LYS SER CYS ASP LYS SEQRES 1 B 214 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 B 214 GLN ASP VAL SER ILE ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 B 214 TYR ILE THR PRO LEU THR PHE GLY ALA GLY THR LYS VAL SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 226 GLN VAL GLN LEU GLN GLN SER GLY SER GLU LEU LYS LYS SEQRES 2 C 226 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 226 TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 C 226 ALA PRO GLY GLN GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 C 226 THR TYR THR GLY GLU PRO THR TYR THR ASP ASP PHE LYS SEQRES 6 C 226 GLY ARG PHE ALA PHE SER LEU ASP THR SER VAL SER THR SEQRES 7 C 226 ALA TYR LEU GLN ILE SER SER LEU LYS ALA ASP ASP THR SEQRES 8 C 226 ALA VAL TYR PHE CYS ALA ARG GLY GLY PHE GLY SER SER SEQRES 9 C 226 TYR TRP TYR PHE ASP VAL TRP GLY GLN GLY SER LEU VAL SEQRES 10 C 226 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 C 226 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 C 226 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 C 226 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 C 226 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 C 226 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 C 226 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 C 226 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 C 226 LYS SER CYS ASP LYS SEQRES 1 D 214 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 D 214 GLN ASP VAL SER ILE ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 D 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 214 GLN PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 D 214 TYR ILE THR PRO LEU THR PHE GLY ALA GLY THR LYS VAL SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS SEQRES 1 E 250 PCA ASP ASN CYS THR CYS PRO THR ASN LYS MET THR VAL SEQRES 2 E 250 CYS SER PRO ASP GLY PRO GLY GLY ARG CYS GLN CYS ARG SEQRES 3 E 250 ALA LEU GLY SER GLY MET ALA VAL ASP CYS SER THR LEU SEQRES 4 E 250 THR SER LYS CYS LEU LEU LEU LYS ALA ARG MET SER ALA SEQRES 5 E 250 PRO LYS ASN ALA ARG THR LEU VAL ARG PRO SER GLU HIS SEQRES 6 E 250 ALA LEU VAL ASP ASN ASP GLY LEU TYR ASP PRO ASP CYS SEQRES 7 E 250 ASP PRO GLU GLY ARG PHE LYS ALA ARG GLN CYS GLN GLN SEQRES 8 E 250 THR SER VAL CYS TRP CYS VAL ASN SER VAL GLY VAL ARG SEQRES 9 E 250 ARG THR ASP LYS GLY ASP LEU SER LEU ARG CYS ASP GLU SEQRES 10 E 250 LEU VAL ARG THR HIS HIS ILE LEU ILE ASP LEU ARG HIS SEQRES 11 E 250 ARG PRO THR ALA GLY ALA PHE ASN HIS SER ASP LEU ASP SEQRES 12 E 250 ALA GLU LEU ARG ARG LEU PHE ARG GLU ARG TYR ARG LEU SEQRES 13 E 250 HIS PRO LYS PHE VAL ALA ALA VAL HIS TYR GLU GLN PRO SEQRES 14 E 250 THR ILE GLN ILE GLU LEU ARG GLN GLN THR SER GLN LYS SEQRES 15 E 250 ALA ALA GLY ASP VAL ASP ILE GLY ASP ALA ALA TYR TYR SEQRES 16 E 250 PHE GLU ARG ASP ILE LYS GLY GLU SER LEU PHE GLN GLY SEQRES 17 E 250 ARG GLY GLY LEU ASP LEU ARG VAL ARG GLY GLU PRO LEU SEQRES 18 E 250 GLN VAL GLU ARG THR LEU ILE TYR TYR LEU ASP GLU ILE SEQRES 19 E 250 PRO PRO LYS PHE SER MET LYS ARG LEU THR HIS HIS HIS SEQRES 20 E 250 HIS HIS HIS SEQRES 1 F 250 PCA ASP ASN CYS THR CYS PRO THR ASN LYS MET THR VAL SEQRES 2 F 250 CYS SER PRO ASP GLY PRO GLY GLY ARG CYS GLN CYS ARG SEQRES 3 F 250 ALA LEU GLY SER GLY MET ALA VAL ASP CYS SER THR LEU SEQRES 4 F 250 THR SER LYS CYS LEU LEU LEU LYS ALA ARG MET SER ALA SEQRES 5 F 250 PRO LYS ASN ALA ARG THR LEU VAL ARG PRO SER GLU HIS SEQRES 6 F 250 ALA LEU VAL ASP ASN ASP GLY LEU TYR ASP PRO ASP CYS SEQRES 7 F 250 ASP PRO GLU GLY ARG PHE LYS ALA ARG GLN CYS GLN GLN SEQRES 8 F 250 THR SER VAL CYS TRP CYS VAL ASN SER VAL GLY VAL ARG SEQRES 9 F 250 ARG THR ASP LYS GLY ASP LEU SER LEU ARG CYS ASP GLU SEQRES 10 F 250 LEU VAL ARG THR HIS HIS ILE LEU ILE ASP LEU ARG HIS SEQRES 11 F 250 ARG PRO THR ALA GLY ALA PHE ASN HIS SER ASP LEU ASP SEQRES 12 F 250 ALA GLU LEU ARG ARG LEU PHE ARG GLU ARG TYR ARG LEU SEQRES 13 F 250 HIS PRO LYS PHE VAL ALA ALA VAL HIS TYR GLU GLN PRO SEQRES 14 F 250 THR ILE GLN ILE GLU LEU ARG GLN GLN THR SER GLN LYS SEQRES 15 F 250 ALA ALA GLY ASP VAL ASP ILE GLY ASP ALA ALA TYR TYR SEQRES 16 F 250 PHE GLU ARG ASP ILE LYS GLY GLU SER LEU PHE GLN GLY SEQRES 17 F 250 ARG GLY GLY LEU ASP LEU ARG VAL ARG GLY GLU PRO LEU SEQRES 18 F 250 GLN VAL GLU ARG THR LEU ILE TYR TYR LEU ASP GLU ILE SEQRES 19 F 250 PRO PRO LYS PHE SER MET LYS ARG LEU THR HIS HIS HIS SEQRES 20 F 250 HIS HIS HIS MODRES 9PI9 PCA E 31 GLN MODIFIED RESIDUE HET PCA E 31 8 HET NAG G 1 14 HET NAG G 2 14 HET EDO A 301 4 HET EDO A 302 4 HET EDO A 303 4 HET EDO B 301 4 HET EDO B 302 4 HET EDO C 301 4 HET EDO C 302 4 HET EDO C 303 4 HET MAN C 304 12 HET EDO D 301 4 HET EDO D 302 4 HET EDO E 301 4 HET NAG E 302 14 HET CIT E 303 13 HET EDO E 304 4 HET CIT F 301 13 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM CIT CITRIC ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN EDO ETHYLENE GLYCOL HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 PCA C5 H7 N O3 FORMUL 7 NAG 3(C8 H15 N O6) FORMUL 8 EDO 12(C2 H6 O2) FORMUL 16 MAN C6 H12 O6 FORMUL 21 CIT 2(C6 H8 O7) FORMUL 24 HOH *1252(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 THR A 74 VAL A 76 5 3 HELIX 3 AA3 LYS A 87 THR A 91 5 5 HELIX 4 AA4 GLY A 102 TRP A 106 5 5 HELIX 5 AA5 SER A 164 ALA A 166 5 3 HELIX 6 AA6 SER A 195 LEU A 197 5 3 HELIX 7 AA7 GLN B 79 PHE B 83 5 5 HELIX 8 AA8 SER B 121 SER B 127 1 7 HELIX 9 AA9 LYS B 183 GLU B 187 1 5 HELIX 10 AB1 THR C 28 TYR C 32 5 5 HELIX 11 AB2 THR C 74 VAL C 76 5 3 HELIX 12 AB3 LYS C 87 THR C 91 5 5 HELIX 13 AB4 GLY C 102 TRP C 106 5 5 HELIX 14 AB5 SER C 164 ALA C 166 5 3 HELIX 15 AB6 SER C 195 LEU C 197 5 3 HELIX 16 AB7 LYS C 209 ASN C 212 5 4 HELIX 17 AB8 GLN D 79 PHE D 83 5 5 HELIX 18 AB9 SER D 121 SER D 127 1 7 HELIX 19 AC1 LYS D 183 GLU D 187 1 5 HELIX 20 AC2 GLY E 48 ARG E 52 5 5 HELIX 21 AC3 SER E 71 SER E 81 1 11 HELIX 22 AC4 ASN E 168 ARG E 183 1 16 HELIX 23 AC5 HIS E 187 LYS E 189 5 3 HELIX 24 AC6 GLN E 208 LYS E 212 5 5 HELIX 25 AC7 ASP E 218 LYS E 231 1 14 HELIX 26 AC8 SER F 71 ALA F 82 1 12 HELIX 27 AC9 ASN F 168 ARG F 183 1 16 HELIX 28 AD1 HIS F 187 LYS F 189 5 3 HELIX 29 AD2 GLN F 208 LYS F 212 5 5 HELIX 30 AD3 ASP F 218 LYS F 231 1 14 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 ILE A 83 -1 O LEU A 81 N VAL A 20 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N ALA A 69 O GLN A 82 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 SER A 115 VAL A 119 1 O LEU A 116 N GLU A 10 SHEET 3 AA2 6 ALA A 92 GLY A 99 -1 N ALA A 92 O VAL A 117 SHEET 4 AA2 6 GLY A 33 GLN A 39 -1 N ASN A 35 O ALA A 97 SHEET 5 AA2 6 LYS A 46 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 PRO A 58 TYR A 60 -1 O THR A 59 N TRP A 50 SHEET 1 AA3 4 SER A 128 LEU A 132 0 SHEET 2 AA3 4 THR A 143 TYR A 153 -1 O GLY A 147 N LEU A 132 SHEET 3 AA3 4 TYR A 184 PRO A 193 -1 O LEU A 186 N VAL A 150 SHEET 4 AA3 4 VAL A 171 THR A 173 -1 N HIS A 172 O VAL A 189 SHEET 1 AA4 4 SER A 128 LEU A 132 0 SHEET 2 AA4 4 THR A 143 TYR A 153 -1 O GLY A 147 N LEU A 132 SHEET 3 AA4 4 TYR A 184 PRO A 193 -1 O LEU A 186 N VAL A 150 SHEET 4 AA4 4 VAL A 177 LEU A 178 -1 N VAL A 177 O SER A 185 SHEET 1 AA5 3 THR A 159 TRP A 162 0 SHEET 2 AA5 3 ILE A 203 HIS A 208 -1 O ASN A 205 N SER A 161 SHEET 3 AA5 3 THR A 213 ARG A 218 -1 O VAL A 215 N VAL A 206 SHEET 1 AA6 4 LEU B 4 SER B 7 0 SHEET 2 AA6 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA6 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA6 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA7 6 SER B 10 ALA B 13 0 SHEET 2 AA7 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA7 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA7 6 VAL B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AA7 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA7 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49 SHEET 1 AA8 4 SER B 10 ALA B 13 0 SHEET 2 AA8 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA8 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA9 4 SER B 114 PHE B 118 0 SHEET 2 AA9 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AA9 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AA9 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB1 4 ALA B 153 LEU B 154 0 SHEET 2 AB1 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB1 4 VAL B 191 THR B 197 -1 O THR B 197 N LYS B 145 SHEET 4 AB1 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB2 4 GLN C 3 GLN C 6 0 SHEET 2 AB2 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AB2 4 THR C 78 ILE C 83 -1 O LEU C 81 N VAL C 20 SHEET 4 AB2 4 PHE C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AB3 6 GLU C 10 LYS C 12 0 SHEET 2 AB3 6 SER C 115 VAL C 119 1 O LEU C 116 N GLU C 10 SHEET 3 AB3 6 ALA C 92 GLY C 99 -1 N ALA C 92 O VAL C 117 SHEET 4 AB3 6 GLY C 33 GLN C 39 -1 N VAL C 37 O PHE C 95 SHEET 5 AB3 6 LYS C 46 ILE C 51 -1 O MET C 48 N TRP C 36 SHEET 6 AB3 6 PRO C 58 TYR C 60 -1 O THR C 59 N TRP C 50 SHEET 1 AB4 4 GLU C 10 LYS C 12 0 SHEET 2 AB4 4 SER C 115 VAL C 119 1 O LEU C 116 N GLU C 10 SHEET 3 AB4 4 ALA C 92 GLY C 99 -1 N ALA C 92 O VAL C 117 SHEET 4 AB4 4 VAL C 110 TRP C 111 -1 O VAL C 110 N ARG C 98 SHEET 1 AB5 4 SER C 128 LEU C 132 0 SHEET 2 AB5 4 THR C 143 TYR C 153 -1 O LEU C 149 N PHE C 130 SHEET 3 AB5 4 TYR C 184 PRO C 193 -1 O LEU C 186 N VAL C 150 SHEET 4 AB5 4 VAL C 171 THR C 173 -1 N HIS C 172 O VAL C 189 SHEET 1 AB6 4 SER C 128 LEU C 132 0 SHEET 2 AB6 4 THR C 143 TYR C 153 -1 O LEU C 149 N PHE C 130 SHEET 3 AB6 4 TYR C 184 PRO C 193 -1 O LEU C 186 N VAL C 150 SHEET 4 AB6 4 VAL C 177 LEU C 178 -1 N VAL C 177 O SER C 185 SHEET 1 AB7 3 THR C 159 TRP C 162 0 SHEET 2 AB7 3 ILE C 203 HIS C 208 -1 O ASN C 205 N SER C 161 SHEET 3 AB7 3 THR C 213 ARG C 218 -1 O VAL C 215 N VAL C 206 SHEET 1 AB8 4 LEU D 4 SER D 7 0 SHEET 2 AB8 4 VAL D 19 ALA D 25 -1 O LYS D 24 N THR D 5 SHEET 3 AB8 4 ASP D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB8 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AB9 6 SER D 10 ALA D 13 0 SHEET 2 AB9 6 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AB9 6 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AB9 6 VAL D 33 GLN D 38 -1 N GLN D 38 O VAL D 85 SHEET 5 AB9 6 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AB9 6 TYR D 53 ARG D 54 -1 O TYR D 53 N TYR D 49 SHEET 1 AC1 4 SER D 10 ALA D 13 0 SHEET 2 AC1 4 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AC1 4 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AC1 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC2 4 SER D 114 PHE D 118 0 SHEET 2 AC2 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC2 4 TYR D 173 SER D 182 -1 O TYR D 173 N PHE D 139 SHEET 4 AC2 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC3 4 ALA D 153 LEU D 154 0 SHEET 2 AC3 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC3 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC3 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AC4 2 THR E 42 SER E 45 0 SHEET 2 AC4 2 GLN E 54 ALA E 57 -1 O GLN E 54 N SER E 45 SHEET 1 AC5 2 ARG E 117 GLN E 118 0 SHEET 2 AC5 2 TRP E 126 CYS E 127 -1 O TRP E 126 N GLN E 118 SHEET 1 AC6 4 VAL E 191 GLU E 197 0 SHEET 2 AC6 4 THR E 200 ARG E 206 -1 O THR E 200 N GLU E 197 SHEET 3 AC6 4 THR E 151 HIS E 160 -1 N LEU E 158 O ILE E 201 SHEET 4 AC6 4 VAL E 253 ASP E 262 -1 O LEU E 257 N ASP E 157 SHEET 1 AC7 2 THR F 42 PRO F 46 0 SHEET 2 AC7 2 CYS F 53 ALA F 57 -1 O ARG F 56 N VAL F 43 SHEET 1 AC8 2 ARG F 117 GLN F 118 0 SHEET 2 AC8 2 TRP F 126 CYS F 127 -1 O TRP F 126 N GLN F 118 SHEET 1 AC9 4 VAL F 191 GLU F 197 0 SHEET 2 AC9 4 THR F 200 ARG F 206 -1 O GLU F 204 N ALA F 193 SHEET 3 AC9 4 THR F 151 HIS F 160 -1 N LEU F 158 O ILE F 201 SHEET 4 AC9 4 VAL F 253 ASP F 262 -1 O GLU F 254 N ARG F 159 SHEET 1 AD1 2 ARG F 245 VAL F 246 0 SHEET 2 AD1 2 GLU F 249 PRO F 250 -1 O GLU F 249 N VAL F 246 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 148 CYS A 204 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.21 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.05 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.05 SSBOND 6 CYS C 148 CYS C 204 1555 1555 2.05 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.23 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.05 SSBOND 9 CYS E 34 CYS E 53 1555 1555 2.04 SSBOND 10 CYS E 36 CYS E 66 1555 1555 2.02 SSBOND 11 CYS E 44 CYS E 55 1555 1555 2.06 SSBOND 12 CYS E 73 CYS E 108 1555 1555 2.04 SSBOND 13 CYS E 119 CYS E 125 1555 1555 2.05 SSBOND 14 CYS E 127 CYS E 145 1555 1555 2.05 SSBOND 15 CYS F 34 CYS F 53 1555 1555 2.05 SSBOND 16 CYS F 36 CYS F 66 1555 1555 2.05 SSBOND 17 CYS F 44 CYS F 55 1555 1555 2.08 SSBOND 18 CYS F 73 CYS F 108 1555 1555 2.05 SSBOND 19 CYS F 119 CYS F 125 1555 1555 2.05 SSBOND 20 CYS F 127 CYS F 145 1555 1555 2.04 LINK C PCA E 31 N ASP E 32 1555 1555 1.33 LINK ND2 ASN E 168 C1 NAG E 302 1555 1555 1.44 LINK ND2 ASN F 168 C1 NAG G 1 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 CISPEP 1 PHE A 154 PRO A 155 0 -8.84 CISPEP 2 GLU A 156 PRO A 157 0 -0.66 CISPEP 3 SER B 7 PRO B 8 0 -7.38 CISPEP 4 THR B 94 PRO B 95 0 -3.82 CISPEP 5 TYR B 140 PRO B 141 0 1.08 CISPEP 6 PHE C 154 PRO C 155 0 -7.24 CISPEP 7 GLU C 156 PRO C 157 0 -0.28 CISPEP 8 SER D 7 PRO D 8 0 -7.49 CISPEP 9 THR D 94 PRO D 95 0 -6.22 CISPEP 10 TYR D 140 PRO D 141 0 0.82 CISPEP 11 GLN E 198 PRO E 199 0 3.57 CISPEP 12 GLN F 198 PRO F 199 0 3.72 CRYST1 50.430 210.600 78.060 90.00 105.56 90.00 P 1 21 1 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 0.019829 0.000000 0.005522 0.00000 SCALE2 0.000000 0.004748 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013298 0.00000