HEADER PLANT PROTEIN 16-OCT-24 9H39 TITLE CRYSTAL STRUCTURE OF LOTUS JAPONICUS CHIP13 EXTRACELLULAR DOMAIN IN TITLE 2 COMPLEX WITH A NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSM TYPE RECEPTOR KINASE; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-LYS13 VHH; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LOTUS JAPONICUS; SOURCE 3 ORGANISM_TAXID: 34305; SOURCE 4 GENE: LYS13; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, LYSM, VHH, PLANT IMMUNITY, PLANT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.GYSEL,K.R.ANDERSEN REVDAT 1 16-JUL-25 9H39 0 JRNL AUTH K.GYSEL,S.B.HANSEN,H.RUEBSAM,H.M.A.B.ALSARRAF,E.MADLAND, JRNL AUTH 2 J.X.J.CHENG,C.BAADEGAARD,E.C.POULSEN,M.VINTHER,S.FORT, JRNL AUTH 3 J.STOUGAARD,K.R.ANDERSEN JRNL TITL STRUCTURAL BASIS FOR SIZE-SELECTIVE PERCEPTION OF CHITIN IN JRNL TITL 2 PLANTS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.66 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) : 1.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 94602 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.790 REMARK 3 FREE R VALUE TEST SET COUNT : 2636 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 49.0800 - 4.4300 0.98 5027 144 0.1429 0.1677 REMARK 3 2 4.4300 - 3.5200 0.99 4919 139 0.1440 0.1959 REMARK 3 3 3.5100 - 3.0700 0.99 4928 139 0.1739 0.2376 REMARK 3 4 3.0700 - 2.7900 0.99 4905 142 0.1836 0.2217 REMARK 3 5 2.7900 - 2.5900 0.99 4878 140 0.2029 0.2427 REMARK 3 6 2.5900 - 2.4400 0.99 4891 141 0.1967 0.2181 REMARK 3 7 2.4400 - 2.3200 0.99 4844 138 0.1962 0.2579 REMARK 3 8 2.3200 - 2.2100 0.99 4851 140 0.1993 0.2551 REMARK 3 9 2.2100 - 2.1300 0.99 4864 138 0.2017 0.2384 REMARK 3 10 2.1300 - 2.0600 0.99 4848 137 0.2207 0.2617 REMARK 3 11 2.0600 - 1.9900 0.99 4847 141 0.2211 0.2612 REMARK 3 12 1.9900 - 1.9300 0.99 4832 137 0.2301 0.2124 REMARK 3 13 1.9300 - 1.8800 0.99 4778 137 0.2519 0.2985 REMARK 3 14 1.8800 - 1.8400 0.98 4798 138 0.2942 0.3689 REMARK 3 15 1.8400 - 1.8000 0.98 4819 138 0.3514 0.4268 REMARK 3 16 1.8000 - 1.7600 0.98 4785 138 0.4080 0.4173 REMARK 3 17 1.7600 - 1.7200 0.98 4713 138 0.4166 0.4219 REMARK 3 18 1.7200 - 1.6900 0.97 4810 139 0.4308 0.4252 REMARK 3 19 1.6900 - 1.6600 0.95 4629 132 0.4609 0.5060 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) : 0.313 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.576 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.01 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.93 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 : 0.003 5751 REMARK 3 ANGLE : 0.677 7890 REMARK 3 CHIRALITY : 0.047 958 REMARK 3 PLANARITY : 0.005 1004 REMARK 3 DIHEDRAL : 12.798 2373 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 26 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.9366 -14.1395 -23.8178 REMARK 3 T TENSOR REMARK 3 T11: 0.3699 T22: 0.2887 REMARK 3 T33: 0.2540 T12: 0.0802 REMARK 3 T13: -0.0246 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 9.8008 L22: 8.8514 REMARK 3 L33: 9.5970 L12: 1.4294 REMARK 3 L13: 5.5753 L23: 1.8907 REMARK 3 S TENSOR REMARK 3 S11: 0.1678 S12: 0.1074 S13: -0.3214 REMARK 3 S21: 0.5137 S22: -0.1429 S23: -0.6703 REMARK 3 S31: 0.8982 S32: 0.7239 S33: -0.0150 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9043 -13.6345 -42.4873 REMARK 3 T TENSOR REMARK 3 T11: 0.3210 T22: 0.3392 REMARK 3 T33: 0.2690 T12: 0.0032 REMARK 3 T13: -0.0061 T23: -0.0442 REMARK 3 L TENSOR REMARK 3 L11: 2.0793 L22: 2.6721 REMARK 3 L33: 7.6523 L12: -0.8645 REMARK 3 L13: 0.9003 L23: -1.9484 REMARK 3 S TENSOR REMARK 3 S11: 0.1502 S12: 0.2911 S13: -0.1218 REMARK 3 S21: -0.0640 S22: 0.0027 S23: 0.0319 REMARK 3 S31: 0.5176 S32: -0.1784 S33: -0.1527 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.5271 -9.9216 -39.7581 REMARK 3 T TENSOR REMARK 3 T11: 0.3033 T22: 0.6438 REMARK 3 T33: 0.3952 T12: 0.0708 REMARK 3 T13: -0.0064 T23: 0.0450 REMARK 3 L TENSOR REMARK 3 L11: 7.0108 L22: 6.4522 REMARK 3 L33: 7.1356 L12: -2.1896 REMARK 3 L13: -4.6568 L23: 5.6982 REMARK 3 S TENSOR REMARK 3 S11: -0.0463 S12: 0.6932 S13: 0.0602 REMARK 3 S21: -0.3234 S22: 0.0644 S23: -0.4502 REMARK 3 S31: 0.0172 S32: 0.8657 S33: -0.0122 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 144 THROUGH 170 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2163 -15.7476 -37.4971 REMARK 3 T TENSOR REMARK 3 T11: 0.3938 T22: 0.6535 REMARK 3 T33: 0.4878 T12: 0.1659 REMARK 3 T13: -0.0158 T23: -0.0223 REMARK 3 L TENSOR REMARK 3 L11: 4.1494 L22: 5.1038 REMARK 3 L33: 2.7354 L12: 1.4921 REMARK 3 L13: -1.0904 L23: -0.3726 REMARK 3 S TENSOR REMARK 3 S11: 0.0271 S12: 0.3199 S13: -0.2983 REMARK 3 S21: 0.0293 S22: -0.0494 S23: -1.1771 REMARK 3 S31: 0.4871 S32: 1.2913 S33: 0.0639 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7810 -18.9703 -33.3084 REMARK 3 T TENSOR REMARK 3 T11: 0.4715 T22: 0.3704 REMARK 3 T33: 0.3143 T12: -0.0907 REMARK 3 T13: -0.0412 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 2.6581 L22: 2.2847 REMARK 3 L33: 3.9665 L12: 0.6143 REMARK 3 L13: -0.6769 L23: -0.6456 REMARK 3 S TENSOR REMARK 3 S11: -0.0001 S12: 0.2442 S13: -0.3277 REMARK 3 S21: 0.0474 S22: 0.0413 S23: 0.2599 REMARK 3 S31: 0.7653 S32: -0.6247 S33: 0.0962 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 248 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.4470 -7.9953 -27.0601 REMARK 3 T TENSOR REMARK 3 T11: 0.3393 T22: 0.3979 REMARK 3 T33: 0.3304 T12: 0.0441 REMARK 3 T13: 0.0445 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 7.0575 L22: 3.5719 REMARK 3 L33: 8.0803 L12: 1.6701 REMARK 3 L13: 2.9747 L23: 0.6698 REMARK 3 S TENSOR REMARK 3 S11: -0.0442 S12: -0.1431 S13: 0.2588 REMARK 3 S21: 0.2433 S22: -0.0649 S23: 0.3680 REMARK 3 S31: -0.0489 S32: -1.0176 S33: 0.0967 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9066 -11.3319 -85.3739 REMARK 3 T TENSOR REMARK 3 T11: 0.3324 T22: 0.4599 REMARK 3 T33: 0.3362 T12: 0.0016 REMARK 3 T13: 0.0234 T23: -0.0494 REMARK 3 L TENSOR REMARK 3 L11: 7.9998 L22: 6.0347 REMARK 3 L33: 3.9873 L12: 1.3123 REMARK 3 L13: 4.5417 L23: -1.6959 REMARK 3 S TENSOR REMARK 3 S11: -0.0991 S12: 0.6651 S13: -0.1222 REMARK 3 S21: -0.4491 S22: -0.0105 S23: 0.5034 REMARK 3 S31: 0.5367 S32: -0.4121 S33: 0.1120 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.4281 -13.8911 -66.5392 REMARK 3 T TENSOR REMARK 3 T11: 0.3201 T22: 0.3946 REMARK 3 T33: 0.3302 T12: 0.0590 REMARK 3 T13: 0.0362 T23: 0.0546 REMARK 3 L TENSOR REMARK 3 L11: 2.1433 L22: 1.5971 REMARK 3 L33: 7.3406 L12: 0.3250 REMARK 3 L13: 0.5193 L23: 1.1369 REMARK 3 S TENSOR REMARK 3 S11: 0.0688 S12: -0.2701 S13: -0.2203 REMARK 3 S21: 0.1371 S22: -0.0437 S23: -0.0257 REMARK 3 S31: 0.5537 S32: 0.3446 S33: -0.0589 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.4508 -6.1721 -69.1497 REMARK 3 T TENSOR REMARK 3 T11: 0.3249 T22: 0.6725 REMARK 3 T33: 0.4084 T12: 0.0800 REMARK 3 T13: 0.0348 T23: -0.0192 REMARK 3 L TENSOR REMARK 3 L11: 2.2028 L22: 6.2110 REMARK 3 L33: 8.1527 L12: 3.3597 REMARK 3 L13: -4.1876 L23: -6.7754 REMARK 3 S TENSOR REMARK 3 S11: -0.1022 S12: -0.4317 S13: 0.2287 REMARK 3 S21: 0.4769 S22: 0.1965 S23: 0.4151 REMARK 3 S31: -0.6200 S32: -0.5319 S33: -0.1404 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 144 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.5783 -14.6406 -74.4235 REMARK 3 T TENSOR REMARK 3 T11: 0.2969 T22: 0.3038 REMARK 3 T33: 0.2500 T12: 0.0030 REMARK 3 T13: -0.0147 T23: 0.0089 REMARK 3 L TENSOR REMARK 3 L11: 6.5303 L22: 2.8342 REMARK 3 L33: 5.9617 L12: -0.6743 REMARK 3 L13: -0.6584 L23: -0.0679 REMARK 3 S TENSOR REMARK 3 S11: -0.0166 S12: -0.1995 S13: -0.4487 REMARK 3 S21: -0.0979 S22: -0.0372 S23: 0.2717 REMARK 3 S31: 0.6192 S32: -0.1662 S33: 0.1135 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 234 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.0030 -9.6254 -85.2030 REMARK 3 T TENSOR REMARK 3 T11: 0.3623 T22: 0.7131 REMARK 3 T33: 0.4019 T12: 0.1228 REMARK 3 T13: 0.0829 T23: 0.0158 REMARK 3 L TENSOR REMARK 3 L11: 4.3926 L22: 3.8605 REMARK 3 L33: 2.5550 L12: -2.0610 REMARK 3 L13: 1.2351 L23: -1.6402 REMARK 3 S TENSOR REMARK 3 S11: 0.2870 S12: 0.5891 S13: 0.1833 REMARK 3 S21: -0.4797 S22: -0.3800 S23: -0.6101 REMARK 3 S31: 0.4521 S32: 1.2350 S33: 0.0432 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 235 THROUGH 250 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1811 -11.2958 -73.4822 REMARK 3 T TENSOR REMARK 3 T11: 0.4023 T22: 0.8338 REMARK 3 T33: 0.4546 T12: 0.0639 REMARK 3 T13: 0.0752 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 6.3787 L22: 3.3979 REMARK 3 L33: 3.9470 L12: 0.0840 REMARK 3 L13: 2.5723 L23: -0.8867 REMARK 3 S TENSOR REMARK 3 S11: 0.2983 S12: -0.0297 S13: 0.4892 REMARK 3 S21: 0.0636 S22: -0.2410 S23: -0.3625 REMARK 3 S31: -0.7309 S32: 1.5727 S33: -0.1598 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.1688 0.5167 -9.3527 REMARK 3 T TENSOR REMARK 3 T11: 0.4617 T22: 0.4724 REMARK 3 T33: 0.5400 T12: 0.1101 REMARK 3 T13: 0.0405 T23: 0.0243 REMARK 3 L TENSOR REMARK 3 L11: 4.5058 L22: 6.9698 REMARK 3 L33: 4.5199 L12: -0.8268 REMARK 3 L13: 4.1765 L23: 1.2806 REMARK 3 S TENSOR REMARK 3 S11: -0.1988 S12: -0.7017 S13: 0.4458 REMARK 3 S21: 1.0008 S22: 0.4196 S23: 0.2229 REMARK 3 S31: -2.6458 S32: -2.0360 S33: -0.1066 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 8 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.7480 -5.3918 12.8536 REMARK 3 T TENSOR REMARK 3 T11: 0.7025 T22: 0.7147 REMARK 3 T33: 0.3919 T12: -0.0096 REMARK 3 T13: 0.0419 T23: 0.0469 REMARK 3 L TENSOR REMARK 3 L11: 7.0578 L22: 5.7793 REMARK 3 L33: 4.7091 L12: -6.3832 REMARK 3 L13: 5.7385 L23: -5.2141 REMARK 3 S TENSOR REMARK 3 S11: -0.3638 S12: -1.9981 S13: -0.4075 REMARK 3 S21: 1.2820 S22: 0.8390 S23: 0.1795 REMARK 3 S31: 0.6657 S32: -0.7469 S33: -0.3145 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4098 -3.5295 -11.8413 REMARK 3 T TENSOR REMARK 3 T11: 0.3890 T22: 0.1980 REMARK 3 T33: 0.3472 T12: -0.0157 REMARK 3 T13: -0.0029 T23: -0.0036 REMARK 3 L TENSOR REMARK 3 L11: 2.8395 L22: 0.1429 REMARK 3 L33: 9.7204 L12: -0.5947 REMARK 3 L13: 2.4298 L23: -0.9568 REMARK 3 S TENSOR REMARK 3 S11: 0.0004 S12: 0.0064 S13: 0.0559 REMARK 3 S21: 0.0105 S22: 0.0207 S23: 0.0448 REMARK 3 S31: -0.3507 S32: -0.1831 S33: 0.0135 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 45 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.7023 6.0670 0.9426 REMARK 3 T TENSOR REMARK 3 T11: 0.4372 T22: 0.2457 REMARK 3 T33: 0.3115 T12: -0.0531 REMARK 3 T13: 0.0084 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 1.7835 L22: 9.6982 REMARK 3 L33: 4.7726 L12: 0.6925 REMARK 3 L13: 0.2354 L23: 6.6440 REMARK 3 S TENSOR REMARK 3 S11: 0.1076 S12: -0.2056 S13: 0.0791 REMARK 3 S21: 0.0498 S22: -0.1424 S23: 0.4468 REMARK 3 S31: 0.1684 S32: 0.1827 S33: 0.0161 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 46 THROUGH 56 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2821 -3.9529 -8.5146 REMARK 3 T TENSOR REMARK 3 T11: 0.4869 T22: 0.3127 REMARK 3 T33: 0.3768 T12: 0.0543 REMARK 3 T13: -0.0182 T23: 0.0378 REMARK 3 L TENSOR REMARK 3 L11: 5.5967 L22: 4.2274 REMARK 3 L33: 4.3239 L12: -3.8734 REMARK 3 L13: -4.2217 L23: 3.9594 REMARK 3 S TENSOR REMARK 3 S11: 0.0723 S12: -0.0302 S13: -0.0280 REMARK 3 S21: -0.8482 S22: 0.3414 S23: -0.7784 REMARK 3 S31: -0.4904 S32: 1.1381 S33: -0.2436 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 57 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7135 -2.1487 -0.0459 REMARK 3 T TENSOR REMARK 3 T11: 0.4226 T22: 0.5818 REMARK 3 T33: 0.5151 T12: -0.0121 REMARK 3 T13: -0.0837 T23: -0.0690 REMARK 3 L TENSOR REMARK 3 L11: 7.3235 L22: 4.0066 REMARK 3 L33: 5.6258 L12: 0.0195 REMARK 3 L13: 0.8781 L23: 4.7297 REMARK 3 S TENSOR REMARK 3 S11: 0.0129 S12: -0.5484 S13: 0.9780 REMARK 3 S21: 0.4068 S22: 0.4761 S23: -1.4295 REMARK 3 S31: -0.2386 S32: 1.8856 S33: -0.5269 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 64 THROUGH 82A ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1695 -8.3316 -3.7882 REMARK 3 T TENSOR REMARK 3 T11: 0.4130 T22: 0.2622 REMARK 3 T33: 0.3409 T12: 0.0188 REMARK 3 T13: 0.0037 T23: 0.0677 REMARK 3 L TENSOR REMARK 3 L11: 6.4944 L22: 4.2177 REMARK 3 L33: 3.8338 L12: -0.2197 REMARK 3 L13: 3.3023 L23: 2.4502 REMARK 3 S TENSOR REMARK 3 S11: -0.1091 S12: -0.3278 S13: -0.1712 REMARK 3 S21: 0.1695 S22: 0.0613 S23: -0.1082 REMARK 3 S31: 0.7983 S32: -0.0035 S33: 0.0286 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 82B THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7527 1.1690 0.7771 REMARK 3 T TENSOR REMARK 3 T11: 0.3695 T22: 0.3434 REMARK 3 T33: 0.3652 T12: -0.0381 REMARK 3 T13: -0.0339 T23: -0.0283 REMARK 3 L TENSOR REMARK 3 L11: 1.7303 L22: 4.1322 REMARK 3 L33: 2.3872 L12: -0.5452 REMARK 3 L13: -0.7161 L23: -2.2165 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: -0.3179 S13: 0.1442 REMARK 3 S21: 0.4664 S22: -0.1720 S23: -0.2076 REMARK 3 S31: 0.0773 S32: 0.9221 S33: 0.1155 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 98 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.8531 5.1629 -17.4502 REMARK 3 T TENSOR REMARK 3 T11: 0.3958 T22: 0.2000 REMARK 3 T33: 0.3949 T12: -0.0384 REMARK 3 T13: -0.0137 T23: 0.0351 REMARK 3 L TENSOR REMARK 3 L11: 2.2205 L22: 4.2493 REMARK 3 L33: 8.3320 L12: -0.8342 REMARK 3 L13: -2.2797 L23: 3.9501 REMARK 3 S TENSOR REMARK 3 S11: -0.0705 S12: 0.2036 S13: 0.0380 REMARK 3 S21: -0.4600 S22: 0.1054 S23: -0.2413 REMARK 3 S31: -0.5341 S32: -0.1108 S33: -0.1313 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 112 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5389 0.2024 12.6924 REMARK 3 T TENSOR REMARK 3 T11: 0.5430 T22: 0.8114 REMARK 3 T33: 0.3839 T12: -0.0976 REMARK 3 T13: -0.0201 T23: -0.0193 REMARK 3 L TENSOR REMARK 3 L11: 4.7038 L22: 3.8828 REMARK 3 L33: 5.0521 L12: -4.1842 REMARK 3 L13: 4.6891 L23: -4.4742 REMARK 3 S TENSOR REMARK 3 S11: 0.0372 S12: -1.5800 S13: 0.0823 REMARK 3 S21: 0.9694 S22: 0.1620 S23: -0.2628 REMARK 3 S31: -0.3689 S32: 0.9904 S33: -0.1799 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.8166 0.2014-103.1545 REMARK 3 T TENSOR REMARK 3 T11: 0.3846 T22: 0.5965 REMARK 3 T33: 0.3783 T12: 0.0417 REMARK 3 T13: 0.0341 T23: 0.0360 REMARK 3 L TENSOR REMARK 3 L11: 2.4077 L22: 1.4051 REMARK 3 L33: 8.2258 L12: -0.8661 REMARK 3 L13: 3.1103 L23: -1.4774 REMARK 3 S TENSOR REMARK 3 S11: 0.0707 S12: 0.6070 S13: 0.3270 REMARK 3 S21: -0.2386 S22: -0.2100 S23: 0.0052 REMARK 3 S31: 0.0237 S32: 0.8301 S33: 0.1165 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 34 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.8736 8.5810-105.1142 REMARK 3 T TENSOR REMARK 3 T11: 0.7322 T22: 0.8510 REMARK 3 T33: 0.5258 T12: 0.2872 REMARK 3 T13: 0.0099 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 8.3465 L22: 2.6697 REMARK 3 L33: 8.7137 L12: 0.1556 REMARK 3 L13: 0.0455 L23: -2.4679 REMARK 3 S TENSOR REMARK 3 S11: 0.4615 S12: 0.0760 S13: 0.6689 REMARK 3 S21: -0.0792 S22: -0.1104 S23: 0.6959 REMARK 3 S31: -1.2829 S32: -1.3483 S33: -0.3174 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 64 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.1122 4.2205-101.8594 REMARK 3 T TENSOR REMARK 3 T11: 0.4213 T22: 0.5690 REMARK 3 T33: 0.3919 T12: 0.0618 REMARK 3 T13: 0.0138 T23: 0.0391 REMARK 3 L TENSOR REMARK 3 L11: 1.6495 L22: 0.8937 REMARK 3 L33: 8.1135 L12: -0.3807 REMARK 3 L13: 0.2362 L23: -0.9783 REMARK 3 S TENSOR REMARK 3 S11: -0.0112 S12: 0.4676 S13: 0.2078 REMARK 3 S21: -0.1197 S22: 0.0621 S23: 0.2879 REMARK 3 S31: -0.4680 S32: -0.7271 S33: -0.0338 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 112 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7158 5.5651-122.6533 REMARK 3 T TENSOR REMARK 3 T11: 0.6658 T22: 1.0253 REMARK 3 T33: 0.3996 T12: 0.0610 REMARK 3 T13: -0.0412 T23: 0.0642 REMARK 3 L TENSOR REMARK 3 L11: 4.8056 L22: 10.0234 REMARK 3 L33: 3.8880 L12: 2.9724 REMARK 3 L13: -4.3126 L23: -2.6665 REMARK 3 S TENSOR REMARK 3 S11: -0.2094 S12: 1.2060 S13: -0.2040 REMARK 3 S21: -1.1711 S22: -0.1209 S23: 0.7266 REMARK 3 S31: -0.0022 S32: 1.3303 S33: 0.1648 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 9H39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1292140906. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-FEB-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX IV REMARK 200 BEAMLINE : BIOMAX REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94949 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660 REMARK 200 RESOLUTION RANGE LOW (A) : 49.080 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.05647 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 3.45200 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE 0.1 M BIS TRIS REMARK 280 PROPANE 7.5 20 % W/V PEG 3350, PH 7.5, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 292.15K 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 27.54500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, N, E, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, M, F 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 GLN A 249 REMARK 465 ILE A 250 REMARK 465 ALA A 251 REMARK 465 ALA A 252 REMARK 465 SER A 253 REMARK 465 HIS A 254 REMARK 465 HIS A 255 REMARK 465 HIS A 256 REMARK 465 HIS A 257 REMARK 465 HIS A 258 REMARK 465 HIS A 259 REMARK 465 ALA B 251 REMARK 465 ALA B 252 REMARK 465 SER B 253 REMARK 465 HIS B 254 REMARK 465 HIS B 255 REMARK 465 HIS B 256 REMARK 465 HIS B 257 REMARK 465 HIS B 258 REMARK 465 HIS B 259 REMARK 465 MET C 0 REMARK 465 HIS C 120 REMARK 465 HIS C 121 REMARK 465 HIS C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 MET D 0 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 HIS D 124 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH C 279 O HOH C 350 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 58 -142.04 -149.89 REMARK 500 SER A 87 -152.83 -106.69 REMARK 500 LYS A 227 66.93 -110.17 REMARK 500 SER B 58 -137.13 -150.60 REMARK 500 SER B 87 -154.88 -112.86 REMARK 500 ASP B 107 -1.91 76.91 REMARK 500 ASN C 32 -128.93 -102.82 REMARK 500 THR D 28 -176.29 -171.46 REMARK 500 ASN D 32 -121.37 -99.38 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 478 DISTANCE = 6.91 ANGSTROMS REMARK 525 HOH B 558 DISTANCE = 5.87 ANGSTROMS DBREF 9H39 A 33 253 UNP D3KU00 D3KU00_LOTJA 33 253 DBREF 9H39 B 33 253 UNP D3KU00 D3KU00_LOTJA 33 253 DBREF 9H39 C 0 124 PDB 9H39 9H39 0 124 DBREF 9H39 D 0 124 PDB 9H39 9H39 0 124 SEQADV 9H39 HIS A 254 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS A 255 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS A 256 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS A 257 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS A 258 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS A 259 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 254 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 255 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 256 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 257 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 258 UNP D3KU00 EXPRESSION TAG SEQADV 9H39 HIS B 259 UNP D3KU00 EXPRESSION TAG SEQRES 1 A 227 PCA GLN GLU TYR LEU ASN ASN ASN GLN LEU ASP CYS ASP SEQRES 2 A 227 ASN THR HIS ASN SER THR TYR GLY ASN VAL CYS ASN SER SEQRES 3 A 227 VAL THR SER CYS GLN SER TYR LEU THR PHE LYS SER SER SEQRES 4 A 227 SER PRO GLU TYR ASN THR PRO SER SER ILE SER TYR LEU SEQRES 5 A 227 LEU ASN SER THR PRO SER LEU VAL ALA LYS SER ASN ASN SEQRES 6 A 227 ILE THR ASP VAL THR PRO ILE ILE THR ASP THR MET VAL SEQRES 7 A 227 THR VAL PRO VAL THR CYS SER CYS SER GLY GLY ARG TYR SEQRES 8 A 227 GLN HIS ASN ALA THR TYR ASN LEU LYS LYS THR GLY GLU SEQRES 9 A 227 THR TYR PHE SER ILE ALA ASN ASN THR TYR GLN SER LEU SEQRES 10 A 227 THR THR CYS GLN ALA LEU MET ALA GLN ASN PRO TYR ASP SEQRES 11 A 227 ALA LYS ASN LEU PHE ALA GLY ASP ASP LEU HIS VAL PRO SEQRES 12 A 227 LEU ARG CYS ALA CYS PRO THR LYS LYS GLN SER ASP ALA SEQRES 13 A 227 GLY PHE LYS TYR LEU LEU THR TYR LEU VAL SER GLN GLY SEQRES 14 A 227 GLU SER PRO ASP SER ILE ALA GLU ILE PHE GLY VAL ASP SEQRES 15 A 227 THR GLN SER VAL LEU ASP ALA ASN GLU LEU ASP SER LYS SEQRES 16 A 227 SER VAL VAL PHE TYR PHE THR PRO LEU LEU VAL PRO LEU SEQRES 17 A 227 LYS THR GLU PRO PRO ALA ARG LEU GLN ILE ALA ALA SER SEQRES 18 A 227 HIS HIS HIS HIS HIS HIS SEQRES 1 B 227 PCA GLN GLU TYR LEU ASN ASN ASN GLN LEU ASP CYS ASP SEQRES 2 B 227 ASN THR HIS ASN SER THR TYR GLY ASN VAL CYS ASN SER SEQRES 3 B 227 VAL THR SER CYS GLN SER TYR LEU THR PHE LYS SER SER SEQRES 4 B 227 SER PRO GLU TYR ASN THR PRO SER SER ILE SER TYR LEU SEQRES 5 B 227 LEU ASN SER THR PRO SER LEU VAL ALA LYS SER ASN ASN SEQRES 6 B 227 ILE THR ASP VAL THR PRO ILE ILE THR ASP THR MET VAL SEQRES 7 B 227 THR VAL PRO VAL THR CYS SER CYS SER GLY GLY ARG TYR SEQRES 8 B 227 GLN HIS ASN ALA THR TYR ASN LEU LYS LYS THR GLY GLU SEQRES 9 B 227 THR TYR PHE SER ILE ALA ASN ASN THR TYR GLN SER LEU SEQRES 10 B 227 THR THR CYS GLN ALA LEU MET ALA GLN ASN PRO TYR ASP SEQRES 11 B 227 ALA LYS ASN LEU PHE ALA GLY ASP ASP LEU HIS VAL PRO SEQRES 12 B 227 LEU ARG CYS ALA CYS PRO THR LYS LYS GLN SER ASP ALA SEQRES 13 B 227 GLY PHE LYS TYR LEU LEU THR TYR LEU VAL SER GLN GLY SEQRES 14 B 227 GLU SER PRO ASP SER ILE ALA GLU ILE PHE GLY VAL ASP SEQRES 15 B 227 THR GLN SER VAL LEU ASP ALA ASN GLU LEU ASP SER LYS SEQRES 16 B 227 SER VAL VAL PHE TYR PHE THR PRO LEU LEU VAL PRO LEU SEQRES 17 B 227 LYS THR GLU PRO PRO ALA ARG LEU GLN ILE ALA ALA SER SEQRES 18 B 227 HIS HIS HIS HIS HIS HIS SEQRES 1 C 128 MET GLN LEU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 C 128 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA THR SER SEQRES 3 C 128 GLY THR THR PHE ARG LEU ASN THR MET GLY TRP TYR ARG SEQRES 4 C 128 GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA THR ILE SEQRES 5 C 128 SER ARG ASP PHE LYS THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 C 128 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS HIS THR SEQRES 7 C 128 VAL ASP LEU GLN MET ASN SER LEU THR PRO GLU ASP THR SEQRES 8 C 128 ALA VAL TYR TYR CYS LEU VAL ARG ASP GLN ARG GLU TRP SEQRES 9 C 128 TYR GLY PRO GLU TYR ASP ASN TRP GLY ARG GLY THR GLN SEQRES 10 C 128 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 128 MET GLN LEU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 D 128 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA THR SER SEQRES 3 D 128 GLY THR THR PHE ARG LEU ASN THR MET GLY TRP TYR ARG SEQRES 4 D 128 GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA THR ILE SEQRES 5 D 128 SER ARG ASP PHE LYS THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 D 128 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS HIS THR SEQRES 7 D 128 VAL ASP LEU GLN MET ASN SER LEU THR PRO GLU ASP THR SEQRES 8 D 128 ALA VAL TYR TYR CYS LEU VAL ARG ASP GLN ARG GLU TRP SEQRES 9 D 128 TYR GLY PRO GLU TYR ASP ASN TRP GLY ARG GLY THR GLN SEQRES 10 D 128 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS MODRES 9H39 PCA A 33 GLN MODIFIED RESIDUE MODRES 9H39 PCA B 33 GLN MODIFIED RESIDUE HET PCA A 33 8 HET PCA B 33 8 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG E 1 14 HET NAG E 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET FUC F 4 10 HET NAG G 1 14 HET NAG G 2 14 HET FUC G 3 10 HET NAG B 301 14 HET NAG B 302 14 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 1 PCA 2(C5 H7 N O3) FORMUL 5 NAG 12(C8 H15 N O6) FORMUL 5 BMA 2(C6 H12 O6) FORMUL 8 FUC 2(C6 H12 O5) FORMUL 12 HOH *582(H2 O) HELIX 1 AA1 ASN A 39 ASP A 43 5 5 HELIX 2 AA2 HIS A 48 GLY A 53 5 6 HELIX 3 AA3 THR A 77 ASN A 86 1 10 HELIX 4 AA4 THR A 88 ASN A 96 1 9 HELIX 5 AA5 THR A 137 ASN A 144 1 8 HELIX 6 AA6 THR A 151 GLN A 158 1 8 HELIX 7 AA7 THR A 182 ALA A 188 1 7 HELIX 8 AA8 SER A 203 PHE A 211 1 9 HELIX 9 AA9 ASP A 214 ASN A 222 1 9 HELIX 10 AB1 ASN B 39 ASP B 43 5 5 HELIX 11 AB2 HIS B 48 GLY B 53 5 6 HELIX 12 AB3 THR B 77 ASN B 86 1 10 HELIX 13 AB4 THR B 88 ASN B 97 1 10 HELIX 14 AB5 THR B 137 ASN B 144 1 8 HELIX 15 AB6 THR B 151 GLN B 158 1 8 HELIX 16 AB7 THR B 182 ALA B 188 1 7 HELIX 17 AB8 SER B 203 PHE B 211 1 9 HELIX 18 AB9 ASP B 214 ASN B 222 1 9 HELIX 19 AC1 ASP C 61 LYS C 64 5 4 HELIX 20 AC2 THR C 83 THR C 87 5 5 HELIX 21 AC3 ASP D 61 LYS D 64 5 4 HELIX 22 AC4 THR D 83 THR D 87 5 5 SHEET 1 AA1 4 ASN A 54 VAL A 55 0 SHEET 2 AA1 4 ARG A 122 ASN A 130 -1 O TYR A 123 N ASN A 54 SHEET 3 AA1 4 MET A 109 SER A 119 -1 N SER A 119 O ARG A 122 SHEET 4 AA1 4 SER A 61 LYS A 69 -1 N CYS A 62 O CYS A 116 SHEET 1 AA2 3 ASN A 54 VAL A 55 0 SHEET 2 AA2 3 ARG A 122 ASN A 130 -1 O TYR A 123 N ASN A 54 SHEET 3 AA2 3 ASP A 171 LEU A 176 -1 O VAL A 174 N ALA A 127 SHEET 1 AA3 2 TYR A 192 LEU A 197 0 SHEET 2 AA3 2 PRO A 235 LEU A 240 -1 O LEU A 236 N TYR A 196 SHEET 1 AA4 3 VAL A 229 PHE A 231 0 SHEET 2 AA4 3 LEU C 18 THR C 28 1 O GLY C 26 N VAL A 230 SHEET 3 AA4 3 LEU C 2 SER C 7 -1 N GLN C 3 O SER C 25 SHEET 1 AA5 4 VAL A 229 PHE A 231 0 SHEET 2 AA5 4 LEU C 18 THR C 28 1 O GLY C 26 N VAL A 230 SHEET 3 AA5 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA5 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AA6 4 ASN B 54 VAL B 55 0 SHEET 2 AA6 4 ARG B 122 ASN B 130 -1 O TYR B 123 N ASN B 54 SHEET 3 AA6 4 MET B 109 SER B 119 -1 N SER B 119 O ARG B 122 SHEET 4 AA6 4 SER B 61 LYS B 69 -1 N LEU B 66 O VAL B 112 SHEET 1 AA7 3 ASN B 54 VAL B 55 0 SHEET 2 AA7 3 ARG B 122 ASN B 130 -1 O TYR B 123 N ASN B 54 SHEET 3 AA7 3 ASP B 171 LEU B 176 -1 O VAL B 174 N ALA B 127 SHEET 1 AA8 2 TYR B 192 LEU B 197 0 SHEET 2 AA8 2 PRO B 235 LEU B 240 -1 O LEU B 240 N TYR B 192 SHEET 1 AA9 3 VAL B 229 PHE B 231 0 SHEET 2 AA9 3 LEU D 18 THR D 28 1 O GLY D 26 N VAL B 230 SHEET 3 AA9 3 LEU D 2 SER D 7 -1 N GLN D 3 O SER D 25 SHEET 1 AB1 4 VAL B 229 PHE B 231 0 SHEET 2 AB1 4 LEU D 18 THR D 28 1 O GLY D 26 N VAL B 230 SHEET 3 AB1 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AB1 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AB2 6 GLY C 10 GLN C 13 0 SHEET 2 AB2 6 THR C 112 SER C 117 1 O SER C 117 N VAL C 12 SHEET 3 AB2 6 ALA C 88 GLN C 97 -1 N TYR C 90 O THR C 112 SHEET 4 AB2 6 ARG C 30 GLN C 39 -1 N TYR C 37 O TYR C 91 SHEET 5 AB2 6 GLU C 46 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AB2 6 THR C 57 TYR C 59 -1 O ASN C 58 N THR C 50 SHEET 1 AB3 4 GLY C 10 GLN C 13 0 SHEET 2 AB3 4 THR C 112 SER C 117 1 O SER C 117 N VAL C 12 SHEET 3 AB3 4 ALA C 88 GLN C 97 -1 N TYR C 90 O THR C 112 SHEET 4 AB3 4 GLU C 104 TRP C 108 -1 O TYR C 105 N ASP C 96 SHEET 1 AB4 6 GLY D 10 GLN D 13 0 SHEET 2 AB4 6 THR D 112 SER D 117 1 O THR D 115 N VAL D 12 SHEET 3 AB4 6 ALA D 88 GLN D 97 -1 N TYR D 90 O THR D 112 SHEET 4 AB4 6 ARG D 30 GLN D 39 -1 N TYR D 37 O TYR D 91 SHEET 5 AB4 6 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AB4 6 THR D 57 TYR D 59 -1 O ASN D 58 N THR D 50 SHEET 1 AB5 4 GLY D 10 GLN D 13 0 SHEET 2 AB5 4 THR D 112 SER D 117 1 O THR D 115 N VAL D 12 SHEET 3 AB5 4 ALA D 88 GLN D 97 -1 N TYR D 90 O THR D 112 SHEET 4 AB5 4 GLU D 104 TRP D 108 -1 O ASN D 107 N VAL D 94 SSBOND 1 CYS A 44 CYS A 152 1555 1555 2.04 SSBOND 2 CYS A 56 CYS A 118 1555 1555 2.03 SSBOND 3 CYS A 62 CYS A 180 1555 1555 2.03 SSBOND 4 CYS A 116 CYS A 178 1555 1555 2.05 SSBOND 5 CYS B 44 CYS B 152 1555 1555 2.04 SSBOND 6 CYS B 56 CYS B 118 1555 1555 2.03 SSBOND 7 CYS B 62 CYS B 180 1555 1555 2.04 SSBOND 8 CYS B 116 CYS B 178 1555 1555 2.04 LINK C PCA A 33 N GLN A 34 1555 1555 1.33 LINK ND2 ASN A 49 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN A 126 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 143 C1 NAG N 1 1555 1555 1.43 LINK C PCA B 33 N GLN B 34 1555 1555 1.33 LINK ND2 ASN B 49 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN B 97 C1 NAG B 302 1555 1555 1.44 LINK ND2 ASN B 126 C1 NAG B 301 1555 1555 1.44 LINK ND2 ASN B 143 C1 NAG M 1 1555 1555 1.43 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.46 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O6 NAG F 1 C1 FUC F 4 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O6 NAG G 1 C1 FUC G 3 1555 1555 1.44 CISPEP 1 SER A 72 PRO A 73 0 -0.64 CISPEP 2 SER B 72 PRO B 73 0 -0.46 CRYST1 68.900 55.090 109.340 90.00 98.91 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 0.014514 0.000000 0.002275 0.00000 SCALE2 0.000000 0.018152 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009257 0.00000