HEADER PLANT PROTEIN 25-OCT-24 9H6V TITLE LOTUS JAPONICUS CERK6 EXTRACELLULAR DOMAIN IN COMPLEX WITH TWO TITLE 2 NANOBODIES 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: NB-ACERK6-2; COMPND 7 CHAIN: E, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NB-ACERK6-1; COMPND 11 CHAIN: D, C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LOTUS JAPONICUS; SOURCE 3 ORGANISM_TAXID: 34305; SOURCE 4 GENE: LYS6; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 14 ORGANISM_TAXID: 9844; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CHITIN RECEPTOR, LYSM, NANOBODY, PLANT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.GYSEL,H.M.A.B.ALSARRAF,S.B.HANSEN,K.R.ANDERSEN REVDAT 1 16-JUL-25 9H6V 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. 2.19 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) : 2.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.42 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930 REMARK 3 COMPLETENESS FOR RANGE (%) : 52.0 REMARK 3 NUMBER OF REFLECTIONS : 25339 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 1259 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 32.4200 - 4.5400 0.99 5105 269 0.1577 0.1940 REMARK 3 2 4.5400 - 3.6100 1.00 5114 270 0.1696 0.2184 REMARK 3 3 3.6100 - 3.1500 0.93 4771 249 0.2281 0.3080 REMARK 3 4 3.1500 - 2.8600 0.71 3648 191 0.2846 0.3576 REMARK 3 5 2.8600 - 2.6600 0.50 2582 136 0.3361 0.3966 REMARK 3 6 2.6600 - 2.5000 0.33 1679 91 0.3564 0.3324 REMARK 3 7 2.5000 - 2.3800 0.16 816 34 0.3639 0.3123 REMARK 3 8 2.3800 - 2.2700 0.06 305 16 0.3937 0.3683 REMARK 3 9 2.2700 - 2.1900 0.01 60 3 0.4391 0.4429 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) : 0.308 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.691 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.23 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 : 0.002 7108 REMARK 3 ANGLE : 0.487 9635 REMARK 3 CHIRALITY : 0.041 1092 REMARK 3 PLANARITY : 0.004 1239 REMARK 3 DIHEDRAL : 11.098 2725 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 23 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5991 -8.6528 -2.6800 REMARK 3 T TENSOR REMARK 3 T11: 0.2920 T22: 0.2533 REMARK 3 T33: 0.1392 T12: -0.1169 REMARK 3 T13: -0.0250 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 3.8215 L22: 4.1102 REMARK 3 L33: 2.6024 L12: -0.6417 REMARK 3 L13: 1.1051 L23: -1.5384 REMARK 3 S TENSOR REMARK 3 S11: 0.1455 S12: -0.4437 S13: -0.1708 REMARK 3 S21: 0.1801 S22: -0.0059 S23: 0.0586 REMARK 3 S31: -0.3913 S32: 0.0305 S33: -0.1063 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.9433 0.4957 -16.0878 REMARK 3 T TENSOR REMARK 3 T11: 0.8059 T22: 0.3874 REMARK 3 T33: 0.3935 T12: -0.0110 REMARK 3 T13: -0.1875 T23: 0.0862 REMARK 3 L TENSOR REMARK 3 L11: 4.0666 L22: 5.2091 REMARK 3 L33: 7.4903 L12: -1.9705 REMARK 3 L13: -5.1182 L23: 1.8528 REMARK 3 S TENSOR REMARK 3 S11: -0.0650 S12: 0.2240 S13: 0.9856 REMARK 3 S21: -0.2339 S22: -0.1869 S23: 0.0486 REMARK 3 S31: -1.1672 S32: -0.2057 S33: -0.1274 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.9884 8.6301 -4.9958 REMARK 3 T TENSOR REMARK 3 T11: 1.0502 T22: 0.3784 REMARK 3 T33: 0.6493 T12: -0.1277 REMARK 3 T13: -0.0880 T23: -0.1025 REMARK 3 L TENSOR REMARK 3 L11: 7.4254 L22: 3.8039 REMARK 3 L33: 2.1972 L12: 0.2990 REMARK 3 L13: -0.0148 L23: 0.8173 REMARK 3 S TENSOR REMARK 3 S11: 0.1706 S12: -0.3520 S13: 1.6298 REMARK 3 S21: 0.1294 S22: 0.0470 S23: -0.3248 REMARK 3 S31: -2.0344 S32: 0.1379 S33: -0.1866 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.1970 11.1036 -8.4857 REMARK 3 T TENSOR REMARK 3 T11: 1.1380 T22: 0.3755 REMARK 3 T33: 0.6124 T12: 0.1437 REMARK 3 T13: -0.1407 T23: -0.0334 REMARK 3 L TENSOR REMARK 3 L11: 4.0513 L22: 4.8077 REMARK 3 L33: 0.5107 L12: 1.4009 REMARK 3 L13: 1.4301 L23: 0.3160 REMARK 3 S TENSOR REMARK 3 S11: 0.0386 S12: -0.3468 S13: 1.6582 REMARK 3 S21: 0.7339 S22: -0.3643 S23: -0.0674 REMARK 3 S31: -1.2066 S32: -0.5364 S33: 0.1494 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.2332 -6.8451 -9.5018 REMARK 3 T TENSOR REMARK 3 T11: 0.3077 T22: 0.5473 REMARK 3 T33: 0.3101 T12: -0.3525 REMARK 3 T13: 0.0165 T23: 0.2259 REMARK 3 L TENSOR REMARK 3 L11: 1.8743 L22: 2.1930 REMARK 3 L33: 1.9638 L12: -1.1568 REMARK 3 L13: -0.6900 L23: 0.3842 REMARK 3 S TENSOR REMARK 3 S11: -0.1330 S12: -0.3149 S13: 0.4025 REMARK 3 S21: -0.2616 S22: -0.2295 S23: -0.7467 REMARK 3 S31: -0.4765 S32: 0.6520 S33: 0.0379 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4336 16.6261 -47.1993 REMARK 3 T TENSOR REMARK 3 T11: 0.7950 T22: 0.2136 REMARK 3 T33: 0.6645 T12: -0.1218 REMARK 3 T13: 0.1610 T23: 0.0792 REMARK 3 L TENSOR REMARK 3 L11: 6.4694 L22: 8.7285 REMARK 3 L33: 3.4861 L12: -0.2728 REMARK 3 L13: -0.0480 L23: 0.0814 REMARK 3 S TENSOR REMARK 3 S11: -0.1360 S12: 0.0718 S13: -0.9982 REMARK 3 S21: -0.8398 S22: 0.1162 S23: 0.1012 REMARK 3 S31: 1.2451 S32: -0.1572 S33: -0.1561 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 50 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.3003 14.0890 -48.7112 REMARK 3 T TENSOR REMARK 3 T11: 0.8759 T22: 0.2743 REMARK 3 T33: 0.6537 T12: -0.2762 REMARK 3 T13: 0.0148 T23: 0.0067 REMARK 3 L TENSOR REMARK 3 L11: 1.7160 L22: 1.6938 REMARK 3 L33: 1.0866 L12: -0.3460 REMARK 3 L13: -0.6695 L23: -1.0253 REMARK 3 S TENSOR REMARK 3 S11: 0.0152 S12: 0.0858 S13: -1.0434 REMARK 3 S21: -0.4346 S22: -0.1850 S23: 0.1788 REMARK 3 S31: 1.4291 S32: -0.7424 S33: -0.0549 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.9070 8.1913 -41.6505 REMARK 3 T TENSOR REMARK 3 T11: 1.1015 T22: 0.5237 REMARK 3 T33: 0.7017 T12: -0.3179 REMARK 3 T13: 0.0087 T23: 0.0530 REMARK 3 L TENSOR REMARK 3 L11: 7.3819 L22: 6.2221 REMARK 3 L33: 1.7497 L12: 2.4132 REMARK 3 L13: 1.1860 L23: 0.9653 REMARK 3 S TENSOR REMARK 3 S11: 0.2955 S12: -0.4560 S13: -1.4720 REMARK 3 S21: 0.5306 S22: -0.3416 S23: 0.5641 REMARK 3 S31: 1.5143 S32: -0.6020 S33: -0.2666 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 166 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.2848 16.6646 -46.0400 REMARK 3 T TENSOR REMARK 3 T11: 0.6925 T22: 0.2622 REMARK 3 T33: 0.4887 T12: 0.2497 REMARK 3 T13: 0.0388 T23: 0.2969 REMARK 3 L TENSOR REMARK 3 L11: 2.6158 L22: 4.3500 REMARK 3 L33: 1.9071 L12: -0.1447 REMARK 3 L13: 0.5250 L23: 0.3695 REMARK 3 S TENSOR REMARK 3 S11: 0.1489 S12: 0.0613 S13: -0.9030 REMARK 3 S21: -0.5493 S22: -0.3152 S23: -0.5643 REMARK 3 S31: 0.8779 S32: 0.4736 S33: 0.0093 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.0268 48.8863 -35.1925 REMARK 3 T TENSOR REMARK 3 T11: 0.9290 T22: 0.7282 REMARK 3 T33: 0.9138 T12: -0.4414 REMARK 3 T13: 0.0858 T23: -0.1574 REMARK 3 L TENSOR REMARK 3 L11: 3.8179 L22: 5.3397 REMARK 3 L33: 7.6268 L12: 0.4072 REMARK 3 L13: -1.8501 L23: -1.1625 REMARK 3 S TENSOR REMARK 3 S11: -0.6126 S12: -0.4292 S13: 0.1356 REMARK 3 S21: -0.5167 S22: 0.2120 S23: -0.6252 REMARK 3 S31: -0.9852 S32: 1.2199 S33: 0.3378 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 26 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.0042 37.0347 -35.3545 REMARK 3 T TENSOR REMARK 3 T11: 0.4331 T22: 0.5171 REMARK 3 T33: 0.4690 T12: -0.2356 REMARK 3 T13: 0.0017 T23: -0.0962 REMARK 3 L TENSOR REMARK 3 L11: 6.3243 L22: 8.8677 REMARK 3 L33: 4.5675 L12: -0.1868 REMARK 3 L13: 4.1252 L23: 3.8301 REMARK 3 S TENSOR REMARK 3 S11: 0.1035 S12: -0.5570 S13: 0.0542 REMARK 3 S21: 0.4082 S22: 0.0004 S23: -1.0708 REMARK 3 S31: -0.1650 S32: 0.5829 S33: 0.0246 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 54 THROUGH 92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5022 41.4862 -38.0358 REMARK 3 T TENSOR REMARK 3 T11: 0.5968 T22: 0.5272 REMARK 3 T33: 0.2866 T12: -0.1820 REMARK 3 T13: 0.0954 T23: -0.0812 REMARK 3 L TENSOR REMARK 3 L11: 5.1724 L22: 7.8024 REMARK 3 L33: 3.4794 L12: -3.0621 REMARK 3 L13: 0.1573 L23: 4.4696 REMARK 3 S TENSOR REMARK 3 S11: 0.1129 S12: -0.4347 S13: 0.2491 REMARK 3 S21: -0.2600 S22: 0.2542 S23: 0.2411 REMARK 3 S31: -0.2016 S32: 0.2551 S33: -0.4900 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 93 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.9622 36.8840 -32.9583 REMARK 3 T TENSOR REMARK 3 T11: 0.5114 T22: 0.7835 REMARK 3 T33: 0.3503 T12: -0.1480 REMARK 3 T13: -0.1943 T23: -0.1086 REMARK 3 L TENSOR REMARK 3 L11: 6.0129 L22: 5.1611 REMARK 3 L33: 5.7331 L12: 0.3210 REMARK 3 L13: -0.8737 L23: 3.6477 REMARK 3 S TENSOR REMARK 3 S11: -0.0420 S12: -0.4678 S13: 0.1220 REMARK 3 S21: 0.5029 S22: 0.7703 S23: -1.3794 REMARK 3 S31: -0.2399 S32: 1.4765 S33: -0.7659 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 2 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8430 -39.8759 -18.5061 REMARK 3 T TENSOR REMARK 3 T11: 0.9057 T22: 0.7793 REMARK 3 T33: 0.4130 T12: 0.4095 REMARK 3 T13: -0.0738 T23: -0.1732 REMARK 3 L TENSOR REMARK 3 L11: 3.9005 L22: 8.7818 REMARK 3 L33: 4.9748 L12: -2.7358 REMARK 3 L13: -3.9190 L23: 0.0800 REMARK 3 S TENSOR REMARK 3 S11: -0.0468 S12: 1.0828 S13: -0.9148 REMARK 3 S21: -0.7434 S22: -0.0121 S23: 0.2949 REMARK 3 S31: 0.9112 S32: 1.1163 S33: 0.4103 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 18 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.5984 -29.1641 -14.3732 REMARK 3 T TENSOR REMARK 3 T11: 0.4979 T22: 0.8120 REMARK 3 T33: 0.2745 T12: 0.2765 REMARK 3 T13: -0.1048 T23: 0.0012 REMARK 3 L TENSOR REMARK 3 L11: 0.5039 L22: 2.8687 REMARK 3 L33: 2.4368 L12: -0.3181 REMARK 3 L13: -0.8952 L23: 2.0646 REMARK 3 S TENSOR REMARK 3 S11: 0.6979 S12: 0.6252 S13: -0.4573 REMARK 3 S21: 0.0289 S22: -0.3889 S23: -0.2861 REMARK 3 S31: 0.9028 S32: 0.7246 S33: -0.1908 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 62 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1843 -25.5958 -21.0098 REMARK 3 T TENSOR REMARK 3 T11: 0.8167 T22: 1.2400 REMARK 3 T33: 0.8005 T12: 0.4182 REMARK 3 T13: -0.2349 T23: -0.0464 REMARK 3 L TENSOR REMARK 3 L11: 6.4816 L22: 4.2192 REMARK 3 L33: 3.8446 L12: 4.9408 REMARK 3 L13: 4.2661 L23: 3.5400 REMARK 3 S TENSOR REMARK 3 S11: -0.8630 S12: 0.7187 S13: 0.9501 REMARK 3 S21: -0.4091 S22: -0.2743 S23: 2.0084 REMARK 3 S31: -1.3395 S32: -0.1759 S33: 0.7807 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 69 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.5574 -31.0737 -17.7919 REMARK 3 T TENSOR REMARK 3 T11: 0.4613 T22: 0.9796 REMARK 3 T33: 0.3824 T12: 0.2793 REMARK 3 T13: -0.0211 T23: 0.1200 REMARK 3 L TENSOR REMARK 3 L11: 4.8887 L22: 5.9925 REMARK 3 L33: 2.2452 L12: -0.0188 REMARK 3 L13: 0.6617 L23: 1.1347 REMARK 3 S TENSOR REMARK 3 S11: 0.1166 S12: 1.2991 S13: -0.2377 REMARK 3 S21: -0.3420 S22: -0.0891 S23: -0.1561 REMARK 3 S31: 0.3168 S32: 0.9494 S33: -0.0330 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6915 49.3626 -68.0537 REMARK 3 T TENSOR REMARK 3 T11: 0.3117 T22: 0.1264 REMARK 3 T33: 0.3011 T12: 0.0866 REMARK 3 T13: 0.0711 T23: 0.0280 REMARK 3 L TENSOR REMARK 3 L11: 3.0106 L22: 2.4257 REMARK 3 L33: 4.8041 L12: 0.3828 REMARK 3 L13: 0.4030 L23: -1.6311 REMARK 3 S TENSOR REMARK 3 S11: -0.0773 S12: 0.0216 S13: 0.6264 REMARK 3 S21: 0.1561 S22: -0.3946 S23: -0.4168 REMARK 3 S31: -0.3668 S32: -0.0135 S33: -0.8013 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 26 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9914 41.0261 -50.6178 REMARK 3 T TENSOR REMARK 3 T11: 0.5934 T22: 1.0447 REMARK 3 T33: 0.7771 T12: 0.3717 REMARK 3 T13: 0.1053 T23: -0.0626 REMARK 3 L TENSOR REMARK 3 L11: 1.7404 L22: 0.8874 REMARK 3 L33: 1.7415 L12: 0.9902 REMARK 3 L13: -1.5732 L23: -0.5733 REMARK 3 S TENSOR REMARK 3 S11: -0.4737 S12: -1.0857 S13: 1.1187 REMARK 3 S21: 1.0041 S22: 0.2951 S23: 0.9087 REMARK 3 S31: -1.0349 S32: -0.9477 S33: -0.1591 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 34 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8241 39.3972 -67.1937 REMARK 3 T TENSOR REMARK 3 T11: -0.1880 T22: 0.3004 REMARK 3 T33: 0.1376 T12: -0.0056 REMARK 3 T13: 0.0470 T23: 0.0268 REMARK 3 L TENSOR REMARK 3 L11: 3.6461 L22: 2.2636 REMARK 3 L33: 1.8059 L12: 0.4378 REMARK 3 L13: -0.5313 L23: -1.2200 REMARK 3 S TENSOR REMARK 3 S11: 0.0383 S12: 0.3417 S13: 0.2303 REMARK 3 S21: -0.0523 S22: 0.2138 S23: -0.0376 REMARK 3 S31: -0.1510 S32: 0.0064 S33: -0.1463 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5327 -37.3314 16.2094 REMARK 3 T TENSOR REMARK 3 T11: 0.2129 T22: 0.1445 REMARK 3 T33: 0.3105 T12: -0.0332 REMARK 3 T13: 0.0283 T23: 0.2659 REMARK 3 L TENSOR REMARK 3 L11: 4.6743 L22: 3.1101 REMARK 3 L33: 6.4055 L12: -0.3526 REMARK 3 L13: 2.4443 L23: -0.6208 REMARK 3 S TENSOR REMARK 3 S11: -0.1349 S12: 0.0912 S13: -0.2264 REMARK 3 S21: -0.2809 S22: -0.3849 S23: -0.5129 REMARK 3 S31: 0.6332 S32: 0.4316 S33: -1.6537 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 19 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4352 -33.9127 6.9137 REMARK 3 T TENSOR REMARK 3 T11: 0.3479 T22: 0.3359 REMARK 3 T33: 0.4255 T12: 0.0984 REMARK 3 T13: -0.1128 T23: -0.1067 REMARK 3 L TENSOR REMARK 3 L11: 6.6779 L22: 5.2824 REMARK 3 L33: 1.3496 L12: 0.2288 REMARK 3 L13: -1.3676 L23: -1.7187 REMARK 3 S TENSOR REMARK 3 S11: 0.1424 S12: 1.0276 S13: 0.0071 REMARK 3 S21: -1.2412 S22: -0.6771 S23: 0.3407 REMARK 3 S31: 0.3934 S32: 0.1048 S33: 0.7533 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.2113 -27.3475 14.3272 REMARK 3 T TENSOR REMARK 3 T11: -0.2902 T22: 0.3825 REMARK 3 T33: -0.0372 T12: -0.0463 REMARK 3 T13: 0.2525 T23: -0.0425 REMARK 3 L TENSOR REMARK 3 L11: 3.4149 L22: 2.0702 REMARK 3 L33: 1.3796 L12: -0.1774 REMARK 3 L13: 0.0788 L23: -0.8110 REMARK 3 S TENSOR REMARK 3 S11: 0.2389 S12: -0.1597 S13: -0.1016 REMARK 3 S21: -0.1452 S22: -0.0730 S23: -0.0195 REMARK 3 S31: 0.0457 S32: 0.1843 S33: 0.1299 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 9H6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1292142731. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-OCT-24 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 : 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 EIGER2 XE CDTE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25361 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.186 REMARK 200 RESOLUTION RANGE LOW (A) : 48.971 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 52.0 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.22600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 7.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 1.55000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 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 (%): 47.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM BROMIDE 20 % W/V PEG REMARK 280 3350, VAPOR DIFFUSION, TEMPERATURE 292.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, C, G, H 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, D, I 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 26 REMARK 465 GLY A 222 REMARK 465 SER A 223 REMARK 465 HIS A 224 REMARK 465 HIS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 SER B 26 REMARK 465 GLY B 222 REMARK 465 SER B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS B 229 REMARK 465 MET E 1 REMARK 465 SER E 127 REMARK 465 HIS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 HIS E 132 REMARK 465 HIS E 133 REMARK 465 MET F 1 REMARK 465 LYS F 44 REMARK 465 GLU F 45 REMARK 465 SER F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 MET D 1 REMARK 465 GLN D 2 REMARK 465 GLU D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 MET C 1 REMARK 465 GLN C 2 REMARK 465 ARG C 28 REMARK 465 THR C 29 REMARK 465 PHE C 30 REMARK 465 GLU C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 HIS C 131 REMARK 465 HIS C 132 REMARK 465 HIS C 133 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 ARG D 3 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 28 CG CD NE CZ NH1 NH2 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 ASN A 43 -113.57 54.38 REMARK 500 ASN A 69 29.95 -143.70 REMARK 500 ASN B 43 -7.03 62.75 REMARK 500 ASN B 46 136.68 82.45 REMARK 500 GLU B 97 -47.17 -133.25 REMARK 500 SER B 135 47.79 -89.70 REMARK 500 ASN B 140 51.12 -153.44 REMARK 500 VAL E 76 -61.75 -97.61 REMARK 500 ASP E 103 -157.58 -160.58 REMARK 500 ASP E 115 -81.70 -110.73 REMARK 500 TRP E 117 -150.67 -99.07 REMARK 500 VAL F 76 -58.59 -128.10 REMARK 500 ASP F 103 -143.95 -122.29 REMARK 500 SER F 112 5.04 -69.68 REMARK 500 SER D 26 -42.33 -138.85 REMARK 500 GLU D 45 -149.04 -83.19 REMARK 500 VAL D 49 -80.35 -116.75 REMARK 500 ASP D 107 39.24 -79.94 REMARK 500 SER C 26 72.57 56.94 REMARK 500 PRO C 42 7.54 -64.32 REMARK 500 LYS C 44 -169.53 -110.80 REMARK 500 VAL C 49 -73.99 -121.50 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 D 336 DISTANCE = 6.74 ANGSTROMS DBREF 9H6V A 26 223 UNP D3KTZ6 D3KTZ6_LOTJA 26 223 DBREF 9H6V B 26 223 UNP D3KTZ6 D3KTZ6_LOTJA 26 223 DBREF 9H6V E 1 133 PDB 9H6V 9H6V 1 133 DBREF 9H6V F 1 133 PDB 9H6V 9H6V 1 133 DBREF 9H6V D 1 133 PDB 9H6V 9H6V 1 133 DBREF 9H6V C 1 133 PDB 9H6V 9H6V 1 133 SEQADV 9H6V HIS A 224 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS A 225 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS A 226 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS A 227 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS A 228 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS A 229 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 224 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 225 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 226 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 227 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 228 UNP D3KTZ6 EXPRESSION TAG SEQADV 9H6V HIS B 229 UNP D3KTZ6 EXPRESSION TAG SEQRES 1 A 204 SER LYS CYS THR HIS GLY CYS ALA LEU ALA GLN ALA SER SEQRES 2 A 204 TYR TYR LEU LEU ASN GLY SER ASN LEU THR TYR ILE SER SEQRES 3 A 204 GLU ILE MET GLN SER SER LEU LEU THR LYS PRO GLU ASP SEQRES 4 A 204 ILE VAL SER TYR ASN GLN ASP THR ILE ALA SER LYS ASP SEQRES 5 A 204 SER VAL GLN ALA GLY GLN ARG ILE ASN VAL PRO PHE PRO SEQRES 6 A 204 CYS ASP CYS ILE GLU GLY GLU PHE LEU GLY HIS THR PHE SEQRES 7 A 204 GLN TYR ASP VAL GLN LYS GLY ASP ARG TYR ASP THR ILE SEQRES 8 A 204 ALA GLY THR ASN TYR ALA ASN LEU THR THR VAL GLU TRP SEQRES 9 A 204 LEU ARG ARG PHE ASN SER TYR PRO PRO ASP ASN ILE PRO SEQRES 10 A 204 ASP THR GLY THR LEU ASN VAL THR VAL ASN CYS SER CYS SEQRES 11 A 204 GLY ASP SER GLY VAL GLY ASP TYR GLY LEU PHE VAL THR SEQRES 12 A 204 TYR PRO LEU ARG PRO GLY GLU THR LEU GLY SER VAL ALA SEQRES 13 A 204 SER ASN VAL LYS LEU ASP SER ALA LEU LEU GLN LYS TYR SEQRES 14 A 204 ASN PRO ASN VAL ASN PHE ASN GLN GLY SER GLY ILE VAL SEQRES 15 A 204 TYR ILE PRO ALA LYS ASP GLN ASN GLY SER TYR VAL LEU SEQRES 16 A 204 LEU GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 204 SER LYS CYS THR HIS GLY CYS ALA LEU ALA GLN ALA SER SEQRES 2 B 204 TYR TYR LEU LEU ASN GLY SER ASN LEU THR TYR ILE SER SEQRES 3 B 204 GLU ILE MET GLN SER SER LEU LEU THR LYS PRO GLU ASP SEQRES 4 B 204 ILE VAL SER TYR ASN GLN ASP THR ILE ALA SER LYS ASP SEQRES 5 B 204 SER VAL GLN ALA GLY GLN ARG ILE ASN VAL PRO PHE PRO SEQRES 6 B 204 CYS ASP CYS ILE GLU GLY GLU PHE LEU GLY HIS THR PHE SEQRES 7 B 204 GLN TYR ASP VAL GLN LYS GLY ASP ARG TYR ASP THR ILE SEQRES 8 B 204 ALA GLY THR ASN TYR ALA ASN LEU THR THR VAL GLU TRP SEQRES 9 B 204 LEU ARG ARG PHE ASN SER TYR PRO PRO ASP ASN ILE PRO SEQRES 10 B 204 ASP THR GLY THR LEU ASN VAL THR VAL ASN CYS SER CYS SEQRES 11 B 204 GLY ASP SER GLY VAL GLY ASP TYR GLY LEU PHE VAL THR SEQRES 12 B 204 TYR PRO LEU ARG PRO GLY GLU THR LEU GLY SER VAL ALA SEQRES 13 B 204 SER ASN VAL LYS LEU ASP SER ALA LEU LEU GLN LYS TYR SEQRES 14 B 204 ASN PRO ASN VAL ASN PHE ASN GLN GLY SER GLY ILE VAL SEQRES 15 B 204 TYR ILE PRO ALA LYS ASP GLN ASN GLY SER TYR VAL LEU SEQRES 16 B 204 LEU GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 E 133 MET GLN VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 E 133 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 E 133 GLY ARG ILE PHE SER ARG THR ILE MET ALA TRP PHE ARG SEQRES 4 E 133 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SEQRES 5 E 133 ARG TRP SER GLY GLY ASP THR TYR TYR THR ASP SER MET SEQRES 6 E 133 LYS GLY ARG PHE THR VAL SER ARG ASP ASN VAL LYS ASN SEQRES 7 E 133 THR LEU TYR LEU GLN ILE ASP SER LEU LYS PRO GLU ASP SEQRES 8 E 133 THR ALA VAL TYR TYR CYS ALA ALA HIS ARG LEU ASP ASP SEQRES 9 E 133 GLU ALA ARG LEU LEU PRO ALA SER VAL TYR ASP TYR TRP SEQRES 10 E 133 GLY ARG GLY THR GLN VAL THR VAL SER SER HIS HIS HIS SEQRES 11 E 133 HIS HIS HIS SEQRES 1 F 133 MET GLN VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 F 133 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 F 133 GLY ARG ILE PHE SER ARG THR ILE MET ALA TRP PHE ARG SEQRES 4 F 133 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SEQRES 5 F 133 ARG TRP SER GLY GLY ASP THR TYR TYR THR ASP SER MET SEQRES 6 F 133 LYS GLY ARG PHE THR VAL SER ARG ASP ASN VAL LYS ASN SEQRES 7 F 133 THR LEU TYR LEU GLN ILE ASP SER LEU LYS PRO GLU ASP SEQRES 8 F 133 THR ALA VAL TYR TYR CYS ALA ALA HIS ARG LEU ASP ASP SEQRES 9 F 133 GLU ALA ARG LEU LEU PRO ALA SER VAL TYR ASP TYR TRP SEQRES 10 F 133 GLY ARG GLY THR GLN VAL THR VAL SER SER HIS HIS HIS SEQRES 11 F 133 HIS HIS HIS SEQRES 1 D 133 MET GLN ARG GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 D 133 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 D 133 GLY ARG THR PHE SER ALA SER THR MET GLY TRP PHE ARG SEQRES 4 D 133 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL VAL CYS VAL SEQRES 5 D 133 SER ARG ASN GLY GLU SER THR TYR TYR ALA ASP SER VAL SEQRES 6 D 133 LYS GLY ARG PHE ILE ILE SER ARG ASP ASN VAL LYS ASN SEQRES 7 D 133 THR VAL TYR LEU GLN MET ASN SER LEU GLU PRO GLU ASP SEQRES 8 D 133 THR ALA VAL TYR TYR CYS ALA ALA ARG THR ARG GLY ILE SEQRES 9 D 133 VAL CYS ASP SER THR ASP SER TYR GLY TYR TRP GLY LYS SEQRES 10 D 133 GLY THR PRO VAL THR VAL SER SER LEU GLU HIS HIS HIS SEQRES 11 D 133 HIS HIS HIS SEQRES 1 C 133 MET GLN ARG GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 C 133 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 C 133 GLY ARG THR PHE SER ALA SER THR MET GLY TRP PHE ARG SEQRES 4 C 133 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL VAL CYS VAL SEQRES 5 C 133 SER ARG ASN GLY GLU SER THR TYR TYR ALA ASP SER VAL SEQRES 6 C 133 LYS GLY ARG PHE ILE ILE SER ARG ASP ASN VAL LYS ASN SEQRES 7 C 133 THR VAL TYR LEU GLN MET ASN SER LEU GLU PRO GLU ASP SEQRES 8 C 133 THR ALA VAL TYR TYR CYS ALA ALA ARG THR ARG GLY ILE SEQRES 9 C 133 VAL CYS ASP SER THR ASP SER TYR GLY TYR TRP GLY LYS SEQRES 10 C 133 GLY THR PRO VAL THR VAL SER SER LEU GLU HIS HIS HIS SEQRES 11 C 133 HIS HIS HIS HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG A 301 14 HET NAG A 302 14 HET EDO A 303 4 HET NAG B 301 14 HET NAG B 302 14 HET EDO B 303 4 HET NAG B 304 14 HET EDO E 201 4 HET EDO F 201 4 HET EDO D 201 4 HET EDO D 202 4 HET EDO D 203 4 HET EDO C 201 4 HET EDO C 202 4 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL 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 FORMUL 7 NAG 11(C8 H15 N O6) FORMUL 12 EDO 9(C2 H6 O2) FORMUL 24 HOH *149(H2 O) HELIX 1 AA1 ASN A 46 MET A 54 1 9 HELIX 2 AA2 LYS A 61 SER A 67 1 7 HELIX 3 AA3 SER A 75 GLY A 82 1 8 HELIX 4 AA4 ARG A 112 THR A 119 1 8 HELIX 5 AA5 THR A 126 ASN A 134 1 9 HELIX 6 AA6 THR A 176 LYS A 185 1 10 HELIX 7 AA7 ASP A 187 ASN A 195 1 9 HELIX 8 AA8 TYR B 49 MET B 54 1 6 HELIX 9 AA9 LYS B 61 SER B 67 1 7 HELIX 10 AB1 SER B 75 GLY B 82 1 8 HELIX 11 AB2 ARG B 112 THR B 119 1 8 HELIX 12 AB3 THR B 126 PHE B 133 1 8 HELIX 13 AB4 THR B 176 LYS B 185 1 10 HELIX 14 AB5 ASP B 187 ASN B 195 1 9 HELIX 15 AB6 LYS E 88 THR E 92 5 5 HELIX 16 AB7 PRO E 110 TYR E 114 5 5 HELIX 17 AB8 LYS F 88 THR F 92 5 5 HELIX 18 AB9 PRO F 110 SER F 112 5 3 HELIX 19 AC1 GLU D 88 THR D 92 5 5 HELIX 20 AC2 SER D 108 TYR D 112 5 5 HELIX 21 AC3 GLU C 88 THR C 92 5 5 HELIX 22 AC4 SER C 108 TYR C 112 5 5 SHEET 1 AA1 6 THR A 146 ASN A 152 0 SHEET 2 AA1 6 PHE A 98 ASP A 106 -1 N PHE A 103 O VAL A 149 SHEET 3 AA1 6 GLN A 83 ILE A 94 -1 N ASP A 92 O GLY A 100 SHEET 4 AA1 6 CYS A 32 LEU A 41 -1 N LEU A 41 O GLN A 83 SHEET 5 AA1 6 PHE A 166 PRO A 170 1 O THR A 168 N GLN A 36 SHEET 6 AA1 6 ILE A 206 PRO A 210 -1 O VAL A 207 N TYR A 169 SHEET 1 AA2 7 SER A 217 LEU A 220 0 SHEET 2 AA2 7 THR F 59 THR F 62 1 O THR F 59 N TYR A 218 SHEET 3 AA2 7 GLU F 47 ARG F 53 -1 N ALA F 51 O TYR F 60 SHEET 4 AA2 7 ILE F 34 GLN F 40 -1 N MET F 35 O ILE F 52 SHEET 5 AA2 7 ALA F 93 HIS F 100 -1 O HIS F 100 N ILE F 34 SHEET 6 AA2 7 THR F 121 VAL F 125 -1 O VAL F 123 N ALA F 93 SHEET 7 AA2 7 GLY F 11 VAL F 13 1 N VAL F 13 O THR F 124 SHEET 1 AA3 6 SER A 217 LEU A 220 0 SHEET 2 AA3 6 THR F 59 THR F 62 1 O THR F 59 N TYR A 218 SHEET 3 AA3 6 GLU F 47 ARG F 53 -1 N ALA F 51 O TYR F 60 SHEET 4 AA3 6 ILE F 34 GLN F 40 -1 N MET F 35 O ILE F 52 SHEET 5 AA3 6 ALA F 93 HIS F 100 -1 O HIS F 100 N ILE F 34 SHEET 6 AA3 6 TYR F 114 TYR F 116 -1 O TYR F 116 N ALA F 99 SHEET 1 AA4 6 THR B 146 ASN B 152 0 SHEET 2 AA4 6 PHE B 98 ASP B 106 -1 N PHE B 103 O VAL B 149 SHEET 3 AA4 6 ARG B 84 ILE B 94 -1 N ASP B 92 O GLY B 100 SHEET 4 AA4 6 CYS B 32 TYR B 40 -1 N TYR B 39 O ILE B 85 SHEET 5 AA4 6 PHE B 166 PRO B 170 1 O THR B 168 N GLN B 36 SHEET 6 AA4 6 ILE B 206 PRO B 210 -1 O VAL B 207 N TYR B 169 SHEET 1 AA5 7 SER B 217 LEU B 220 0 SHEET 2 AA5 7 THR E 59 THR E 62 1 O TYR E 61 N LEU B 220 SHEET 3 AA5 7 GLU E 47 ARG E 53 -1 N ALA E 51 O TYR E 60 SHEET 4 AA5 7 ILE E 34 GLN E 40 -1 N ARG E 39 O GLU E 47 SHEET 5 AA5 7 ALA E 93 ALA E 99 -1 O TYR E 96 N PHE E 38 SHEET 6 AA5 7 THR E 121 VAL E 125 -1 O VAL E 123 N ALA E 93 SHEET 7 AA5 7 LEU E 12 VAL E 13 1 N VAL E 13 O THR E 124 SHEET 1 AA6 5 PHE E 69 ARG E 73 0 SHEET 2 AA6 5 THR E 79 ILE E 84 -1 O TYR E 81 N SER E 72 SHEET 3 AA6 5 LEU E 19 ALA E 24 -1 N CYS E 23 O LEU E 80 SHEET 4 AA6 5 LEU E 5 THR E 8 -1 N THR E 8 O SER E 22 SHEET 5 AA6 5 GLY E 118 ARG E 119 1 O ARG E 119 N GLU E 7 SHEET 1 AA7 4 VAL F 6 THR F 8 0 SHEET 2 AA7 4 SER F 18 ALA F 24 -1 O SER F 22 N THR F 8 SHEET 3 AA7 4 THR F 79 ASP F 85 -1 O ILE F 84 N LEU F 19 SHEET 4 AA7 4 PHE F 69 ARG F 73 -1 N SER F 72 O TYR F 81 SHEET 1 AA8 4 LEU D 5 SER D 8 0 SHEET 2 AA8 4 LEU D 19 ALA D 25 -1 O SER D 22 N SER D 8 SHEET 3 AA8 4 THR D 79 MET D 84 -1 O MET D 84 N LEU D 19 SHEET 4 AA8 4 PHE D 69 ASP D 74 -1 N SER D 72 O TYR D 81 SHEET 1 AA9 6 LEU D 12 VAL D 13 0 SHEET 2 AA9 6 THR D 119 VAL D 123 1 O THR D 122 N VAL D 13 SHEET 3 AA9 6 ALA D 93 ARG D 100 -1 N ALA D 93 O VAL D 121 SHEET 4 AA9 6 THR D 34 GLN D 40 -1 N PHE D 38 O TYR D 96 SHEET 5 AA9 6 ARG D 46 VAL D 52 -1 O VAL D 50 N TRP D 37 SHEET 6 AA9 6 THR D 59 TYR D 61 -1 O TYR D 60 N CYS D 51 SHEET 1 AB1 4 VAL C 6 SER C 8 0 SHEET 2 AB1 4 LEU C 19 ALA C 24 -1 O SER C 22 N SER C 8 SHEET 3 AB1 4 THR C 79 MET C 84 -1 O MET C 84 N LEU C 19 SHEET 4 AB1 4 PHE C 69 ASP C 74 -1 N SER C 72 O TYR C 81 SHEET 1 AB2 6 LEU C 12 VAL C 13 0 SHEET 2 AB2 6 THR C 119 VAL C 123 1 O THR C 122 N VAL C 13 SHEET 3 AB2 6 ALA C 93 ARG C 100 -1 N TYR C 95 O THR C 119 SHEET 4 AB2 6 THR C 34 GLN C 40 -1 N PHE C 38 O TYR C 96 SHEET 5 AB2 6 ARG C 46 VAL C 52 -1 O VAL C 52 N MET C 35 SHEET 6 AB2 6 THR C 59 TYR C 61 -1 O TYR C 60 N CYS C 51 SSBOND 1 CYS A 28 CYS A 93 1555 1555 2.04 SSBOND 2 CYS A 32 CYS A 155 1555 1555 2.03 SSBOND 3 CYS A 91 CYS A 153 1555 1555 2.03 SSBOND 4 CYS B 28 CYS B 93 1555 1555 2.04 SSBOND 5 CYS B 32 CYS B 155 1555 1555 2.03 SSBOND 6 CYS B 91 CYS B 153 1555 1555 2.03 SSBOND 7 CYS E 23 CYS E 97 1555 1555 2.03 SSBOND 8 CYS F 23 CYS F 97 1555 1555 2.04 SSBOND 9 CYS D 23 CYS D 97 1555 1555 2.03 SSBOND 10 CYS D 51 CYS D 106 1555 1555 2.03 SSBOND 11 CYS C 23 CYS C 97 1555 1555 2.04 SSBOND 12 CYS C 51 CYS C 106 1555 1555 2.03 LINK ND2 ASN A 46 C1 NAG A 301 1555 1555 1.44 LINK ND2 ASN A 123 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A 148 C1 NAG H 1 1555 1555 1.45 LINK ND2 ASN A 215 C1 NAG A 302 1555 1555 1.44 LINK ND2 ASN B 46 C1 NAG B 301 1555 1555 1.43 LINK ND2 ASN B 123 C1 NAG B 302 1555 1555 1.44 LINK ND2 ASN B 148 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN B 215 C1 NAG B 304 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 CRYST1 49.280 57.580 86.810 96.97 88.98 96.42 P 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.020292 0.002283 -0.000087 0.00000 SCALE2 0.000000 0.017477 0.002115 0.00000 SCALE3 0.000000 0.000000 0.011605 0.00000