HEADER IMMUNE SYSTEM 12-SEP-25 9WRN TITLE CRYSTAL STRUCTURE OF CHIMERIC ANTI-Z-DNA FAB CZ22-FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: CZ22-FAB HEAVY CHAIN; COMPND 3 CHAIN: H, I, J, K; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CZ22-FAB LIGHT CHAIN; COMPND 7 CHAIN: L, M, N, O; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.C.LEE,S.F.HSU,A.H.J.WANG REVDAT 1 18-FEB-26 9WRN 0 JRNL AUTH C.C.LEE,S.F.HSU,Y.W.CHANG,Y.W.CHEN,M.R.HO,H.SUGIYAMA, JRNL AUTH 2 A.H.J.WANG JRNL TITL STRUCTURAL BASIS OF B-TO-Z DNA TRANSITION DRIVEN BY AN JRNL TITL 2 ANTI-Z-DNA ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.02 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 100652 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.192 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5037 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 18.0200 - 6.5800 0.99 3326 175 0.1712 0.2114 REMARK 3 2 6.5800 - 5.2600 1.00 3285 173 0.1787 0.2105 REMARK 3 3 5.2600 - 4.6100 0.99 3243 171 0.1405 0.1566 REMARK 3 4 4.6100 - 4.2000 0.96 3147 165 0.1354 0.1834 REMARK 3 5 4.2000 - 3.9000 0.98 3183 168 0.1566 0.1817 REMARK 3 6 3.9000 - 3.6700 0.96 3148 166 0.1751 0.2078 REMARK 3 7 3.6700 - 3.4900 0.97 3151 166 0.1765 0.2309 REMARK 3 8 3.4900 - 3.3400 0.99 3208 169 0.1829 0.2143 REMARK 3 9 3.3400 - 3.2100 1.00 3230 170 0.1850 0.2276 REMARK 3 10 3.2100 - 3.1000 1.00 3212 169 0.1924 0.2268 REMARK 3 11 3.1000 - 3.0000 1.00 3252 171 0.1993 0.2863 REMARK 3 12 3.0000 - 2.9200 1.00 3224 169 0.1987 0.2527 REMARK 3 13 2.9200 - 2.8400 1.00 3235 171 0.2097 0.2506 REMARK 3 14 2.8400 - 2.7700 1.00 3236 170 0.2016 0.2415 REMARK 3 15 2.7700 - 2.7100 1.00 3216 170 0.2015 0.2928 REMARK 3 16 2.7100 - 2.6500 1.00 3223 169 0.2028 0.2189 REMARK 3 17 2.6500 - 2.6000 1.00 3252 171 0.2130 0.2648 REMARK 3 18 2.6000 - 2.5500 1.00 3169 167 0.2145 0.2893 REMARK 3 19 2.5500 - 2.5000 1.00 3274 173 0.2188 0.2614 REMARK 3 20 2.5000 - 2.4600 1.00 3210 169 0.2218 0.2533 REMARK 3 21 2.4600 - 2.4200 1.00 3231 170 0.2211 0.2816 REMARK 3 22 2.4200 - 2.3800 0.99 3168 167 0.2519 0.3249 REMARK 3 23 2.3800 - 2.3500 0.94 3049 159 0.2618 0.3465 REMARK 3 24 2.3500 - 2.3200 0.94 3020 160 0.2701 0.3141 REMARK 3 25 2.3200 - 2.2900 0.95 3045 160 0.2817 0.3960 REMARK 3 26 2.2900 - 2.2600 0.98 3171 167 0.2810 0.3315 REMARK 3 27 2.2600 - 2.2300 0.97 3094 164 0.3382 0.4058 REMARK 3 28 2.2300 - 2.2000 0.97 3158 168 0.2617 0.3531 REMARK 3 29 2.2000 - 2.1800 0.98 3123 164 0.2539 0.2975 REMARK 3 30 2.1800 - 2.1500 0.95 3132 166 0.2512 0.3077 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) : 0.271 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.776 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.24 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.84 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 : 0.004 13419 REMARK 3 ANGLE : 0.774 18222 REMARK 3 CHIRALITY : 0.050 2034 REMARK 3 PLANARITY : 0.006 2329 REMARK 3 DIHEDRAL : 12.687 4833 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 34 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 4 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.2041 -9.1032 -0.5994 REMARK 3 T TENSOR REMARK 3 T11: 0.1237 T22: 0.1885 REMARK 3 T33: 0.2148 T12: -0.0174 REMARK 3 T13: -0.0107 T23: -0.0146 REMARK 3 L TENSOR REMARK 3 L11: 2.9594 L22: 4.9240 REMARK 3 L33: 2.3072 L12: 0.8099 REMARK 3 L13: 0.1007 L23: 0.2191 REMARK 3 S TENSOR REMARK 3 S11: -0.1926 S12: 0.1382 S13: 0.1544 REMARK 3 S21: -0.0460 S22: 0.1114 S23: 0.2455 REMARK 3 S31: -0.0905 S32: 0.0288 S33: -0.0009 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 121 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.0958 -12.8168 33.5240 REMARK 3 T TENSOR REMARK 3 T11: 0.7410 T22: 0.3790 REMARK 3 T33: 0.3931 T12: 0.1443 REMARK 3 T13: 0.1063 T23: -0.0116 REMARK 3 L TENSOR REMARK 3 L11: 0.2637 L22: 0.2159 REMARK 3 L33: 0.2274 L12: 0.1164 REMARK 3 L13: -0.2434 L23: -0.2266 REMARK 3 S TENSOR REMARK 3 S11: -0.3104 S12: -0.2130 S13: -0.0626 REMARK 3 S21: 0.5976 S22: 0.0334 S23: 0.1005 REMARK 3 S31: 0.1196 S32: 0.2210 S33: -0.0011 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 144 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.9384 -7.9205 30.0348 REMARK 3 T TENSOR REMARK 3 T11: 0.4957 T22: 0.3703 REMARK 3 T33: 0.3821 T12: 0.1076 REMARK 3 T13: 0.1224 T23: -0.0326 REMARK 3 L TENSOR REMARK 3 L11: 1.1737 L22: 1.3952 REMARK 3 L33: 1.0652 L12: -0.2541 REMARK 3 L13: -0.4835 L23: -0.5069 REMARK 3 S TENSOR REMARK 3 S11: -0.0648 S12: 0.1809 S13: -0.4444 REMARK 3 S21: -0.4888 S22: -0.1958 S23: -0.0590 REMARK 3 S31: 0.6169 S32: -0.1021 S33: -0.0088 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 4 THROUGH 78 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.3682 6.6979 -2.0729 REMARK 3 T TENSOR REMARK 3 T11: 0.1450 T22: 0.1982 REMARK 3 T33: 0.1347 T12: 0.0175 REMARK 3 T13: -0.0553 T23: 0.0002 REMARK 3 L TENSOR REMARK 3 L11: 2.0432 L22: 3.7006 REMARK 3 L33: 2.0184 L12: -0.1627 REMARK 3 L13: -0.8150 L23: 0.2364 REMARK 3 S TENSOR REMARK 3 S11: 0.0808 S12: 0.0644 S13: -0.1047 REMARK 3 S21: -0.1147 S22: -0.1246 S23: -0.0730 REMARK 3 S31: 0.1293 S32: 0.1150 S33: -0.0102 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 79 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4678 9.3278 1.6089 REMARK 3 T TENSOR REMARK 3 T11: 0.2326 T22: 0.2603 REMARK 3 T33: 0.1659 T12: 0.0111 REMARK 3 T13: -0.0387 T23: -0.0141 REMARK 3 L TENSOR REMARK 3 L11: 1.5719 L22: 1.6618 REMARK 3 L33: 0.7031 L12: -0.1633 REMARK 3 L13: 0.3127 L23: 0.6427 REMARK 3 S TENSOR REMARK 3 S11: 0.1314 S12: -0.1278 S13: 0.0608 REMARK 3 S21: 0.0150 S22: -0.1761 S23: 0.0301 REMARK 3 S31: 0.1329 S32: 0.1889 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 121 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9151 2.0179 31.8742 REMARK 3 T TENSOR REMARK 3 T11: 0.3664 T22: 0.4077 REMARK 3 T33: 0.5921 T12: -0.1060 REMARK 3 T13: 0.0649 T23: -0.0527 REMARK 3 L TENSOR REMARK 3 L11: 0.2829 L22: 0.3895 REMARK 3 L33: 0.6770 L12: -0.2199 REMARK 3 L13: 0.2300 L23: -0.2882 REMARK 3 S TENSOR REMARK 3 S11: 0.1015 S12: -0.3026 S13: 0.1745 REMARK 3 S21: 0.4609 S22: 0.0010 S23: 0.6342 REMARK 3 S31: 0.2438 S32: -0.0391 S33: 0.0042 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 144 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.1072 7.3649 29.8406 REMARK 3 T TENSOR REMARK 3 T11: -0.0055 T22: 0.3936 REMARK 3 T33: 0.9133 T12: -0.0821 REMARK 3 T13: -0.0848 T23: -0.0846 REMARK 3 L TENSOR REMARK 3 L11: 0.4464 L22: 1.4626 REMARK 3 L33: 1.3738 L12: -0.1924 REMARK 3 L13: 0.5749 L23: -0.3629 REMARK 3 S TENSOR REMARK 3 S11: 0.3656 S12: -0.0976 S13: -0.0386 REMARK 3 S21: -0.1224 S22: -0.1287 S23: 1.5315 REMARK 3 S31: 0.3548 S32: -0.2878 S33: 0.1268 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 4 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.2191 47.3240 74.8742 REMARK 3 T TENSOR REMARK 3 T11: 0.1945 T22: 0.2311 REMARK 3 T33: 0.2419 T12: -0.0029 REMARK 3 T13: 0.0118 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: 2.1124 L22: 5.1743 REMARK 3 L33: 2.1733 L12: 0.4810 REMARK 3 L13: 0.1464 L23: -0.4442 REMARK 3 S TENSOR REMARK 3 S11: 0.0965 S12: -0.0178 S13: -0.0314 REMARK 3 S21: 0.0507 S22: -0.2694 S23: -0.2351 REMARK 3 S31: -0.0391 S32: 0.2331 S33: -0.0026 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 121 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.4483 47.5191 43.6728 REMARK 3 T TENSOR REMARK 3 T11: 0.6950 T22: 0.4620 REMARK 3 T33: 0.5290 T12: 0.1720 REMARK 3 T13: -0.0505 T23: -0.0759 REMARK 3 L TENSOR REMARK 3 L11: 0.3235 L22: 0.8539 REMARK 3 L33: 1.2006 L12: -0.3730 REMARK 3 L13: -0.0476 L23: -0.6497 REMARK 3 S TENSOR REMARK 3 S11: 0.1069 S12: 0.0182 S13: -0.1227 REMARK 3 S21: -0.4914 S22: -0.2409 S23: 0.6799 REMARK 3 S31: -0.3505 S32: -0.3106 S33: 0.0003 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 185 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4001 45.8621 38.6396 REMARK 3 T TENSOR REMARK 3 T11: 0.7492 T22: 0.6300 REMARK 3 T33: 0.7773 T12: 0.1637 REMARK 3 T13: -0.1782 T23: -0.0833 REMARK 3 L TENSOR REMARK 3 L11: 0.4266 L22: 0.5622 REMARK 3 L33: 0.5143 L12: 0.1905 REMARK 3 L13: -0.3070 L23: -0.4908 REMARK 3 S TENSOR REMARK 3 S11: -0.0211 S12: 0.3194 S13: -0.1345 REMARK 3 S21: -0.2733 S22: 0.0250 S23: 1.1037 REMARK 3 S31: -0.0388 S32: -0.4722 S33: -0.0063 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 4 THROUGH 78 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.0711 63.4378 76.3326 REMARK 3 T TENSOR REMARK 3 T11: 0.2503 T22: 0.1616 REMARK 3 T33: 0.1727 T12: 0.0163 REMARK 3 T13: 0.0630 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 1.3367 L22: 3.1560 REMARK 3 L33: 2.3900 L12: 0.5937 REMARK 3 L13: 0.0096 L23: -0.0220 REMARK 3 S TENSOR REMARK 3 S11: 0.0153 S12: -0.0406 S13: 0.0488 REMARK 3 S21: -0.4021 S22: -0.1109 S23: -0.1117 REMARK 3 S31: 0.2824 S32: 0.0890 S33: -0.0118 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 79 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.0088 60.7486 72.6546 REMARK 3 T TENSOR REMARK 3 T11: 0.3258 T22: 0.1935 REMARK 3 T33: 0.2149 T12: -0.0044 REMARK 3 T13: 0.0448 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 1.3332 L22: 2.2097 REMARK 3 L33: 0.8841 L12: 0.1738 REMARK 3 L13: -0.0878 L23: 0.8763 REMARK 3 S TENSOR REMARK 3 S11: 0.0073 S12: 0.0114 S13: -0.0887 REMARK 3 S21: -0.2763 S22: 0.0391 S23: -0.0989 REMARK 3 S31: -0.0483 S32: -0.0180 S33: 0.0001 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 121 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8593 62.3026 42.1161 REMARK 3 T TENSOR REMARK 3 T11: 0.4249 T22: 0.3773 REMARK 3 T33: 0.3818 T12: 0.0205 REMARK 3 T13: 0.0443 T23: -0.0406 REMARK 3 L TENSOR REMARK 3 L11: 0.7707 L22: 0.4979 REMARK 3 L33: 0.6152 L12: -0.1666 REMARK 3 L13: 0.1099 L23: -0.4913 REMARK 3 S TENSOR REMARK 3 S11: 0.0832 S12: 0.0054 S13: 0.1769 REMARK 3 S21: 0.2457 S22: -0.1883 S23: 0.7296 REMARK 3 S31: -0.0828 S32: -0.5099 S33: -0.0002 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 175 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.4322 61.9014 39.1871 REMARK 3 T TENSOR REMARK 3 T11: 0.4171 T22: 0.4313 REMARK 3 T33: 0.4603 T12: 0.0896 REMARK 3 T13: -0.0139 T23: -0.0412 REMARK 3 L TENSOR REMARK 3 L11: 1.1034 L22: 1.0234 REMARK 3 L33: 0.9707 L12: -0.0708 REMARK 3 L13: -0.4914 L23: -0.8317 REMARK 3 S TENSOR REMARK 3 S11: 0.1445 S12: 0.3026 S13: 0.1768 REMARK 3 S21: 0.0403 S22: -0.0823 S23: 0.6606 REMARK 3 S31: -0.2044 S32: -0.3486 S33: -0.0020 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.3848 12.4068 13.8476 REMARK 3 T TENSOR REMARK 3 T11: 0.4001 T22: 0.3232 REMARK 3 T33: 0.3405 T12: 0.0250 REMARK 3 T13: 0.0157 T23: -0.0013 REMARK 3 L TENSOR REMARK 3 L11: 0.8474 L22: 1.8453 REMARK 3 L33: 0.2978 L12: -1.2092 REMARK 3 L13: -0.0536 L23: -0.0056 REMARK 3 S TENSOR REMARK 3 S11: -0.3404 S12: -0.5632 S13: -0.1640 REMARK 3 S21: 0.7506 S22: 0.4754 S23: -0.0419 REMARK 3 S31: -0.1421 S32: 0.3277 S33: 0.0018 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.5295 12.5818 3.4344 REMARK 3 T TENSOR REMARK 3 T11: 0.0870 T22: 0.2060 REMARK 3 T33: 0.2435 T12: 0.0002 REMARK 3 T13: 0.0518 T23: 0.0127 REMARK 3 L TENSOR REMARK 3 L11: 1.1323 L22: 1.6814 REMARK 3 L33: 1.1334 L12: -0.4984 REMARK 3 L13: 0.3485 L23: -0.1467 REMARK 3 S TENSOR REMARK 3 S11: 0.1214 S12: -0.0980 S13: -0.1029 REMARK 3 S21: 0.2436 S22: 0.0464 S23: 0.1726 REMARK 3 S31: -0.0958 S32: -0.0455 S33: 0.0389 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.1470 4.5619 20.5275 REMARK 3 T TENSOR REMARK 3 T11: 0.1822 T22: 0.3199 REMARK 3 T33: 0.2679 T12: 0.0492 REMARK 3 T13: 0.0211 T23: 0.0095 REMARK 3 L TENSOR REMARK 3 L11: 1.0370 L22: 0.3179 REMARK 3 L33: 2.0336 L12: 0.0080 REMARK 3 L13: -1.2535 L23: 0.0572 REMARK 3 S TENSOR REMARK 3 S11: 0.0724 S12: -0.1577 S13: 0.0123 REMARK 3 S21: 0.2878 S22: 0.1309 S23: -0.0414 REMARK 3 S31: -0.1405 S32: 0.0546 S33: -0.0126 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 129 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.6010 -0.6272 40.5194 REMARK 3 T TENSOR REMARK 3 T11: 0.2998 T22: 0.6045 REMARK 3 T33: 0.3011 T12: 0.1990 REMARK 3 T13: 0.1176 T23: 0.1039 REMARK 3 L TENSOR REMARK 3 L11: 1.4223 L22: 1.7442 REMARK 3 L33: 1.8736 L12: 0.0248 REMARK 3 L13: -0.4354 L23: 0.3178 REMARK 3 S TENSOR REMARK 3 S11: -0.2175 S12: -0.3498 S13: -0.1293 REMARK 3 S21: 0.2880 S22: -0.1701 S23: -0.3678 REMARK 3 S31: 0.1447 S32: 1.0061 S33: -0.1551 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.4945 29.6954 5.5073 REMARK 3 T TENSOR REMARK 3 T11: -0.1385 T22: 0.2720 REMARK 3 T33: 0.3460 T12: -0.1075 REMARK 3 T13: -0.0652 T23: 0.0253 REMARK 3 L TENSOR REMARK 3 L11: 0.8313 L22: 1.4659 REMARK 3 L33: 0.8665 L12: -0.3751 REMARK 3 L13: 0.6815 L23: 0.1504 REMARK 3 S TENSOR REMARK 3 S11: -0.1768 S12: 0.0768 S13: -0.0829 REMARK 3 S21: 0.6681 S22: -0.1052 S23: -0.4004 REMARK 3 S31: -0.0018 S32: 0.1841 S33: -0.3091 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 76 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.6049 21.2170 20.3485 REMARK 3 T TENSOR REMARK 3 T11: 0.1228 T22: 0.2149 REMARK 3 T33: 0.2926 T12: -0.0361 REMARK 3 T13: 0.0027 T23: -0.0191 REMARK 3 L TENSOR REMARK 3 L11: 0.9117 L22: 1.1829 REMARK 3 L33: 1.9835 L12: -0.3090 REMARK 3 L13: -0.2067 L23: -0.3854 REMARK 3 S TENSOR REMARK 3 S11: -0.0489 S12: 0.1582 S13: -0.2303 REMARK 3 S21: 0.2573 S22: 0.0225 S23: 0.0925 REMARK 3 S31: -0.0699 S32: -0.3497 S33: 0.1800 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.4835 18.4181 38.0399 REMARK 3 T TENSOR REMARK 3 T11: 0.2707 T22: 0.2628 REMARK 3 T33: 0.2452 T12: 0.0277 REMARK 3 T13: 0.0529 T23: 0.0248 REMARK 3 L TENSOR REMARK 3 L11: 0.1847 L22: 0.3816 REMARK 3 L33: 0.5399 L12: -0.2386 REMARK 3 L13: 0.0916 L23: 0.0111 REMARK 3 S TENSOR REMARK 3 S11: -0.2139 S12: 0.0884 S13: -0.1309 REMARK 3 S21: 0.2989 S22: 0.0557 S23: 0.0646 REMARK 3 S31: -0.0782 S32: 0.2116 S33: -0.0115 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 151 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.4593 18.5869 33.7639 REMARK 3 T TENSOR REMARK 3 T11: 0.2835 T22: 0.2820 REMARK 3 T33: 0.2233 T12: 0.0343 REMARK 3 T13: 0.0304 T23: -0.0285 REMARK 3 L TENSOR REMARK 3 L11: 0.8781 L22: 0.9241 REMARK 3 L33: 0.5781 L12: 0.5574 REMARK 3 L13: -0.5306 L23: 0.0192 REMARK 3 S TENSOR REMARK 3 S11: -0.2269 S12: 0.0734 S13: 0.0753 REMARK 3 S21: 0.2429 S22: 0.0729 S23: 0.0824 REMARK 3 S31: 0.0664 S32: -0.0976 S33: -0.0010 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 175 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5927 13.1280 46.3471 REMARK 3 T TENSOR REMARK 3 T11: 0.5494 T22: 0.2665 REMARK 3 T33: 0.2806 T12: 0.0328 REMARK 3 T13: 0.1092 T23: 0.0434 REMARK 3 L TENSOR REMARK 3 L11: 0.7923 L22: 0.3212 REMARK 3 L33: 0.9796 L12: -0.1513 REMARK 3 L13: -0.3749 L23: -0.1460 REMARK 3 S TENSOR REMARK 3 S11: -0.0853 S12: -0.1508 S13: -0.2529 REMARK 3 S21: 0.9771 S22: -0.0329 S23: 0.2653 REMARK 3 S31: -0.1864 S32: 0.0808 S33: -0.0034 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.7075 26.0586 66.3487 REMARK 3 T TENSOR REMARK 3 T11: 0.5283 T22: 0.3633 REMARK 3 T33: 0.6163 T12: 0.1150 REMARK 3 T13: 0.1473 T23: 0.0375 REMARK 3 L TENSOR REMARK 3 L11: 0.4051 L22: 3.3673 REMARK 3 L33: 1.5874 L12: 0.1889 REMARK 3 L13: -0.1308 L23: 0.3290 REMARK 3 S TENSOR REMARK 3 S11: 0.0282 S12: 0.0985 S13: 0.0723 REMARK 3 S21: -1.1155 S22: -0.2031 S23: -1.0400 REMARK 3 S31: 0.1565 S32: 0.5032 S33: -0.4485 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 33 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.5144 25.3856 69.7117 REMARK 3 T TENSOR REMARK 3 T11: 0.3210 T22: 0.2261 REMARK 3 T33: 0.3008 T12: 0.0937 REMARK 3 T13: 0.0007 T23: 0.0172 REMARK 3 L TENSOR REMARK 3 L11: 0.8188 L22: 2.4370 REMARK 3 L33: 1.4724 L12: 0.1270 REMARK 3 L13: -0.9825 L23: 0.1205 REMARK 3 S TENSOR REMARK 3 S11: 0.0733 S12: 0.0182 S13: 0.0580 REMARK 3 S21: -0.8519 S22: -0.2639 S23: -0.3876 REMARK 3 S31: 0.3605 S32: -0.0837 S33: -0.0397 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 91 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.5441 37.8078 42.8330 REMARK 3 T TENSOR REMARK 3 T11: 0.8764 T22: 0.4363 REMARK 3 T33: 0.3341 T12: 0.2752 REMARK 3 T13: 0.0319 T23: -0.0281 REMARK 3 L TENSOR REMARK 3 L11: 0.4026 L22: 0.5831 REMARK 3 L33: 0.5823 L12: -0.0264 REMARK 3 L13: -0.0929 L23: 0.0815 REMARK 3 S TENSOR REMARK 3 S11: 0.1100 S12: 0.2291 S13: 0.1599 REMARK 3 S21: -0.7900 S22: -0.4162 S23: -0.2641 REMARK 3 S31: 0.3285 S32: 0.2516 S33: -0.0884 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 164 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.2175 38.8484 32.5241 REMARK 3 T TENSOR REMARK 3 T11: 1.3162 T22: 0.4961 REMARK 3 T33: 0.0216 T12: 0.3866 REMARK 3 T13: -0.0275 T23: -0.0918 REMARK 3 L TENSOR REMARK 3 L11: 0.3218 L22: 0.6869 REMARK 3 L33: 0.8321 L12: 0.2108 REMARK 3 L13: 0.0224 L23: 0.3204 REMARK 3 S TENSOR REMARK 3 S11: -0.1065 S12: 0.1035 S13: -0.0751 REMARK 3 S21: -0.4944 S22: -0.1908 S23: 0.0988 REMARK 3 S31: 0.1578 S32: 0.2037 S33: -0.1968 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.1685 41.2450 60.7183 REMARK 3 T TENSOR REMARK 3 T11: 0.2751 T22: 0.2579 REMARK 3 T33: 0.2848 T12: 0.0322 REMARK 3 T13: 0.0423 T23: -0.0054 REMARK 3 L TENSOR REMARK 3 L11: 1.0144 L22: 3.8606 REMARK 3 L33: 1.1107 L12: 1.6183 REMARK 3 L13: 0.4895 L23: 0.4333 REMARK 3 S TENSOR REMARK 3 S11: -0.0637 S12: 0.3587 S13: -0.0124 REMARK 3 S21: -0.6477 S22: 0.1233 S23: -0.6182 REMARK 3 S31: 0.1603 S32: 0.3578 S33: -0.1269 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.6947 40.8590 71.0577 REMARK 3 T TENSOR REMARK 3 T11: 0.1759 T22: 0.1627 REMARK 3 T33: 0.1582 T12: 0.0220 REMARK 3 T13: 0.0033 T23: -0.0038 REMARK 3 L TENSOR REMARK 3 L11: 1.1449 L22: 2.4072 REMARK 3 L33: 1.0095 L12: 0.4130 REMARK 3 L13: -0.2948 L23: 0.2704 REMARK 3 S TENSOR REMARK 3 S11: 0.1675 S12: 0.0354 S13: -0.1019 REMARK 3 S21: -0.1037 S22: -0.1157 S23: -0.1086 REMARK 3 S31: 0.0476 S32: -0.0598 S33: 0.0000 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 76 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.8461 48.9638 53.2736 REMARK 3 T TENSOR REMARK 3 T11: 0.3217 T22: 0.1980 REMARK 3 T33: 0.2252 T12: 0.0478 REMARK 3 T13: 0.0437 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 0.6948 L22: 0.5273 REMARK 3 L33: 1.5156 L12: -0.0153 REMARK 3 L13: 0.5642 L23: -0.5525 REMARK 3 S TENSOR REMARK 3 S11: 0.0244 S12: -0.0054 S13: 0.0730 REMARK 3 S21: -0.2049 S22: 0.0183 S23: -0.1321 REMARK 3 S31: -0.1228 S32: -0.2131 S33: 0.0001 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.2672 52.1556 37.0549 REMARK 3 T TENSOR REMARK 3 T11: 0.5216 T22: 0.3005 REMARK 3 T33: 0.1814 T12: -0.0069 REMARK 3 T13: -0.0247 T23: 0.0624 REMARK 3 L TENSOR REMARK 3 L11: 0.1436 L22: 0.6818 REMARK 3 L33: 0.5313 L12: 0.0696 REMARK 3 L13: -0.1966 L23: -0.0049 REMARK 3 S TENSOR REMARK 3 S11: 0.1506 S12: 0.1472 S13: 0.0039 REMARK 3 S21: 0.1103 S22: -0.1765 S23: -0.3854 REMARK 3 S31: -0.1659 S32: 0.1003 S33: -0.0054 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 151 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.5116 59.0889 35.5996 REMARK 3 T TENSOR REMARK 3 T11: 0.4386 T22: 0.4363 REMARK 3 T33: 0.2848 T12: -0.0468 REMARK 3 T13: 0.0477 T23: 0.0470 REMARK 3 L TENSOR REMARK 3 L11: 0.1511 L22: 0.3806 REMARK 3 L33: 0.1572 L12: 0.0456 REMARK 3 L13: 0.1083 L23: -0.1472 REMARK 3 S TENSOR REMARK 3 S11: -0.5806 S12: 0.1984 S13: -0.2123 REMARK 3 S21: -0.2674 S22: 0.1132 S23: -0.7417 REMARK 3 S31: 0.4385 S32: 0.4458 S33: -0.0598 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 164 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6606 56.2281 38.4984 REMARK 3 T TENSOR REMARK 3 T11: 0.3834 T22: 0.2412 REMARK 3 T33: 0.1658 T12: -0.0040 REMARK 3 T13: -0.0120 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 0.9023 L22: 0.9518 REMARK 3 L33: 1.1510 L12: -0.5664 REMARK 3 L13: 0.5699 L23: 0.3481 REMARK 3 S TENSOR REMARK 3 S11: 0.0143 S12: 0.0068 S13: 0.0095 REMARK 3 S21: 0.1682 S22: 0.0591 S23: -0.0063 REMARK 3 S31: -0.1739 S32: 0.0797 S33: 0.0002 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 189 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.9619 53.4824 26.9716 REMARK 3 T TENSOR REMARK 3 T11: 0.5320 T22: 0.3712 REMARK 3 T33: 0.2840 T12: 0.0044 REMARK 3 T13: 0.0441 T23: 0.0249 REMARK 3 L TENSOR REMARK 3 L11: 1.0597 L22: 0.5762 REMARK 3 L33: 0.5603 L12: 0.4814 REMARK 3 L13: -0.4475 L23: 0.0260 REMARK 3 S TENSOR REMARK 3 S11: -0.2725 S12: 0.3166 S13: -0.1437 REMARK 3 S21: -0.9276 S22: 0.0868 S23: -0.1801 REMARK 3 S31: 0.4510 S32: 0.2018 S33: -0.0002 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 3 through 135 or REMARK 3 resid 144 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "I" and (resid 3 through 135 or REMARK 3 resid 144 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "J" and resid 3 through 222) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "K" and (resid 3 through 135 or REMARK 3 resid 144 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "M" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "N" and resid 1 through 212) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "O" and resid 1 through 212) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9WRN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-25. REMARK 100 THE DEPOSITION ID IS D_1300063653. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JAN-24 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : TPS 07A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101636 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150 REMARK 200 RESOLUTION RANGE LOW (A) : 18.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 3.430 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M AMMONIUM SULFATE, 20% (W/V) REMARK 280 POLYETHYLENE GLYCOL (PEG) 4,000, 20% (V/V) GLYCEROL, AND 0.08 M REMARK 280 SODIUM ACETATE TRIHYDRATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K 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 43.51250 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, 3, 4 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: H, L 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: I, M 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, N 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, O 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 LYS H 1 REMARK 465 VAL H 2 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 SER H 224 REMARK 465 CYS H 225 REMARK 465 ASP H 226 REMARK 465 LYS H 227 REMARK 465 THR H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 LYS I 1 REMARK 465 VAL I 2 REMARK 465 SER I 137 REMARK 465 LYS I 138 REMARK 465 SER I 139 REMARK 465 THR I 140 REMARK 465 SER I 141 REMARK 465 LYS I 223 REMARK 465 SER I 224 REMARK 465 CYS I 225 REMARK 465 ASP I 226 REMARK 465 LYS I 227 REMARK 465 THR I 228 REMARK 465 HIS I 229 REMARK 465 HIS I 230 REMARK 465 HIS I 231 REMARK 465 HIS I 232 REMARK 465 HIS I 233 REMARK 465 HIS I 234 REMARK 465 HIS I 235 REMARK 465 HIS I 236 REMARK 465 LYS J 1 REMARK 465 VAL J 2 REMARK 465 SER J 136 REMARK 465 SER J 137 REMARK 465 LYS J 138 REMARK 465 SER J 139 REMARK 465 THR J 140 REMARK 465 SER J 141 REMARK 465 GLY J 142 REMARK 465 GLY J 143 REMARK 465 SER J 224 REMARK 465 CYS J 225 REMARK 465 ASP J 226 REMARK 465 LYS J 227 REMARK 465 THR J 228 REMARK 465 HIS J 229 REMARK 465 HIS J 230 REMARK 465 HIS J 231 REMARK 465 HIS J 232 REMARK 465 HIS J 233 REMARK 465 HIS J 234 REMARK 465 HIS J 235 REMARK 465 HIS J 236 REMARK 465 LYS K 1 REMARK 465 VAL K 2 REMARK 465 SER K 136 REMARK 465 SER K 137 REMARK 465 LYS K 138 REMARK 465 SER K 139 REMARK 465 THR K 140 REMARK 465 SER K 141 REMARK 465 GLY K 142 REMARK 465 SER K 224 REMARK 465 CYS K 225 REMARK 465 ASP K 226 REMARK 465 LYS K 227 REMARK 465 THR K 228 REMARK 465 HIS K 229 REMARK 465 HIS K 230 REMARK 465 HIS K 231 REMARK 465 HIS K 232 REMARK 465 HIS K 233 REMARK 465 HIS K 234 REMARK 465 HIS K 235 REMARK 465 HIS K 236 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLU M 213 REMARK 465 CYS M 214 REMARK 465 CYS N 214 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 I 326 O HOH I 367 1.95 REMARK 500 OG SER L 60 O HOH L 301 2.02 REMARK 500 OE1 GLU O 187 O HOH O 301 2.16 REMARK 500 O HOH L 308 O HOH L 367 2.16 REMARK 500 O ALA H 134 O HOH H 301 2.19 REMARK 500 O HOH O 326 O HOH O 434 2.19 REMARK 500 O SER O 56 O HOH O 302 2.19 REMARK 500 O HOH O 308 O HOH O 451 2.19 REMARK 500 O HOH J 390 O HOH O 472 2.19 REMARK 500 OD2 ASP O 1 O HOH O 303 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 J 98 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 LYS H 15 -2.76 72.87 REMARK 500 ASP H 153 66.01 60.99 REMARK 500 LYS I 15 -2.48 72.63 REMARK 500 ASP I 153 64.43 63.09 REMARK 500 LYS J 15 -2.30 72.78 REMARK 500 ASP J 153 64.72 63.12 REMARK 500 LYS K 15 -0.47 70.81 REMARK 500 ASP K 153 64.55 62.21 REMARK 500 THR L 51 -51.89 71.28 REMARK 500 ALA L 84 -178.96 -173.29 REMARK 500 LYS L 190 -55.32 -121.04 REMARK 500 THR M 51 -52.02 71.36 REMARK 500 ALA M 84 -177.87 -173.41 REMARK 500 THR N 51 -52.75 71.03 REMARK 500 ALA N 84 -178.03 -173.25 REMARK 500 ASN N 138 70.14 56.31 REMARK 500 LYS N 190 -53.78 -121.84 REMARK 500 THR O 51 -52.19 71.98 REMARK 500 ALA O 84 -178.68 -173.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 423 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH J 403 DISTANCE = 6.43 ANGSTROMS REMARK 525 HOH K 442 DISTANCE = 6.47 ANGSTROMS REMARK 525 HOH M 473 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH M 474 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH N 366 DISTANCE = 9.93 ANGSTROMS REMARK 525 HOH O 488 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH O 489 DISTANCE = 6.75 ANGSTROMS DBREF 9WRN H 1 236 PDB 9WRN 9WRN 1 236 DBREF 9WRN I 1 236 PDB 9WRN 9WRN 1 236 DBREF 9WRN J 1 236 PDB 9WRN 9WRN 1 236 DBREF 9WRN K 1 236 PDB 9WRN 9WRN 1 236 DBREF 9WRN L 1 214 PDB 9WRN 9WRN 1 214 DBREF 9WRN M 1 214 PDB 9WRN 9WRN 1 214 DBREF 9WRN N 1 214 PDB 9WRN 9WRN 1 214 DBREF 9WRN O 1 214 PDB 9WRN 9WRN 1 214 SEQRES 1 H 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 H 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 H 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 H 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 H 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 H 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 H 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 H 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 H 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 H 236 HIS HIS SEQRES 1 I 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 I 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 I 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 I 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 I 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 I 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 I 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 I 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 I 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 I 236 HIS HIS SEQRES 1 J 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 J 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 J 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 J 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 J 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 J 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 J 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 J 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 J 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 J 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 J 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 J 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 J 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 J 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 J 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 J 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 J 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 J 236 HIS HIS SEQRES 1 K 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 K 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 K 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 K 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 K 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 K 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 K 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 K 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 K 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 K 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 K 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 K 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 K 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 K 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 K 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 K 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 K 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 K 236 HIS HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 L 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 L 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 L 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 L 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 L 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 M 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 M 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 M 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 M 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 M 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 M 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 M 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 M 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 M 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 M 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 M 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 M 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 M 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 M 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 M 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 M 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 M 214 PHE ASN ARG ASN GLU CYS SEQRES 1 N 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 N 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 N 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 N 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 N 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 N 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 N 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 N 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 N 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 N 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 N 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 N 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 N 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 N 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 N 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 N 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 N 214 PHE ASN ARG ASN GLU CYS SEQRES 1 O 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 O 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 O 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 O 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 O 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 O 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 O 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 O 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 O 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 O 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 O 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 O 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 O 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 O 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 O 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 O 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 O 214 PHE ASN ARG ASN GLU CYS HET PCA H 3 8 HET PCA I 3 8 HET PCA J 3 8 HET PCA K 3 8 HETNAM PCA PYROGLUTAMIC ACID FORMUL 1 PCA 4(C5 H7 N O3) FORMUL 9 HOH *1081(H2 O) HELIX 1 AA1 ASN H 28 TYR H 32 5 5 HELIX 2 AA2 SER H 53 ASN H 57 5 5 HELIX 3 AA3 ASP H 64 LYS H 67 5 4 HELIX 4 AA4 LYS H 89 THR H 93 5 5 HELIX 5 AA5 SER H 165 ALA H 167 5 3 HELIX 6 AA6 SER H 196 LEU H 198 5 3 HELIX 7 AA7 LYS H 210 ASN H 213 5 4 HELIX 8 AA8 ASN I 28 TYR I 32 5 5 HELIX 9 AA9 SER I 53 ASN I 57 5 5 HELIX 10 AB1 ASP I 64 LYS I 67 5 4 HELIX 11 AB2 LYS I 89 THR I 93 5 5 HELIX 12 AB3 SER I 165 ALA I 167 5 3 HELIX 13 AB4 SER I 196 LEU I 198 5 3 HELIX 14 AB5 LYS I 210 ASN I 213 5 4 HELIX 15 AB6 ASN J 28 TYR J 32 5 5 HELIX 16 AB7 SER J 53 ASN J 57 5 5 HELIX 17 AB8 LYS J 89 THR J 93 5 5 HELIX 18 AB9 PRO J 194 LEU J 198 5 5 HELIX 19 AC1 LYS J 210 ASN J 213 5 4 HELIX 20 AC2 ASN K 28 TYR K 32 5 5 HELIX 21 AC3 SER K 53 ASN K 57 5 5 HELIX 22 AC4 ASP K 64 LYS K 67 5 4 HELIX 23 AC5 LYS K 89 THR K 93 5 5 HELIX 24 AC6 SER K 196 LEU K 198 5 3 HELIX 25 AC7 LYS K 210 ASN K 213 5 4 HELIX 26 AC8 GLU L 79 ILE L 83 5 5 HELIX 27 AC9 SER L 121 SER L 127 1 7 HELIX 28 AD1 LYS L 183 LYS L 188 1 6 HELIX 29 AD2 GLU M 79 ILE M 83 5 5 HELIX 30 AD3 SER M 121 LYS M 126 1 6 HELIX 31 AD4 LYS M 183 HIS M 189 1 7 HELIX 32 AD5 GLU N 79 ILE N 83 5 5 HELIX 33 AD6 SER N 121 LYS N 126 1 6 HELIX 34 AD7 LYS N 183 LYS N 188 1 6 HELIX 35 AD8 GLU O 79 ILE O 83 5 5 HELIX 36 AD9 SER O 121 SER O 127 1 7 HELIX 37 AE1 LYS O 183 LYS O 188 1 6 SHEET 1 AA1 4 LEU H 4 SER H 7 0 SHEET 2 AA1 4 LEU H 18 ALA H 24 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 MET H 80 MET H 85 -1 O LEU H 83 N LEU H 20 SHEET 4 AA1 4 PHE H 70 ASP H 75 -1 N SER H 73 O TYR H 82 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 ILE H 116 VAL H 120 1 O THR H 119 N GLY H 10 SHEET 3 AA2 6 ALA H 94 GLN H 101 -1 N TYR H 96 O ILE H 116 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 97 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 60 TYR H 62 -1 O TYR H 61 N ARG H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 ILE H 116 VAL H 120 1 O THR H 119 N GLY H 10 SHEET 3 AA3 4 ALA H 94 GLN H 101 -1 N TYR H 96 O ILE H 116 SHEET 4 AA3 4 MET H 109 TRP H 112 -1 O TYR H 111 N ARG H 100 SHEET 1 AA4 4 SER H 129 LEU H 133 0 SHEET 2 AA4 4 THR H 144 TYR H 154 -1 O LYS H 152 N SER H 129 SHEET 3 AA4 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 154 SHEET 4 AA4 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AA5 4 SER H 129 LEU H 133 0 SHEET 2 AA5 4 THR H 144 TYR H 154 -1 O LYS H 152 N SER H 129 SHEET 3 AA5 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 154 SHEET 4 AA5 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AA6 3 THR H 160 TRP H 163 0 SHEET 2 AA6 3 ILE H 204 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AA6 3 THR H 214 LYS H 219 -1 O THR H 214 N HIS H 209 SHEET 1 AA7 4 LEU I 4 SER I 7 0 SHEET 2 AA7 4 LEU I 18 ALA I 24 -1 O SER I 21 N SER I 7 SHEET 3 AA7 4 MET I 80 MET I 85 -1 O LEU I 83 N LEU I 20 SHEET 4 AA7 4 PHE I 70 ASP I 75 -1 N THR I 71 O GLN I 84 SHEET 1 AA8 6 GLY I 10 VAL I 12 0 SHEET 2 AA8 6 ILE I 116 VAL I 120 1 O SER I 117 N GLY I 10 SHEET 3 AA8 6 ALA I 94 ARG I 100 -1 N TYR I 96 O ILE I 116 SHEET 4 AA8 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 97 SHEET 5 AA8 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AA8 6 THR I 60 TYR I 62 -1 O TYR I 61 N ARG I 50 SHEET 1 AA9 4 GLY I 10 VAL I 12 0 SHEET 2 AA9 4 ILE I 116 VAL I 120 1 O SER I 117 N GLY I 10 SHEET 3 AA9 4 ALA I 94 ARG I 100 -1 N TYR I 96 O ILE I 116 SHEET 4 AA9 4 TYR I 111 TRP I 112 -1 O TYR I 111 N ARG I 100 SHEET 1 AB1 4 SER I 129 LEU I 133 0 SHEET 2 AB1 4 THR I 144 TYR I 154 -1 O LYS I 152 N SER I 129 SHEET 3 AB1 4 TYR I 185 PRO I 194 -1 O TYR I 185 N TYR I 154 SHEET 4 AB1 4 VAL I 172 THR I 174 -1 N HIS I 173 O VAL I 190 SHEET 1 AB2 4 SER I 129 LEU I 133 0 SHEET 2 AB2 4 THR I 144 TYR I 154 -1 O LYS I 152 N SER I 129 SHEET 3 AB2 4 TYR I 185 PRO I 194 -1 O TYR I 185 N TYR I 154 SHEET 4 AB2 4 VAL I 178 LEU I 179 -1 N VAL I 178 O SER I 186 SHEET 1 AB3 3 THR I 160 TRP I 163 0 SHEET 2 AB3 3 ILE I 204 HIS I 209 -1 O ASN I 206 N SER I 162 SHEET 3 AB3 3 THR I 214 LYS I 219 -1 O VAL I 216 N VAL I 207 SHEET 1 AB4 4 LEU J 4 SER J 7 0 SHEET 2 AB4 4 LEU J 18 ALA J 24 -1 O SER J 21 N SER J 7 SHEET 3 AB4 4 MET J 80 MET J 85 -1 O LEU J 83 N LEU J 20 SHEET 4 AB4 4 PHE J 70 ASP J 75 -1 N SER J 73 O TYR J 82 SHEET 1 AB5 6 GLY J 10 VAL J 12 0 SHEET 2 AB5 6 ILE J 116 VAL J 120 1 O SER J 117 N GLY J 10 SHEET 3 AB5 6 ALA J 94 ARG J 100 -1 N TYR J 96 O ILE J 116 SHEET 4 AB5 6 MET J 34 GLN J 39 -1 N VAL J 37 O TYR J 97 SHEET 5 AB5 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AB5 6 THR J 60 TYR J 62 -1 O TYR J 61 N ARG J 50 SHEET 1 AB6 4 GLY J 10 VAL J 12 0 SHEET 2 AB6 4 ILE J 116 VAL J 120 1 O SER J 117 N GLY J 10 SHEET 3 AB6 4 ALA J 94 ARG J 100 -1 N TYR J 96 O ILE J 116 SHEET 4 AB6 4 TYR J 111 TRP J 112 -1 O TYR J 111 N ARG J 100 SHEET 1 AB7 4 SER J 129 LEU J 133 0 SHEET 2 AB7 4 ALA J 145 TYR J 154 -1 O GLY J 148 N LEU J 133 SHEET 3 AB7 4 TYR J 185 VAL J 193 -1 O TYR J 185 N TYR J 154 SHEET 4 AB7 4 VAL J 172 THR J 174 -1 N HIS J 173 O VAL J 190 SHEET 1 AB8 4 SER J 129 LEU J 133 0 SHEET 2 AB8 4 ALA J 145 TYR J 154 -1 O GLY J 148 N LEU J 133 SHEET 3 AB8 4 TYR J 185 VAL J 193 -1 O TYR J 185 N TYR J 154 SHEET 4 AB8 4 VAL J 178 LEU J 179 -1 N VAL J 178 O SER J 186 SHEET 1 AB9 3 THR J 160 TRP J 163 0 SHEET 2 AB9 3 ILE J 204 HIS J 209 -1 O ASN J 206 N SER J 162 SHEET 3 AB9 3 THR J 214 LYS J 219 -1 O VAL J 216 N VAL J 207 SHEET 1 AC1 4 LEU K 4 SER K 7 0 SHEET 2 AC1 4 LEU K 18 ALA K 24 -1 O SER K 21 N SER K 7 SHEET 3 AC1 4 MET K 80 MET K 85 -1 O MET K 85 N LEU K 18 SHEET 4 AC1 4 PHE K 70 ASP K 75 -1 N SER K 73 O TYR K 82 SHEET 1 AC2 6 GLY K 10 VAL K 12 0 SHEET 2 AC2 6 ILE K 116 VAL K 120 1 O SER K 117 N GLY K 10 SHEET 3 AC2 6 ALA K 94 ARG K 100 -1 N TYR K 96 O ILE K 116 SHEET 4 AC2 6 MET K 34 GLN K 39 -1 N VAL K 37 O TYR K 97 SHEET 5 AC2 6 LEU K 45 ILE K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AC2 6 THR K 60 TYR K 62 -1 O TYR K 61 N ARG K 50 SHEET 1 AC3 4 GLY K 10 VAL K 12 0 SHEET 2 AC3 4 ILE K 116 VAL K 120 1 O SER K 117 N GLY K 10 SHEET 3 AC3 4 ALA K 94 ARG K 100 -1 N TYR K 96 O ILE K 116 SHEET 4 AC3 4 TYR K 111 TRP K 112 -1 O TYR K 111 N ARG K 100 SHEET 1 AC4 4 SER K 129 LEU K 133 0 SHEET 2 AC4 4 THR K 144 TYR K 154 -1 O LYS K 152 N SER K 129 SHEET 3 AC4 4 TYR K 185 PRO K 194 -1 O TYR K 185 N TYR K 154 SHEET 4 AC4 4 VAL K 172 THR K 174 -1 N HIS K 173 O VAL K 190 SHEET 1 AC5 4 SER K 129 LEU K 133 0 SHEET 2 AC5 4 THR K 144 TYR K 154 -1 O LYS K 152 N SER K 129 SHEET 3 AC5 4 TYR K 185 PRO K 194 -1 O TYR K 185 N TYR K 154 SHEET 4 AC5 4 VAL K 178 LEU K 179 -1 N VAL K 178 O SER K 186 SHEET 1 AC6 3 THR K 160 TRP K 163 0 SHEET 2 AC6 3 ILE K 204 HIS K 209 -1 O ASN K 206 N SER K 162 SHEET 3 AC6 3 THR K 214 LYS K 219 -1 O VAL K 216 N VAL K 207 SHEET 1 AC7 4 MET L 4 THR L 5 0 SHEET 2 AC7 4 VAL L 19 ALA L 25 -1 O SER L 24 N THR L 5 SHEET 3 AC7 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 AC7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC8 6 SER L 10 ALA L 13 0 SHEET 2 AC8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AC8 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AC8 6 VAL L 44 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC8 6 ARG L 53 LEU L 54 -1 O ARG L 53 N TYR L 49 SHEET 1 AC9 4 SER L 10 ALA L 13 0 SHEET 2 AC9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AC9 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AD1 4 SER L 114 PHE L 118 0 SHEET 2 AD1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AD1 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AD1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AD2 4 ALA L 153 LEU L 154 0 SHEET 2 AD2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AD2 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AD2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AD3 4 MET M 4 THR M 5 0 SHEET 2 AD3 4 VAL M 19 ALA M 25 -1 O SER M 24 N THR M 5 SHEET 3 AD3 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 4 AD3 4 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74 SHEET 1 AD4 6 SER M 10 ALA M 13 0 SHEET 2 AD4 6 THR M 102 ILE M 106 1 O LYS M 103 N LEU M 11 SHEET 3 AD4 6 THR M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AD4 6 LEU M 33 GLN M 38 -1 N GLN M 38 O THR M 85 SHEET 5 AD4 6 VAL M 44 TYR M 49 -1 O ILE M 48 N TRP M 35 SHEET 6 AD4 6 ARG M 53 LEU M 54 -1 O ARG M 53 N TYR M 49 SHEET 1 AD5 4 SER M 10 ALA M 13 0 SHEET 2 AD5 4 THR M 102 ILE M 106 1 O LYS M 103 N LEU M 11 SHEET 3 AD5 4 THR M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AD5 4 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90 SHEET 1 AD6 4 SER M 114 PHE M 118 0 SHEET 2 AD6 4 THR M 129 PHE M 139 -1 O LEU M 135 N PHE M 116 SHEET 3 AD6 4 TYR M 173 SER M 182 -1 O TYR M 173 N PHE M 139 SHEET 4 AD6 4 SER M 159 VAL M 163 -1 N GLN M 160 O THR M 178 SHEET 1 AD7 4 ALA M 153 LEU M 154 0 SHEET 2 AD7 4 LYS M 145 VAL M 150 -1 N VAL M 150 O ALA M 153 SHEET 3 AD7 4 VAL M 191 THR M 197 -1 O GLU M 195 N GLN M 147 SHEET 4 AD7 4 VAL M 205 ASN M 210 -1 O PHE M 209 N TYR M 192 SHEET 1 AD8 4 MET N 4 THR N 5 0 SHEET 2 AD8 4 VAL N 19 ALA N 25 -1 O SER N 24 N THR N 5 SHEET 3 AD8 4 ASP N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 4 AD8 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AD9 6 SER N 10 ALA N 13 0 SHEET 2 AD9 6 THR N 102 ILE N 106 1 O GLU N 105 N LEU N 11 SHEET 3 AD9 6 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AD9 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AD9 6 VAL N 44 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AD9 6 ARG N 53 LEU N 54 -1 O ARG N 53 N TYR N 49 SHEET 1 AE1 4 SER N 10 ALA N 13 0 SHEET 2 AE1 4 THR N 102 ILE N 106 1 O GLU N 105 N LEU N 11 SHEET 3 AE1 4 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE1 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90 SHEET 1 AE2 4 SER N 114 PHE N 118 0 SHEET 2 AE2 4 THR N 129 PHE N 139 -1 O LEU N 135 N PHE N 116 SHEET 3 AE2 4 TYR N 173 SER N 182 -1 O TYR N 173 N PHE N 139 SHEET 4 AE2 4 SER N 159 VAL N 163 -1 N SER N 162 O SER N 176 SHEET 1 AE3 4 ALA N 153 LEU N 154 0 SHEET 2 AE3 4 LYS N 145 VAL N 150 -1 N VAL N 150 O ALA N 153 SHEET 3 AE3 4 VAL N 191 THR N 197 -1 O ALA N 193 N LYS N 149 SHEET 4 AE3 4 VAL N 205 ASN N 210 -1 O VAL N 205 N VAL N 196 SHEET 1 AE4 4 MET O 4 THR O 5 0 SHEET 2 AE4 4 VAL O 19 ALA O 25 -1 O SER O 24 N THR O 5 SHEET 3 AE4 4 ASP O 70 ILE O 75 -1 O LEU O 73 N ILE O 21 SHEET 4 AE4 4 PHE O 62 SER O 67 -1 N SER O 63 O THR O 74 SHEET 1 AE5 6 SER O 10 ALA O 13 0 SHEET 2 AE5 6 THR O 102 ILE O 106 1 O LYS O 103 N LEU O 11 SHEET 3 AE5 6 THR O 85 GLN O 90 -1 N TYR O 86 O THR O 102 SHEET 4 AE5 6 LEU O 33 GLN O 38 -1 N GLN O 38 O THR O 85 SHEET 5 AE5 6 VAL O 44 TYR O 49 -1 O LEU O 47 N TRP O 35 SHEET 6 AE5 6 ARG O 53 LEU O 54 -1 O ARG O 53 N TYR O 49 SHEET 1 AE6 4 SER O 10 ALA O 13 0 SHEET 2 AE6 4 THR O 102 ILE O 106 1 O LYS O 103 N LEU O 11 SHEET 3 AE6 4 THR O 85 GLN O 90 -1 N TYR O 86 O THR O 102 SHEET 4 AE6 4 THR O 97 PHE O 98 -1 O THR O 97 N GLN O 90 SHEET 1 AE7 4 SER O 114 PHE O 118 0 SHEET 2 AE7 4 THR O 129 PHE O 139 -1 O LEU O 135 N PHE O 116 SHEET 3 AE7 4 TYR O 173 SER O 182 -1 O LEU O 181 N ALA O 130 SHEET 4 AE7 4 SER O 159 VAL O 163 -1 N SER O 162 O SER O 176 SHEET 1 AE8 4 ALA O 153 LEU O 154 0 SHEET 2 AE8 4 LYS O 145 VAL O 150 -1 N VAL O 150 O ALA O 153 SHEET 3 AE8 4 VAL O 191 THR O 197 -1 O ALA O 193 N LYS O 149 SHEET 4 AE8 4 VAL O 205 ASN O 210 -1 O VAL O 205 N VAL O 196 SSBOND 1 CYS H 22 CYS H 98 1555 1555 2.04 SSBOND 2 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 3 CYS I 22 CYS I 98 1555 1555 2.05 SSBOND 4 CYS I 149 CYS I 205 1555 1555 2.03 SSBOND 5 CYS J 22 CYS J 98 1555 1555 2.05 SSBOND 6 CYS J 149 CYS J 205 1555 1555 2.03 SSBOND 7 CYS K 22 CYS K 98 1555 1555 2.04 SSBOND 8 CYS K 149 CYS K 205 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 10 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 11 CYS M 23 CYS M 88 1555 1555 2.05 SSBOND 12 CYS M 134 CYS M 194 1555 1555 2.04 SSBOND 13 CYS N 23 CYS N 88 1555 1555 2.05 SSBOND 14 CYS N 134 CYS N 194 1555 1555 2.04 SSBOND 15 CYS O 23 CYS O 88 1555 1555 2.05 SSBOND 16 CYS O 134 CYS O 194 1555 1555 2.03 LINK C PCA H 3 N LEU H 4 1555 1555 1.33 LINK C PCA I 3 N LEU I 4 1555 1555 1.33 LINK C PCA J 3 N LEU J 4 1555 1555 1.33 LINK C PCA K 3 N LEU K 4 1555 1555 1.33 CISPEP 1 PHE H 155 PRO H 156 0 -3.31 CISPEP 2 GLU H 157 PRO H 158 0 1.06 CISPEP 3 PHE I 155 PRO I 156 0 -3.78 CISPEP 4 GLU I 157 PRO I 158 0 1.59 CISPEP 5 PHE J 155 PRO J 156 0 -3.87 CISPEP 6 GLU J 157 PRO J 158 0 0.66 CISPEP 7 PHE K 155 PRO K 156 0 -4.00 CISPEP 8 GLU K 157 PRO K 158 0 0.94 CISPEP 9 PHE L 94 PRO L 95 0 -1.48 CISPEP 10 TYR L 140 PRO L 141 0 6.65 CISPEP 11 PHE M 94 PRO M 95 0 -0.97 CISPEP 12 TYR M 140 PRO M 141 0 5.64 CISPEP 13 PHE N 94 PRO N 95 0 -3.64 CISPEP 14 TYR N 140 PRO N 141 0 2.43 CISPEP 15 PHE O 94 PRO O 95 0 -1.59 CISPEP 16 TYR O 140 PRO O 141 0 8.23 CRYST1 74.016 87.025 149.400 90.00 95.47 90.00 P 1 21 1 8 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 0.013511 0.000000 0.001294 0.00000 SCALE2 0.000000 0.011491 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006724 0.00000 MTRIX1 1 0.993844 -0.105428 0.034053 -36.85596 1 MTRIX2 1 0.105276 0.994424 0.006231 12.81234 1 MTRIX3 1 -0.034520 -0.002607 0.999401 1.01241 1 MTRIX1 2 0.987372 0.027440 0.156024 -6.32195 1 MTRIX2 2 0.028730 -0.999569 -0.006018 37.18309 1 MTRIX3 2 0.155791 0.010424 -0.987735 68.28352 1 MTRIX1 3 0.989953 0.073985 0.120497 -43.81957 1 MTRIX2 3 0.071941 -0.997183 0.021235 50.77232 1 MTRIX3 3 0.121728 -0.012353 -0.992487 68.86976 1 MTRIX1 4 0.996910 -0.074420 0.025141 -36.91883 1 MTRIX2 4 0.074285 0.997217 0.006270 13.96950 1 MTRIX3 4 -0.025537 -0.004383 0.999664 0.83629 1 MTRIX1 5 0.983849 -0.006470 0.178886 -6.82657 1 MTRIX2 5 -0.005596 -0.999970 -0.005391 38.45746 1 MTRIX3 5 0.178915 0.004303 -0.983855 67.80330 1 MTRIX1 6 0.988523 -0.014177 0.150406 -44.36992 1 MTRIX2 6 -0.015801 -0.999829 0.009612 54.02020 1 MTRIX3 6 0.150244 -0.011878 -0.988578 68.82495 1