HEADER TRANSFERASE 26-JAN-24 8RTF TITLE CRYSTAL STRUCTURE OF TRYPANOSOMA CONGOLENSE PYRUVATE KINASE IN COMPLEX TITLE 2 WITH A SINGLE-DOMAIN ANTIBODY (TCOPYK-SDAB42) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PYRUVATE KINASE; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 EC: 2.7.1.40; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: GOL IS GLYCEROL; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: CAMELID SINGLE-DOMAIN ANTIBODY 42 (SDAB42); COMPND 9 CHAIN: G, H, I, J, K, L; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CONGOLENSE; SOURCE 3 ORGANISM_TAXID: 5692; SOURCE 4 GENE: TCIL3000_10_12020; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PYRUVATE KINASE, SINGLE-DOMAIN ANTIBODY, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR Y.G.-J.STERCKX REVDAT 1 16-APR-25 8RTF 0 JRNL AUTH J.E.PINTO TORRES,M.CLAES,R.HENDRICKX,M.YUAN,N.SMIEJKOWSKA, JRNL AUTH 2 P.VAN WIELENDAELE,A.HACISULEYMAN,H.DE WINTER,S.MUYLDERMANS, JRNL AUTH 3 P.A.M.MICHELS,M.D.WALKINSHAW,W.VERSEES,G.CALJON,S.MAGEZ, JRNL AUTH 4 Y.G.STERCKX JRNL TITL ALLOSTERIC INHIBITION OF TRYPANOSOMATID PYRUVATE KINASES BY JRNL TITL 2 A CAMELID SINGLE-DOMAIN ANTIBODY. JRNL REF ELIFE V. 13 2025 JRNL REFN ESSN 2050-084X JRNL PMID 40163365 JRNL DOI 10.7554/ELIFE.100066 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.35 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 125399 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6268 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 48.3500 - 8.6800 0.99 4235 221 0.1977 0.2092 REMARK 3 2 8.6800 - 6.9000 1.00 4083 214 0.1890 0.2121 REMARK 3 3 6.9000 - 6.0300 1.00 4054 214 0.2180 0.2767 REMARK 3 4 6.0300 - 5.4800 1.00 4039 212 0.2187 0.2748 REMARK 3 5 5.4800 - 5.0900 1.00 4011 212 0.1985 0.2362 REMARK 3 6 5.0900 - 4.7900 1.00 3992 210 0.1841 0.2323 REMARK 3 7 4.7900 - 4.5500 1.00 4024 211 0.1815 0.2241 REMARK 3 8 4.5500 - 4.3500 1.00 3975 209 0.1912 0.2382 REMARK 3 9 4.3500 - 4.1800 1.00 3978 209 0.1987 0.2446 REMARK 3 10 4.1800 - 4.0400 1.00 3964 209 0.2067 0.2549 REMARK 3 11 4.0400 - 3.9100 1.00 3992 210 0.2191 0.2775 REMARK 3 12 3.9100 - 3.8000 1.00 3950 208 0.2358 0.2932 REMARK 3 13 3.8000 - 3.7000 1.00 3966 209 0.2465 0.3151 REMARK 3 14 3.7000 - 3.6100 1.00 4002 211 0.2506 0.3239 REMARK 3 15 3.6100 - 3.5300 1.00 3946 207 0.2435 0.3275 REMARK 3 16 3.5300 - 3.4500 1.00 3952 208 0.2565 0.3016 REMARK 3 17 3.4500 - 3.3800 1.00 3925 207 0.2658 0.3212 REMARK 3 18 3.3800 - 3.3200 1.00 3982 210 0.2866 0.3391 REMARK 3 19 3.3200 - 3.2600 1.00 3947 208 0.3230 0.3696 REMARK 3 20 3.2600 - 3.2000 1.00 3944 207 0.3325 0.3832 REMARK 3 21 3.2000 - 3.1500 1.00 3936 207 0.3142 0.3426 REMARK 3 22 3.1500 - 3.1000 1.00 3899 206 0.3042 0.3607 REMARK 3 23 3.1000 - 3.0600 1.00 3968 209 0.2967 0.3253 REMARK 3 24 3.0600 - 3.0200 1.00 3948 208 0.2957 0.3226 REMARK 3 25 3.0200 - 2.9700 1.00 3942 207 0.3023 0.3160 REMARK 3 26 2.9700 - 2.9400 1.00 3950 208 0.3040 0.3475 REMARK 3 27 2.9400 - 2.9000 1.00 3913 205 0.3446 0.3960 REMARK 3 28 2.9000 - 2.8600 1.00 3939 208 0.3763 0.4447 REMARK 3 29 2.8600 - 2.8300 1.00 3945 208 0.3961 0.4308 REMARK 3 30 2.8300 - 2.8000 0.96 3730 196 0.4497 0.4789 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.480 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.100 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.016 26310 REMARK 3 ANGLE : 1.823 35735 REMARK 3 CHIRALITY : 0.124 4148 REMARK 3 PLANARITY : 0.023 4685 REMARK 3 DIHEDRAL : 9.329 3762 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 66 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 2:98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.924 32.718 -51.542 REMARK 3 T TENSOR REMARK 3 T11: 0.6956 T22: 0.6916 REMARK 3 T33: 0.6052 T12: -0.2215 REMARK 3 T13: -0.0145 T23: 0.0248 REMARK 3 L TENSOR REMARK 3 L11: 1.1446 L22: 1.8957 REMARK 3 L33: 0.8698 L12: 0.6064 REMARK 3 L13: -0.2730 L23: 0.0208 REMARK 3 S TENSOR REMARK 3 S11: -0.0008 S12: -0.2140 S13: -0.0593 REMARK 3 S21: 0.2335 S22: -0.0043 S23: 0.0878 REMARK 3 S31: 0.1119 S32: -0.0178 S33: 0.0188 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 99:183 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.736 27.055 -32.920 REMARK 3 T TENSOR REMARK 3 T11: 1.8701 T22: 2.1323 REMARK 3 T33: 1.5630 T12: -0.5599 REMARK 3 T13: -0.2278 T23: 0.1620 REMARK 3 L TENSOR REMARK 3 L11: 1.8556 L22: 0.9389 REMARK 3 L33: 1.5437 L12: 0.2755 REMARK 3 L13: -0.1754 L23: -0.5484 REMARK 3 S TENSOR REMARK 3 S11: 0.6627 S12: -1.4479 S13: -0.0771 REMARK 3 S21: 1.1911 S22: -0.6528 S23: -0.3799 REMARK 3 S31: -0.4363 S32: 0.7046 S33: -0.1848 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN A AND RESID 184:404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.485 32.853 -61.125 REMARK 3 T TENSOR REMARK 3 T11: 0.6421 T22: 0.6127 REMARK 3 T33: 0.6783 T12: -0.1675 REMARK 3 T13: 0.0023 T23: 0.0462 REMARK 3 L TENSOR REMARK 3 L11: 1.2583 L22: 0.4360 REMARK 3 L33: 1.9177 L12: 0.2131 REMARK 3 L13: 0.2231 L23: -0.2172 REMARK 3 S TENSOR REMARK 3 S11: 0.0385 S12: -0.0901 S13: -0.0928 REMARK 3 S21: 0.0982 S22: -0.1382 S23: -0.1308 REMARK 3 S31: 0.0947 S32: 0.1765 S33: 0.0726 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN A AND RESID 405:500 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.253 28.587 -74.694 REMARK 3 T TENSOR REMARK 3 T11: 0.6489 T22: 0.6946 REMARK 3 T33: 0.6206 T12: -0.2335 REMARK 3 T13: -0.0753 T23: -0.0313 REMARK 3 L TENSOR REMARK 3 L11: 3.1062 L22: 2.7308 REMARK 3 L33: 4.6977 L12: -0.5824 REMARK 3 L13: -1.9246 L23: -2.9508 REMARK 3 S TENSOR REMARK 3 S11: 0.0695 S12: 0.1784 S13: -0.3358 REMARK 3 S21: -0.2471 S22: 0.0549 S23: 0.3882 REMARK 3 S31: 0.6466 S32: -0.5414 S33: -0.0613 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN B AND RESID 2:44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.198 54.980 -58.299 REMARK 3 T TENSOR REMARK 3 T11: 0.7853 T22: 0.8837 REMARK 3 T33: 0.8466 T12: -0.3158 REMARK 3 T13: -0.0186 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 0.2789 L22: 1.1561 REMARK 3 L33: 0.5886 L12: 0.2001 REMARK 3 L13: 0.6090 L23: 0.2486 REMARK 3 S TENSOR REMARK 3 S11: -0.1000 S12: 0.0694 S13: -0.0026 REMARK 3 S21: -0.0398 S22: 0.1234 S23: -0.4452 REMARK 3 S31: -0.2992 S32: 0.4034 S33: 0.0351 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN B AND RESID 45:75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.168 74.582 -47.589 REMARK 3 T TENSOR REMARK 3 T11: 1.0514 T22: 1.0687 REMARK 3 T33: 1.0226 T12: -0.4556 REMARK 3 T13: -0.0213 T23: -0.1339 REMARK 3 L TENSOR REMARK 3 L11: 0.2172 L22: 1.6403 REMARK 3 L33: 1.0473 L12: -0.1687 REMARK 3 L13: 0.3501 L23: 0.4933 REMARK 3 S TENSOR REMARK 3 S11: -0.2402 S12: -0.4140 S13: 0.3764 REMARK 3 S21: 0.5178 S22: 0.3086 S23: -0.0345 REMARK 3 S31: -0.3895 S32: 0.7951 S33: -0.0887 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN B AND RESID 76:204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.728 79.981 -50.915 REMARK 3 T TENSOR REMARK 3 T11: 1.1304 T22: 0.8481 REMARK 3 T33: 0.9977 T12: -0.2921 REMARK 3 T13: -0.0145 T23: -0.1485 REMARK 3 L TENSOR REMARK 3 L11: 1.3004 L22: 1.4911 REMARK 3 L33: 1.4843 L12: -1.0664 REMARK 3 L13: -0.0124 L23: -0.8883 REMARK 3 S TENSOR REMARK 3 S11: -0.1486 S12: 0.4805 S13: 0.6029 REMARK 3 S21: 0.6947 S22: 0.0136 S23: -0.2957 REMARK 3 S31: -0.4475 S32: -0.2491 S33: -0.0817 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN B AND RESID 205:392 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.249 63.389 -61.583 REMARK 3 T TENSOR REMARK 3 T11: 0.7949 T22: 0.6566 REMARK 3 T33: 0.7807 T12: -0.2751 REMARK 3 T13: -0.0448 T23: 0.0176 REMARK 3 L TENSOR REMARK 3 L11: 1.1598 L22: 1.3124 REMARK 3 L33: 1.8058 L12: 0.0953 REMARK 3 L13: -0.7325 L23: -0.0045 REMARK 3 S TENSOR REMARK 3 S11: 0.0668 S12: -0.1535 S13: 0.1341 REMARK 3 S21: 0.0954 S22: -0.1123 S23: -0.0281 REMARK 3 S31: -0.4659 S32: 0.1915 S33: 0.0198 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN B AND RESID 393:442 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.725 68.136 -70.864 REMARK 3 T TENSOR REMARK 3 T11: 0.8826 T22: 0.8285 REMARK 3 T33: 0.8461 T12: -0.3942 REMARK 3 T13: -0.0078 T23: 0.0118 REMARK 3 L TENSOR REMARK 3 L11: 0.7522 L22: 1.1723 REMARK 3 L33: 1.6508 L12: 0.3964 REMARK 3 L13: -0.4454 L23: 1.0405 REMARK 3 S TENSOR REMARK 3 S11: 0.0053 S12: -0.1503 S13: 0.2069 REMARK 3 S21: 0.0756 S22: 0.0189 S23: 0.1047 REMARK 3 S31: -0.2584 S32: 0.2068 S33: -0.0039 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN B AND RESID 443:467 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.386 73.947 -73.347 REMARK 3 T TENSOR REMARK 3 T11: 1.3392 T22: 1.2425 REMARK 3 T33: 1.2889 T12: -0.6149 REMARK 3 T13: -0.0047 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.5268 L22: 2.8062 REMARK 3 L33: 0.6385 L12: -0.0852 REMARK 3 L13: -0.5069 L23: 0.0373 REMARK 3 S TENSOR REMARK 3 S11: -0.0999 S12: 0.2873 S13: 0.5490 REMARK 3 S21: 0.2836 S22: 0.7835 S23: -1.5010 REMARK 3 S31: -1.3221 S32: 1.2806 S33: -0.4519 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: ( CHAIN B AND RESID 468:501 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.905 66.272 -80.997 REMARK 3 T TENSOR REMARK 3 T11: 1.1366 T22: 1.1244 REMARK 3 T33: 0.9440 T12: -0.4876 REMARK 3 T13: 0.0600 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 4.4111 L22: 4.4257 REMARK 3 L33: 4.2465 L12: -0.2459 REMARK 3 L13: -0.0770 L23: 1.5734 REMARK 3 S TENSOR REMARK 3 S11: -0.1588 S12: 0.2506 S13: 1.1234 REMARK 3 S21: -0.4397 S22: 0.0900 S23: -1.2232 REMARK 3 S31: -1.0156 S32: 0.4620 S33: -0.1528 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: ( CHAIN C AND RESID 2:75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.331 31.209 -122.375 REMARK 3 T TENSOR REMARK 3 T11: 0.6800 T22: 0.9278 REMARK 3 T33: 0.7138 T12: -0.0290 REMARK 3 T13: 0.0140 T23: -0.0885 REMARK 3 L TENSOR REMARK 3 L11: 2.2338 L22: 1.3876 REMARK 3 L33: 1.3472 L12: 1.0789 REMARK 3 L13: 0.2065 L23: -0.0010 REMARK 3 S TENSOR REMARK 3 S11: -0.0009 S12: 0.6208 S13: -0.2819 REMARK 3 S21: -0.0229 S22: 0.0230 S23: 0.0366 REMARK 3 S31: 0.2120 S32: -0.1762 S33: -0.0172 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: ( CHAIN C AND RESID 76:166 ) REMARK 3 ORIGIN FOR THE GROUP (A): -61.105 56.056 -142.458 REMARK 3 T TENSOR REMARK 3 T11: 1.6798 T22: 1.3499 REMARK 3 T33: 1.1618 T12: -0.2310 REMARK 3 T13: -0.1340 T23: 0.2230 REMARK 3 L TENSOR REMARK 3 L11: 1.1952 L22: 2.6029 REMARK 3 L33: 2.3014 L12: 1.3914 REMARK 3 L13: -0.3869 L23: 0.3024 REMARK 3 S TENSOR REMARK 3 S11: -0.4441 S12: 0.6871 S13: 0.6975 REMARK 3 S21: -1.0114 S22: 0.2022 S23: 0.1052 REMARK 3 S31: -1.2860 S32: 0.0792 S33: 0.0240 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: ( CHAIN C AND RESID 167:204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.567 50.684 -133.569 REMARK 3 T TENSOR REMARK 3 T11: 1.1352 T22: 1.3137 REMARK 3 T33: 1.2891 T12: 0.0495 REMARK 3 T13: 0.0207 T23: 0.2537 REMARK 3 L TENSOR REMARK 3 L11: 2.2441 L22: 2.5734 REMARK 3 L33: 2.2850 L12: 0.3750 REMARK 3 L13: -0.9647 L23: -1.0241 REMARK 3 S TENSOR REMARK 3 S11: -0.0752 S12: 0.4634 S13: 0.9471 REMARK 3 S21: -0.8029 S22: 0.2396 S23: -0.2338 REMARK 3 S31: -0.5532 S32: -0.2774 S33: -0.1537 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: ( CHAIN C AND RESID 205:404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.041 43.118 -114.300 REMARK 3 T TENSOR REMARK 3 T11: 0.6314 T22: 0.7621 REMARK 3 T33: 0.6609 T12: 0.0083 REMARK 3 T13: -0.0023 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 1.4093 L22: 1.1282 REMARK 3 L33: 2.1335 L12: 0.2260 REMARK 3 L13: -0.0722 L23: -0.3940 REMARK 3 S TENSOR REMARK 3 S11: 0.0775 S12: 0.3987 S13: 0.1709 REMARK 3 S21: 0.0442 S22: -0.0408 S23: 0.0583 REMARK 3 S31: -0.2117 S32: -0.3109 S33: -0.0502 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: ( CHAIN C AND RESID 405:499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -59.612 26.084 -101.728 REMARK 3 T TENSOR REMARK 3 T11: 0.7172 T22: 0.8519 REMARK 3 T33: 0.6709 T12: -0.1225 REMARK 3 T13: 0.0124 T23: -0.0645 REMARK 3 L TENSOR REMARK 3 L11: 2.2344 L22: 3.1137 REMARK 3 L33: 4.6563 L12: 0.6626 REMARK 3 L13: 2.3804 L23: -0.6930 REMARK 3 S TENSOR REMARK 3 S11: 0.3018 S12: -0.1473 S13: -0.3369 REMARK 3 S21: 0.2236 S22: -0.0870 S23: 0.2306 REMARK 3 S31: 0.5325 S32: -0.9949 S33: -0.0826 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: ( CHAIN C AND RESID 515:515 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.455 9.504 -96.686 REMARK 3 T TENSOR REMARK 3 T11: 1.4878 T22: 1.1521 REMARK 3 T33: 1.5783 T12: 0.0794 REMARK 3 T13: -0.2512 T23: 0.0881 REMARK 3 L TENSOR REMARK 3 L11: 5.3312 L22: 3.1288 REMARK 3 L33: 5.3990 L12: 0.8616 REMARK 3 L13: -4.7791 L23: 0.4665 REMARK 3 S TENSOR REMARK 3 S11: 1.1875 S12: -14.3411 S13: -17.7490 REMARK 3 S21: -4.3051 S22: -2.3417 S23: 6.5305 REMARK 3 S31: 10.0597 S32: -4.5189 S33: 1.1435 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: ( CHAIN D AND RESID 2:99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.060 60.089 -124.538 REMARK 3 T TENSOR REMARK 3 T11: 0.8924 T22: 0.9452 REMARK 3 T33: 0.7536 T12: -0.1500 REMARK 3 T13: 0.0527 T23: 0.1577 REMARK 3 L TENSOR REMARK 3 L11: 0.8969 L22: 2.0183 REMARK 3 L33: 1.3251 L12: 0.2899 REMARK 3 L13: 0.3022 L23: -0.6041 REMARK 3 S TENSOR REMARK 3 S11: 0.3699 S12: 0.2231 S13: 0.3665 REMARK 3 S21: -0.2308 S22: -0.2112 S23: -0.3827 REMARK 3 S31: -0.8372 S32: 0.4624 S33: -0.0789 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: ( CHAIN D AND RESID 100:204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.175 34.495 -137.084 REMARK 3 T TENSOR REMARK 3 T11: 0.9304 T22: 1.1967 REMARK 3 T33: 1.0655 T12: 0.1695 REMARK 3 T13: 0.2036 T23: 0.1028 REMARK 3 L TENSOR REMARK 3 L11: 2.4046 L22: 3.1585 REMARK 3 L33: 1.8449 L12: 0.2438 REMARK 3 L13: 0.0166 L23: 0.7295 REMARK 3 S TENSOR REMARK 3 S11: 0.3112 S12: 0.3291 S13: -0.3022 REMARK 3 S21: -0.7296 S22: -0.5624 S23: -0.2353 REMARK 3 S31: 0.0102 S32: 0.2910 S33: 0.1677 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: ( CHAIN D AND RESID 205:442 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.504 54.049 -112.030 REMARK 3 T TENSOR REMARK 3 T11: 0.6927 T22: 0.7827 REMARK 3 T33: 0.7263 T12: -0.1740 REMARK 3 T13: 0.0606 T23: 0.0865 REMARK 3 L TENSOR REMARK 3 L11: 1.2166 L22: 1.3228 REMARK 3 L33: 1.5061 L12: 0.5417 REMARK 3 L13: -0.0304 L23: 0.2622 REMARK 3 S TENSOR REMARK 3 S11: 0.1338 S12: 0.0120 S13: 0.1020 REMARK 3 S21: 0.1239 S22: -0.1732 S23: -0.2299 REMARK 3 S31: -0.4668 S32: 0.6097 S33: 0.0328 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: ( CHAIN D AND RESID 443:468 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.231 78.416 -102.335 REMARK 3 T TENSOR REMARK 3 T11: 1.4960 T22: 1.2736 REMARK 3 T33: 1.3238 T12: -0.7091 REMARK 3 T13: 0.1801 T23: 0.0690 REMARK 3 L TENSOR REMARK 3 L11: 3.1673 L22: 3.7400 REMARK 3 L33: 2.4074 L12: 0.2565 REMARK 3 L13: -0.7041 L23: 0.8787 REMARK 3 S TENSOR REMARK 3 S11: 0.5274 S12: -0.1229 S13: 1.5395 REMARK 3 S21: 0.4365 S22: 0.2523 S23: -0.2696 REMARK 3 S31: -1.1808 S32: 0.8806 S33: -0.8215 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: ( CHAIN D AND RESID 469:499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.135 71.966 -94.460 REMARK 3 T TENSOR REMARK 3 T11: 1.2098 T22: 1.0837 REMARK 3 T33: 0.9233 T12: -0.2531 REMARK 3 T13: 0.1332 T23: 0.0256 REMARK 3 L TENSOR REMARK 3 L11: 3.5922 L22: 6.3289 REMARK 3 L33: 6.9649 L12: 0.7891 REMARK 3 L13: -0.2801 L23: 0.8903 REMARK 3 S TENSOR REMARK 3 S11: -0.0574 S12: -0.3388 S13: 0.9556 REMARK 3 S21: 0.7217 S22: 0.0170 S23: -0.6811 REMARK 3 S31: -0.7723 S32: 1.4563 S33: -0.0304 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: ( CHAIN D AND RESID 515:515 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.579 87.289 -98.616 REMARK 3 T TENSOR REMARK 3 T11: 1.4982 T22: 1.2492 REMARK 3 T33: 1.3635 T12: -0.0710 REMARK 3 T13: -0.4477 T23: 0.2451 REMARK 3 L TENSOR REMARK 3 L11: 2.9767 L22: 3.0393 REMARK 3 L33: 2.9713 L12: -2.4764 REMARK 3 L13: -0.2528 L23: 1.3071 REMARK 3 S TENSOR REMARK 3 S11: -2.9161 S12: -5.5231 S13: -0.5092 REMARK 3 S21: -5.1779 S22: 5.6854 S23: -13.2581 REMARK 3 S31: 6.7439 S32: 2.6590 S33: -2.8588 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: ( CHAIN E AND RESID 2:44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -58.113 17.489 -14.954 REMARK 3 T TENSOR REMARK 3 T11: 1.3764 T22: 1.2538 REMARK 3 T33: 0.7625 T12: -0.7521 REMARK 3 T13: -0.3222 T23: 0.0720 REMARK 3 L TENSOR REMARK 3 L11: 1.7421 L22: 1.2740 REMARK 3 L33: 2.0719 L12: 0.1522 REMARK 3 L13: -1.4995 L23: -0.5718 REMARK 3 S TENSOR REMARK 3 S11: 0.4572 S12: -0.4327 S13: -0.4421 REMARK 3 S21: 0.6482 S22: -0.7484 S23: -0.7494 REMARK 3 S31: 0.0233 S32: 0.9315 S33: -0.0242 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: ( CHAIN E AND RESID 45:75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.365 33.764 -28.478 REMARK 3 T TENSOR REMARK 3 T11: 1.2345 T22: 0.9680 REMARK 3 T33: 0.6170 T12: -0.5863 REMARK 3 T13: 0.0904 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 2.1285 L22: 1.0349 REMARK 3 L33: 1.9182 L12: 0.3306 REMARK 3 L13: -0.5396 L23: -0.9495 REMARK 3 S TENSOR REMARK 3 S11: 0.7808 S12: -0.5684 S13: 0.1792 REMARK 3 S21: 1.1272 S22: -0.8551 S23: -0.3537 REMARK 3 S31: -0.0400 S32: -0.2546 S33: -0.1129 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: ( CHAIN E AND RESID 76:274 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.429 35.496 -18.487 REMARK 3 T TENSOR REMARK 3 T11: 1.2962 T22: 1.0918 REMARK 3 T33: 0.8807 T12: -0.4718 REMARK 3 T13: 0.1629 T23: -0.1634 REMARK 3 L TENSOR REMARK 3 L11: 1.6205 L22: 1.7551 REMARK 3 L33: 2.4458 L12: -0.9360 REMARK 3 L13: -0.8010 L23: -0.6347 REMARK 3 S TENSOR REMARK 3 S11: 0.2060 S12: -0.4164 S13: 0.4379 REMARK 3 S21: 0.3767 S22: -0.1869 S23: 0.1094 REMARK 3 S31: -0.8043 S32: -0.4317 S33: -0.0065 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: ( CHAIN E AND RESID 275:425 ) REMARK 3 ORIGIN FOR THE GROUP (A): -69.443 17.232 -13.346 REMARK 3 T TENSOR REMARK 3 T11: 1.5664 T22: 1.3677 REMARK 3 T33: 0.6507 T12: -0.8587 REMARK 3 T13: -0.0416 T23: 0.0828 REMARK 3 L TENSOR REMARK 3 L11: 0.0136 L22: 1.7975 REMARK 3 L33: 1.7119 L12: 0.0504 REMARK 3 L13: 0.2841 L23: 1.3811 REMARK 3 S TENSOR REMARK 3 S11: 0.6744 S12: -0.6908 S13: 0.1475 REMARK 3 S21: 1.1005 S22: -0.7845 S23: -0.0590 REMARK 3 S31: 0.1266 S32: -0.0973 S33: 0.0902 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: ( CHAIN E AND RESID 426:480 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.043 9.490 -31.728 REMARK 3 T TENSOR REMARK 3 T11: 1.1045 T22: 0.8779 REMARK 3 T33: 0.6946 T12: -0.5076 REMARK 3 T13: 0.0051 T23: 0.0598 REMARK 3 L TENSOR REMARK 3 L11: 1.7076 L22: 4.2498 REMARK 3 L33: 1.9905 L12: 0.7999 REMARK 3 L13: -1.0673 L23: 0.2948 REMARK 3 S TENSOR REMARK 3 S11: 0.2466 S12: 0.0283 S13: -0.0713 REMARK 3 S21: -0.2594 S22: -0.3896 S23: -0.5766 REMARK 3 S31: -0.1215 S32: 0.4636 S33: 0.1285 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: ( CHAIN E AND RESID 481:500 ) REMARK 3 ORIGIN FOR THE GROUP (A): -77.864 1.083 -29.266 REMARK 3 T TENSOR REMARK 3 T11: 1.2843 T22: 1.2721 REMARK 3 T33: 0.9154 T12: -0.4708 REMARK 3 T13: -0.0270 T23: 0.1178 REMARK 3 L TENSOR REMARK 3 L11: 4.0124 L22: 2.2400 REMARK 3 L33: 3.3019 L12: 2.3433 REMARK 3 L13: -0.8122 L23: 1.2788 REMARK 3 S TENSOR REMARK 3 S11: 0.5556 S12: 0.8351 S13: 0.3191 REMARK 3 S21: -0.2540 S22: -0.3184 S23: -0.1778 REMARK 3 S31: -0.0516 S32: -0.4169 S33: -0.0701 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: ( CHAIN F AND RESID 2:22 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.109 109.311 -6.228 REMARK 3 T TENSOR REMARK 3 T11: 1.4994 T22: 1.6027 REMARK 3 T33: 1.0100 T12: 0.5804 REMARK 3 T13: 0.1791 T23: 0.1898 REMARK 3 L TENSOR REMARK 3 L11: 0.9170 L22: 0.9191 REMARK 3 L33: 2.1512 L12: -0.2042 REMARK 3 L13: 1.2075 L23: 0.7098 REMARK 3 S TENSOR REMARK 3 S11: -0.5226 S12: 0.7832 S13: 0.1689 REMARK 3 S21: 0.5887 S22: 0.2293 S23: -1.0325 REMARK 3 S31: 0.8208 S32: 1.6193 S33: 0.3186 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: ( CHAIN F AND RESID 23:248 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.792 104.189 -25.213 REMARK 3 T TENSOR REMARK 3 T11: 1.3968 T22: 1.6978 REMARK 3 T33: 0.9733 T12: 0.1928 REMARK 3 T13: -0.0116 T23: 0.0605 REMARK 3 L TENSOR REMARK 3 L11: 0.6521 L22: 1.4298 REMARK 3 L33: 2.5091 L12: 0.6810 REMARK 3 L13: 0.4302 L23: -1.4420 REMARK 3 S TENSOR REMARK 3 S11: -0.0877 S12: 0.1822 S13: 0.0221 REMARK 3 S21: -0.1339 S22: 0.1773 S23: -0.0124 REMARK 3 S31: 0.8502 S32: -0.1386 S33: -0.0377 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: ( CHAIN F AND RESID 249:273 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.548 96.629 -9.927 REMARK 3 T TENSOR REMARK 3 T11: 1.6557 T22: 1.1946 REMARK 3 T33: 1.0057 T12: 0.5304 REMARK 3 T13: -0.3455 T23: -0.0741 REMARK 3 L TENSOR REMARK 3 L11: 2.9992 L22: 1.5822 REMARK 3 L33: 3.7540 L12: -0.2816 REMARK 3 L13: -1.3562 L23: 0.3321 REMARK 3 S TENSOR REMARK 3 S11: 0.5282 S12: 0.1838 S13: 0.0265 REMARK 3 S21: -0.9406 S22: 0.1810 S23: 0.3439 REMARK 3 S31: 2.2252 S32: 0.3301 S33: -0.8154 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: ( CHAIN F AND RESID 274:425 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.156 101.988 -14.367 REMARK 3 T TENSOR REMARK 3 T11: 1.8274 T22: 1.6773 REMARK 3 T33: 0.7860 T12: 0.7844 REMARK 3 T13: 0.0006 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 0.9937 L22: 0.3818 REMARK 3 L33: 1.5842 L12: -0.3207 REMARK 3 L13: 0.6997 L23: -0.8042 REMARK 3 S TENSOR REMARK 3 S11: 0.6118 S12: 0.5290 S13: 0.1053 REMARK 3 S21: -0.4551 S22: -0.6112 S23: -0.2187 REMARK 3 S31: 0.9479 S32: 0.7763 S33: -0.0590 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: ( CHAIN F AND RESID 426:499 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.002 97.906 -32.504 REMARK 3 T TENSOR REMARK 3 T11: 2.5594 T22: 2.4776 REMARK 3 T33: 0.6389 T12: 1.3610 REMARK 3 T13: 0.0249 T23: 0.2304 REMARK 3 L TENSOR REMARK 3 L11: 3.1518 L22: 0.9752 REMARK 3 L33: 0.2686 L12: 1.1464 REMARK 3 L13: -0.1649 L23: -0.2272 REMARK 3 S TENSOR REMARK 3 S11: 0.7803 S12: 1.0964 S13: 1.1734 REMARK 3 S21: -0.6477 S22: -0.8096 S23: 0.6003 REMARK 3 S31: 2.0694 S32: 1.9714 S33: -0.1207 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: ( CHAIN G AND RESID 1:17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -80.852 62.200 -45.933 REMARK 3 T TENSOR REMARK 3 T11: 0.8507 T22: 1.0968 REMARK 3 T33: 1.1175 T12: -0.1714 REMARK 3 T13: 0.0720 T23: -0.0954 REMARK 3 L TENSOR REMARK 3 L11: 1.5954 L22: 0.2814 REMARK 3 L33: 1.1017 L12: 0.2160 REMARK 3 L13: -0.0973 L23: -0.3939 REMARK 3 S TENSOR REMARK 3 S11: 0.1626 S12: 0.1339 S13: 0.4594 REMARK 3 S21: 0.0977 S22: -0.3960 S23: 0.3474 REMARK 3 S31: 0.3253 S32: -0.7944 S33: 0.1368 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: ( CHAIN G AND RESID 18:73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -71.056 62.787 -52.459 REMARK 3 T TENSOR REMARK 3 T11: 0.6500 T22: 0.7404 REMARK 3 T33: 0.8885 T12: -0.2101 REMARK 3 T13: -0.0125 T23: 0.0114 REMARK 3 L TENSOR REMARK 3 L11: 1.6557 L22: 2.3022 REMARK 3 L33: 2.5802 L12: 0.6719 REMARK 3 L13: -1.4002 L23: 0.2174 REMARK 3 S TENSOR REMARK 3 S11: -0.1075 S12: 0.2832 S13: 0.2456 REMARK 3 S21: -0.0102 S22: 0.2417 S23: 0.4044 REMARK 3 S31: -0.1244 S32: -0.4365 S33: -0.2226 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: ( CHAIN G AND RESID 74:89 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.254 62.018 -43.619 REMARK 3 T TENSOR REMARK 3 T11: 0.8426 T22: 0.7655 REMARK 3 T33: 0.9728 T12: -0.1239 REMARK 3 T13: -0.0078 T23: -0.0379 REMARK 3 L TENSOR REMARK 3 L11: 3.0049 L22: 5.1575 REMARK 3 L33: 1.7011 L12: -1.8577 REMARK 3 L13: -0.2445 L23: 0.5568 REMARK 3 S TENSOR REMARK 3 S11: -0.2078 S12: -0.6338 S13: 0.2863 REMARK 3 S21: 0.9599 S22: 0.4803 S23: 0.9595 REMARK 3 S31: 0.1237 S32: -0.1112 S33: 0.0068 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: ( CHAIN G AND RESID 90:104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -80.840 70.348 -49.688 REMARK 3 T TENSOR REMARK 3 T11: 0.7753 T22: 0.7950 REMARK 3 T33: 1.2005 T12: -0.1666 REMARK 3 T13: -0.0816 T23: 0.0378 REMARK 3 L TENSOR REMARK 3 L11: 1.7073 L22: 0.7690 REMARK 3 L33: 1.5374 L12: -0.1061 REMARK 3 L13: 0.2845 L23: -0.1804 REMARK 3 S TENSOR REMARK 3 S11: 0.2310 S12: -0.2125 S13: 1.1763 REMARK 3 S21: -0.1493 S22: -0.0684 S23: -0.4549 REMARK 3 S31: -0.3576 S32: -0.2031 S33: -0.0180 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: ( CHAIN G AND RESID 105:113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.426 62.051 -58.670 REMARK 3 T TENSOR REMARK 3 T11: 0.7709 T22: 0.7664 REMARK 3 T33: 0.8958 T12: -0.1353 REMARK 3 T13: -0.0093 T23: 0.0361 REMARK 3 L TENSOR REMARK 3 L11: 4.7166 L22: 0.6713 REMARK 3 L33: 2.4266 L12: -1.5545 REMARK 3 L13: 2.4225 L23: -1.3160 REMARK 3 S TENSOR REMARK 3 S11: 0.1056 S12: 0.5312 S13: 0.8367 REMARK 3 S21: -0.9353 S22: 0.1748 S23: -0.4076 REMARK 3 S31: 0.0726 S32: -0.1907 S33: 0.3338 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: ( CHAIN G AND RESID 114:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -74.360 57.978 -58.781 REMARK 3 T TENSOR REMARK 3 T11: 0.6997 T22: 0.8424 REMARK 3 T33: 0.7768 T12: -0.1082 REMARK 3 T13: -0.0870 T23: -0.0703 REMARK 3 L TENSOR REMARK 3 L11: 3.0668 L22: 7.8745 REMARK 3 L33: 3.2458 L12: 0.9378 REMARK 3 L13: 2.5824 L23: -2.0084 REMARK 3 S TENSOR REMARK 3 S11: 0.1032 S12: 0.2755 S13: 0.5188 REMARK 3 S21: -0.9690 S22: 0.2792 S23: 1.1375 REMARK 3 S31: 0.2366 S32: -0.6497 S33: -0.3578 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: ( CHAIN G AND RESID 124:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -87.701 70.504 -46.722 REMARK 3 T TENSOR REMARK 3 T11: 0.7917 T22: 0.7930 REMARK 3 T33: 1.4926 T12: 0.1539 REMARK 3 T13: -0.0277 T23: -0.1408 REMARK 3 L TENSOR REMARK 3 L11: 3.1968 L22: 3.6344 REMARK 3 L33: 3.0828 L12: -0.3029 REMARK 3 L13: 0.0476 L23: 0.7677 REMARK 3 S TENSOR REMARK 3 S11: 0.1583 S12: 0.3224 S13: 1.2228 REMARK 3 S21: 0.3731 S22: 0.3063 S23: 0.4207 REMARK 3 S31: -0.4082 S32: -0.1186 S33: -0.3952 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: ( CHAIN H AND RESID 1:17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.684 35.238 -45.901 REMARK 3 T TENSOR REMARK 3 T11: 0.8393 T22: 1.6130 REMARK 3 T33: 1.3388 T12: -0.1498 REMARK 3 T13: -0.0834 T23: 0.1074 REMARK 3 L TENSOR REMARK 3 L11: 2.5754 L22: 2.0123 REMARK 3 L33: 1.4386 L12: 0.8973 REMARK 3 L13: -0.3933 L23: 0.5734 REMARK 3 S TENSOR REMARK 3 S11: 0.2777 S12: -0.4275 S13: -0.8630 REMARK 3 S21: -0.1048 S22: -0.2562 S23: -0.6568 REMARK 3 S31: 0.3091 S32: 0.9064 S33: 0.0465 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: ( CHAIN H AND RESID 18:70 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.534 36.148 -52.419 REMARK 3 T TENSOR REMARK 3 T11: 0.6213 T22: 1.2133 REMARK 3 T33: 0.9322 T12: -0.1653 REMARK 3 T13: 0.0165 T23: 0.1412 REMARK 3 L TENSOR REMARK 3 L11: 1.9521 L22: 1.9916 REMARK 3 L33: 1.9133 L12: -0.6471 REMARK 3 L13: 1.6378 L23: -0.2388 REMARK 3 S TENSOR REMARK 3 S11: -0.0811 S12: -0.3009 S13: -0.1670 REMARK 3 S21: -0.2299 S22: 0.1131 S23: -0.2549 REMARK 3 S31: 0.0016 S32: 0.3708 S33: -0.0510 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: ( CHAIN H AND RESID 71:89 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.970 33.476 -43.887 REMARK 3 T TENSOR REMARK 3 T11: 0.7524 T22: 1.1958 REMARK 3 T33: 1.0816 T12: -0.1299 REMARK 3 T13: 0.0305 T23: 0.1528 REMARK 3 L TENSOR REMARK 3 L11: 2.0849 L22: 3.9688 REMARK 3 L33: 1.7758 L12: -1.1743 REMARK 3 L13: -0.1945 L23: -0.1521 REMARK 3 S TENSOR REMARK 3 S11: -0.1331 S12: -1.1531 S13: -0.3267 REMARK 3 S21: 1.0694 S22: 0.3108 S23: -0.5747 REMARK 3 S31: 0.2476 S32: 0.5407 S33: -0.2116 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: ( CHAIN H AND RESID 90:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.628 33.078 -53.733 REMARK 3 T TENSOR REMARK 3 T11: 0.7017 T22: 1.2879 REMARK 3 T33: 0.9813 T12: -0.1580 REMARK 3 T13: 0.0762 T23: -0.0703 REMARK 3 L TENSOR REMARK 3 L11: 3.1083 L22: 2.1321 REMARK 3 L33: 2.9597 L12: -0.1124 REMARK 3 L13: -0.1873 L23: 0.4612 REMARK 3 S TENSOR REMARK 3 S11: -0.0210 S12: 0.5039 S13: -0.0977 REMARK 3 S21: -0.5219 S22: 0.0304 S23: -0.5961 REMARK 3 S31: 0.1541 S32: 1.1951 S33: -0.0420 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: ( CHAIN I AND RESID 1:9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.454 83.199 -129.436 REMARK 3 T TENSOR REMARK 3 T11: 1.7472 T22: 1.2807 REMARK 3 T33: 2.0232 T12: -0.0594 REMARK 3 T13: 0.1648 T23: 0.2006 REMARK 3 L TENSOR REMARK 3 L11: 0.2369 L22: 1.5412 REMARK 3 L33: 4.9625 L12: -0.5799 REMARK 3 L13: 1.0493 L23: -2.4489 REMARK 3 S TENSOR REMARK 3 S11: 0.2317 S12: -0.6481 S13: 1.1876 REMARK 3 S21: 0.3346 S22: -0.2321 S23: 1.0487 REMARK 3 S31: -0.8383 S32: -0.6505 S33: -0.3261 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: ( CHAIN I AND RESID 10:73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -53.460 78.352 -127.626 REMARK 3 T TENSOR REMARK 3 T11: 1.3912 T22: 1.1085 REMARK 3 T33: 1.6510 T12: 0.1856 REMARK 3 T13: -0.0448 T23: 0.2943 REMARK 3 L TENSOR REMARK 3 L11: 1.8138 L22: 1.6657 REMARK 3 L33: 1.2358 L12: 0.1752 REMARK 3 L13: 0.3277 L23: -0.9797 REMARK 3 S TENSOR REMARK 3 S11: -0.5394 S12: -0.4913 S13: 0.9868 REMARK 3 S21: -0.1962 S22: 0.4528 S23: 0.7778 REMARK 3 S31: -0.7291 S32: -0.4961 S33: 0.1309 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: ( CHAIN I AND RESID 74:90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.121 75.882 -135.206 REMARK 3 T TENSOR REMARK 3 T11: 1.4886 T22: 1.2031 REMARK 3 T33: 1.5995 T12: 0.0821 REMARK 3 T13: -0.2091 T23: 0.3476 REMARK 3 L TENSOR REMARK 3 L11: 2.4931 L22: 1.7883 REMARK 3 L33: 2.5948 L12: 0.8941 REMARK 3 L13: 0.7009 L23: -0.2289 REMARK 3 S TENSOR REMARK 3 S11: -0.6808 S12: 0.8001 S13: 1.1841 REMARK 3 S21: -1.3787 S22: 0.3257 S23: 1.1922 REMARK 3 S31: -0.8183 S32: -0.5679 S33: 0.0435 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: ( CHAIN I AND RESID 91:105 ) REMARK 3 ORIGIN FOR THE GROUP (A): -58.714 85.312 -128.201 REMARK 3 T TENSOR REMARK 3 T11: 1.7513 T22: 1.4351 REMARK 3 T33: 2.5516 T12: 0.3496 REMARK 3 T13: -0.0868 T23: 0.1916 REMARK 3 L TENSOR REMARK 3 L11: 0.5837 L22: 0.3812 REMARK 3 L33: 0.5146 L12: -0.4008 REMARK 3 L13: 0.3751 L23: -0.2375 REMARK 3 S TENSOR REMARK 3 S11: -0.2224 S12: -0.4082 S13: 0.5562 REMARK 3 S21: -0.5399 S22: 0.7261 S23: 1.3899 REMARK 3 S31: -0.2884 S32: -1.1026 S33: -0.3204 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: ( CHAIN I AND RESID 106:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.898 76.176 -119.724 REMARK 3 T TENSOR REMARK 3 T11: 1.4193 T22: 0.9242 REMARK 3 T33: 1.4638 T12: 0.0905 REMARK 3 T13: -0.0015 T23: 0.2052 REMARK 3 L TENSOR REMARK 3 L11: 2.9304 L22: 2.6165 REMARK 3 L33: 1.3735 L12: -0.5766 REMARK 3 L13: 0.2182 L23: 1.0480 REMARK 3 S TENSOR REMARK 3 S11: -0.2017 S12: -0.3974 S13: 1.0809 REMARK 3 S21: 0.4261 S22: 0.1208 S23: 0.1429 REMARK 3 S31: -0.1090 S32: -0.4080 S33: 0.2873 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: ( CHAIN I AND RESID 124:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.276 92.888 -133.281 REMARK 3 T TENSOR REMARK 3 T11: 2.2903 T22: 1.3227 REMARK 3 T33: 3.8678 T12: -0.1075 REMARK 3 T13: -0.9879 T23: 0.6872 REMARK 3 L TENSOR REMARK 3 L11: 0.3474 L22: 1.1922 REMARK 3 L33: 1.4602 L12: 0.4004 REMARK 3 L13: -0.3492 L23: 0.2157 REMARK 3 S TENSOR REMARK 3 S11: -0.0068 S12: -0.0524 S13: -0.0130 REMARK 3 S21: 0.1878 S22: -0.4555 S23: 0.2348 REMARK 3 S31: 0.0111 S32: 0.5333 S33: 0.3001 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: ( CHAIN J AND RESID 1:17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.118 6.745 -126.922 REMARK 3 T TENSOR REMARK 3 T11: 1.0145 T22: 0.8593 REMARK 3 T33: 1.3417 T12: -0.0043 REMARK 3 T13: 0.0282 T23: -0.0447 REMARK 3 L TENSOR REMARK 3 L11: 2.5339 L22: 1.6500 REMARK 3 L33: 1.2891 L12: -1.2655 REMARK 3 L13: -0.2951 L23: 0.9748 REMARK 3 S TENSOR REMARK 3 S11: 0.1853 S12: -0.4211 S13: 0.1113 REMARK 3 S21: -0.7493 S22: 0.2905 S23: -1.0721 REMARK 3 S31: 0.0020 S32: 0.1865 S33: -0.3873 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: ( CHAIN J AND RESID 18:39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.102 18.911 -124.017 REMARK 3 T TENSOR REMARK 3 T11: 0.6236 T22: 0.8904 REMARK 3 T33: 0.9626 T12: 0.0586 REMARK 3 T13: -0.0726 T23: -0.0856 REMARK 3 L TENSOR REMARK 3 L11: 0.9025 L22: 1.7115 REMARK 3 L33: 0.7233 L12: 0.3662 REMARK 3 L13: 0.3434 L23: -0.3038 REMARK 3 S TENSOR REMARK 3 S11: 0.1650 S12: -0.1664 S13: -0.9428 REMARK 3 S21: -0.2761 S22: -0.6453 S23: 0.8953 REMARK 3 S31: 0.1205 S32: -0.5475 S33: 0.3102 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: ( CHAIN J AND RESID 40:51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.004 8.747 -115.543 REMARK 3 T TENSOR REMARK 3 T11: 1.0713 T22: 1.0955 REMARK 3 T33: 1.2777 T12: 0.0644 REMARK 3 T13: -0.0976 T23: 0.2086 REMARK 3 L TENSOR REMARK 3 L11: 3.5093 L22: 5.6032 REMARK 3 L33: 4.6949 L12: -0.8970 REMARK 3 L13: 0.2863 L23: -1.9568 REMARK 3 S TENSOR REMARK 3 S11: 0.1667 S12: -0.9521 S13: -1.4831 REMARK 3 S21: 1.7720 S22: 0.0116 S23: 0.6871 REMARK 3 S31: 1.1769 S32: 0.3064 S33: -0.5362 REMARK 3 TLS GROUP : 55 REMARK 3 SELECTION: ( CHAIN J AND RESID 52:104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.392 15.575 -124.291 REMARK 3 T TENSOR REMARK 3 T11: 0.6899 T22: 0.8355 REMARK 3 T33: 1.0551 T12: 0.0865 REMARK 3 T13: -0.0400 T23: 0.0877 REMARK 3 L TENSOR REMARK 3 L11: 2.3467 L22: 2.0912 REMARK 3 L33: 1.1837 L12: -0.4323 REMARK 3 L13: -1.1892 L23: 1.1286 REMARK 3 S TENSOR REMARK 3 S11: 0.1191 S12: -0.4317 S13: -0.7735 REMARK 3 S21: -0.0595 S22: 0.0986 S23: 0.0339 REMARK 3 S31: 0.2588 S32: 0.2730 S33: -0.2419 REMARK 3 TLS GROUP : 56 REMARK 3 SELECTION: ( CHAIN J AND RESID 105:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.108 18.875 -115.062 REMARK 3 T TENSOR REMARK 3 T11: 0.8888 T22: 0.9964 REMARK 3 T33: 0.9959 T12: -0.0715 REMARK 3 T13: -0.0444 T23: 0.1493 REMARK 3 L TENSOR REMARK 3 L11: 2.5834 L22: 3.7930 REMARK 3 L33: 1.6631 L12: 0.4197 REMARK 3 L13: -0.0596 L23: -0.8687 REMARK 3 S TENSOR REMARK 3 S11: 0.4696 S12: -1.3453 S13: -0.6669 REMARK 3 S21: 1.1000 S22: -0.1527 S23: 0.3024 REMARK 3 S31: 0.6368 S32: -0.5567 S33: -0.3189 REMARK 3 TLS GROUP : 57 REMARK 3 SELECTION: ( CHAIN J AND RESID 124:131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.240 0.096 -125.102 REMARK 3 T TENSOR REMARK 3 T11: 1.0156 T22: 0.6896 REMARK 3 T33: 1.8145 T12: 0.2332 REMARK 3 T13: 0.2313 T23: 0.1957 REMARK 3 L TENSOR REMARK 3 L11: 2.9174 L22: 1.5474 REMARK 3 L33: 0.1162 L12: -2.0221 REMARK 3 L13: -0.0863 L23: 0.1336 REMARK 3 S TENSOR REMARK 3 S11: -0.1518 S12: 0.0494 S13: -0.2496 REMARK 3 S21: 0.6304 S22: -0.6543 S23: -0.6003 REMARK 3 S31: -0.4877 S32: -0.1287 S33: 0.2606 REMARK 3 TLS GROUP : 58 REMARK 3 SELECTION: ( CHAIN K AND RESID 1:9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.855 7.851 -20.276 REMARK 3 T TENSOR REMARK 3 T11: 1.6252 T22: 2.1775 REMARK 3 T33: 1.9760 T12: 0.2874 REMARK 3 T13: 0.4008 T23: 0.1177 REMARK 3 L TENSOR REMARK 3 L11: 2.0764 L22: 0.5004 REMARK 3 L33: 0.5133 L12: 0.7308 REMARK 3 L13: -0.5545 L23: 0.1154 REMARK 3 S TENSOR REMARK 3 S11: -0.3904 S12: 0.0422 S13: -0.2960 REMARK 3 S21: -0.8075 S22: 0.5853 S23: 0.3277 REMARK 3 S31: 0.5719 S32: 0.5864 S33: -0.1174 REMARK 3 TLS GROUP : 59 REMARK 3 SELECTION: ( CHAIN K AND RESID 10:23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.398 4.027 -12.443 REMARK 3 T TENSOR REMARK 3 T11: 1.9397 T22: 2.6700 REMARK 3 T33: 1.5149 T12: -0.0427 REMARK 3 T13: -0.2621 T23: 0.1443 REMARK 3 L TENSOR REMARK 3 L11: 0.7890 L22: 3.2501 REMARK 3 L33: 1.8173 L12: -0.3222 REMARK 3 L13: -1.0649 L23: 1.1064 REMARK 3 S TENSOR REMARK 3 S11: -0.6579 S12: -0.5990 S13: -0.2165 REMARK 3 S21: 1.3761 S22: -1.3126 S23: -0.6344 REMARK 3 S31: -0.0972 S32: -0.4817 S33: 0.5803 REMARK 3 TLS GROUP : 60 REMARK 3 SELECTION: ( CHAIN K AND RESID 24:34 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.610 13.594 -18.427 REMARK 3 T TENSOR REMARK 3 T11: 2.0217 T22: 1.8047 REMARK 3 T33: 1.3132 T12: -0.7790 REMARK 3 T13: -0.5391 T23: 0.6209 REMARK 3 L TENSOR REMARK 3 L11: 0.4063 L22: 2.5342 REMARK 3 L33: 4.2663 L12: -0.7054 REMARK 3 L13: 1.1014 L23: -1.4264 REMARK 3 S TENSOR REMARK 3 S11: 0.0561 S12: 0.5285 S13: -0.4637 REMARK 3 S21: -0.3274 S22: -0.3644 S23: 0.4929 REMARK 3 S31: 1.0982 S32: 0.0663 S33: -0.0887 REMARK 3 TLS GROUP : 61 REMARK 3 SELECTION: ( CHAIN K AND RESID 35:51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.662 0.020 -12.302 REMARK 3 T TENSOR REMARK 3 T11: 2.1681 T22: 1.9611 REMARK 3 T33: 1.6790 T12: 0.5767 REMARK 3 T13: 0.4368 T23: 0.0950 REMARK 3 L TENSOR REMARK 3 L11: 0.5597 L22: 3.6017 REMARK 3 L33: 0.2083 L12: -1.2144 REMARK 3 L13: -0.2653 L23: 0.7429 REMARK 3 S TENSOR REMARK 3 S11: -0.2456 S12: 0.4183 S13: -0.3162 REMARK 3 S21: 0.5386 S22: 0.0489 S23: -0.4703 REMARK 3 S31: 1.4583 S32: 0.7157 S33: -0.0141 REMARK 3 TLS GROUP : 62 REMARK 3 SELECTION: ( CHAIN K AND RESID 52:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.027 3.443 -8.445 REMARK 3 T TENSOR REMARK 3 T11: 1.8373 T22: 1.9911 REMARK 3 T33: 1.7063 T12: 0.4035 REMARK 3 T13: -0.1322 T23: 0.0712 REMARK 3 L TENSOR REMARK 3 L11: 1.4116 L22: 1.0219 REMARK 3 L33: 0.7378 L12: -0.3581 REMARK 3 L13: 0.8281 L23: 0.5049 REMARK 3 S TENSOR REMARK 3 S11: 0.0464 S12: -0.6940 S13: -0.4711 REMARK 3 S21: 0.1113 S22: -0.0279 S23: -1.0338 REMARK 3 S31: 1.1759 S32: 1.2618 S33: -0.0493 REMARK 3 TLS GROUP : 63 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.004 133.912 -21.584 REMARK 3 T TENSOR REMARK 3 T11: 2.1911 T22: 1.2971 REMARK 3 T33: 1.7418 T12: -0.1589 REMARK 3 T13: -0.2836 T23: -0.1215 REMARK 3 L TENSOR REMARK 3 L11: 1.2827 L22: 3.4456 REMARK 3 L33: 0.5874 L12: -1.3955 REMARK 3 L13: 0.1793 L23: -1.2330 REMARK 3 S TENSOR REMARK 3 S11: -0.1510 S12: 0.7892 S13: -0.7579 REMARK 3 S21: -0.1080 S22: 0.2654 S23: -0.0745 REMARK 3 S31: -2.0595 S32: 0.3917 S33: -0.4205 REMARK 3 TLS GROUP : 64 REMARK 3 SELECTION: ( CHAIN L AND RESID 8:70 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.579 135.627 -11.687 REMARK 3 T TENSOR REMARK 3 T11: 1.9780 T22: 1.8114 REMARK 3 T33: 1.3922 T12: -0.2109 REMARK 3 T13: -0.0206 T23: 0.2599 REMARK 3 L TENSOR REMARK 3 L11: 1.7838 L22: 1.5693 REMARK 3 L33: 1.6783 L12: -0.8073 REMARK 3 L13: 0.9497 L23: 0.1632 REMARK 3 S TENSOR REMARK 3 S11: -0.5333 S12: -0.0192 S13: 0.0507 REMARK 3 S21: -0.9331 S22: 0.2447 S23: -0.5548 REMARK 3 S31: -1.7068 S32: 1.3026 S33: 0.2043 REMARK 3 TLS GROUP : 65 REMARK 3 SELECTION: ( CHAIN L AND RESID 71:98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.233 143.063 -8.846 REMARK 3 T TENSOR REMARK 3 T11: 1.9226 T22: 1.9893 REMARK 3 T33: 1.2523 T12: -0.2301 REMARK 3 T13: -0.0352 T23: 0.0296 REMARK 3 L TENSOR REMARK 3 L11: 1.5782 L22: 2.3282 REMARK 3 L33: 2.3967 L12: 0.3948 REMARK 3 L13: -0.1948 L23: 0.1994 REMARK 3 S TENSOR REMARK 3 S11: 0.5308 S12: 0.6157 S13: 0.6396 REMARK 3 S21: 0.3307 S22: 0.3084 S23: -0.3219 REMARK 3 S31: -1.0854 S32: -0.6668 S33: -0.4882 REMARK 3 TLS GROUP : 66 REMARK 3 SELECTION: ( CHAIN L AND RESID 99:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.983 132.879 -13.283 REMARK 3 T TENSOR REMARK 3 T11: 1.5685 T22: 2.1465 REMARK 3 T33: 1.6511 T12: -0.3216 REMARK 3 T13: -0.1359 T23: 0.2594 REMARK 3 L TENSOR REMARK 3 L11: 1.3299 L22: 0.4190 REMARK 3 L33: 1.3932 L12: 0.1602 REMARK 3 L13: -0.0844 L23: 0.7414 REMARK 3 S TENSOR REMARK 3 S11: -1.1437 S12: 0.1882 S13: 0.8747 REMARK 3 S21: -0.8112 S22: 1.0757 S23: -0.7377 REMARK 3 S31: -1.0410 S32: 1.2149 S33: 0.7300 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 8RTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1292136186. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-JUL-16 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 125473 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 48.350 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 10.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1 REMARK 200 DATA REDUNDANCY IN SHELL : 10.20 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.5, 200 MM MGCL2, 10% REMARK 280 PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 83.76000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.40500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.76000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.40500 REMARK 290 SMTRY3 4 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: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G, H, I, J 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: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K 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 APPLY THE FOLLOWING TO CHAINS: E, K REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -167.52000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -83.76000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -85.40500 REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -83.76000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 85.40500 REMARK 350 BIOMT3 4 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 MET A 1 REMARK 465 ASN A 501 REMARK 465 LEU A 502 REMARK 465 TYR A 503 REMARK 465 PHE A 504 REMARK 465 GLN A 505 REMARK 465 SER A 506 REMARK 465 GLY A 507 REMARK 465 GLY A 508 REMARK 465 HIS A 509 REMARK 465 HIS A 510 REMARK 465 HIS A 511 REMARK 465 HIS A 512 REMARK 465 HIS A 513 REMARK 465 HIS A 514 REMARK 465 MET B 1 REMARK 465 ARG B 91 REMARK 465 THR B 92 REMARK 465 GLY B 93 REMARK 465 LEU B 94 REMARK 465 PHE B 95 REMARK 465 LYS B 96 REMARK 465 ASP B 97 REMARK 465 GLY B 98 REMARK 465 GLU B 99 REMARK 465 ALA B 100 REMARK 465 THR B 101 REMARK 465 TYR B 102 REMARK 465 ALA B 103 REMARK 465 PRO B 104 REMARK 465 GLY B 105 REMARK 465 ASP B 106 REMARK 465 THR B 107 REMARK 465 VAL B 108 REMARK 465 LEU B 109 REMARK 465 VAL B 110 REMARK 465 THR B 111 REMARK 465 THR B 112 REMARK 465 ASP B 113 REMARK 465 PRO B 114 REMARK 465 ALA B 115 REMARK 465 PHE B 116 REMARK 465 GLU B 117 REMARK 465 LYS B 118 REMARK 465 ILE B 119 REMARK 465 GLY B 120 REMARK 465 THR B 121 REMARK 465 LYS B 122 REMARK 465 GLU B 123 REMARK 465 LYS B 124 REMARK 465 PHE B 125 REMARK 465 TYR B 126 REMARK 465 VAL B 127 REMARK 465 ASP B 128 REMARK 465 TYR B 129 REMARK 465 PRO B 130 REMARK 465 GLN B 131 REMARK 465 LEU B 132 REMARK 465 PRO B 133 REMARK 465 ASN B 134 REMARK 465 VAL B 135 REMARK 465 VAL B 136 REMARK 465 ARG B 137 REMARK 465 PRO B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 LEU B 141 REMARK 465 ILE B 142 REMARK 465 TYR B 143 REMARK 465 VAL B 144 REMARK 465 ASP B 145 REMARK 465 ASP B 146 REMARK 465 GLY B 147 REMARK 465 VAL B 148 REMARK 465 LEU B 149 REMARK 465 THR B 150 REMARK 465 LEU B 151 REMARK 465 ARG B 152 REMARK 465 VAL B 153 REMARK 465 LEU B 154 REMARK 465 SER B 155 REMARK 465 LYS B 156 REMARK 465 GLU B 157 REMARK 465 ASP B 158 REMARK 465 ASP B 159 REMARK 465 CYS B 160 REMARK 465 THR B 161 REMARK 465 LEU B 162 REMARK 465 LYS B 163 REMARK 465 CYS B 164 REMARK 465 HIS B 165 REMARK 465 VAL B 166 REMARK 465 ASN B 167 REMARK 465 ASN B 168 REMARK 465 HIS B 169 REMARK 465 HIS B 170 REMARK 465 ARG B 171 REMARK 465 LEU B 172 REMARK 465 THR B 173 REMARK 465 ASP B 174 REMARK 465 ARG B 175 REMARK 465 LYS B 176 REMARK 465 GLY B 177 REMARK 465 ILE B 178 REMARK 465 ASN B 179 REMARK 465 LEU B 180 REMARK 465 PRO B 181 REMARK 465 GLY B 182 REMARK 465 CYS B 183 REMARK 465 GLU B 184 REMARK 465 VAL B 185 REMARK 465 ASP B 186 REMARK 465 LEU B 502 REMARK 465 TYR B 503 REMARK 465 PHE B 504 REMARK 465 GLN B 505 REMARK 465 SER B 506 REMARK 465 GLY B 507 REMARK 465 GLY B 508 REMARK 465 HIS B 509 REMARK 465 HIS B 510 REMARK 465 HIS B 511 REMARK 465 HIS B 512 REMARK 465 HIS B 513 REMARK 465 HIS B 514 REMARK 465 MET C 1 REMARK 465 ASN C 516 REMARK 465 LEU C 517 REMARK 465 TYR C 518 REMARK 465 PHE C 519 REMARK 465 GLN C 520 REMARK 465 SER C 521 REMARK 465 GLY C 522 REMARK 465 GLY C 523 REMARK 465 HIS C 524 REMARK 465 HIS C 525 REMARK 465 HIS C 526 REMARK 465 HIS C 527 REMARK 465 HIS C 528 REMARK 465 HIS C 529 REMARK 465 MET D 1 REMARK 465 ASN D 516 REMARK 465 LEU D 517 REMARK 465 TYR D 518 REMARK 465 PHE D 519 REMARK 465 GLN D 520 REMARK 465 SER D 521 REMARK 465 GLY D 522 REMARK 465 GLY D 523 REMARK 465 HIS D 524 REMARK 465 HIS D 525 REMARK 465 HIS D 526 REMARK 465 HIS D 527 REMARK 465 HIS D 528 REMARK 465 HIS D 529 REMARK 465 MET E 1 REMARK 465 ILE E 90 REMARK 465 ARG E 91 REMARK 465 THR E 92 REMARK 465 GLY E 93 REMARK 465 LEU E 94 REMARK 465 PHE E 95 REMARK 465 LYS E 96 REMARK 465 ASP E 97 REMARK 465 GLY E 98 REMARK 465 GLU E 99 REMARK 465 ALA E 100 REMARK 465 THR E 101 REMARK 465 TYR E 102 REMARK 465 ALA E 103 REMARK 465 PRO E 104 REMARK 465 GLY E 105 REMARK 465 ASP E 106 REMARK 465 THR E 107 REMARK 465 VAL E 108 REMARK 465 LEU E 109 REMARK 465 VAL E 110 REMARK 465 THR E 111 REMARK 465 THR E 112 REMARK 465 ASP E 113 REMARK 465 PRO E 114 REMARK 465 ALA E 115 REMARK 465 PHE E 116 REMARK 465 GLU E 117 REMARK 465 LYS E 118 REMARK 465 ILE E 119 REMARK 465 GLY E 120 REMARK 465 THR E 121 REMARK 465 LYS E 122 REMARK 465 GLU E 123 REMARK 465 LYS E 124 REMARK 465 PHE E 125 REMARK 465 TYR E 126 REMARK 465 VAL E 127 REMARK 465 ASP E 128 REMARK 465 TYR E 129 REMARK 465 PRO E 130 REMARK 465 GLN E 131 REMARK 465 LEU E 132 REMARK 465 PRO E 133 REMARK 465 ASN E 134 REMARK 465 VAL E 135 REMARK 465 VAL E 136 REMARK 465 ARG E 137 REMARK 465 PRO E 138 REMARK 465 GLY E 139 REMARK 465 GLY E 140 REMARK 465 LEU E 141 REMARK 465 ILE E 142 REMARK 465 TYR E 143 REMARK 465 VAL E 144 REMARK 465 ASP E 145 REMARK 465 ASP E 146 REMARK 465 GLY E 147 REMARK 465 VAL E 148 REMARK 465 LEU E 149 REMARK 465 THR E 150 REMARK 465 LEU E 151 REMARK 465 ARG E 152 REMARK 465 VAL E 153 REMARK 465 LEU E 154 REMARK 465 SER E 155 REMARK 465 LYS E 156 REMARK 465 GLU E 157 REMARK 465 ASP E 158 REMARK 465 ASP E 159 REMARK 465 CYS E 160 REMARK 465 THR E 161 REMARK 465 LEU E 162 REMARK 465 LYS E 163 REMARK 465 CYS E 164 REMARK 465 HIS E 165 REMARK 465 VAL E 166 REMARK 465 ASN E 167 REMARK 465 ASN E 168 REMARK 465 HIS E 169 REMARK 465 HIS E 170 REMARK 465 ARG E 171 REMARK 465 LEU E 172 REMARK 465 THR E 173 REMARK 465 ASP E 174 REMARK 465 ARG E 175 REMARK 465 LYS E 176 REMARK 465 GLY E 177 REMARK 465 ILE E 178 REMARK 465 ASN E 179 REMARK 465 LEU E 180 REMARK 465 PRO E 181 REMARK 465 GLY E 182 REMARK 465 CYS E 183 REMARK 465 GLU E 184 REMARK 465 VAL E 185 REMARK 465 ASP E 186 REMARK 465 LEU E 187 REMARK 465 PRO E 188 REMARK 465 ASP E 483 REMARK 465 HIS E 484 REMARK 465 SER E 485 REMARK 465 VAL E 486 REMARK 465 LYS E 487 REMARK 465 ASN E 501 REMARK 465 LEU E 502 REMARK 465 TYR E 503 REMARK 465 PHE E 504 REMARK 465 GLN E 505 REMARK 465 SER E 506 REMARK 465 GLY E 507 REMARK 465 GLY E 508 REMARK 465 HIS E 509 REMARK 465 HIS E 510 REMARK 465 HIS E 511 REMARK 465 HIS E 512 REMARK 465 HIS E 513 REMARK 465 HIS E 514 REMARK 465 MET F 1 REMARK 465 ILE F 90 REMARK 465 ARG F 91 REMARK 465 THR F 92 REMARK 465 GLY F 93 REMARK 465 LEU F 94 REMARK 465 PHE F 95 REMARK 465 LYS F 96 REMARK 465 ASP F 97 REMARK 465 GLY F 98 REMARK 465 GLU F 99 REMARK 465 ALA F 100 REMARK 465 THR F 101 REMARK 465 TYR F 102 REMARK 465 ALA F 103 REMARK 465 PRO F 104 REMARK 465 GLY F 105 REMARK 465 ASP F 106 REMARK 465 THR F 107 REMARK 465 VAL F 108 REMARK 465 LEU F 109 REMARK 465 VAL F 110 REMARK 465 THR F 111 REMARK 465 THR F 112 REMARK 465 ASP F 113 REMARK 465 PRO F 114 REMARK 465 ALA F 115 REMARK 465 PHE F 116 REMARK 465 GLU F 117 REMARK 465 LYS F 118 REMARK 465 ILE F 119 REMARK 465 GLY F 120 REMARK 465 THR F 121 REMARK 465 LYS F 122 REMARK 465 GLU F 123 REMARK 465 LYS F 124 REMARK 465 PHE F 125 REMARK 465 TYR F 126 REMARK 465 VAL F 127 REMARK 465 ASP F 128 REMARK 465 TYR F 129 REMARK 465 PRO F 130 REMARK 465 GLN F 131 REMARK 465 LEU F 132 REMARK 465 PRO F 133 REMARK 465 ASN F 134 REMARK 465 VAL F 135 REMARK 465 VAL F 136 REMARK 465 ARG F 137 REMARK 465 PRO F 138 REMARK 465 GLY F 139 REMARK 465 GLY F 140 REMARK 465 LEU F 141 REMARK 465 ILE F 142 REMARK 465 TYR F 143 REMARK 465 VAL F 144 REMARK 465 ASP F 145 REMARK 465 ASP F 146 REMARK 465 GLY F 147 REMARK 465 VAL F 148 REMARK 465 LEU F 149 REMARK 465 THR F 150 REMARK 465 LEU F 151 REMARK 465 ARG F 152 REMARK 465 VAL F 153 REMARK 465 LEU F 154 REMARK 465 SER F 155 REMARK 465 LYS F 156 REMARK 465 GLU F 157 REMARK 465 ASP F 158 REMARK 465 ASP F 159 REMARK 465 CYS F 160 REMARK 465 THR F 161 REMARK 465 LEU F 162 REMARK 465 LYS F 163 REMARK 465 CYS F 164 REMARK 465 HIS F 165 REMARK 465 VAL F 166 REMARK 465 ASN F 167 REMARK 465 ASN F 168 REMARK 465 HIS F 169 REMARK 465 HIS F 170 REMARK 465 ARG F 171 REMARK 465 LEU F 172 REMARK 465 THR F 173 REMARK 465 ASP F 174 REMARK 465 ARG F 175 REMARK 465 LYS F 176 REMARK 465 GLY F 177 REMARK 465 ILE F 178 REMARK 465 ASN F 179 REMARK 465 LEU F 180 REMARK 465 PRO F 181 REMARK 465 GLY F 182 REMARK 465 CYS F 183 REMARK 465 GLU F 184 REMARK 465 VAL F 185 REMARK 465 ASP F 186 REMARK 465 LEU F 187 REMARK 465 PRO F 188 REMARK 465 GLU F 500 REMARK 465 ASN F 501 REMARK 465 LEU F 502 REMARK 465 TYR F 503 REMARK 465 PHE F 504 REMARK 465 GLN F 505 REMARK 465 SER F 506 REMARK 465 GLY F 507 REMARK 465 GLY F 508 REMARK 465 HIS F 509 REMARK 465 HIS F 510 REMARK 465 HIS F 511 REMARK 465 HIS F 512 REMARK 465 HIS F 513 REMARK 465 HIS F 514 REMARK 465 ALA G 131 REMARK 465 ALA G 132 REMARK 465 ALA G 133 REMARK 465 TYR G 134 REMARK 465 PRO G 135 REMARK 465 TYR G 136 REMARK 465 ASP G 137 REMARK 465 VAL G 138 REMARK 465 PRO G 139 REMARK 465 ASP G 140 REMARK 465 TYR G 141 REMARK 465 GLY G 142 REMARK 465 SER G 143 REMARK 465 HIS G 144 REMARK 465 HIS G 145 REMARK 465 HIS G 146 REMARK 465 HIS G 147 REMARK 465 HIS G 148 REMARK 465 HIS G 149 REMARK 465 ALA H 131 REMARK 465 ALA H 132 REMARK 465 ALA H 133 REMARK 465 TYR H 134 REMARK 465 PRO H 135 REMARK 465 TYR H 136 REMARK 465 ASP H 137 REMARK 465 VAL H 138 REMARK 465 PRO H 139 REMARK 465 ASP H 140 REMARK 465 TYR H 141 REMARK 465 GLY H 142 REMARK 465 SER H 143 REMARK 465 HIS H 144 REMARK 465 HIS H 145 REMARK 465 HIS H 146 REMARK 465 HIS H 147 REMARK 465 HIS H 148 REMARK 465 HIS H 149 REMARK 465 ALA I 131 REMARK 465 ALA I 132 REMARK 465 ALA I 133 REMARK 465 TYR I 134 REMARK 465 PRO I 135 REMARK 465 TYR I 136 REMARK 465 ASP I 137 REMARK 465 VAL I 138 REMARK 465 PRO I 139 REMARK 465 ASP I 140 REMARK 465 TYR I 141 REMARK 465 GLY I 142 REMARK 465 SER I 143 REMARK 465 HIS I 144 REMARK 465 HIS I 145 REMARK 465 HIS I 146 REMARK 465 HIS I 147 REMARK 465 HIS I 148 REMARK 465 HIS I 149 REMARK 465 ALA J 132 REMARK 465 ALA J 133 REMARK 465 TYR J 134 REMARK 465 PRO J 135 REMARK 465 TYR J 136 REMARK 465 ASP J 137 REMARK 465 VAL J 138 REMARK 465 PRO J 139 REMARK 465 ASP J 140 REMARK 465 TYR J 141 REMARK 465 GLY J 142 REMARK 465 SER J 143 REMARK 465 HIS J 144 REMARK 465 HIS J 145 REMARK 465 HIS J 146 REMARK 465 HIS J 147 REMARK 465 HIS J 148 REMARK 465 HIS J 149 REMARK 465 ALA K 131 REMARK 465 ALA K 132 REMARK 465 ALA K 133 REMARK 465 TYR K 134 REMARK 465 PRO K 135 REMARK 465 TYR K 136 REMARK 465 ASP K 137 REMARK 465 VAL K 138 REMARK 465 PRO K 139 REMARK 465 ASP K 140 REMARK 465 TYR K 141 REMARK 465 GLY K 142 REMARK 465 SER K 143 REMARK 465 HIS K 144 REMARK 465 HIS K 145 REMARK 465 HIS K 146 REMARK 465 HIS K 147 REMARK 465 HIS K 148 REMARK 465 HIS K 149 REMARK 465 ALA L 131 REMARK 465 ALA L 132 REMARK 465 ALA L 133 REMARK 465 TYR L 134 REMARK 465 PRO L 135 REMARK 465 TYR L 136 REMARK 465 ASP L 137 REMARK 465 VAL L 138 REMARK 465 PRO L 139 REMARK 465 ASP L 140 REMARK 465 TYR L 141 REMARK 465 GLY L 142 REMARK 465 SER L 143 REMARK 465 HIS L 144 REMARK 465 HIS L 145 REMARK 465 HIS L 146 REMARK 465 HIS L 147 REMARK 465 HIS L 148 REMARK 465 HIS L 149 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 GLU A 14 CG CD OE1 OE2 REMARK 470 LYS A 18 CG CD CE NZ REMARK 470 ARG A 91 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 96 CG CD CE NZ REMARK 470 LYS A 122 CG CD CE NZ REMARK 470 LYS A 124 CG CD CE NZ REMARK 470 ASN A 134 CG OD1 ND2 REMARK 470 ARG A 137 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 157 CG CD OE1 OE2 REMARK 470 LYS A 163 CG CD CE NZ REMARK 470 ASP A 174 CG OD1 OD2 REMARK 470 LYS A 176 CG CD CE NZ REMARK 470 ASN A 179 CG OD1 ND2 REMARK 470 GLU A 184 CG CD OE1 OE2 REMARK 470 ASP A 186 CG OD1 OD2 REMARK 470 GLU A 192 CG CD OE1 OE2 REMARK 470 LYS A 193 CG CD CE NZ REMARK 470 LYS A 196 CG CD CE NZ REMARK 470 LYS A 230 CG CD CE NZ REMARK 470 LYS A 338 CG CD CE NZ REMARK 470 LYS A 372 CG CD CE NZ REMARK 470 ARG A 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 455 CG CD OE1 OE2 REMARK 470 LYS A 456 CG CD CE NZ REMARK 470 LYS A 466 CG CD CE NZ REMARK 470 LYS A 468 CG CD CE NZ REMARK 470 ASP A 483 CG OD1 OD2 REMARK 470 HIS A 484 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 487 CG CD CE NZ REMARK 470 GLU A 500 CG CD OE1 OE2 REMARK 470 GLU B 36 CG CD OE1 OE2 REMARK 470 LYS B 39 CG CD CE NZ REMARK 470 GLU B 59 CG CD OE1 OE2 REMARK 470 LYS B 196 CG CD CE NZ REMARK 470 LYS B 230 CG CD CE NZ REMARK 470 LYS B 232 CG CD CE NZ REMARK 470 GLU B 254 CG CD OE1 OE2 REMARK 470 LYS B 338 CG CD CE NZ REMARK 470 LYS B 372 CG CD CE NZ REMARK 470 ARG B 425 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 450 CG CD OE1 OE2 REMARK 470 ARG B 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 455 CG CD OE1 OE2 REMARK 470 LYS B 456 CG CD CE NZ REMARK 470 LYS B 466 CG CD CE NZ REMARK 470 LYS B 468 CG CD CE NZ REMARK 470 ASP B 483 CG OD1 OD2 REMARK 470 LYS B 487 CG CD CE NZ REMARK 470 ASN B 501 CG OD1 ND2 REMARK 470 LYS C 86 CG CD CE NZ REMARK 470 GLU C 89 CG CD OE1 OE2 REMARK 470 LYS C 96 CB CG CD CE NZ REMARK 470 ASP C 97 CG OD1 OD2 REMARK 470 GLU C 99 CG CD OE1 OE2 REMARK 470 THR C 107 OG1 CG2 REMARK 470 GLU C 117 CG CD OE1 OE2 REMARK 470 LYS C 118 CG CD CE NZ REMARK 470 ILE C 119 CG1 CG2 CD1 REMARK 470 THR C 121 OG1 CG2 REMARK 470 LYS C 122 CG CD CE NZ REMARK 470 GLU C 123 CG CD OE1 OE2 REMARK 470 LYS C 124 CG CD CE NZ REMARK 470 GLN C 131 CG CD OE1 NE2 REMARK 470 VAL C 153 CG1 CG2 REMARK 470 LYS C 156 CG CD CE NZ REMARK 470 ASP C 158 CG OD1 OD2 REMARK 470 ASP C 159 CG OD1 OD2 REMARK 470 LYS C 163 CG CD CE NZ REMARK 470 ASP C 174 CG OD1 OD2 REMARK 470 ARG C 175 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 176 CE NZ REMARK 470 GLU C 184 CG CD OE1 OE2 REMARK 470 LYS C 196 CG CD CE NZ REMARK 470 GLU C 229 CG CD OE1 OE2 REMARK 470 LYS C 230 CG CD CE NZ REMARK 470 LYS C 232 CG CD CE NZ REMARK 470 LYS C 338 CG CD CE NZ REMARK 470 LYS C 372 CG CD CE NZ REMARK 470 GLU C 450 CG CD OE1 OE2 REMARK 470 ARG C 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 455 CG CD OE1 OE2 REMARK 470 LYS C 456 CG CD CE NZ REMARK 470 LYS C 466 CG CD CE NZ REMARK 470 LYS C 468 CG CD CE NZ REMARK 470 LYS C 487 CG CD CE NZ REMARK 470 ARG C 499 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 515 CG CD OE1 OE2 REMARK 470 LYS D 18 CG CD CE NZ REMARK 470 GLU D 36 CG CD OE1 OE2 REMARK 470 LYS D 39 CG CD CE NZ REMARK 470 GLU D 59 CG CD OE1 OE2 REMARK 470 LYS D 86 CG CD CE NZ REMARK 470 GLU D 89 CG CD OE1 OE2 REMARK 470 ARG D 91 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 122 CG CD CE NZ REMARK 470 GLU D 123 CG CD OE1 OE2 REMARK 470 LYS D 124 CG CD CE NZ REMARK 470 ASN D 134 CG OD1 ND2 REMARK 470 ASP D 159 CG OD1 OD2 REMARK 470 LYS D 163 CG CD CE NZ REMARK 470 LYS D 176 CG CD CE NZ REMARK 470 GLU D 184 CG CD OE1 OE2 REMARK 470 ASP D 186 CG OD1 OD2 REMARK 470 GLU D 192 CG CD OE1 OE2 REMARK 470 LYS D 193 CG CD CE NZ REMARK 470 LYS D 196 CG CD CE NZ REMARK 470 LYS D 230 CG CD CE NZ REMARK 470 ARG D 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 372 CG CD CE NZ REMARK 470 ARG D 405 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 450 CG CD OE1 OE2 REMARK 470 ASP D 453 CG OD1 OD2 REMARK 470 LYS D 456 CG CD CE NZ REMARK 470 LYS D 466 CG CD CE NZ REMARK 470 LYS D 468 CG CD CE NZ REMARK 470 HIS D 484 CG ND1 CD2 CE1 NE2 REMARK 470 LYS D 487 CG CD CE NZ REMARK 470 GLU D 515 CG CD OE1 OE2 REMARK 470 LEU E 4 CG CD1 CD2 REMARK 470 GLN E 5 CG CD OE1 NE2 REMARK 470 ILE E 8 CG1 CG2 CD1 REMARK 470 LYS E 18 CG CD CE NZ REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 GLU E 192 CG CD OE1 OE2 REMARK 470 LYS E 193 CG CD CE NZ REMARK 470 LYS E 196 CG CD CE NZ REMARK 470 LYS E 230 CG CD CE NZ REMARK 470 GLU E 254 CG CD OE1 OE2 REMARK 470 ARG E 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 338 CG CD CE NZ REMARK 470 LYS E 368 CG CD CE NZ REMARK 470 LYS E 372 CG CD CE NZ REMARK 470 GLU E 450 CG CD OE1 OE2 REMARK 470 ASN E 452 CG OD1 ND2 REMARK 470 GLU E 455 CG CD OE1 OE2 REMARK 470 LYS E 456 CG CD CE NZ REMARK 470 LYS E 466 CG CD CE NZ REMARK 470 LYS E 468 CG CD CE NZ REMARK 470 LYS F 18 CG CD CE NZ REMARK 470 GLU F 36 CG CD OE1 OE2 REMARK 470 LYS F 39 CG CD CE NZ REMARK 470 GLU F 59 CG CD OE1 OE2 REMARK 470 GLU F 89 CG CD OE1 OE2 REMARK 470 GLU F 192 CG CD OE1 OE2 REMARK 470 LYS F 193 CG CD CE NZ REMARK 470 LYS F 196 CG CD CE NZ REMARK 470 ARG F 221 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 229 CG CD OE1 OE2 REMARK 470 LYS F 230 CG CD CE NZ REMARK 470 LYS F 232 CG CD CE NZ REMARK 470 GLU F 273 CG CD OE1 OE2 REMARK 470 ARG F 308 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 338 CG CD CE NZ REMARK 470 LYS F 372 CG CD CE NZ REMARK 470 MET F 375 CG SD CE REMARK 470 SER F 376 OG REMARK 470 GLU F 378 CG CD OE1 OE2 REMARK 470 GLU F 450 CG CD OE1 OE2 REMARK 470 ARG F 454 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 455 CG CD OE1 OE2 REMARK 470 LYS F 456 CG CD CE NZ REMARK 470 GLN F 459 CG CD OE1 NE2 REMARK 470 LYS F 466 CG CD CE NZ REMARK 470 LYS F 468 CG CD CE NZ REMARK 470 HIS F 481 CG ND1 CD2 CE1 NE2 REMARK 470 LYS F 487 CG CD CE NZ REMARK 470 ARG F 494 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 497 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 499 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 115 CG OD1 OD2 REMARK 470 GLN G 122 CG CD OE1 NE2 REMARK 470 GLN H 122 CG CD OE1 NE2 REMARK 470 GLN I 5 CG CD OE1 NE2 REMARK 470 GLN I 13 CG CD OE1 NE2 REMARK 470 LYS I 49 CG CD CE NZ REMARK 470 ARG I 51 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 71 CG CD CE NZ REMARK 470 GLU I 95 CG CD OE1 OE2 REMARK 470 GLN K 3 CG CD OE1 NE2 REMARK 470 ARG K 44 CG CD NE CZ NH1 NH2 REMARK 470 LYS K 49 CG CD CE NZ REMARK 470 LYS K 82 CG CD CE NZ REMARK 470 GLU K 95 CG CD OE1 OE2 REMARK 470 TYR K 100 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG K 118 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 GLU L 6 CG CD OE1 OE2 REMARK 470 VAL L 12 CG1 CG2 REMARK 470 LEU L 18 CG CD1 CD2 REMARK 470 LYS L 19 CG CD CE NZ REMARK 470 ARG L 44 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 49 CG CD CE NZ REMARK 470 LYS L 71 CG CD CE NZ REMARK 470 LYS L 82 CG CD CE NZ REMARK 470 TYR L 100 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS L 112 CG CD CE NZ REMARK 470 ARG L 118 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 122 CG CD OE1 NE2 REMARK 470 GLN L 125 CG CD OE1 NE2 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 SER E 361 ND2 ASN E 365 1.34 REMARK 500 CD1 PHE C 95 O GLY C 120 1.44 REMARK 500 CE1 PHE C 95 O GLY C 120 1.49 REMARK 500 O THR D 92 O TYR D 126 1.70 REMARK 500 O PRO I 94 OG1 THR I 97 1.84 REMARK 500 OG1 THR K 84 OH TYR K 86 1.85 REMARK 500 O PRO L 94 OG1 THR L 97 1.91 REMARK 500 O SER A 472 CG2 VAL A 498 1.92 REMARK 500 OG SER L 111 OE1 GLU L 116 1.94 REMARK 500 O ASP D 451 NH2 ARG D 457 1.96 REMARK 500 O LYS F 18 NE2 GLN F 355 1.97 REMARK 500 NH1 ARG G 33 OD1 ASP G 38 1.97 REMARK 500 OD2 ASP J 79 NZ LYS J 82 1.99 REMARK 500 OG SER F 411 O ARG F 436 2.01 REMARK 500 O SER B 44 CG1 VAL B 344 2.02 REMARK 500 N THR C 297 O HOH C 701 2.02 REMARK 500 O SER F 383 OG SER F 387 2.03 REMARK 500 O GLY I 16 CD1 LEU I 92 2.04 REMARK 500 O ARG A 195 OE1 GLN A 199 2.05 REMARK 500 OE1 GLN K 1 CG ASN K 28 2.08 REMARK 500 O SER A 44 CG1 VAL A 344 2.08 REMARK 500 O SER K 69 NH2 ARG K 73 2.10 REMARK 500 OE1 GLN K 1 OD1 ASN K 28 2.10 REMARK 500 O ASP D 451 O ASP D 453 2.11 REMARK 500 O SER K 111 OH TYR K 117 2.13 REMARK 500 OE2 GLU E 378 NH1 ARG E 405 2.14 REMARK 500 O SER F 384 OG SER F 388 2.15 REMARK 500 O SER L 58 NH1 ARG L 78 2.16 REMARK 500 O VAL F 445 O HIS F 448 2.16 REMARK 500 N LYS A 372 O HOH A 701 2.16 REMARK 500 O GLN I 5 N ALA I 23 2.16 REMARK 500 O LEU A 94 O LYS A 118 2.18 REMARK 500 OD1 ASN B 52 OG SER B 54 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 NZ LYS F 274 CD1 TRP K 108 3455 1.04 REMARK 500 NZ LYS F 274 NE1 TRP K 108 3455 1.49 REMARK 500 NZ LYS F 274 CG TRP K 108 3455 1.59 REMARK 500 NH2 ARG E 311 OD1 ASP F 316 3445 1.77 REMARK 500 O VAL G 128 OG SER J 91 4454 2.10 REMARK 500 NZ LYS F 274 CE2 TRP K 108 3455 2.12 REMARK 500 NZ LYS F 274 CD2 TRP K 108 3455 2.18 REMARK 500 CE LYS F 274 CD1 TRP K 108 3455 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS B 327 CB CYS B 327 SG -0.122 REMARK 500 CYS D 295 CB CYS D 295 SG -0.148 REMARK 500 PRO F 374 CD PRO F 374 N 0.151 REMARK 500 GLU F 391 C GLU F 391 O 0.159 REMARK 500 LYS G 82 CD LYS G 82 CE 0.161 REMARK 500 LYS G 82 CE LYS G 82 NZ 0.189 REMARK 500 GLN I 88 CG GLN I 88 CD -0.184 REMARK 500 SER K 91 CB SER K 91 OG -0.183 REMARK 500 ARG L 51 CG ARG L 51 CD 0.185 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 SER A 44 CB - CA - C ANGL. DEV. = -22.5 DEGREES REMARK 500 SER A 472 CB - CA - C ANGL. DEV. = 17.2 DEGREES REMARK 500 HIS A 484 CB - CA - C ANGL. DEV. = 16.2 DEGREES REMARK 500 SER B 44 CB - CA - C ANGL. DEV. = -20.7 DEGREES REMARK 500 ASP B 453 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 LYS B 468 CB - CA - C ANGL. DEV. = 19.0 DEGREES REMARK 500 SER B 485 CB - CA - C ANGL. DEV. = -15.7 DEGREES REMARK 500 SER B 485 N - CA - C ANGL. DEV. = 22.7 DEGREES REMARK 500 GLY C 120 N - CA - C ANGL. DEV. = 35.5 DEGREES REMARK 500 LEU C 149 CA - CB - CG ANGL. DEV. = -14.4 DEGREES REMARK 500 THR C 173 CB - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 THR C 173 N - CA - C ANGL. DEV. = -20.9 DEGREES REMARK 500 ILE C 178 CA - CB - CG1 ANGL. DEV. = 21.2 DEGREES REMARK 500 CYS C 183 CB - CA - C ANGL. DEV. = -13.9 DEGREES REMARK 500 SER C 331 N - CA - C ANGL. DEV. = 19.0 DEGREES REMARK 500 ASP C 453 CB - CA - C ANGL. DEV. = 13.2 DEGREES REMARK 500 SER C 472 CB - CA - C ANGL. DEV. = 11.4 DEGREES REMARK 500 THR D 92 CB - CA - C ANGL. DEV. = -22.7 DEGREES REMARK 500 THR D 92 N - CA - C ANGL. DEV. = 17.5 DEGREES REMARK 500 THR D 173 CB - CA - C ANGL. DEV. = -19.6 DEGREES REMARK 500 THR D 173 N - CA - C ANGL. DEV. = -17.2 DEGREES REMARK 500 PRO D 181 CB - CA - C ANGL. DEV. = -13.8 DEGREES REMARK 500 VAL D 202 CG1 - CB - CG2 ANGL. DEV. = -19.2 DEGREES REMARK 500 ILE D 270 CG1 - CB - CG2 ANGL. DEV. = -22.2 DEGREES REMARK 500 ASP D 453 CB - CA - C ANGL. DEV. = 21.2 DEGREES REMARK 500 ASP D 453 N - CA - C ANGL. DEV. = -25.0 DEGREES REMARK 500 LYS E 18 N - CA - C ANGL. DEV. = -18.4 DEGREES REMARK 500 SER E 44 CB - CA - C ANGL. DEV. = -20.5 DEGREES REMARK 500 ASP E 360 N - CA - C ANGL. DEV. = 24.1 DEGREES REMARK 500 SER E 361 C - N - CA ANGL. DEV. = 17.9 DEGREES REMARK 500 SER E 361 CB - CA - C ANGL. DEV. = -24.3 DEGREES REMARK 500 SER E 361 N - CA - CB ANGL. DEV. = -19.4 DEGREES REMARK 500 SER E 361 N - CA - C ANGL. DEV. = 42.0 DEGREES REMARK 500 VAL E 362 CB - CA - C ANGL. DEV. = -11.5 DEGREES REMARK 500 LYS E 468 CB - CA - C ANGL. DEV. = 17.1 DEGREES REMARK 500 ALA F 17 N - CA - C ANGL. DEV. = 21.9 DEGREES REMARK 500 HIS F 19 N - CA - C ANGL. DEV. = 16.3 DEGREES REMARK 500 SER F 44 CB - CA - C ANGL. DEV. = -19.0 DEGREES REMARK 500 LEU F 227 CB - CA - C ANGL. DEV. = 16.4 DEGREES REMARK 500 LEU F 227 N - CA - C ANGL. DEV. = -22.6 DEGREES REMARK 500 CYS F 281 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 ARG F 311 CB - CG - CD ANGL. DEV. = -21.7 DEGREES REMARK 500 ASP F 360 CB - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 LYS F 372 CB - CA - C ANGL. DEV. = -24.2 DEGREES REMARK 500 PRO F 374 N - CA - C ANGL. DEV. = -39.4 DEGREES REMARK 500 MET F 375 CB - CA - C ANGL. DEV. = -13.1 DEGREES REMARK 500 MET F 375 N - CA - CB ANGL. DEV. = -22.0 DEGREES REMARK 500 GLU F 391 CA - CB - CG ANGL. DEV. = 27.5 DEGREES REMARK 500 GLU F 391 CB - CG - CD ANGL. DEV. = 16.4 DEGREES REMARK 500 GLU F 391 OE1 - CD - OE2 ANGL. DEV. = -23.8 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 98 ANGLE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 44 31.47 -95.23 REMARK 500 ASP A 97 10.02 81.61 REMARK 500 ASP A 145 63.22 62.89 REMARK 500 ARG A 175 66.80 63.85 REMARK 500 LEU A 180 102.94 -39.79 REMARK 500 CYS A 183 -155.98 -100.71 REMARK 500 ALA A 296 -94.54 -121.93 REMARK 500 GLN A 298 62.60 61.86 REMARK 500 MET A 299 -69.38 -102.99 REMARK 500 ARG A 414 64.03 62.54 REMARK 500 SER A 437 -9.14 74.68 REMARK 500 HIS A 448 -156.96 -144.06 REMARK 500 ARG A 454 15.32 53.88 REMARK 500 TYR A 489 150.12 78.99 REMARK 500 GLU B 89 -156.11 -101.11 REMARK 500 ALA B 296 -62.68 -122.34 REMARK 500 GLN B 298 57.43 39.24 REMARK 500 MET B 299 -66.79 -96.01 REMARK 500 SER B 331 -82.74 -120.09 REMARK 500 TYR B 339 56.96 -140.05 REMARK 500 ARG B 414 71.84 44.44 REMARK 500 ARG B 454 16.68 57.42 REMARK 500 ASN B 491 -4.41 -141.27 REMARK 500 THR C 32 -2.50 -144.15 REMARK 500 THR C 92 50.56 -107.81 REMARK 500 ASP C 97 19.06 58.09 REMARK 500 ASP C 145 -120.76 47.97 REMARK 500 ASP C 146 55.30 -117.50 REMARK 500 GLU C 157 -138.88 60.04 REMARK 500 ASN C 167 53.83 -112.99 REMARK 500 ARG C 175 43.37 33.84 REMARK 500 GLU C 241 20.54 -140.48 REMARK 500 MET C 299 -65.72 -92.23 REMARK 500 SER C 331 -79.29 -103.18 REMARK 500 SER C 437 -2.12 76.62 REMARK 500 HIS C 448 -152.16 -115.48 REMARK 500 ASP C 451 43.18 36.96 REMARK 500 THR D 32 -5.80 -146.84 REMARK 500 ASP D 97 -5.83 78.02 REMARK 500 ALA D 100 136.69 -170.34 REMARK 500 PRO D 138 142.70 -38.65 REMARK 500 ASP D 145 -114.12 50.18 REMARK 500 CYS D 160 39.04 -155.12 REMARK 500 CYS D 183 -135.48 56.80 REMARK 500 GLU D 184 46.97 32.85 REMARK 500 PRO D 188 -178.59 -66.60 REMARK 500 LEU D 300 50.83 -140.86 REMARK 500 SER D 331 -92.85 -113.64 REMARK 500 SER D 437 -14.22 84.22 REMARK 500 HIS D 448 -151.73 -112.54 REMARK 500 REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY A 332 GLU A 333 148.02 REMARK 500 LYS B 372 ILE B 373 -149.72 REMARK 500 GLY C 120 THR C 121 -146.41 REMARK 500 ASN C 168 HIS C 169 124.32 REMARK 500 THR C 173 ASP C 174 -148.45 REMARK 500 ILE C 373 PRO C 374 54.87 REMARK 500 THR D 173 ASP D 174 -138.88 REMARK 500 ASP E 360 SER E 361 137.08 REMARK 500 ALA F 17 LYS F 18 -146.72 REMARK 500 SER F 44 GLY F 45 149.06 REMARK 500 ASP F 233 THR F 234 125.97 REMARK 500 ILE F 373 PRO F 374 69.00 REMARK 500 HIS F 448 GLY F 449 -147.35 REMARK 500 GLN F 492 THR F 493 149.17 REMARK 500 LYS G 49 GLU G 50 145.34 REMARK 500 GLN I 5 GLU I 6 -148.98 REMARK 500 ASP I 106 SER I 107 -148.65 REMARK 500 ARG J 51 GLU J 52 137.16 REMARK 500 GLU K 50 ARG K 51 -138.13 REMARK 500 ILE K 76 SER K 77 137.47 REMARK 500 ASN K 90 SER K 91 -126.16 REMARK 500 GLU L 6 SER L 7 141.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG D 195 0.08 SIDE CHAIN REMARK 500 ARG D 499 0.12 SIDE CHAIN REMARK 500 ARG F 311 0.21 SIDE CHAIN REMARK 500 ARG F 425 0.26 SIDE CHAIN REMARK 500 ARG I 73 0.14 SIDE CHAIN REMARK 500 GLN I 88 0.09 SIDE CHAIN REMARK 500 ARG I 118 0.24 SIDE CHAIN REMARK 500 GLU J 52 0.09 SIDE CHAIN REMARK 500 TYR K 101 0.07 SIDE CHAIN REMARK 500 ARG L 51 0.16 SIDE CHAIN REMARK 500 ARG L 73 0.24 SIDE CHAIN REMARK 500 ARG L 78 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLU K 50 -12.14 REMARK 500 REMARK 500 REMARK: NULL DBREF 8RTF A 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF B 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF C 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF D 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF E 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF F 1 499 UNP G0UYF4 G0UYF4_TRYCI 1 499 DBREF 8RTF G 1 149 PDB 8RTF 8RTF 1 149 DBREF 8RTF H 1 149 PDB 8RTF 8RTF 1 149 DBREF 8RTF I 1 149 PDB 8RTF 8RTF 1 149 DBREF 8RTF J 1 149 PDB 8RTF 8RTF 1 149 DBREF 8RTF K 1 149 PDB 8RTF 8RTF 1 149 DBREF 8RTF L 1 149 PDB 8RTF 8RTF 1 149 SEQADV 8RTF GLU A 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN A 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU A 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR A 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE A 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN A 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER A 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY A 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY A 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS A 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLU B 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN B 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU B 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR B 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE B 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN B 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER B 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY B 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY B 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS B 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLU C 515 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN C 516 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU C 517 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR C 518 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE C 519 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN C 520 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER C 521 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY C 522 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY C 523 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 524 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 525 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 526 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 527 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 528 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS C 529 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLU D 515 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN D 516 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU D 517 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR D 518 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE D 519 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN D 520 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER D 521 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY D 522 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY D 523 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 524 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 525 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 526 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 527 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 528 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS D 529 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLU E 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN E 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU E 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR E 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE E 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN E 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER E 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY E 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY E 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS E 514 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLU F 500 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF ASN F 501 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF LEU F 502 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF TYR F 503 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF PHE F 504 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLN F 505 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF SER F 506 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY F 507 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF GLY F 508 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 509 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 510 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 511 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 512 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 513 UNP G0UYF4 EXPRESSION TAG SEQADV 8RTF HIS F 514 UNP G0UYF4 EXPRESSION TAG SEQRES 1 A 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 A 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 A 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 A 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 A 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 A 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 A 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 A 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 A 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 A 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 A 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 A 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 A 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 A 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 A 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 A 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 A 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 A 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 A 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 A 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 A 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 A 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 A 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 A 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 A 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 A 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 A 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 A 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 A 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 A 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 A 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 A 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 A 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 A 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 A 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 A 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 A 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 A 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 A 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 A 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 B 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 B 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 B 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 B 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 B 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 B 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 B 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 B 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 B 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 B 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 B 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 B 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 B 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 B 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 B 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 B 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 B 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 B 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 B 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 B 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 B 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 B 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 B 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 B 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 B 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 B 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 B 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 B 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 B 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 B 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 B 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 B 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 B 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 B 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 B 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 B 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 B 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 B 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 B 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 B 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 C 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 C 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 C 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 C 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 C 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 C 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 C 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 C 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 C 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 C 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 C 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 C 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 C 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 C 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 C 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 C 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 C 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 C 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 C 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 C 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 C 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 C 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 C 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 C 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 C 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 C 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 C 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 C 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 C 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 C 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 C 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 C 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 C 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 C 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 C 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 C 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 C 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 C 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 C 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 C 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 D 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 D 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 D 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 D 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 D 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 D 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 D 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 D 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 D 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 D 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 D 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 D 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 D 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 D 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 D 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 D 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 D 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 D 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 D 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 D 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 D 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 D 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 D 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 D 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 D 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 D 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 D 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 D 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 D 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 D 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 D 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 D 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 D 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 D 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 D 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 D 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 D 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 D 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 D 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 D 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 E 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 E 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 E 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 E 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 E 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 E 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 E 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 E 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 E 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 E 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 E 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 E 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 E 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 E 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 E 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 E 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 E 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 E 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 E 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 E 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 E 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 E 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 E 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 E 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 E 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 E 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 E 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 E 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 E 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 E 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 E 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 E 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 E 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 E 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 E 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 E 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 E 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 E 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 E 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 F 514 MET SER GLN LEU GLN HIS ASN ILE GLY LEU SER ILE PHE SEQRES 2 F 514 GLU PRO VAL ALA LYS HIS ARG ALA ASN ARG ILE ILE CYS SEQRES 3 F 514 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS SEQRES 4 F 514 GLY LEU MET LYS SER GLY MET SER VAL ALA ARG MET ASN SEQRES 5 F 514 PHE SER HIS GLY SER TYR GLU TYR HIS GLN THR THR ILE SEQRES 6 F 514 ASN ASN VAL ARG ALA ALA ALA ALA GLU LEU GLY LEU HIS SEQRES 7 F 514 ILE GLY ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG SEQRES 8 F 514 THR GLY LEU PHE LYS ASP GLY GLU ALA THR TYR ALA PRO SEQRES 9 F 514 GLY ASP THR VAL LEU VAL THR THR ASP PRO ALA PHE GLU SEQRES 10 F 514 LYS ILE GLY THR LYS GLU LYS PHE TYR VAL ASP TYR PRO SEQRES 11 F 514 GLN LEU PRO ASN VAL VAL ARG PRO GLY GLY LEU ILE TYR SEQRES 12 F 514 VAL ASP ASP GLY VAL LEU THR LEU ARG VAL LEU SER LYS SEQRES 13 F 514 GLU ASP ASP CYS THR LEU LYS CYS HIS VAL ASN ASN HIS SEQRES 14 F 514 HIS ARG LEU THR ASP ARG LYS GLY ILE ASN LEU PRO GLY SEQRES 15 F 514 CYS GLU VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ARG SEQRES 16 F 514 LYS ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET SEQRES 17 F 514 ILE PHE ALA SER PHE ILE ARG THR ALA ASP GLN VAL ARG SEQRES 18 F 514 GLU VAL ARG ALA ALA LEU GLY GLU LYS GLY LYS ASP THR SEQRES 19 F 514 LEU ILE ILE SER LYS ILE GLU ASN HIS GLN GLY VAL GLN SEQRES 20 F 514 ASN ILE ASP ALA ILE ILE GLU ALA SER ASP GLY ILE MET SEQRES 21 F 514 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU SEQRES 22 F 514 LYS VAL VAL VAL ALA GLN MET CYS ILE ILE SER LYS CYS SEQRES 23 F 514 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET SEQRES 24 F 514 LEU GLU SER MET THR THR ASN PRO ARG PRO THR ARG ALA SEQRES 25 F 514 GLU VAL THR ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA SEQRES 26 F 514 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS SEQRES 27 F 514 TYR PRO ASN GLU VAL VAL GLN TYR MET VAL ARG ILE CYS SEQRES 28 F 514 ILE GLU ALA GLN SER ALA THR HIS ASP SER VAL MET PHE SEQRES 29 F 514 ASN SER ILE LYS ASN LEU GLN LYS ILE PRO MET SER PRO SEQRES 30 F 514 GLU GLU ALA VAL CYS SER SER ALA VAL SER SER ALA PHE SEQRES 31 F 514 GLU VAL GLN ALA LYS ALA ILE LEU VAL LEU SER ASN THR SEQRES 32 F 514 GLY ARG SER ALA ARG LEU ILE SER LYS TYR ARG PRO ASN SEQRES 33 F 514 CYS PRO ILE ILE CYS ALA THR THR ARG LEU LEU THR CYS SEQRES 34 F 514 ARG GLN LEU ASN VAL THR ARG SER VAL GLU SER VAL TYR SEQRES 35 F 514 TYR ASP VAL ASP ALA HIS GLY GLU ASP ASN ASP ARG GLU SEQRES 36 F 514 LYS ARG VAL GLN LEU GLY VAL ASP TRP ALA LYS THR LYS SEQRES 37 F 514 GLY TYR VAL SER ALA GLY ASP VAL MET VAL ILE VAL HIS SEQRES 38 F 514 ALA ASP HIS SER VAL LYS GLY TYR PRO ASN GLN THR ARG SEQRES 39 F 514 LEU VAL ARG VAL ARG GLU ASN LEU TYR PHE GLN SER GLY SEQRES 40 F 514 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 G 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 G 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 G 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 G 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 G 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 G 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 G 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 G 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 G 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 G 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 G 149 HIS HIS HIS HIS HIS HIS SEQRES 1 H 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 H 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 H 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 H 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 H 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 H 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 H 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 H 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 H 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 H 149 HIS HIS HIS HIS HIS HIS SEQRES 1 I 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 I 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 I 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 I 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 I 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 I 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 I 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 I 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 I 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 I 149 HIS HIS HIS HIS HIS HIS SEQRES 1 J 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 J 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 J 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 J 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 J 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 J 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 J 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 J 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 J 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 J 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 J 149 HIS HIS HIS HIS HIS HIS SEQRES 1 K 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 K 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 K 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 K 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 K 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 K 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 K 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 K 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 K 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 K 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 K 149 HIS HIS HIS HIS HIS HIS SEQRES 1 L 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 L 149 SER GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 L 149 SER ASN PHE SER SER GLY ARG THR PHE SER THR ASP ALA SEQRES 4 L 149 ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 L 149 PHE VAL GLY GLY ILE SER TRP ASN GLY GLY ILE THR ASP SEQRES 6 L 149 TYR VAL ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 L 149 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 L 149 LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA GLY SEQRES 9 L 149 ARG ASP SER TRP TYR PHE SER LYS VAL PRO ASP GLU TYR SEQRES 10 L 149 ARG TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 L 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 L 149 HIS HIS HIS HIS HIS HIS HET GOL A 601 6 HET GOL B 701 6 HET GOL B 702 6 HET GOL B 703 6 HET GOL C 601 6 HET GOL C 602 6 HET GOL D 601 6 HET GOL D 602 6 HET GOL E 601 6 HET GOL F 601 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 13 GOL 10(C3 H8 O3) FORMUL 23 HOH *86(H2 O) HELIX 1 AA1 SER A 2 GLY A 9 1 8 HELIX 2 AA2 SER A 34 SER A 44 1 11 HELIX 3 AA3 SER A 57 GLY A 76 1 20 HELIX 4 AA4 ASP A 113 GLU A 117 5 5 HELIX 5 AA5 GLN A 131 VAL A 136 1 6 HELIX 6 AA6 SER A 191 GLY A 205 1 15 HELIX 7 AA7 THR A 216 GLY A 228 1 13 HELIX 8 AA8 ASN A 242 ASN A 248 1 7 HELIX 9 AA9 ASN A 248 SER A 256 1 9 HELIX 10 AB1 ALA A 262 ILE A 270 1 9 HELIX 11 AB2 PRO A 271 GLY A 290 1 20 HELIX 12 AB3 LEU A 300 THR A 305 5 6 HELIX 13 AB4 THR A 310 ASN A 323 1 14 HELIX 14 AB5 TYR A 339 THR A 358 1 20 HELIX 15 AB6 SER A 361 LEU A 370 1 10 HELIX 16 AB7 SER A 376 GLN A 393 1 18 HELIX 17 AB8 GLY A 404 ARG A 414 1 11 HELIX 18 AB9 ARG A 425 ASN A 433 1 9 HELIX 19 AC1 ARG A 454 LYS A 468 1 15 HELIX 20 AC2 GLN B 3 GLY B 9 1 7 HELIX 21 AC3 SER B 34 SER B 44 1 11 HELIX 22 AC4 SER B 57 GLY B 76 1 20 HELIX 23 AC5 SER B 191 GLY B 205 1 15 HELIX 24 AC6 THR B 216 GLY B 228 1 13 HELIX 25 AC7 GLU B 229 LYS B 232 5 4 HELIX 26 AC8 ASN B 242 ASN B 248 1 7 HELIX 27 AC9 ASN B 248 SER B 256 1 9 HELIX 28 AD1 ALA B 262 ILE B 270 1 9 HELIX 29 AD2 PRO B 271 GLY B 290 1 20 HELIX 30 AD3 LEU B 300 THR B 305 5 6 HELIX 31 AD4 THR B 310 GLY B 324 1 15 HELIX 32 AD5 SER B 331 LYS B 336 1 6 HELIX 33 AD6 TYR B 339 THR B 358 1 20 HELIX 34 AD7 SER B 361 LEU B 370 1 10 HELIX 35 AD8 SER B 376 GLN B 393 1 18 HELIX 36 AD9 GLY B 404 TYR B 413 1 10 HELIX 37 AE1 ARG B 425 LEU B 432 1 8 HELIX 38 AE2 ASN B 433 THR B 435 5 3 HELIX 39 AE3 ARG B 454 LYS B 468 1 15 HELIX 40 AE4 GLN C 3 GLY C 9 1 7 HELIX 41 AE5 SER C 34 GLY C 45 1 12 HELIX 42 AE6 SER C 57 GLY C 76 1 20 HELIX 43 AE7 GLN C 131 VAL C 136 1 6 HELIX 44 AE8 SER C 191 GLY C 205 1 15 HELIX 45 AE9 THR C 216 LEU C 227 1 12 HELIX 46 AF1 GLY C 228 LYS C 232 5 5 HELIX 47 AF2 ASN C 242 ASN C 248 1 7 HELIX 48 AF3 ASN C 248 SER C 256 1 9 HELIX 49 AF4 ALA C 262 ILE C 270 1 9 HELIX 50 AF5 PRO C 271 GLY C 290 1 20 HELIX 51 AF6 LEU C 300 THR C 305 5 6 HELIX 52 AF7 THR C 310 GLY C 324 1 15 HELIX 53 AF8 SER C 331 LYS C 336 1 6 HELIX 54 AF9 TYR C 339 THR C 358 1 20 HELIX 55 AG1 SER C 361 GLN C 371 1 11 HELIX 56 AG2 SER C 376 GLN C 393 1 18 HELIX 57 AG3 GLY C 404 TYR C 413 1 10 HELIX 58 AG4 ARG C 425 LEU C 432 1 8 HELIX 59 AG5 ASN C 433 THR C 435 5 3 HELIX 60 AG6 GLU C 455 LYS C 468 1 14 HELIX 61 AG7 GLN D 3 GLY D 9 1 7 HELIX 62 AG8 SER D 34 GLY D 45 1 12 HELIX 63 AG9 SER D 57 GLY D 76 1 20 HELIX 64 AH1 PHE D 95 GLU D 99 5 5 HELIX 65 AH2 ASP D 113 LYS D 118 5 6 HELIX 66 AH3 GLN D 131 VAL D 136 1 6 HELIX 67 AH4 SER D 191 GLY D 205 1 15 HELIX 68 AH5 THR D 216 LEU D 227 1 12 HELIX 69 AH6 ASN D 242 ASN D 248 1 7 HELIX 70 AH7 ASN D 248 SER D 256 1 9 HELIX 71 AH8 ALA D 262 ILE D 270 1 9 HELIX 72 AH9 PRO D 271 GLY D 290 1 20 HELIX 73 AI1 LEU D 300 THR D 305 5 6 HELIX 74 AI2 THR D 310 GLY D 324 1 15 HELIX 75 AI3 SER D 331 LYS D 336 1 6 HELIX 76 AI4 TYR D 339 THR D 358 1 20 HELIX 77 AI5 SER D 361 GLN D 371 1 11 HELIX 78 AI6 SER D 376 GLN D 393 1 18 HELIX 79 AI7 GLY D 404 TYR D 413 1 10 HELIX 80 AI8 ARG D 425 LEU D 432 1 8 HELIX 81 AI9 ASN D 433 THR D 435 5 3 HELIX 82 AJ1 ARG D 454 LYS D 468 1 15 HELIX 83 AJ2 GLN E 3 GLY E 9 1 7 HELIX 84 AJ3 SER E 34 SER E 44 1 11 HELIX 85 AJ4 SER E 57 GLY E 76 1 20 HELIX 86 AJ5 SER E 191 GLY E 205 1 15 HELIX 87 AJ6 THR E 216 LEU E 227 1 12 HELIX 88 AJ7 GLY E 228 LYS E 232 5 5 HELIX 89 AJ8 ASN E 242 ASN E 248 1 7 HELIX 90 AJ9 ASN E 248 SER E 256 1 9 HELIX 91 AK1 ALA E 262 VAL E 268 1 7 HELIX 92 AK2 LYS E 274 GLY E 290 1 17 HELIX 93 AK3 LEU E 300 THR E 305 5 6 HELIX 94 AK4 THR E 310 GLY E 324 1 15 HELIX 95 AK5 SER E 331 LYS E 336 1 6 HELIX 96 AK6 TYR E 339 THR E 358 1 20 HELIX 97 AK7 SER E 361 LEU E 370 1 10 HELIX 98 AK8 SER E 376 GLN E 393 1 18 HELIX 99 AK9 GLY E 404 TYR E 413 1 10 HELIX 100 AL1 ARG E 425 LEU E 432 1 8 HELIX 101 AL2 ASN E 433 THR E 435 5 3 HELIX 102 AL3 GLU E 455 LYS E 468 1 14 HELIX 103 AL4 GLN F 3 GLY F 9 1 7 HELIX 104 AL5 SER F 34 SER F 44 1 11 HELIX 105 AL6 SER F 57 GLY F 76 1 20 HELIX 106 AL7 SER F 191 GLY F 205 1 15 HELIX 107 AL8 THR F 216 LEU F 227 1 12 HELIX 108 AL9 GLY F 228 LYS F 232 5 5 HELIX 109 AM1 ASN F 242 ASN F 248 1 7 HELIX 110 AM2 ASN F 248 SER F 256 1 9 HELIX 111 AM3 ALA F 262 GLY F 267 1 6 HELIX 112 AM4 PRO F 271 GLY F 290 1 20 HELIX 113 AM5 LEU F 300 THR F 305 5 6 HELIX 114 AM6 THR F 310 GLY F 324 1 15 HELIX 115 AM7 SER F 331 LYS F 336 1 6 HELIX 116 AM8 TYR F 339 THR F 358 1 20 HELIX 117 AM9 SER F 361 LEU F 370 1 10 HELIX 118 AN1 GLU F 378 GLN F 393 1 16 HELIX 119 AN2 GLY F 404 TYR F 413 1 10 HELIX 120 AN3 ARG F 425 LEU F 432 1 8 HELIX 121 AN4 ASN F 433 THR F 435 5 3 HELIX 122 AN5 GLU F 455 LYS F 468 1 14 HELIX 123 AN6 ASP G 68 LYS G 71 5 4 HELIX 124 AN7 GLN G 93 THR G 97 5 5 HELIX 125 AN8 VAL G 113 TYR G 117 5 5 HELIX 126 AN9 PHE H 29 GLY H 32 5 4 HELIX 127 AO1 SER H 36 ASP H 38 5 3 HELIX 128 AO2 ASP H 68 LYS H 71 5 4 HELIX 129 AO3 GLN H 93 THR H 97 5 5 HELIX 130 AO4 VAL H 113 TYR H 117 5 5 HELIX 131 AO5 THR I 34 ASP I 38 5 5 HELIX 132 AO6 ASP I 68 LYS I 71 5 4 HELIX 133 AO7 GLN I 93 THR I 97 5 5 HELIX 134 AO8 VAL I 113 TYR I 117 5 5 HELIX 135 AO9 THR J 34 ASP J 38 5 5 HELIX 136 AP1 ASP J 68 LYS J 71 5 4 HELIX 137 AP2 GLN J 93 THR J 97 5 5 HELIX 138 AP3 VAL J 113 TYR J 117 5 5 HELIX 139 AP4 ASP K 68 LYS K 71 5 4 HELIX 140 AP5 GLN K 93 THR K 97 5 5 HELIX 141 AP6 VAL K 113 TYR K 117 5 5 HELIX 142 AP7 ASP L 68 LYS L 71 5 4 HELIX 143 AP8 GLN L 93 THR L 97 5 5 HELIX 144 AP9 VAL L 113 TYR L 117 5 5 SHEET 1 AA1 9 ARG A 23 THR A 27 0 SHEET 2 AA1 9 VAL A 48 ASN A 52 1 O ARG A 50 N CYS A 26 SHEET 3 AA1 9 GLY A 80 ASP A 84 1 O ALA A 82 N ALA A 49 SHEET 4 AA1 9 MET A 208 ALA A 211 1 O PHE A 210 N LEU A 83 SHEET 5 AA1 9 LEU A 235 ILE A 240 1 O LEU A 235 N ILE A 209 SHEET 6 AA1 9 GLY A 258 VAL A 261 1 O MET A 260 N ILE A 240 SHEET 7 AA1 9 VAL A 293 CYS A 295 1 O ILE A 294 N VAL A 261 SHEET 8 AA1 9 CYS A 327 LEU A 330 1 O MET A 329 N CYS A 295 SHEET 9 AA1 9 ARG A 23 THR A 27 1 N ILE A 25 O LEU A 330 SHEET 1 AA2 2 GLU A 99 TYR A 102 0 SHEET 2 AA2 2 HIS A 170 THR A 173 -1 O LEU A 172 N ALA A 100 SHEET 1 AA3 5 LYS A 124 TYR A 126 0 SHEET 2 AA3 5 THR A 107 THR A 111 1 N THR A 111 O PHE A 125 SHEET 3 AA3 5 THR A 161 VAL A 166 -1 O LEU A 162 N VAL A 110 SHEET 4 AA3 5 LEU A 149 SER A 155 -1 N ARG A 152 O HIS A 165 SHEET 5 AA3 5 LEU A 141 VAL A 144 -1 N VAL A 144 O LEU A 149 SHEET 1 AA410 VAL A 438 TYR A 442 0 SHEET 2 AA410 ILE A 419 THR A 423 1 N CYS A 421 O GLU A 439 SHEET 3 AA410 ILE A 397 LEU A 400 1 N ILE A 397 O ILE A 420 SHEET 4 AA410 VAL A 476 HIS A 481 1 O VAL A 478 N LEU A 398 SHEET 5 AA410 GLN A 492 ARG A 497 -1 O ARG A 494 N ILE A 479 SHEET 6 AA410 GLN C 492 ARG C 497 -1 O THR C 493 N THR A 493 SHEET 7 AA410 VAL C 476 HIS C 481 -1 N ILE C 479 O ARG C 494 SHEET 8 AA410 ALA C 396 LEU C 400 1 N LEU C 398 O VAL C 478 SHEET 9 AA410 ILE C 419 THR C 423 1 O ILE C 420 N ILE C 397 SHEET 10 AA410 VAL C 438 TYR C 442 1 O VAL C 441 N CYS C 421 SHEET 1 AA5 9 ARG B 23 THR B 27 0 SHEET 2 AA5 9 MET B 46 ASN B 52 1 O ARG B 50 N CYS B 26 SHEET 3 AA5 9 GLY B 80 ASP B 84 1 O ASP B 84 N MET B 51 SHEET 4 AA5 9 MET B 208 ALA B 211 1 O MET B 208 N LEU B 83 SHEET 5 AA5 9 LEU B 235 ILE B 240 1 O ILE B 237 N ILE B 209 SHEET 6 AA5 9 GLY B 258 VAL B 261 1 O MET B 260 N SER B 238 SHEET 7 AA5 9 VAL B 293 CYS B 295 1 O ILE B 294 N VAL B 261 SHEET 8 AA5 9 CYS B 327 LEU B 330 1 O MET B 329 N CYS B 295 SHEET 9 AA5 9 ARG B 23 THR B 27 1 N ILE B 25 O LEU B 330 SHEET 1 AA610 VAL B 438 TYR B 442 0 SHEET 2 AA610 ILE B 419 THR B 423 1 N CYS B 421 O VAL B 441 SHEET 3 AA610 ILE B 397 VAL B 399 1 N ILE B 397 O ILE B 420 SHEET 4 AA610 VAL B 476 HIS B 481 1 O VAL B 478 N LEU B 398 SHEET 5 AA610 GLN B 492 ARG B 497 -1 O ARG B 494 N ILE B 479 SHEET 6 AA610 GLN D 492 ARG D 497 -1 O THR D 493 N THR B 493 SHEET 7 AA610 VAL D 476 HIS D 481 -1 N MET D 477 O VAL D 496 SHEET 8 AA610 ALA D 396 LEU D 400 1 N LEU D 398 O VAL D 478 SHEET 9 AA610 ILE D 419 THR D 423 1 O ILE D 420 N ILE D 397 SHEET 10 AA610 VAL D 438 TYR D 442 1 O GLU D 439 N CYS D 421 SHEET 1 AA7 9 ARG C 23 THR C 27 0 SHEET 2 AA7 9 VAL C 48 ASN C 52 1 O ARG C 50 N CYS C 26 SHEET 3 AA7 9 GLY C 80 ASP C 84 1 O GLY C 80 N ALA C 49 SHEET 4 AA7 9 MET C 208 ALA C 211 1 O MET C 208 N LEU C 83 SHEET 5 AA7 9 LEU C 235 ILE C 240 1 O ILE C 237 N ILE C 209 SHEET 6 AA7 9 GLY C 258 VAL C 261 1 O MET C 260 N SER C 238 SHEET 7 AA7 9 VAL C 293 CYS C 295 1 O ILE C 294 N VAL C 261 SHEET 8 AA7 9 CYS C 327 LEU C 330 1 O MET C 329 N CYS C 295 SHEET 9 AA7 9 ARG C 23 THR C 27 1 N ILE C 25 O LEU C 330 SHEET 1 AA8 2 ILE C 90 ARG C 91 0 SHEET 2 AA8 2 GLY C 177 ILE C 178 -1 O ILE C 178 N ILE C 90 SHEET 1 AA9 2 ALA C 100 TYR C 102 0 SHEET 2 AA9 2 HIS C 170 LEU C 172 -1 O LEU C 172 N ALA C 100 SHEET 1 AB1 5 LYS C 124 TYR C 126 0 SHEET 2 AB1 5 THR C 107 THR C 111 1 N THR C 111 O PHE C 125 SHEET 3 AB1 5 THR C 161 VAL C 166 -1 O CYS C 164 N VAL C 108 SHEET 4 AB1 5 LEU C 149 VAL C 153 -1 N ARG C 152 O HIS C 165 SHEET 5 AB1 5 LEU C 141 VAL C 144 -1 N ILE C 142 O LEU C 151 SHEET 1 AB2 9 ARG D 23 THR D 27 0 SHEET 2 AB2 9 VAL D 48 ASN D 52 1 O ARG D 50 N CYS D 26 SHEET 3 AB2 9 GLY D 80 ASP D 84 1 O GLY D 80 N ALA D 49 SHEET 4 AB2 9 MET D 208 ALA D 211 1 O MET D 208 N LEU D 83 SHEET 5 AB2 9 LEU D 235 ILE D 240 1 O ILE D 237 N ILE D 209 SHEET 6 AB2 9 GLY D 258 VAL D 261 1 O MET D 260 N SER D 238 SHEET 7 AB2 9 VAL D 293 CYS D 295 1 O ILE D 294 N VAL D 261 SHEET 8 AB2 9 CYS D 327 LEU D 330 1 O CYS D 327 N CYS D 295 SHEET 9 AB2 9 ARG D 23 THR D 27 1 N ILE D 25 O LEU D 330 SHEET 1 AB3 2 ALA D 100 TYR D 102 0 SHEET 2 AB3 2 HIS D 170 LEU D 172 -1 O LEU D 172 N ALA D 100 SHEET 1 AB4 5 LYS D 124 TYR D 126 0 SHEET 2 AB4 5 THR D 107 THR D 111 1 N THR D 111 O PHE D 125 SHEET 3 AB4 5 THR D 161 VAL D 166 -1 O CYS D 164 N VAL D 108 SHEET 4 AB4 5 THR D 150 ASP D 158 -1 N ARG D 152 O HIS D 165 SHEET 5 AB4 5 LEU D 141 TYR D 143 -1 N ILE D 142 O LEU D 151 SHEET 1 AB5 9 ARG E 23 THR E 27 0 SHEET 2 AB5 9 MET E 46 ASN E 52 1 O ARG E 50 N CYS E 26 SHEET 3 AB5 9 GLY E 80 ASP E 84 1 O ALA E 82 N ALA E 49 SHEET 4 AB5 9 MET E 208 ALA E 211 1 O PHE E 210 N LEU E 83 SHEET 5 AB5 9 LEU E 235 ILE E 240 1 O LEU E 235 N ILE E 209 SHEET 6 AB5 9 GLY E 258 VAL E 261 1 O MET E 260 N SER E 238 SHEET 7 AB5 9 VAL E 293 CYS E 295 1 O ILE E 294 N ILE E 259 SHEET 8 AB5 9 CYS E 327 LEU E 330 1 O CYS E 327 N CYS E 295 SHEET 9 AB5 9 ARG E 23 THR E 27 1 N ILE E 25 O LEU E 330 SHEET 1 AB6 5 VAL E 438 TYR E 442 0 SHEET 2 AB6 5 ILE E 419 THR E 423 1 N CYS E 421 O VAL E 441 SHEET 3 AB6 5 ILE E 397 VAL E 399 1 N VAL E 399 O ALA E 422 SHEET 4 AB6 5 VAL E 476 VAL E 480 1 O VAL E 478 N LEU E 398 SHEET 5 AB6 5 THR E 493 ARG E 497 -1 O ARG E 494 N ILE E 479 SHEET 1 AB7 9 ARG F 23 THR F 27 0 SHEET 2 AB7 9 MET F 46 ASN F 52 1 O SER F 47 N ILE F 24 SHEET 3 AB7 9 GLY F 80 ASP F 84 1 O ALA F 82 N ALA F 49 SHEET 4 AB7 9 MET F 208 ALA F 211 1 O PHE F 210 N LEU F 83 SHEET 5 AB7 9 LEU F 235 ILE F 240 1 O LYS F 239 N ALA F 211 SHEET 6 AB7 9 GLY F 258 VAL F 261 1 O MET F 260 N ILE F 240 SHEET 7 AB7 9 VAL F 293 CYS F 295 1 O ILE F 294 N ILE F 259 SHEET 8 AB7 9 CYS F 327 LEU F 330 1 O CYS F 327 N CYS F 295 SHEET 9 AB7 9 ARG F 23 THR F 27 1 N ILE F 25 O LEU F 330 SHEET 1 AB8 5 VAL F 438 TYR F 442 0 SHEET 2 AB8 5 ILE F 419 THR F 423 1 N CYS F 421 O VAL F 441 SHEET 3 AB8 5 ILE F 397 VAL F 399 1 N VAL F 399 O ALA F 422 SHEET 4 AB8 5 VAL F 476 VAL F 480 1 O VAL F 480 N LEU F 398 SHEET 5 AB8 5 ARG F 494 ARG F 497 -1 O ARG F 494 N ILE F 479 SHEET 1 AB9 4 VAL G 2 SER G 7 0 SHEET 2 AB9 4 LEU G 18 GLY G 26 -1 O SER G 21 N SER G 7 SHEET 3 AB9 4 THR G 84 MET G 89 -1 O MET G 89 N LEU G 18 SHEET 4 AB9 4 PHE G 74 ASP G 79 -1 N SER G 77 O TYR G 86 SHEET 1 AC1 6 GLY G 10 GLN G 13 0 SHEET 2 AC1 6 THR G 124 SER G 129 1 O THR G 127 N GLY G 10 SHEET 3 AC1 6 ALA G 98 GLY G 104 -1 N ALA G 98 O VAL G 126 SHEET 4 AC1 6 ILE G 40 GLN G 45 -1 N GLY G 41 O ALA G 103 SHEET 5 AC1 6 ARG G 51 ILE G 57 -1 O GLU G 52 N ARG G 44 SHEET 6 AC1 6 THR G 64 TYR G 66 -1 O ASP G 65 N GLY G 56 SHEET 1 AC2 4 GLY G 10 GLN G 13 0 SHEET 2 AC2 4 THR G 124 SER G 129 1 O THR G 127 N GLY G 10 SHEET 3 AC2 4 ALA G 98 GLY G 104 -1 N ALA G 98 O VAL G 126 SHEET 4 AC2 4 TYR G 119 TRP G 120 -1 O TYR G 119 N GLY G 104 SHEET 1 AC3 4 GLN H 3 SER H 7 0 SHEET 2 AC3 4 GLY H 16 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AC3 4 THR H 84 LEU H 92 -1 O MET H 89 N LEU H 18 SHEET 4 AC3 4 PHE H 74 ASP H 79 -1 N THR H 75 O GLN H 88 SHEET 1 AC4 6 GLY H 10 GLN H 13 0 SHEET 2 AC4 6 THR H 124 SER H 129 1 O THR H 127 N GLY H 10 SHEET 3 AC4 6 ALA H 98 GLY H 104 -1 N TYR H 100 O THR H 124 SHEET 4 AC4 6 ILE H 40 GLN H 45 -1 N PHE H 43 O TYR H 101 SHEET 5 AC4 6 GLU H 52 ILE H 57 -1 O GLY H 55 N TRP H 42 SHEET 6 AC4 6 THR H 64 TYR H 66 -1 O ASP H 65 N GLY H 56 SHEET 1 AC5 4 GLY H 10 GLN H 13 0 SHEET 2 AC5 4 THR H 124 SER H 129 1 O THR H 127 N GLY H 10 SHEET 3 AC5 4 ALA H 98 GLY H 104 -1 N TYR H 100 O THR H 124 SHEET 4 AC5 4 TYR H 119 TRP H 120 -1 O TYR H 119 N GLY H 104 SHEET 1 AC6 2 SER H 27 ASN H 28 0 SHEET 2 AC6 2 ARG H 33 THR H 34 -1 O ARG H 33 N ASN H 28 SHEET 1 AC7 4 LEU I 4 SER I 7 0 SHEET 2 AC7 4 LYS I 19 ALA I 24 -1 O ALA I 23 N GLN I 5 SHEET 3 AC7 4 THR I 84 MET I 89 -1 O VAL I 85 N CYS I 22 SHEET 4 AC7 4 PHE I 74 ASP I 79 -1 N ASP I 79 O THR I 84 SHEET 1 AC8 6 GLY I 10 GLN I 13 0 SHEET 2 AC8 6 THR I 124 SER I 129 1 O THR I 127 N GLY I 10 SHEET 3 AC8 6 ALA I 98 GLY I 104 -1 N TYR I 100 O THR I 124 SHEET 4 AC8 6 ILE I 40 GLN I 45 -1 N GLN I 45 O VAL I 99 SHEET 5 AC8 6 GLU I 52 ILE I 57 -1 O VAL I 54 N TRP I 42 SHEET 6 AC8 6 THR I 64 TYR I 66 -1 O ASP I 65 N GLY I 56 SHEET 1 AC9 4 GLY I 10 GLN I 13 0 SHEET 2 AC9 4 THR I 124 SER I 129 1 O THR I 127 N GLY I 10 SHEET 3 AC9 4 ALA I 98 GLY I 104 -1 N TYR I 100 O THR I 124 SHEET 4 AC9 4 TYR I 119 TRP I 120 -1 O TYR I 119 N GLY I 104 SHEET 1 AD1 4 GLN J 3 SER J 7 0 SHEET 2 AD1 4 LEU J 18 SER J 25 -1 O SER J 25 N GLN J 3 SHEET 3 AD1 4 THR J 84 MET J 89 -1 O MET J 89 N LEU J 18 SHEET 4 AD1 4 PHE J 74 ASP J 79 -1 N THR J 75 O GLN J 88 SHEET 1 AD2 6 GLY J 10 GLN J 13 0 SHEET 2 AD2 6 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AD2 6 ALA J 98 ARG J 105 -1 N ALA J 98 O VAL J 126 SHEET 4 AD2 6 ALA J 39 GLN J 45 -1 N PHE J 43 O TYR J 101 SHEET 5 AD2 6 ARG J 51 ILE J 57 -1 O GLY J 55 N TRP J 42 SHEET 6 AD2 6 THR J 64 TYR J 66 -1 O ASP J 65 N GLY J 56 SHEET 1 AD3 4 GLY J 10 GLN J 13 0 SHEET 2 AD3 4 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AD3 4 ALA J 98 ARG J 105 -1 N ALA J 98 O VAL J 126 SHEET 4 AD3 4 TYR J 119 TRP J 120 -1 O TYR J 119 N GLY J 104 SHEET 1 AD4 4 GLN K 3 SER K 7 0 SHEET 2 AD4 4 LYS K 19 SER K 25 -1 O SER K 21 N SER K 7 SHEET 3 AD4 4 THR K 84 MET K 89 -1 O LEU K 87 N LEU K 20 SHEET 4 AD4 4 PHE K 74 ASP K 79 -1 N ASP K 79 O THR K 84 SHEET 1 AD5 6 LEU K 11 GLN K 13 0 SHEET 2 AD5 6 THR K 124 SER K 129 1 O THR K 127 N VAL K 12 SHEET 3 AD5 6 ALA K 98 ARG K 105 -1 N ALA K 98 O VAL K 126 SHEET 4 AD5 6 ALA K 39 GLN K 45 -1 N GLY K 41 O ALA K 103 SHEET 5 AD5 6 ARG K 51 ILE K 57 -1 O VAL K 54 N TRP K 42 SHEET 6 AD5 6 THR K 64 TYR K 66 -1 O ASP K 65 N GLY K 56 SHEET 1 AD6 4 LEU K 11 GLN K 13 0 SHEET 2 AD6 4 THR K 124 SER K 129 1 O THR K 127 N VAL K 12 SHEET 3 AD6 4 ALA K 98 ARG K 105 -1 N ALA K 98 O VAL K 126 SHEET 4 AD6 4 TYR K 119 TRP K 120 -1 O TYR K 119 N GLY K 104 SHEET 1 AD7 4 GLN L 3 GLN L 5 0 SHEET 2 AD7 4 SER L 17 SER L 25 -1 O SER L 25 N GLN L 3 SHEET 3 AD7 4 THR L 84 ASN L 90 -1 O LEU L 87 N LEU L 20 SHEET 4 AD7 4 PHE L 74 ASP L 79 -1 N THR L 75 O GLN L 88 SHEET 1 AD8 6 GLY L 10 GLN L 13 0 SHEET 2 AD8 6 THR L 124 SER L 129 1 O THR L 127 N VAL L 12 SHEET 3 AD8 6 ALA L 98 GLY L 104 -1 N ALA L 98 O VAL L 126 SHEET 4 AD8 6 ILE L 40 GLN L 45 -1 N PHE L 43 O TYR L 101 SHEET 5 AD8 6 GLU L 52 ILE L 57 -1 O GLY L 55 N TRP L 42 SHEET 6 AD8 6 THR L 64 TYR L 66 -1 O ASP L 65 N GLY L 56 SHEET 1 AD9 4 GLY L 10 GLN L 13 0 SHEET 2 AD9 4 THR L 124 SER L 129 1 O THR L 127 N VAL L 12 SHEET 3 AD9 4 ALA L 98 GLY L 104 -1 N ALA L 98 O VAL L 126 SHEET 4 AD9 4 TYR L 119 TRP L 120 -1 O TYR L 119 N GLY L 104 SSBOND 1 CYS G 22 CYS G 102 1555 1555 2.04 SSBOND 2 CYS H 22 CYS H 102 1555 1555 2.05 SSBOND 3 CYS I 22 CYS I 102 1555 1555 2.05 SSBOND 4 CYS J 22 CYS J 102 1555 1555 2.03 SSBOND 5 CYS K 22 CYS K 102 1555 1555 2.05 SSBOND 6 CYS L 22 CYS L 102 1555 1555 2.05 CISPEP 1 ILE A 373 PRO A 374 0 14.00 CISPEP 2 ILE D 373 PRO D 374 0 8.69 CRYST1 167.520 170.810 177.620 90.00 90.00 90.00 P 21 21 2 24 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 0.005969 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005854 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005630 0.00000