HEADER IMMUNE SYSTEM 23-APR-20 6YSQ TITLE THE HC4NB8 COMPLEMENT INHIBITORY NANOBODY IN COMPLEX WITH C4B COMPND MOL_ID: 1; COMPND 2 MOLECULE: COMPLEMENT C4-B,COMPLEMENT C4-B; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: BASIC COMPLEMENT C4,C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN COMPND 5 DOMAIN-CONTAINING PROTEIN 3,BASIC COMPLEMENT C4,C3 AND PZP-LIKE COMPND 6 ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 3; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HC4NB8 NANOBODY; COMPND 9 CHAIN: C, D; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 7 ORGANISM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, INHIBITOR, COMPLEMENT C4B, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.ZARANTONELLO,N.S.LAURSEN,G.R.ANDERSEN REVDAT 1 24-JUN-20 6YSQ 0 JRNL AUTH A.ZARANTONELLO,G.R.ANDERSEN JRNL TITL AN ULTRA-HIGH AFFINITY COMPLEMENT C4B SPECIFIC NANOBODY JRNL TITL 2 INHIBITS IN VIVO ASSEMBLY OF THE CLASSICAL PATHWAY JRNL TITL 3 PROCONVERTASE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.16_3549 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 80453 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1566 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 48.2600 - 7.3300 0.99 7359 146 0.1711 0.2016 REMARK 3 2 7.3300 - 5.8200 1.00 7248 144 0.2326 0.3003 REMARK 3 3 5.8200 - 5.0900 1.00 7215 143 0.2114 0.2713 REMARK 3 4 5.0900 - 4.6200 1.00 7166 142 0.1977 0.2580 REMARK 3 5 4.6200 - 4.2900 1.00 7139 142 0.2168 0.2832 REMARK 3 6 4.2900 - 4.0400 1.00 7159 142 0.2485 0.2724 REMARK 3 7 4.0400 - 3.8400 1.00 7159 142 0.2768 0.3425 REMARK 3 8 3.8400 - 3.6700 1.00 7139 141 0.3058 0.3701 REMARK 3 9 3.6700 - 3.5300 1.00 7097 142 0.3357 0.3859 REMARK 3 10 3.5300 - 3.4100 1.00 7143 142 0.3530 0.4331 REMARK 3 11 3.4100 - 3.3000 1.00 7063 140 0.3747 0.4176 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) : 0.599 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.082 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 147.9 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 195.3 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 : 0.005 26860 REMARK 3 ANGLE : 0.929 36442 REMARK 3 CHIRALITY : 0.058 4100 REMARK 3 PLANARITY : 0.009 4733 REMARK 3 DIHEDRAL : 8.328 16126 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 26 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: RESID 20:139 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -23.4019 40.0868 -77.4891 REMARK 3 T TENSOR REMARK 3 T11: 1.6170 T22: 0.7552 REMARK 3 T33: 1.0288 T12: -0.1779 REMARK 3 T13: 0.0206 T23: 0.0603 REMARK 3 L TENSOR REMARK 3 L11: 5.8095 L22: 6.6194 REMARK 3 L33: 4.9911 L12: 0.2018 REMARK 3 L13: 0.8346 L23: -1.1235 REMARK 3 S TENSOR REMARK 3 S11: 0.0069 S12: 0.0462 S13: 1.0659 REMARK 3 S21: -0.3373 S22: -0.0430 S23: -0.1409 REMARK 3 S31: -0.6347 S32: 0.1423 S33: 0.0301 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: RESID 140:236 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -24.2765 9.2702 -54.0197 REMARK 3 T TENSOR REMARK 3 T11: 1.1212 T22: 0.8207 REMARK 3 T33: 0.7652 T12: -0.0722 REMARK 3 T13: 0.1678 T23: -0.1718 REMARK 3 L TENSOR REMARK 3 L11: 5.8419 L22: 8.9502 REMARK 3 L33: 8.9516 L12: -3.5306 REMARK 3 L13: 3.4196 L23: -5.9706 REMARK 3 S TENSOR REMARK 3 S11: -0.2440 S12: 0.5549 S13: -0.2543 REMARK 3 S21: -0.0541 S22: 0.0435 S23: -0.2704 REMARK 3 S31: 0.0837 S32: -0.0129 S33: 0.1705 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: RESID 237:361 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 10.2463 1.7114 -40.4168 REMARK 3 T TENSOR REMARK 3 T11: 0.9690 T22: 2.0603 REMARK 3 T33: 1.5740 T12: -0.0209 REMARK 3 T13: 0.0406 T23: 0.3091 REMARK 3 L TENSOR REMARK 3 L11: 7.9654 L22: 3.0696 REMARK 3 L33: 1.5690 L12: 1.2862 REMARK 3 L13: -0.8430 L23: -2.1894 REMARK 3 S TENSOR REMARK 3 S11: 0.5006 S12: -0.7137 S13: 0.2830 REMARK 3 S21: -0.3411 S22: -0.7589 S23: -0.3964 REMARK 3 S31: 0.1533 S32: 1.3905 S33: 0.2630 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: RESID 362:468 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 14.0847 33.8671 -59.6760 REMARK 3 T TENSOR REMARK 3 T11: 1.2991 T22: 1.8177 REMARK 3 T33: 2.1122 T12: -0.4949 REMARK 3 T13: 0.0160 T23: 0.4713 REMARK 3 L TENSOR REMARK 3 L11: 4.8547 L22: 6.2971 REMARK 3 L33: 3.9026 L12: 1.2840 REMARK 3 L13: -1.4371 L23: -2.7273 REMARK 3 S TENSOR REMARK 3 S11: -0.3316 S12: 0.1094 S13: 0.4711 REMARK 3 S21: -0.0023 S22: -0.1367 S23: -1.3067 REMARK 3 S31: -1.0093 S32: 1.4194 S33: 0.3431 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: RESID 469:568 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -6.2443 46.1390 -61.6146 REMARK 3 T TENSOR REMARK 3 T11: 1.7866 T22: 1.1441 REMARK 3 T33: 1.8640 T12: -0.6328 REMARK 3 T13: -0.0724 T23: 0.0204 REMARK 3 L TENSOR REMARK 3 L11: 4.7430 L22: 5.3403 REMARK 3 L33: 6.7774 L12: 1.6472 REMARK 3 L13: -1.7008 L23: -4.4879 REMARK 3 S TENSOR REMARK 3 S11: -0.5442 S12: -0.2128 S13: 1.7490 REMARK 3 S21: -0.2157 S22: -0.4913 S23: -0.0679 REMARK 3 S31: -0.7529 S32: 1.1859 S33: 0.9881 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (RESID 569:605 OR RESID 757:831) AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -21.6628 11.3056 -28.2374 REMARK 3 T TENSOR REMARK 3 T11: 1.1991 T22: 1.2915 REMARK 3 T33: 1.0223 T12: -0.3304 REMARK 3 T13: -0.0055 T23: -0.2288 REMARK 3 L TENSOR REMARK 3 L11: 1.7873 L22: 8.6376 REMARK 3 L33: 7.0347 L12: -2.9053 REMARK 3 L13: 2.7933 L23: -5.1995 REMARK 3 S TENSOR REMARK 3 S11: -0.3295 S12: -0.5174 S13: 0.2605 REMARK 3 S21: 0.2400 S22: 0.1702 S23: -0.4700 REMARK 3 S31: -0.4783 S32: -0.6667 S33: 0.2088 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: RESID 606:679 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -9.1801 27.0121 -63.8433 REMARK 3 T TENSOR REMARK 3 T11: 1.2755 T22: 1.5688 REMARK 3 T33: 1.5466 T12: -0.0731 REMARK 3 T13: 0.2311 T23: 0.2605 REMARK 3 L TENSOR REMARK 3 L11: -0.1488 L22: 5.2575 REMARK 3 L33: 8.0813 L12: 2.7326 REMARK 3 L13: -2.5210 L23: -7.1883 REMARK 3 S TENSOR REMARK 3 S11: 0.0584 S12: -0.3024 S13: 0.0402 REMARK 3 S21: -1.1040 S22: -0.5938 S23: -0.6592 REMARK 3 S31: 0.7975 S32: 0.9957 S33: 0.8426 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: RESID 832:934 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -15.4607 -13.0852 -22.5478 REMARK 3 T TENSOR REMARK 3 T11: 0.8495 T22: 1.1741 REMARK 3 T33: 0.9566 T12: -0.1457 REMARK 3 T13: 0.0087 T23: 0.1179 REMARK 3 L TENSOR REMARK 3 L11: 5.9894 L22: 8.6803 REMARK 3 L33: 4.5842 L12: -0.5054 REMARK 3 L13: -0.9305 L23: -1.6765 REMARK 3 S TENSOR REMARK 3 S11: -0.1899 S12: 0.0084 S13: 0.0212 REMARK 3 S21: -0.4116 S22: -0.4412 S23: -0.3028 REMARK 3 S31: 0.1256 S32: 1.6550 S33: 0.6506 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (RESID 935:982 OR RESID 1321:1392) AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -27.4317 -13.3200 -65.8812 REMARK 3 T TENSOR REMARK 3 T11: 2.0184 T22: 0.9902 REMARK 3 T33: 1.3271 T12: -0.2436 REMARK 3 T13: 0.0726 T23: -0.2303 REMARK 3 L TENSOR REMARK 3 L11: 2.6915 L22: 7.8379 REMARK 3 L33: 8.4149 L12: -2.2241 REMARK 3 L13: 1.1858 L23: -6.5484 REMARK 3 S TENSOR REMARK 3 S11: 0.2456 S12: 0.1881 S13: -0.5356 REMARK 3 S21: -1.6520 S22: -0.1372 S23: 0.8177 REMARK 3 S31: 1.9012 S32: 0.0086 S33: -0.2474 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: RESID 983:1320 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -26.4498 21.5796-107.5767 REMARK 3 T TENSOR REMARK 3 T11: 2.8772 T22: 1.0901 REMARK 3 T33: 1.2801 T12: -0.0527 REMARK 3 T13: 0.2496 T23: -0.0665 REMARK 3 L TENSOR REMARK 3 L11: 1.2738 L22: 3.4179 REMARK 3 L33: 3.1628 L12: 0.7243 REMARK 3 L13: -0.9433 L23: -1.1429 REMARK 3 S TENSOR REMARK 3 S11: -0.1996 S12: 0.4034 S13: -0.2904 REMARK 3 S21: -1.0424 S22: 0.0497 S23: 0.4153 REMARK 3 S31: 1.1297 S32: 0.0401 S33: 0.1188 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN C REMARK 3 ORIGIN FOR THE GROUP (A): -41.5378 7.9804 -17.0831 REMARK 3 T TENSOR REMARK 3 T11: 1.0139 T22: 1.6633 REMARK 3 T33: 0.8897 T12: -0.2389 REMARK 3 T13: 0.1533 T23: -0.0748 REMARK 3 L TENSOR REMARK 3 L11: 10.0237 L22: 4.9081 REMARK 3 L33: 10.3304 L12: -2.5758 REMARK 3 L13: 0.3076 L23: 1.2798 REMARK 3 S TENSOR REMARK 3 S11: -0.0341 S12: -1.8869 S13: -0.0029 REMARK 3 S21: 1.1848 S22: 0.0051 S23: 0.5518 REMARK 3 S31: -0.3158 S32: -0.8351 S33: 0.0128 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: RESID 20:139 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -83.1167 40.1765 -77.8070 REMARK 3 T TENSOR REMARK 3 T11: 1.9103 T22: 0.9824 REMARK 3 T33: 1.0379 T12: 0.1710 REMARK 3 T13: -0.3303 T23: -0.0591 REMARK 3 L TENSOR REMARK 3 L11: 6.2010 L22: 8.3977 REMARK 3 L33: 3.6159 L12: 3.2219 REMARK 3 L13: 0.8224 L23: -1.3055 REMARK 3 S TENSOR REMARK 3 S11: -0.3475 S12: -0.3331 S13: 0.9834 REMARK 3 S21: -0.8964 S22: 0.0317 S23: 0.4674 REMARK 3 S31: 0.0855 S32: -0.1897 S33: 0.3278 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: RESID 140:236 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -86.7235 9.3201 -54.7974 REMARK 3 T TENSOR REMARK 3 T11: 1.2409 T22: 1.0626 REMARK 3 T33: 0.9020 T12: -0.0654 REMARK 3 T13: 0.0879 T23: -0.1934 REMARK 3 L TENSOR REMARK 3 L11: 5.1544 L22: 7.2722 REMARK 3 L33: 9.2466 L12: -1.4485 REMARK 3 L13: 0.2645 L23: -4.6923 REMARK 3 S TENSOR REMARK 3 S11: -0.0106 S12: 0.3453 S13: -0.1492 REMARK 3 S21: 0.0655 S22: 0.1135 S23: 0.5629 REMARK 3 S31: 0.1677 S32: -0.6887 S33: -0.1329 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: RESID 237:361 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -54.1109 1.4640 -37.9429 REMARK 3 T TENSOR REMARK 3 T11: 0.7192 T22: 1.0450 REMARK 3 T33: 0.7491 T12: -0.1223 REMARK 3 T13: -0.1327 T23: -0.0801 REMARK 3 L TENSOR REMARK 3 L11: 8.1863 L22: 7.0590 REMARK 3 L33: 4.3394 L12: 2.6472 REMARK 3 L13: -3.4017 L23: -0.8633 REMARK 3 S TENSOR REMARK 3 S11: 0.3045 S12: -0.7613 S13: 0.4454 REMARK 3 S21: -0.3560 S22: -0.1416 S23: -0.1431 REMARK 3 S31: -0.1349 S32: 0.4512 S33: -0.1828 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: RESID 362:468 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -48.1887 34.1836 -55.4196 REMARK 3 T TENSOR REMARK 3 T11: 1.3474 T22: 0.7562 REMARK 3 T33: 1.3185 T12: 0.0797 REMARK 3 T13: 0.2125 T23: -0.0508 REMARK 3 L TENSOR REMARK 3 L11: 3.3496 L22: 8.1015 REMARK 3 L33: 7.2054 L12: 2.2245 REMARK 3 L13: -0.7966 L23: -5.2194 REMARK 3 S TENSOR REMARK 3 S11: -0.1243 S12: -0.4622 S13: 0.0869 REMARK 3 S21: 0.4647 S22: 0.2072 S23: 0.0055 REMARK 3 S31: -1.0778 S32: 0.0121 S33: -0.1709 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: RESID 469:568 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -67.8400 46.2829 -60.2591 REMARK 3 T TENSOR REMARK 3 T11: 1.4811 T22: 0.7281 REMARK 3 T33: 1.3847 T12: 0.0263 REMARK 3 T13: -0.1192 T23: -0.2794 REMARK 3 L TENSOR REMARK 3 L11: 9.8230 L22: 5.7222 REMARK 3 L33: 9.3139 L12: 1.4567 REMARK 3 L13: -3.7142 L23: -3.0690 REMARK 3 S TENSOR REMARK 3 S11: -0.2131 S12: -0.2471 S13: 1.3472 REMARK 3 S21: -0.6531 S22: -0.0722 S23: 0.7170 REMARK 3 S31: -0.3501 S32: 0.2127 S33: 0.2754 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (RESID 569:605 OR RESID 757:831) AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -86.8557 10.9077 -28.8903 REMARK 3 T TENSOR REMARK 3 T11: 0.9989 T22: 1.2402 REMARK 3 T33: 1.0151 T12: -0.0840 REMARK 3 T13: 0.1174 T23: -0.3092 REMARK 3 L TENSOR REMARK 3 L11: 1.1414 L22: 5.4817 REMARK 3 L33: 7.2059 L12: -1.7235 REMARK 3 L13: 2.3665 L23: -5.6731 REMARK 3 S TENSOR REMARK 3 S11: -0.4965 S12: -0.4022 S13: 0.0120 REMARK 3 S21: 0.6679 S22: 0.3411 S23: -0.1309 REMARK 3 S31: -0.6164 S32: -1.0098 S33: 0.1527 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: RESID 606:679 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -70.5076 27.1202 -62.7276 REMARK 3 T TENSOR REMARK 3 T11: 1.4033 T22: 1.2838 REMARK 3 T33: 1.3434 T12: 0.1593 REMARK 3 T13: -0.0485 T23: 0.1763 REMARK 3 L TENSOR REMARK 3 L11: 0.3904 L22: 4.6574 REMARK 3 L33: 5.1002 L12: 3.0274 REMARK 3 L13: -2.5500 L23: -4.7687 REMARK 3 S TENSOR REMARK 3 S11: -0.0804 S12: -0.3464 S13: 0.1628 REMARK 3 S21: -1.4472 S22: -0.4950 S23: -0.3770 REMARK 3 S31: 0.6945 S32: 0.1520 S33: 0.7564 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: RESID 832:934 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -81.4701 -13.7150 -23.1174 REMARK 3 T TENSOR REMARK 3 T11: 0.8270 T22: 1.2131 REMARK 3 T33: 0.9512 T12: -0.2129 REMARK 3 T13: 0.1593 T23: 0.0897 REMARK 3 L TENSOR REMARK 3 L11: 6.2343 L22: 9.2313 REMARK 3 L33: 10.0301 L12: 3.1552 REMARK 3 L13: 4.7552 L23: 2.4854 REMARK 3 S TENSOR REMARK 3 S11: -0.2398 S12: -0.4415 S13: -0.4918 REMARK 3 S21: -0.0710 S22: 0.2783 S23: -0.0240 REMARK 3 S31: -0.5891 S32: 1.0545 S33: -0.0516 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (RESID 935:982 OR RESID 1321:1392) AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -88.8789 -13.0722 -67.0766 REMARK 3 T TENSOR REMARK 3 T11: 2.5280 T22: 1.2506 REMARK 3 T33: 1.3894 T12: -0.5157 REMARK 3 T13: 0.0018 T23: -0.2583 REMARK 3 L TENSOR REMARK 3 L11: 4.1696 L22: 7.0553 REMARK 3 L33: 3.5688 L12: -3.2751 REMARK 3 L13: 2.8222 L23: -4.1638 REMARK 3 S TENSOR REMARK 3 S11: 0.1773 S12: 0.1748 S13: -0.5909 REMARK 3 S21: -2.3240 S22: -0.0418 S23: 0.7442 REMARK 3 S31: 1.4122 S32: -0.0378 S33: -0.1552 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: RESID 983:1320 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -82.8300 21.3741-107.8620 REMARK 3 T TENSOR REMARK 3 T11: 3.5792 T22: 1.2040 REMARK 3 T33: 1.3429 T12: -0.2424 REMARK 3 T13: 0.0943 T23: 0.0326 REMARK 3 L TENSOR REMARK 3 L11: 2.3639 L22: 4.5224 REMARK 3 L33: 3.3599 L12: -1.1643 REMARK 3 L13: -1.1728 L23: 0.3217 REMARK 3 S TENSOR REMARK 3 S11: -0.4181 S12: 0.6467 S13: -0.2768 REMARK 3 S21: -2.0969 S22: 0.4059 S23: -0.1916 REMARK 3 S31: 0.9242 S32: 0.1752 S33: 0.0348 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A):-107.7679 7.6339 -19.9879 REMARK 3 T TENSOR REMARK 3 T11: 0.7497 T22: 1.6973 REMARK 3 T33: 1.3384 T12: -0.1651 REMARK 3 T13: 0.1884 T23: -0.1057 REMARK 3 L TENSOR REMARK 3 L11: 6.5186 L22: 4.8924 REMARK 3 L33: 6.9588 L12: -2.6213 REMARK 3 L13: -1.3398 L23: 0.4986 REMARK 3 S TENSOR REMARK 3 S11: -0.4788 S12: -0.7839 S13: -0.5194 REMARK 3 S21: 0.6596 S22: 0.2654 S23: 1.3223 REMARK 3 S31: 0.1099 S32: -0.5925 S33: 0.1924 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: RESID 1574:1744 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -33.1576 -43.4263 -22.2135 REMARK 3 T TENSOR REMARK 3 T11: 2.1664 T22: 1.2708 REMARK 3 T33: 1.8808 T12: -0.0364 REMARK 3 T13: 0.6042 T23: -0.2962 REMARK 3 L TENSOR REMARK 3 L11: 8.4680 L22: 9.4407 REMARK 3 L33: 2.1218 L12: 6.3759 REMARK 3 L13: -1.3690 L23: -3.8990 REMARK 3 S TENSOR REMARK 3 S11: -0.8838 S12: -0.5882 S13: -0.4413 REMARK 3 S21: 0.4178 S22: 0.3737 S23: 0.5079 REMARK 3 S31: 0.8527 S32: -0.5824 S33: 0.5509 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: RESID 1574:1744 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -99.2326 -43.7023 -24.3294 REMARK 3 T TENSOR REMARK 3 T11: 1.4582 T22: 1.0318 REMARK 3 T33: 2.0123 T12: 0.1662 REMARK 3 T13: 0.3324 T23: 0.0545 REMARK 3 L TENSOR REMARK 3 L11: 8.2250 L22: 5.7201 REMARK 3 L33: 4.4203 L12: 6.8811 REMARK 3 L13: 0.0817 L23: -0.1923 REMARK 3 S TENSOR REMARK 3 S11: -0.5320 S12: -0.2844 S13: -0.7809 REMARK 3 S21: -0.0416 S22: 0.3459 S23: -0.9340 REMARK 3 S31: -0.3319 S32: -0.5427 S33: 0.1541 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: RESID 1393:1573 AND CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 4.5418 -21.5870 -26.9950 REMARK 3 T TENSOR REMARK 3 T11: 1.1615 T22: 2.7808 REMARK 3 T33: 1.5339 T12: 0.6400 REMARK 3 T13: 0.0547 T23: 0.7712 REMARK 3 L TENSOR REMARK 3 L11: 4.3455 L22: 8.4372 REMARK 3 L33: 3.1500 L12: 4.4419 REMARK 3 L13: -3.1887 L23: -0.3322 REMARK 3 S TENSOR REMARK 3 S11: -0.1571 S12: 0.0830 S13: -0.1209 REMARK 3 S21: -0.2226 S22: -0.7186 S23: -0.6690 REMARK 3 S31: 1.2076 S32: 1.7587 S33: 0.7179 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: RESID 1393:1573 AND CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -61.2400 -22.3300 -26.1632 REMARK 3 T TENSOR REMARK 3 T11: 0.8751 T22: 2.1802 REMARK 3 T33: 1.6004 T12: 0.1574 REMARK 3 T13: -0.0403 T23: 0.2449 REMARK 3 L TENSOR REMARK 3 L11: 5.3004 L22: 9.1295 REMARK 3 L33: 7.8815 L12: 5.3719 REMARK 3 L13: -6.0653 L23: -3.9558 REMARK 3 S TENSOR REMARK 3 S11: -0.3363 S12: -0.0279 S13: -0.5170 REMARK 3 S21: -0.4563 S22: 0.0860 S23: -0.0220 REMARK 3 S31: 0.7100 S32: 0.0776 S33: 0.2821 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'A' REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 20 THROUGH 1230 OR REMARK 3 RESID 1256 THROUGH 2006)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'C' REMARK 3 SELECTION : CHAIN 'D' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6YSQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-20. REMARK 100 THE DEPOSITION ID IS D_1292108092. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUL-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P13 (MX1) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80517 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 48.260 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.650 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: 5JTW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: THE RESERVOIR CONTAINING 100 MM HEPES REMARK 280 -NAOH PH=7, 10% W/W PEG4000, 10% V/V 2-PROPANOL WAS MIXED 1:1 REMARK 280 WITH THE CONCENTRATED PROTEIN SAMPLE., PH 7, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 292.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.75500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ARG A 2 REMARK 465 LEU A 3 REMARK 465 LEU A 4 REMARK 465 TRP A 5 REMARK 465 GLY A 6 REMARK 465 LEU A 7 REMARK 465 ILE A 8 REMARK 465 TRP A 9 REMARK 465 ALA A 10 REMARK 465 SER A 11 REMARK 465 SER A 12 REMARK 465 PHE A 13 REMARK 465 PHE A 14 REMARK 465 THR A 15 REMARK 465 LEU A 16 REMARK 465 SER A 17 REMARK 465 LEU A 18 REMARK 465 GLN A 19 REMARK 465 LYS A 748 REMARK 465 GLU A 749 REMARK 465 LYS A 750 REMARK 465 THR A 751 REMARK 465 THR A 752 REMARK 465 ARG A 753 REMARK 465 LYS A 754 REMARK 465 LYS A 755 REMARK 465 ARG A 756 REMARK 465 GLY A 1231 REMARK 465 SER A 1232 REMARK 465 VAL A 1233 REMARK 465 THR A 1234 REMARK 465 GLY A 1235 REMARK 465 SER A 1236 REMARK 465 GLN A 1237 REMARK 465 SER A 1238 REMARK 465 ASN A 1239 REMARK 465 ALA A 1240 REMARK 465 VAL A 1241 REMARK 465 SER A 1242 REMARK 465 PRO A 1243 REMARK 465 THR A 1244 REMARK 465 PRO A 1245 REMARK 465 ALA A 1246 REMARK 465 PRO A 1247 REMARK 465 ARG A 1248 REMARK 465 ASN A 1249 REMARK 465 PRO A 1250 REMARK 465 SER A 1251 REMARK 465 ASP A 1252 REMARK 465 PRO A 1253 REMARK 465 MET A 1254 REMARK 465 PRO A 1255 REMARK 465 GLU A 1415 REMARK 465 ASP A 1416 REMARK 465 TYR A 1417 REMARK 465 GLU A 1418 REMARK 465 ASP A 1419 REMARK 465 TYR A 1420 REMARK 465 GLU A 1421 REMARK 465 TYR A 1422 REMARK 465 ASP A 1423 REMARK 465 GLU A 1424 REMARK 465 LEU A 1425 REMARK 465 PRO A 1426 REMARK 465 ALA A 1427 REMARK 465 LYS A 1428 REMARK 465 ASP A 1429 REMARK 465 ASP A 1430 REMARK 465 PRO A 1431 REMARK 465 ASP A 1432 REMARK 465 ALA A 1433 REMARK 465 PRO A 1434 REMARK 465 LEU A 1435 REMARK 465 GLN A 1436 REMARK 465 PRO A 1437 REMARK 465 VAL A 1438 REMARK 465 THR A 1439 REMARK 465 PRO A 1440 REMARK 465 LEU A 1441 REMARK 465 GLN A 1442 REMARK 465 LEU A 1443 REMARK 465 PHE A 1444 REMARK 465 GLU A 1445 REMARK 465 GLY A 1446 REMARK 465 ARG A 1447 REMARK 465 ARG A 1448 REMARK 465 ASN A 1449 REMARK 465 ARG A 1450 REMARK 465 ARG A 1451 REMARK 465 ARG A 1452 REMARK 465 ARG A 1453 REMARK 465 GLU A 1454 REMARK 465 ALA A 1455 REMARK 465 PRO A 1456 REMARK 465 LYS A 1457 REMARK 465 VAL A 1458 REMARK 465 VAL A 1459 REMARK 465 GLU A 1460 REMARK 465 GLU A 1461 REMARK 465 GLY A 1605 REMARK 465 LEU A 1606 REMARK 465 GLN A 1607 REMARK 465 ASP A 1608 REMARK 465 GLU A 1609 REMARK 465 ASP A 1610 REMARK 465 MET B 1 REMARK 465 ARG B 2 REMARK 465 LEU B 3 REMARK 465 LEU B 4 REMARK 465 TRP B 5 REMARK 465 GLY B 6 REMARK 465 LEU B 7 REMARK 465 ILE B 8 REMARK 465 TRP B 9 REMARK 465 ALA B 10 REMARK 465 SER B 11 REMARK 465 SER B 12 REMARK 465 PHE B 13 REMARK 465 PHE B 14 REMARK 465 THR B 15 REMARK 465 LEU B 16 REMARK 465 SER B 17 REMARK 465 LEU B 18 REMARK 465 GLN B 19 REMARK 465 LYS B 748 REMARK 465 GLU B 749 REMARK 465 LYS B 750 REMARK 465 THR B 751 REMARK 465 THR B 752 REMARK 465 ARG B 753 REMARK 465 LYS B 754 REMARK 465 LYS B 755 REMARK 465 ARG B 756 REMARK 465 GLY B 1231 REMARK 465 SER B 1232 REMARK 465 VAL B 1233 REMARK 465 THR B 1234 REMARK 465 GLY B 1235 REMARK 465 SER B 1236 REMARK 465 GLN B 1237 REMARK 465 SER B 1238 REMARK 465 ASN B 1239 REMARK 465 ALA B 1240 REMARK 465 VAL B 1241 REMARK 465 SER B 1242 REMARK 465 PRO B 1243 REMARK 465 THR B 1244 REMARK 465 PRO B 1245 REMARK 465 ALA B 1246 REMARK 465 PRO B 1247 REMARK 465 ARG B 1248 REMARK 465 ASN B 1249 REMARK 465 PRO B 1250 REMARK 465 SER B 1251 REMARK 465 ASP B 1252 REMARK 465 PRO B 1253 REMARK 465 GLU B 1415 REMARK 465 ASP B 1416 REMARK 465 TYR B 1417 REMARK 465 GLU B 1418 REMARK 465 ASP B 1419 REMARK 465 TYR B 1420 REMARK 465 GLU B 1421 REMARK 465 TYR B 1422 REMARK 465 ASP B 1423 REMARK 465 GLU B 1424 REMARK 465 LEU B 1425 REMARK 465 PRO B 1426 REMARK 465 ALA B 1427 REMARK 465 LYS B 1428 REMARK 465 ASP B 1429 REMARK 465 ASP B 1430 REMARK 465 PRO B 1431 REMARK 465 ASP B 1432 REMARK 465 ALA B 1433 REMARK 465 PRO B 1434 REMARK 465 LEU B 1435 REMARK 465 GLN B 1436 REMARK 465 PRO B 1437 REMARK 465 VAL B 1438 REMARK 465 THR B 1439 REMARK 465 PRO B 1440 REMARK 465 LEU B 1441 REMARK 465 GLN B 1442 REMARK 465 LEU B 1443 REMARK 465 PHE B 1444 REMARK 465 GLU B 1445 REMARK 465 GLY B 1446 REMARK 465 ARG B 1447 REMARK 465 ARG B 1448 REMARK 465 ASN B 1449 REMARK 465 ARG B 1450 REMARK 465 ARG B 1451 REMARK 465 ARG B 1452 REMARK 465 ARG B 1453 REMARK 465 GLU B 1454 REMARK 465 ALA B 1455 REMARK 465 PRO B 1456 REMARK 465 LYS B 1457 REMARK 465 VAL B 1458 REMARK 465 VAL B 1459 REMARK 465 GLU B 1460 REMARK 465 GLU B 1461 REMARK 465 GLY B 1605 REMARK 465 LEU B 1606 REMARK 465 GLN B 1607 REMARK 465 ASP B 1608 REMARK 465 GLU B 1609 REMARK 465 ASP B 1610 REMARK 465 LEU C 125 REMARK 465 GLU C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 HIS C 131 REMARK 465 HIS C 132 REMARK 465 LEU D 125 REMARK 465 GLU D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 64 -122.31 49.57 REMARK 500 ARG A 104 -80.13 53.00 REMARK 500 SER A 120 -53.91 -149.71 REMARK 500 ASP A 164 -155.85 -107.87 REMARK 500 ASN A 180 -156.97 -89.36 REMARK 500 LEU A 333 44.82 -100.98 REMARK 500 LEU A 336 174.88 65.26 REMARK 500 SER A 359 43.24 -142.26 REMARK 500 ASP A 426 -88.72 -78.48 REMARK 500 HIS A 454 80.22 54.78 REMARK 500 LEU A 526 84.56 52.69 REMARK 500 ALA A 538 -175.41 65.85 REMARK 500 ALA A 564 -79.58 -95.66 REMARK 500 LYS A 579 -134.35 53.02 REMARK 500 PRO A 618 -151.10 -81.69 REMARK 500 LYS A 665 76.56 -113.51 REMARK 500 ARG A 666 -148.44 60.76 REMARK 500 LEU A 667 52.45 -97.81 REMARK 500 CYS A 669 85.50 54.69 REMARK 500 GLU A 759 37.32 -145.58 REMARK 500 GLU A 769 -45.52 66.18 REMARK 500 ARG A 791 -59.32 59.08 REMARK 500 THR A 804 -151.89 -130.85 REMARK 500 GLU A 832 -45.97 72.21 REMARK 500 ASP A 860 44.12 -102.66 REMARK 500 ALA A 907 -102.07 -94.68 REMARK 500 ASP A 952 -137.95 58.23 REMARK 500 ALA A 982 71.22 -112.25 REMARK 500 PRO A 985 -153.98 -75.83 REMARK 500 LEU A 989 84.13 -67.69 REMARK 500 SER A 991 77.71 -154.64 REMARK 500 PRO A 997 47.03 -88.18 REMARK 500 ARG A1008 -82.54 -119.26 REMARK 500 ALA A1062 31.08 -89.71 REMARK 500 GLN A1110 43.26 -100.04 REMARK 500 ASP A1136 60.61 -109.57 REMARK 500 PHE A1156 86.49 -66.90 REMARK 500 ASP A1158 -153.62 59.26 REMARK 500 LYS A1204 72.63 59.88 REMARK 500 ALA A1221 70.91 -153.15 REMARK 500 LYS A1278 83.34 51.00 REMARK 500 THR A1321 26.04 -151.79 REMARK 500 GLU A1323 26.90 -157.86 REMARK 500 ARG A1325 -153.83 -147.41 REMARK 500 ARG A1349 19.93 57.52 REMARK 500 LEU A1358 69.36 60.34 REMARK 500 SER A1361 -102.11 30.14 REMARK 500 LEU A1362 -155.10 -143.39 REMARK 500 LYS A1365 83.46 62.61 REMARK 500 ASN A1373 39.76 -154.19 REMARK 500 REMARK 500 THIS ENTRY HAS 149 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 LEU A 1346 ASN A 1347 -146.74 REMARK 500 LEU B 1346 ASN B 1347 -146.29 REMARK 500 REMARK 500 REMARK: NULL DBREF 6YSQ A 1 755 UNP P0C0L5 CO4B_HUMAN 1 678 DBREF 6YSQ A 679 1744 UNP P0C0L5 CO4B_HUMAN 755 1744 DBREF 6YSQ B 1 755 UNP P0C0L5 CO4B_HUMAN 1 678 DBREF 6YSQ B 679 1744 UNP P0C0L5 CO4B_HUMAN 755 1744 DBREF 6YSQ C 1 132 PDB 6YSQ 6YSQ 1 132 DBREF 6YSQ D 1 132 PDB 6YSQ 6YSQ 1 132 SEQADV 6YSQ ALA A 907 UNP P0C0L5 THR 907 CONFLICT SEQADV 6YSQ GLU A 1013 UNP P0C0L5 GLN 1013 CONFLICT SEQADV 6YSQ ASP A 1073 UNP P0C0L5 GLY 1073 CONFLICT SEQADV 6YSQ PRO A 1120 UNP P0C0L5 LEU 1120 CONFLICT SEQADV 6YSQ CYS A 1121 UNP P0C0L5 SER 1121 CONFLICT SEQADV 6YSQ LEU A 1124 UNP P0C0L5 ILE 1124 CONFLICT SEQADV 6YSQ ASP A 1125 UNP P0C0L5 HIS 1125 CONFLICT SEQADV 6YSQ ASN A 1176 UNP P0C0L5 SER 1176 CONFLICT SEQADV 6YSQ SER A 1201 UNP P0C0L5 THR 1201 CONFLICT SEQADV 6YSQ VAL A 1207 UNP P0C0L5 ALA 1207 CONFLICT SEQADV 6YSQ LEU A 1210 UNP P0C0L5 ARG 1210 CONFLICT SEQADV 6YSQ SER A 1286 UNP P0C0L5 ALA 1286 CONFLICT SEQADV 6YSQ ASN A 1735 UNP P0C0L5 GLN 1735 CONFLICT SEQADV 6YSQ PHE A 1737 UNP P0C0L5 TYR 1737 CONFLICT SEQADV 6YSQ ALA B 907 UNP P0C0L5 THR 907 CONFLICT SEQADV 6YSQ GLU B 1013 UNP P0C0L5 GLN 1013 CONFLICT SEQADV 6YSQ ASP B 1073 UNP P0C0L5 GLY 1073 CONFLICT SEQADV 6YSQ PRO B 1120 UNP P0C0L5 LEU 1120 CONFLICT SEQADV 6YSQ CYS B 1121 UNP P0C0L5 SER 1121 CONFLICT SEQADV 6YSQ LEU B 1124 UNP P0C0L5 ILE 1124 CONFLICT SEQADV 6YSQ ASP B 1125 UNP P0C0L5 HIS 1125 CONFLICT SEQADV 6YSQ ASN B 1176 UNP P0C0L5 SER 1176 CONFLICT SEQADV 6YSQ SER B 1201 UNP P0C0L5 THR 1201 CONFLICT SEQADV 6YSQ VAL B 1207 UNP P0C0L5 ALA 1207 CONFLICT SEQADV 6YSQ LEU B 1210 UNP P0C0L5 ARG 1210 CONFLICT SEQADV 6YSQ SER B 1286 UNP P0C0L5 ALA 1286 CONFLICT SEQADV 6YSQ ASN B 1735 UNP P0C0L5 GLN 1735 CONFLICT SEQADV 6YSQ PHE B 1737 UNP P0C0L5 TYR 1737 CONFLICT SEQRES 1 A 1667 MET ARG LEU LEU TRP GLY LEU ILE TRP ALA SER SER PHE SEQRES 2 A 1667 PHE THR LEU SER LEU GLN LYS PRO ARG LEU LEU LEU PHE SEQRES 3 A 1667 SER PRO SER VAL VAL HIS LEU GLY VAL PRO LEU SER VAL SEQRES 4 A 1667 GLY VAL GLN LEU GLN ASP VAL PRO ARG GLY GLN VAL VAL SEQRES 5 A 1667 LYS GLY SER VAL PHE LEU ARG ASN PRO SER ARG ASN ASN SEQRES 6 A 1667 VAL PRO CYS SER PRO LYS VAL ASP PHE THR LEU SER SER SEQRES 7 A 1667 GLU ARG ASP PHE ALA LEU LEU SER LEU GLN VAL PRO LEU SEQRES 8 A 1667 LYS ASP ALA LYS SER CYS GLY LEU HIS GLN LEU LEU ARG SEQRES 9 A 1667 GLY PRO GLU VAL GLN LEU VAL ALA HIS SER PRO TRP LEU SEQRES 10 A 1667 LYS ASP SER LEU SER ARG THR THR ASN ILE GLN GLY ILE SEQRES 11 A 1667 ASN LEU LEU PHE SER SER ARG ARG GLY HIS LEU PHE LEU SEQRES 12 A 1667 GLN THR ASP GLN PRO ILE TYR ASN PRO GLY GLN ARG VAL SEQRES 13 A 1667 ARG TYR ARG VAL PHE ALA LEU ASP GLN LYS MET ARG PRO SEQRES 14 A 1667 SER THR ASP THR ILE THR VAL MET VAL GLU ASN SER HIS SEQRES 15 A 1667 GLY LEU ARG VAL ARG LYS LYS GLU VAL TYR MET PRO SER SEQRES 16 A 1667 SER ILE PHE GLN ASP ASP PHE VAL ILE PRO ASP ILE SER SEQRES 17 A 1667 GLU PRO GLY THR TRP LYS ILE SER ALA ARG PHE SER ASP SEQRES 18 A 1667 GLY LEU GLU SER ASN SER SER THR GLN PHE GLU VAL LYS SEQRES 19 A 1667 LYS TYR VAL LEU PRO ASN PHE GLU VAL LYS ILE THR PRO SEQRES 20 A 1667 GLY LYS PRO TYR ILE LEU THR VAL PRO GLY HIS LEU ASP SEQRES 21 A 1667 GLU MET GLN LEU ASP ILE GLN ALA ARG TYR ILE TYR GLY SEQRES 22 A 1667 LYS PRO VAL GLN GLY VAL ALA TYR VAL ARG PHE GLY LEU SEQRES 23 A 1667 LEU ASP GLU ASP GLY LYS LYS THR PHE PHE ARG GLY LEU SEQRES 24 A 1667 GLU SER GLN THR LYS LEU VAL ASN GLY GLN SER HIS ILE SEQRES 25 A 1667 SER LEU SER LYS ALA GLU PHE GLN ASP ALA LEU GLU LYS SEQRES 26 A 1667 LEU ASN MET GLY ILE THR ASP LEU GLN GLY LEU ARG LEU SEQRES 27 A 1667 TYR VAL ALA ALA ALA ILE ILE GLU SER PRO GLY GLY GLU SEQRES 28 A 1667 MET GLU GLU ALA GLU LEU THR SER TRP TYR PHE VAL SER SEQRES 29 A 1667 SER PRO PHE SER LEU ASP LEU SER LYS THR LYS ARG HIS SEQRES 30 A 1667 LEU VAL PRO GLY ALA PRO PHE LEU LEU GLN ALA LEU VAL SEQRES 31 A 1667 ARG GLU MET SER GLY SER PRO ALA SER GLY ILE PRO VAL SEQRES 32 A 1667 LYS VAL SER ALA THR VAL SER SER PRO GLY SER VAL PRO SEQRES 33 A 1667 GLU VAL GLN ASP ILE GLN GLN ASN THR ASP GLY SER GLY SEQRES 34 A 1667 GLN VAL SER ILE PRO ILE ILE ILE PRO GLN THR ILE SER SEQRES 35 A 1667 GLU LEU GLN LEU SER VAL SER ALA GLY SER PRO HIS PRO SEQRES 36 A 1667 ALA ILE ALA ARG LEU THR VAL ALA ALA PRO PRO SER GLY SEQRES 37 A 1667 GLY PRO GLY PHE LEU SER ILE GLU ARG PRO ASP SER ARG SEQRES 38 A 1667 PRO PRO ARG VAL GLY ASP THR LEU ASN LEU ASN LEU ARG SEQRES 39 A 1667 ALA VAL GLY SER GLY ALA THR PHE SER HIS TYR TYR TYR SEQRES 40 A 1667 MET ILE LEU SER ARG GLY GLN ILE VAL PHE MET ASN ARG SEQRES 41 A 1667 GLU PRO LYS ARG THR LEU THR SER VAL SER VAL PHE VAL SEQRES 42 A 1667 ASP HIS HIS LEU ALA PRO SER PHE TYR PHE VAL ALA PHE SEQRES 43 A 1667 TYR TYR HIS GLY ASP HIS PRO VAL ALA ASN SER LEU ARG SEQRES 44 A 1667 VAL ASP VAL GLN ALA GLY ALA CYS GLU GLY LYS LEU GLU SEQRES 45 A 1667 LEU SER VAL ASP GLY ALA LYS GLN TYR ARG ASN GLY GLU SEQRES 46 A 1667 SER VAL LYS LEU HIS LEU GLU THR ASP SER LEU ALA LEU SEQRES 47 A 1667 VAL ALA LEU GLY ALA LEU ASP THR ALA LEU TYR ALA ALA SEQRES 48 A 1667 GLY SER LYS SER HIS LYS PRO LEU ASN MET GLY LYS VAL SEQRES 49 A 1667 PHE GLU ALA MET ASN SER TYR ASP LEU GLY CYS GLY PRO SEQRES 50 A 1667 GLY GLY GLY ASP SER ALA LEU GLN VAL PHE GLN ALA ALA SEQRES 51 A 1667 GLY LEU ALA PHE SER ASP GLY ASP GLN TRP THR LEU SER SEQRES 52 A 1667 ARG LYS ARG LEU SER CYS PRO LYS GLU LYS THR THR ARG SEQRES 53 A 1667 LYS LYS ARG ALA LEU GLU ILE LEU GLN GLU GLU ASP LEU SEQRES 54 A 1667 ILE ASP GLU ASP ASP ILE PRO VAL ARG SER PHE PHE PRO SEQRES 55 A 1667 GLU ASN TRP LEU TRP ARG VAL GLU THR VAL ASP ARG PHE SEQRES 56 A 1667 GLN ILE LEU THR LEU TRP LEU PRO ASP SER LEU THR THR SEQRES 57 A 1667 TRP GLU ILE HIS GLY LEU SER LEU SER LYS THR LYS GLY SEQRES 58 A 1667 LEU CYS VAL ALA THR PRO VAL GLN LEU ARG VAL PHE ARG SEQRES 59 A 1667 GLU PHE HIS LEU HIS LEU ARG LEU PRO MET SER VAL ARG SEQRES 60 A 1667 ARG PHE GLU GLN LEU GLU LEU ARG PRO VAL LEU TYR ASN SEQRES 61 A 1667 TYR LEU ASP LYS ASN LEU THR VAL SER VAL HIS VAL SER SEQRES 62 A 1667 PRO VAL GLU GLY LEU CYS LEU ALA GLY GLY GLY GLY LEU SEQRES 63 A 1667 ALA GLN GLN VAL LEU VAL PRO ALA GLY SER ALA ARG PRO SEQRES 64 A 1667 VAL ALA PHE SER VAL VAL PRO THR ALA ALA ALA ALA VAL SEQRES 65 A 1667 SER LEU LYS VAL VAL ALA ARG GLY SER PHE GLU PHE PRO SEQRES 66 A 1667 VAL GLY ASP ALA VAL SER LYS VAL LEU GLN ILE GLU LYS SEQRES 67 A 1667 GLU GLY ALA ILE HIS ARG GLU GLU LEU VAL TYR GLU LEU SEQRES 68 A 1667 ASN PRO LEU ASP HIS ARG GLY ARG THR LEU GLU ILE PRO SEQRES 69 A 1667 GLY ASN SER ASP PRO ASN MET ILE PRO ASP GLY ASP PHE SEQRES 70 A 1667 ASN SER TYR VAL ARG VAL THR ALA SER ASP PRO LEU ASP SEQRES 71 A 1667 THR LEU GLY SER GLU GLY ALA LEU SER PRO GLY GLY VAL SEQRES 72 A 1667 ALA SER LEU LEU ARG LEU PRO ARG GLY CYS GLY GLU GLU SEQRES 73 A 1667 THR MET ILE TYR LEU ALA PRO THR LEU ALA ALA SER ARG SEQRES 74 A 1667 TYR LEU ASP LYS THR GLU GLN TRP SER THR LEU PRO PRO SEQRES 75 A 1667 GLU THR LYS ASP HIS ALA VAL ASP LEU ILE GLN LYS GLY SEQRES 76 A 1667 TYR MET ARG ILE GLN GLN PHE ARG LYS ALA ASP GLY SER SEQRES 77 A 1667 TYR ALA ALA TRP LEU SER ARG ASP SER SER THR TRP LEU SEQRES 78 A 1667 THR ALA PHE VAL LEU LYS VAL LEU SER LEU ALA GLN GLU SEQRES 79 A 1667 GLN VAL GLY GLY SER PRO GLU LYS LEU GLN GLU THR SER SEQRES 80 A 1667 ASN TRP LEU LEU SER GLN GLN GLN ALA ASP GLY SER PHE SEQRES 81 A 1667 GLN ASP PRO CYS PRO VAL LEU ASP ARG SER MET GLN GLY SEQRES 82 A 1667 GLY LEU VAL GLY ASN ASP GLU THR VAL ALA LEU THR ALA SEQRES 83 A 1667 PHE VAL THR ILE ALA LEU HIS HIS GLY LEU ALA VAL PHE SEQRES 84 A 1667 GLN ASP GLU GLY ALA GLU PRO LEU LYS GLN ARG VAL GLU SEQRES 85 A 1667 ALA SER ILE SER LYS ALA ASN SER PHE LEU GLY GLU LYS SEQRES 86 A 1667 ALA SER ALA GLY LEU LEU GLY ALA HIS ALA ALA ALA ILE SEQRES 87 A 1667 THR ALA TYR ALA LEU SER LEU THR LYS ALA PRO VAL ASP SEQRES 88 A 1667 LEU LEU GLY VAL ALA HIS ASN ASN LEU MET ALA MET ALA SEQRES 89 A 1667 GLN GLU THR GLY ASP ASN LEU TYR TRP GLY SER VAL THR SEQRES 90 A 1667 GLY SER GLN SER ASN ALA VAL SER PRO THR PRO ALA PRO SEQRES 91 A 1667 ARG ASN PRO SER ASP PRO MET PRO GLN ALA PRO ALA LEU SEQRES 92 A 1667 TRP ILE GLU THR THR ALA TYR ALA LEU LEU HIS LEU LEU SEQRES 93 A 1667 LEU HIS GLU GLY LYS ALA GLU MET ALA ASP GLN ALA SER SEQRES 94 A 1667 ALA TRP LEU THR ARG GLN GLY SER PHE GLN GLY GLY PHE SEQRES 95 A 1667 ARG SER THR GLN ASP THR VAL ILE ALA LEU ASP ALA LEU SEQRES 96 A 1667 SER ALA TYR TRP ILE ALA SER HIS THR THR GLU GLU ARG SEQRES 97 A 1667 GLY LEU ASN VAL THR LEU SER SER THR GLY ARG ASN GLY SEQRES 98 A 1667 PHE LYS SER HIS ALA LEU GLN LEU ASN ASN ARG GLN ILE SEQRES 99 A 1667 ARG GLY LEU GLU GLU GLU LEU GLN PHE SER LEU GLY SER SEQRES 100 A 1667 LYS ILE ASN VAL LYS VAL GLY GLY ASN SER LYS GLY THR SEQRES 101 A 1667 LEU LYS VAL LEU ARG THR TYR ASN VAL LEU ASP MET LYS SEQRES 102 A 1667 ASN THR THR CYS GLN ASP LEU GLN ILE GLU VAL THR VAL SEQRES 103 A 1667 LYS GLY HIS VAL GLU TYR THR MET GLU ALA ASN GLU ASP SEQRES 104 A 1667 TYR GLU ASP TYR GLU TYR ASP GLU LEU PRO ALA LYS ASP SEQRES 105 A 1667 ASP PRO ASP ALA PRO LEU GLN PRO VAL THR PRO LEU GLN SEQRES 106 A 1667 LEU PHE GLU GLY ARG ARG ASN ARG ARG ARG ARG GLU ALA SEQRES 107 A 1667 PRO LYS VAL VAL GLU GLU GLN GLU SER ARG VAL HIS TYR SEQRES 108 A 1667 THR VAL CYS ILE TRP ARG ASN GLY LYS VAL GLY LEU SER SEQRES 109 A 1667 GLY MET ALA ILE ALA ASP VAL THR LEU LEU SER GLY PHE SEQRES 110 A 1667 HIS ALA LEU ARG ALA ASP LEU GLU LYS LEU THR SER LEU SEQRES 111 A 1667 SER ASP ARG TYR VAL SER HIS PHE GLU THR GLU GLY PRO SEQRES 112 A 1667 HIS VAL LEU LEU TYR PHE ASP SER VAL PRO THR SER ARG SEQRES 113 A 1667 GLU CYS VAL GLY PHE GLU ALA VAL GLN GLU VAL PRO VAL SEQRES 114 A 1667 GLY LEU VAL GLN PRO ALA SER ALA THR LEU TYR ASP TYR SEQRES 115 A 1667 TYR ASN PRO GLU ARG ARG CYS SER VAL PHE TYR GLY ALA SEQRES 116 A 1667 PRO SER LYS SER ARG LEU LEU ALA THR LEU CYS SER ALA SEQRES 117 A 1667 GLU VAL CYS GLN CYS ALA GLU GLY LYS CYS PRO ARG GLN SEQRES 118 A 1667 ARG ARG ALA LEU GLU ARG GLY LEU GLN ASP GLU ASP GLY SEQRES 119 A 1667 TYR ARG MET LYS PHE ALA CYS TYR TYR PRO ARG VAL GLU SEQRES 120 A 1667 TYR GLY PHE GLN VAL LYS VAL LEU ARG GLU ASP SER ARG SEQRES 121 A 1667 ALA ALA PHE ARG LEU PHE GLU THR LYS ILE THR GLN VAL SEQRES 122 A 1667 LEU HIS PHE THR LYS ASP VAL LYS ALA ALA ALA ASN GLN SEQRES 123 A 1667 MET ARG ASN PHE LEU VAL ARG ALA SER CYS ARG LEU ARG SEQRES 124 A 1667 LEU GLU PRO GLY LYS GLU TYR LEU ILE MET GLY LEU ASP SEQRES 125 A 1667 GLY ALA THR TYR ASP LEU GLU GLY HIS PRO GLN TYR LEU SEQRES 126 A 1667 LEU ASP SER ASN SER TRP ILE GLU GLU MET PRO SER GLU SEQRES 127 A 1667 ARG LEU CYS ARG SER THR ARG GLN ARG ALA ALA CYS ALA SEQRES 128 A 1667 GLN LEU ASN ASP PHE LEU ASN GLU PHE GLY THR GLN GLY SEQRES 129 A 1667 CYS GLN VAL SEQRES 1 B 1667 MET ARG LEU LEU TRP GLY LEU ILE TRP ALA SER SER PHE SEQRES 2 B 1667 PHE THR LEU SER LEU GLN LYS PRO ARG LEU LEU LEU PHE SEQRES 3 B 1667 SER PRO SER VAL VAL HIS LEU GLY VAL PRO LEU SER VAL SEQRES 4 B 1667 GLY VAL GLN LEU GLN ASP VAL PRO ARG GLY GLN VAL VAL SEQRES 5 B 1667 LYS GLY SER VAL PHE LEU ARG ASN PRO SER ARG ASN ASN SEQRES 6 B 1667 VAL PRO CYS SER PRO LYS VAL ASP PHE THR LEU SER SER SEQRES 7 B 1667 GLU ARG ASP PHE ALA LEU LEU SER LEU GLN VAL PRO LEU SEQRES 8 B 1667 LYS ASP ALA LYS SER CYS GLY LEU HIS GLN LEU LEU ARG SEQRES 9 B 1667 GLY PRO GLU VAL GLN LEU VAL ALA HIS SER PRO TRP LEU SEQRES 10 B 1667 LYS ASP SER LEU SER ARG THR THR ASN ILE GLN GLY ILE SEQRES 11 B 1667 ASN LEU LEU PHE SER SER ARG ARG GLY HIS LEU PHE LEU SEQRES 12 B 1667 GLN THR ASP GLN PRO ILE TYR ASN PRO GLY GLN ARG VAL SEQRES 13 B 1667 ARG TYR ARG VAL PHE ALA LEU ASP GLN LYS MET ARG PRO SEQRES 14 B 1667 SER THR ASP THR ILE THR VAL MET VAL GLU ASN SER HIS SEQRES 15 B 1667 GLY LEU ARG VAL ARG LYS LYS GLU VAL TYR MET PRO SER SEQRES 16 B 1667 SER ILE PHE GLN ASP ASP PHE VAL ILE PRO ASP ILE SER SEQRES 17 B 1667 GLU PRO GLY THR TRP LYS ILE SER ALA ARG PHE SER ASP SEQRES 18 B 1667 GLY LEU GLU SER ASN SER SER THR GLN PHE GLU VAL LYS SEQRES 19 B 1667 LYS TYR VAL LEU PRO ASN PHE GLU VAL LYS ILE THR PRO SEQRES 20 B 1667 GLY LYS PRO TYR ILE LEU THR VAL PRO GLY HIS LEU ASP SEQRES 21 B 1667 GLU MET GLN LEU ASP ILE GLN ALA ARG TYR ILE TYR GLY SEQRES 22 B 1667 LYS PRO VAL GLN GLY VAL ALA TYR VAL ARG PHE GLY LEU SEQRES 23 B 1667 LEU ASP GLU ASP GLY LYS LYS THR PHE PHE ARG GLY LEU SEQRES 24 B 1667 GLU SER GLN THR LYS LEU VAL ASN GLY GLN SER HIS ILE SEQRES 25 B 1667 SER LEU SER LYS ALA GLU PHE GLN ASP ALA LEU GLU LYS SEQRES 26 B 1667 LEU ASN MET GLY ILE THR ASP LEU GLN GLY LEU ARG LEU SEQRES 27 B 1667 TYR VAL ALA ALA ALA ILE ILE GLU SER PRO GLY GLY GLU SEQRES 28 B 1667 MET GLU GLU ALA GLU LEU THR SER TRP TYR PHE VAL SER SEQRES 29 B 1667 SER PRO PHE SER LEU ASP LEU SER LYS THR LYS ARG HIS SEQRES 30 B 1667 LEU VAL PRO GLY ALA PRO PHE LEU LEU GLN ALA LEU VAL SEQRES 31 B 1667 ARG GLU MET SER GLY SER PRO ALA SER GLY ILE PRO VAL SEQRES 32 B 1667 LYS VAL SER ALA THR VAL SER SER PRO GLY SER VAL PRO SEQRES 33 B 1667 GLU VAL GLN ASP ILE GLN GLN ASN THR ASP GLY SER GLY SEQRES 34 B 1667 GLN VAL SER ILE PRO ILE ILE ILE PRO GLN THR ILE SER SEQRES 35 B 1667 GLU LEU GLN LEU SER VAL SER ALA GLY SER PRO HIS PRO SEQRES 36 B 1667 ALA ILE ALA ARG LEU THR VAL ALA ALA PRO PRO SER GLY SEQRES 37 B 1667 GLY PRO GLY PHE LEU SER ILE GLU ARG PRO ASP SER ARG SEQRES 38 B 1667 PRO PRO ARG VAL GLY ASP THR LEU ASN LEU ASN LEU ARG SEQRES 39 B 1667 ALA VAL GLY SER GLY ALA THR PHE SER HIS TYR TYR TYR SEQRES 40 B 1667 MET ILE LEU SER ARG GLY GLN ILE VAL PHE MET ASN ARG SEQRES 41 B 1667 GLU PRO LYS ARG THR LEU THR SER VAL SER VAL PHE VAL SEQRES 42 B 1667 ASP HIS HIS LEU ALA PRO SER PHE TYR PHE VAL ALA PHE SEQRES 43 B 1667 TYR TYR HIS GLY ASP HIS PRO VAL ALA ASN SER LEU ARG SEQRES 44 B 1667 VAL ASP VAL GLN ALA GLY ALA CYS GLU GLY LYS LEU GLU SEQRES 45 B 1667 LEU SER VAL ASP GLY ALA LYS GLN TYR ARG ASN GLY GLU SEQRES 46 B 1667 SER VAL LYS LEU HIS LEU GLU THR ASP SER LEU ALA LEU SEQRES 47 B 1667 VAL ALA LEU GLY ALA LEU ASP THR ALA LEU TYR ALA ALA SEQRES 48 B 1667 GLY SER LYS SER HIS LYS PRO LEU ASN MET GLY LYS VAL SEQRES 49 B 1667 PHE GLU ALA MET ASN SER TYR ASP LEU GLY CYS GLY PRO SEQRES 50 B 1667 GLY GLY GLY ASP SER ALA LEU GLN VAL PHE GLN ALA ALA SEQRES 51 B 1667 GLY LEU ALA PHE SER ASP GLY ASP GLN TRP THR LEU SER SEQRES 52 B 1667 ARG LYS ARG LEU SER CYS PRO LYS GLU LYS THR THR ARG SEQRES 53 B 1667 LYS LYS ARG ALA LEU GLU ILE LEU GLN GLU GLU ASP LEU SEQRES 54 B 1667 ILE ASP GLU ASP ASP ILE PRO VAL ARG SER PHE PHE PRO SEQRES 55 B 1667 GLU ASN TRP LEU TRP ARG VAL GLU THR VAL ASP ARG PHE SEQRES 56 B 1667 GLN ILE LEU THR LEU TRP LEU PRO ASP SER LEU THR THR SEQRES 57 B 1667 TRP GLU ILE HIS GLY LEU SER LEU SER LYS THR LYS GLY SEQRES 58 B 1667 LEU CYS VAL ALA THR PRO VAL GLN LEU ARG VAL PHE ARG SEQRES 59 B 1667 GLU PHE HIS LEU HIS LEU ARG LEU PRO MET SER VAL ARG SEQRES 60 B 1667 ARG PHE GLU GLN LEU GLU LEU ARG PRO VAL LEU TYR ASN SEQRES 61 B 1667 TYR LEU ASP LYS ASN LEU THR VAL SER VAL HIS VAL SER SEQRES 62 B 1667 PRO VAL GLU GLY LEU CYS LEU ALA GLY GLY GLY GLY LEU SEQRES 63 B 1667 ALA GLN GLN VAL LEU VAL PRO ALA GLY SER ALA ARG PRO SEQRES 64 B 1667 VAL ALA PHE SER VAL VAL PRO THR ALA ALA ALA ALA VAL SEQRES 65 B 1667 SER LEU LYS VAL VAL ALA ARG GLY SER PHE GLU PHE PRO SEQRES 66 B 1667 VAL GLY ASP ALA VAL SER LYS VAL LEU GLN ILE GLU LYS SEQRES 67 B 1667 GLU GLY ALA ILE HIS ARG GLU GLU LEU VAL TYR GLU LEU SEQRES 68 B 1667 ASN PRO LEU ASP HIS ARG GLY ARG THR LEU GLU ILE PRO SEQRES 69 B 1667 GLY ASN SER ASP PRO ASN MET ILE PRO ASP GLY ASP PHE SEQRES 70 B 1667 ASN SER TYR VAL ARG VAL THR ALA SER ASP PRO LEU ASP SEQRES 71 B 1667 THR LEU GLY SER GLU GLY ALA LEU SER PRO GLY GLY VAL SEQRES 72 B 1667 ALA SER LEU LEU ARG LEU PRO ARG GLY CYS GLY GLU GLU SEQRES 73 B 1667 THR MET ILE TYR LEU ALA PRO THR LEU ALA ALA SER ARG SEQRES 74 B 1667 TYR LEU ASP LYS THR GLU GLN TRP SER THR LEU PRO PRO SEQRES 75 B 1667 GLU THR LYS ASP HIS ALA VAL ASP LEU ILE GLN LYS GLY SEQRES 76 B 1667 TYR MET ARG ILE GLN GLN PHE ARG LYS ALA ASP GLY SER SEQRES 77 B 1667 TYR ALA ALA TRP LEU SER ARG ASP SER SER THR TRP LEU SEQRES 78 B 1667 THR ALA PHE VAL LEU LYS VAL LEU SER LEU ALA GLN GLU SEQRES 79 B 1667 GLN VAL GLY GLY SER PRO GLU LYS LEU GLN GLU THR SER SEQRES 80 B 1667 ASN TRP LEU LEU SER GLN GLN GLN ALA ASP GLY SER PHE SEQRES 81 B 1667 GLN ASP PRO CYS PRO VAL LEU ASP ARG SER MET GLN GLY SEQRES 82 B 1667 GLY LEU VAL GLY ASN ASP GLU THR VAL ALA LEU THR ALA SEQRES 83 B 1667 PHE VAL THR ILE ALA LEU HIS HIS GLY LEU ALA VAL PHE SEQRES 84 B 1667 GLN ASP GLU GLY ALA GLU PRO LEU LYS GLN ARG VAL GLU SEQRES 85 B 1667 ALA SER ILE SER LYS ALA ASN SER PHE LEU GLY GLU LYS SEQRES 86 B 1667 ALA SER ALA GLY LEU LEU GLY ALA HIS ALA ALA ALA ILE SEQRES 87 B 1667 THR ALA TYR ALA LEU SER LEU THR LYS ALA PRO VAL ASP SEQRES 88 B 1667 LEU LEU GLY VAL ALA HIS ASN ASN LEU MET ALA MET ALA SEQRES 89 B 1667 GLN GLU THR GLY ASP ASN LEU TYR TRP GLY SER VAL THR SEQRES 90 B 1667 GLY SER GLN SER ASN ALA VAL SER PRO THR PRO ALA PRO SEQRES 91 B 1667 ARG ASN PRO SER ASP PRO MET PRO GLN ALA PRO ALA LEU SEQRES 92 B 1667 TRP ILE GLU THR THR ALA TYR ALA LEU LEU HIS LEU LEU SEQRES 93 B 1667 LEU HIS GLU GLY LYS ALA GLU MET ALA ASP GLN ALA SER SEQRES 94 B 1667 ALA TRP LEU THR ARG GLN GLY SER PHE GLN GLY GLY PHE SEQRES 95 B 1667 ARG SER THR GLN ASP THR VAL ILE ALA LEU ASP ALA LEU SEQRES 96 B 1667 SER ALA TYR TRP ILE ALA SER HIS THR THR GLU GLU ARG SEQRES 97 B 1667 GLY LEU ASN VAL THR LEU SER SER THR GLY ARG ASN GLY SEQRES 98 B 1667 PHE LYS SER HIS ALA LEU GLN LEU ASN ASN ARG GLN ILE SEQRES 99 B 1667 ARG GLY LEU GLU GLU GLU LEU GLN PHE SER LEU GLY SER SEQRES 100 B 1667 LYS ILE ASN VAL LYS VAL GLY GLY ASN SER LYS GLY THR SEQRES 101 B 1667 LEU LYS VAL LEU ARG THR TYR ASN VAL LEU ASP MET LYS SEQRES 102 B 1667 ASN THR THR CYS GLN ASP LEU GLN ILE GLU VAL THR VAL SEQRES 103 B 1667 LYS GLY HIS VAL GLU TYR THR MET GLU ALA ASN GLU ASP SEQRES 104 B 1667 TYR GLU ASP TYR GLU TYR ASP GLU LEU PRO ALA LYS ASP SEQRES 105 B 1667 ASP PRO ASP ALA PRO LEU GLN PRO VAL THR PRO LEU GLN SEQRES 106 B 1667 LEU PHE GLU GLY ARG ARG ASN ARG ARG ARG ARG GLU ALA SEQRES 107 B 1667 PRO LYS VAL VAL GLU GLU GLN GLU SER ARG VAL HIS TYR SEQRES 108 B 1667 THR VAL CYS ILE TRP ARG ASN GLY LYS VAL GLY LEU SER SEQRES 109 B 1667 GLY MET ALA ILE ALA ASP VAL THR LEU LEU SER GLY PHE SEQRES 110 B 1667 HIS ALA LEU ARG ALA ASP LEU GLU LYS LEU THR SER LEU SEQRES 111 B 1667 SER ASP ARG TYR VAL SER HIS PHE GLU THR GLU GLY PRO SEQRES 112 B 1667 HIS VAL LEU LEU TYR PHE ASP SER VAL PRO THR SER ARG SEQRES 113 B 1667 GLU CYS VAL GLY PHE GLU ALA VAL GLN GLU VAL PRO VAL SEQRES 114 B 1667 GLY LEU VAL GLN PRO ALA SER ALA THR LEU TYR ASP TYR SEQRES 115 B 1667 TYR ASN PRO GLU ARG ARG CYS SER VAL PHE TYR GLY ALA SEQRES 116 B 1667 PRO SER LYS SER ARG LEU LEU ALA THR LEU CYS SER ALA SEQRES 117 B 1667 GLU VAL CYS GLN CYS ALA GLU GLY LYS CYS PRO ARG GLN SEQRES 118 B 1667 ARG ARG ALA LEU GLU ARG GLY LEU GLN ASP GLU ASP GLY SEQRES 119 B 1667 TYR ARG MET LYS PHE ALA CYS TYR TYR PRO ARG VAL GLU SEQRES 120 B 1667 TYR GLY PHE GLN VAL LYS VAL LEU ARG GLU ASP SER ARG SEQRES 121 B 1667 ALA ALA PHE ARG LEU PHE GLU THR LYS ILE THR GLN VAL SEQRES 122 B 1667 LEU HIS PHE THR LYS ASP VAL LYS ALA ALA ALA ASN GLN SEQRES 123 B 1667 MET ARG ASN PHE LEU VAL ARG ALA SER CYS ARG LEU ARG SEQRES 124 B 1667 LEU GLU PRO GLY LYS GLU TYR LEU ILE MET GLY LEU ASP SEQRES 125 B 1667 GLY ALA THR TYR ASP LEU GLU GLY HIS PRO GLN TYR LEU SEQRES 126 B 1667 LEU ASP SER ASN SER TRP ILE GLU GLU MET PRO SER GLU SEQRES 127 B 1667 ARG LEU CYS ARG SER THR ARG GLN ARG ALA ALA CYS ALA SEQRES 128 B 1667 GLN LEU ASN ASP PHE LEU ASN GLU PHE GLY THR GLN GLY SEQRES 129 B 1667 CYS GLN VAL SEQRES 1 C 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 132 THR GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 132 ARG THR PHE SER ARG TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 C 132 ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA ALA ILE ASN SEQRES 5 C 132 TRP SER GLY GLY SER THR TYR TYR ALA ASP PHE ALA LYS SEQRES 6 C 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 C 132 LEU TYR LEU ARG MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 C 132 ALA VAL TYR TYR CYS ALA ALA GLY GLY PRO GLU VAL GLU SEQRES 9 C 132 ILE THR ARG ALA ASN GLU TYR ASP TYR TRP GLY GLN GLY SEQRES 10 C 132 THR GLN VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS SEQRES 11 C 132 HIS HIS SEQRES 1 D 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 132 THR GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 132 ARG THR PHE SER ARG TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 D 132 ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA ALA ILE ASN SEQRES 5 D 132 TRP SER GLY GLY SER THR TYR TYR ALA ASP PHE ALA LYS SEQRES 6 D 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 D 132 LEU TYR LEU ARG MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 D 132 ALA VAL TYR TYR CYS ALA ALA GLY GLY PRO GLU VAL GLU SEQRES 9 D 132 ILE THR ARG ALA ASN GLU TYR ASP TYR TRP GLY GLN GLY SEQRES 10 D 132 THR GLN VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS SEQRES 11 D 132 HIS HIS HET NAG A2001 14 HET NAG A2002 14 HET BMA A2003 11 HET NAG A2004 14 HET NAG A2005 14 HET BMA A2006 11 HET NAG B2001 14 HET NAG B2002 14 HET BMA B2003 11 HET NAG B2004 14 HET NAG B2005 14 HET BMA B2006 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE FORMUL 5 NAG 8(C8 H15 N O6) FORMUL 5 BMA 4(C6 H12 O6) HELIX 1 AA1 PRO A 90 GLY A 98 1 9 HELIX 2 AA2 SER A 315 LEU A 326 1 12 HELIX 3 AA3 GLY A 329 LEU A 333 5 5 HELIX 4 AA4 ASP A 534 ALA A 538 5 5 HELIX 5 AA5 ALA A 607 GLY A 612 1 6 HELIX 6 AA6 MET A 621 ASN A 629 1 9 HELIX 7 AA7 SER A 630 ASP A 632 5 3 HELIX 8 AA8 ALA A 643 GLY A 651 1 9 HELIX 9 AA9 LEU A 877 GLY A 881 5 5 HELIX 10 AB1 VAL A 1000 LEU A 1004 5 5 HELIX 11 AB2 CYS A 1010 THR A 1031 1 22 HELIX 12 AB3 PRO A 1039 MET A 1054 1 16 HELIX 13 AB4 SER A 1075 ALA A 1089 1 15 HELIX 14 AB5 SER A 1096 GLU A 1102 1 7 HELIX 15 AB6 GLU A 1102 GLN A 1110 1 9 HELIX 16 AB7 ASP A 1136 GLY A 1152 1 17 HELIX 17 AB8 ALA A 1161 SER A 1184 1 24 HELIX 18 AB9 GLY A 1189 THR A 1203 1 15 HELIX 19 AC1 PRO A 1206 MET A 1220 1 15 HELIX 20 AC2 LEU A 1260 GLU A 1276 1 17 HELIX 21 AC3 MET A 1281 GLY A 1293 1 13 HELIX 22 AC4 THR A 1302 SER A 1319 1 18 HELIX 23 AC5 LEU A 1497 GLU A 1502 1 6 HELIX 24 AC6 LYS A 1503 THR A 1505 5 3 HELIX 25 AC7 TYR A 1612 TYR A 1619 1 8 HELIX 26 AC8 SER A 1714 ARG A 1719 1 6 HELIX 27 AC9 GLN A 1723 GLN A 1740 1 18 HELIX 28 AD1 PRO B 90 GLY B 98 1 9 HELIX 29 AD2 SER B 315 LEU B 326 1 12 HELIX 30 AD3 GLY B 329 LEU B 333 5 5 HELIX 31 AD4 ASP B 534 ALA B 538 5 5 HELIX 32 AD5 ALA B 607 GLY B 612 1 6 HELIX 33 AD6 MET B 621 ASN B 629 1 9 HELIX 34 AD7 ALA B 643 GLY B 651 1 9 HELIX 35 AD8 LEU B 877 GLY B 881 5 5 HELIX 36 AD9 VAL B 1000 LEU B 1004 5 5 HELIX 37 AE1 CYS B 1010 THR B 1031 1 22 HELIX 38 AE2 PRO B 1039 GLN B 1057 1 19 HELIX 39 AE3 SER B 1075 ALA B 1089 1 15 HELIX 40 AE4 SER B 1096 GLU B 1102 1 7 HELIX 41 AE5 GLU B 1102 LEU B 1108 1 7 HELIX 42 AE6 GLN B 1129 VAL B 1133 5 5 HELIX 43 AE7 ASP B 1136 GLY B 1152 1 17 HELIX 44 AE8 LEU B 1153 VAL B 1155 5 3 HELIX 45 AE9 ALA B 1161 SER B 1184 1 24 HELIX 46 AF1 GLY B 1189 THR B 1203 1 15 HELIX 47 AF2 PRO B 1206 MET B 1220 1 15 HELIX 48 AF3 PRO B 1258 GLU B 1276 1 19 HELIX 49 AF4 MET B 1281 GLY B 1293 1 13 HELIX 50 AF5 THR B 1302 SER B 1319 1 18 HELIX 51 AF6 LEU B 1497 GLU B 1502 1 6 HELIX 52 AF7 LYS B 1503 THR B 1505 5 3 HELIX 53 AF8 TYR B 1612 TYR B 1619 1 8 HELIX 54 AF9 SER B 1714 ARG B 1719 1 6 HELIX 55 AG1 GLN B 1723 GLN B 1740 1 18 HELIX 56 AG2 LYS C 87 THR C 91 5 5 HELIX 57 AG3 LYS D 87 THR D 91 5 5 SHEET 1 A 4 LEU A 652 PHE A 654 0 SHEET 2 A 4 ARG A 22 PRO A 28 -1 SHEET 3 A 4 LEU A 37 GLN A 44 -1 SHEET 4 A 4 PHE A 82 LEU A 87 -1 SHEET 1 B 5 VAL A 30 HIS A 32 0 SHEET 2 B 5 ILE A 127 SER A 135 1 SHEET 3 B 5 GLU A 107 HIS A 113 -1 SHEET 4 B 5 VAL A 52 ARG A 59 -1 SHEET 5 B 5 VAL A 72 LEU A 76 -1 SHEET 1 C 3 HIS A 140 THR A 145 0 SHEET 2 C 3 ARG A 155 LEU A 163 -1 SHEET 3 C 3 ILE A 197 VAL A 203 -1 SHEET 1 D 4 SER A 227 VAL A 233 0 SHEET 2 D 4 GLY A 211 PHE A 219 -1 SHEET 3 D 4 ILE A 174 GLU A 179 -1 SHEET 4 D 4 ARG A 185 VAL A 191 -1 SHEET 1 E 3 PHE A 241 PRO A 247 0 SHEET 2 E 3 GLN A 263 TYR A 270 -1 SHEET 3 E 3 GLN A 309 SER A 313 -1 SHEET 1 F 4 SER A 301 LYS A 304 0 SHEET 2 F 4 GLY A 278 LEU A 287 -1 SHEET 3 F 4 ARG A 337 GLU A 346 -1 SHEET 4 F 4 MET A 352 LEU A 357 -1 SHEET 1 G 2 GLY A 285 LEU A 287 0 SHEET 2 G 2 LYS A 293 PHE A 295 -1 SHEET 1 H 3 PHE A 367 ASP A 370 0 SHEET 2 H 3 PHE A 384 GLU A 392 -1 SHEET 3 H 3 GLN A 430 ILE A 435 -1 SHEET 1 I 4 GLU A 417 ASN A 424 0 SHEET 2 I 4 PRO A 402 VAL A 409 -1 SHEET 3 I 4 GLU A 443 ALA A 450 -1 SHEET 4 I 4 ALA A 456 ALA A 463 -1 SHEET 1 J 3 PHE A 472 ARG A 477 0 SHEET 2 J 3 THR A 488 VAL A 496 -1 SHEET 3 J 3 THR A 527 PHE A 532 -1 SHEET 1 K 4 HIS A 552 ASP A 561 0 SHEET 2 K 4 SER A 540 HIS A 549 -1 SHEET 3 K 4 HIS A 504 SER A 511 -1 SHEET 4 K 4 GLN A 514 PRO A 522 -1 SHEET 1 L 3 LEU A 571 VAL A 575 0 SHEET 2 L 3 SER A 586 THR A 593 -1 SHEET 3 L 3 PHE A 792 TRP A 798 -1 SHEET 1 M 4 VAL A 786 ASP A 790 0 SHEET 2 M 4 LEU A 596 ASP A 605 -1 SHEET 3 M 4 THR A 805 SER A 814 -1 SHEET 4 M 4 VAL A 825 ARG A 828 -1 SHEET 1 N 2 LEU A 811 SER A 814 0 SHEET 2 N 2 GLY A 818 VAL A 821 -1 SHEET 1 O 3 PHE A 833 LEU A 837 0 SHEET 2 O 3 GLN A 848 ASN A 857 -1 SHEET 3 O 3 ALA A 894 VAL A 902 -1 SHEET 1 P 4 ALA A 884 VAL A 889 0 SHEET 2 P 4 LEU A 863 VAL A 869 -1 SHEET 3 P 4 ALA A 908 GLY A 917 -1 SHEET 4 P 4 GLY A 924 GLN A 932 -1 SHEET 1 Q 4 ALA A 938 ASN A 949 0 SHEET 2 Q 4 LYS A1375 VAL A1386 -1 SHEET 3 Q 4 TYR A 977 THR A 981 -1 SHEET 4 Q 4 LEU A1354 GLU A1356 -1 SHEET 1 R 4 THR A 957 ILE A 960 0 SHEET 2 R 4 ILE A1366 VAL A1370 -1 SHEET 3 R 4 ASN A1328 GLY A1335 -1 SHEET 4 R 4 GLY A1338 GLN A1345 -1 SHEET 1 S 4 LEU A1397 LYS A1404 0 SHEET 2 S 4 ARG A1465 ARG A1474 -1 SHEET 3 S 4 GLU A1539 GLN A1542 -1 SHEET 4 S 4 PHE A1494 ALA A1496 -1 SHEET 1 T 2 VAL A1470 ILE A1472 0 SHEET 2 T 2 GLU A1534 VAL A1536 -1 SHEET 1 U 5 ARG A1565 SER A1567 0 SHEET 2 U 5 ALA A1554 ASP A1558 -1 SHEET 3 U 5 ALA A1484 THR A1489 -1 SHEET 4 U 5 HIS A1521 PHE A1526 -1 SHEET 5 U 5 VAL A1512 THR A1517 -1 SHEET 1 V 2 THR A1581 SER A1584 0 SHEET 2 V 2 VAL A1587 CYS A1590 -1 SHEET 1 W 4 TRP A1708 GLU A1711 0 SHEET 2 W 4 GLU A1682 GLY A1687 -1 SHEET 3 W 4 TYR A1625 LYS A1630 -1 SHEET 4 W 4 GLN A1649 HIS A1652 -1 SHEET 1 X 3 MET A1664 ARG A1670 0 SHEET 2 X 3 PHE A1640 ILE A1647 -1 SHEET 3 X 3 VAL A1629 GLU A1634 -1 SHEET 1 Y 4 LEU B 652 SER B 655 0 SHEET 2 Y 4 ARG B 22 PRO B 28 -1 SHEET 3 Y 4 LEU B 37 GLN B 44 -1 SHEET 4 Y 4 PHE B 82 LEU B 87 -1 SHEET 1 Z 5 VAL B 30 HIS B 32 0 SHEET 2 Z 5 ILE B 127 SER B 135 1 SHEET 3 Z 5 GLU B 107 HIS B 113 -1 SHEET 4 Z 5 VAL B 52 ARG B 59 -1 SHEET 5 Z 5 VAL B 72 LEU B 76 -1 SHEET 1 AA 3 HIS B 140 THR B 145 0 SHEET 2 AA 3 ARG B 155 LEU B 163 -1 SHEET 3 AA 3 ILE B 197 VAL B 203 -1 SHEET 1 AB 4 SER B 227 VAL B 233 0 SHEET 2 AB 4 GLY B 211 PHE B 219 -1 SHEET 3 AB 4 ILE B 174 GLU B 179 -1 SHEET 4 AB 4 ARG B 185 VAL B 191 -1 SHEET 1 AC 3 PHE B 241 PRO B 247 0 SHEET 2 AC 3 MET B 262 TYR B 270 -1 SHEET 3 AC 3 GLN B 309 LEU B 314 -1 SHEET 1 AD 2 TYR B 251 LEU B 253 0 SHEET 2 AD 2 TYR B 361 VAL B 363 1 SHEET 1 AE 4 SER B 301 LYS B 304 0 SHEET 2 AE 4 GLY B 278 LEU B 287 -1 SHEET 3 AE 4 ARG B 337 GLU B 346 -1 SHEET 4 AE 4 MET B 352 ALA B 355 -1 SHEET 1 AF 2 GLY B 285 LEU B 287 0 SHEET 2 AF 2 LYS B 293 PHE B 295 -1 SHEET 1 AG 3 PHE B 367 ASP B 370 0 SHEET 2 AG 3 PHE B 384 GLU B 392 -1 SHEET 3 AG 3 GLN B 430 ILE B 435 -1 SHEET 1 AH 4 GLU B 417 ASN B 424 0 SHEET 2 AH 4 PRO B 402 VAL B 409 -1 SHEET 3 AH 4 GLU B 443 ALA B 450 -1 SHEET 4 AH 4 ALA B 456 ALA B 463 -1 SHEET 1 AI 3 PHE B 472 GLU B 476 0 SHEET 2 AI 3 THR B 488 VAL B 496 -1 SHEET 3 AI 3 THR B 527 PHE B 532 -1 SHEET 1 AJ 4 HIS B 552 ASP B 561 0 SHEET 2 AJ 4 SER B 540 HIS B 549 -1 SHEET 3 AJ 4 HIS B 504 SER B 511 -1 SHEET 4 AJ 4 GLN B 514 PRO B 522 -1 SHEET 1 AK 3 LEU B 571 VAL B 575 0 SHEET 2 AK 3 SER B 586 THR B 593 -1 SHEET 3 AK 3 PHE B 792 TRP B 798 -1 SHEET 1 AL 4 VAL B 786 ASP B 790 0 SHEET 2 AL 4 LEU B 596 ASP B 605 -1 SHEET 3 AL 4 THR B 805 SER B 814 -1 SHEET 4 AL 4 VAL B 825 ARG B 828 -1 SHEET 1 AM 2 LEU B 811 SER B 814 0 SHEET 2 AM 2 GLY B 818 VAL B 821 -1 SHEET 1 AN 3 PHE B 833 LEU B 837 0 SHEET 2 AN 3 GLN B 848 ASN B 857 -1 SHEET 3 AN 3 ALA B 894 VAL B 902 -1 SHEET 1 AO 4 GLN B 885 VAL B 889 0 SHEET 2 AO 4 LEU B 863 VAL B 869 -1 SHEET 3 AO 4 ALA B 908 GLY B 917 -1 SHEET 4 AO 4 GLY B 924 GLN B 932 -1 SHEET 1 AP 4 ALA B 938 ASN B 949 0 SHEET 2 AP 4 LYS B1375 VAL B1386 -1 SHEET 3 AP 4 TYR B 977 THR B 981 -1 SHEET 4 AP 4 LEU B1354 GLU B1356 -1 SHEET 1 AQ 4 THR B 957 ILE B 960 0 SHEET 2 AQ 4 ILE B1366 VAL B1370 -1 SHEET 3 AQ 4 ASN B1328 GLY B1335 -1 SHEET 4 AQ 4 GLY B1338 GLN B1345 -1 SHEET 1 AR 4 GLU B1400 LYS B1404 0 SHEET 2 AR 4 ARG B1465 ILE B1472 -1 SHEET 3 AR 4 GLU B1534 GLN B1542 -1 SHEET 4 AR 4 PHE B1494 ALA B1496 -1 SHEET 1 AS 5 ARG B1565 TYR B1570 0 SHEET 2 AS 5 ALA B1552 ASP B1558 -1 SHEET 3 AS 5 ALA B1484 THR B1489 -1 SHEET 4 AS 5 HIS B1521 PHE B1526 -1 SHEET 5 AS 5 VAL B1512 THR B1517 -1 SHEET 1 AT 2 THR B1581 SER B1584 0 SHEET 2 AT 2 VAL B1587 CYS B1590 -1 SHEET 1 AU 4 TRP B1708 GLU B1711 0 SHEET 2 AU 4 GLU B1682 GLY B1687 -1 SHEET 3 AU 4 TYR B1625 LYS B1630 -1 SHEET 4 AU 4 GLN B1649 HIS B1652 -1 SHEET 1 AV 3 MET B1664 ARG B1670 0 SHEET 2 AV 3 PHE B1640 ILE B1647 -1 SHEET 3 AV 3 VAL B1629 GLU B1634 -1 SHEET 1 AW 4 GLN C 3 SER C 7 0 SHEET 2 AW 4 LEU C 18 SER C 25 -1 SHEET 3 AW 4 MET C 78 MET C 83 -1 SHEET 4 AW 4 PHE C 68 ASP C 73 -1 SHEET 1 AX 2 LEU C 11 GLN C 13 0 SHEET 2 AX 2 THR C 121 SER C 123 1 SHEET 1 AY 5 THR C 118 VAL C 120 0 SHEET 2 AY 5 ALA C 92 GLY C 99 -1 SHEET 3 AY 5 ALA C 33 GLN C 39 -1 SHEET 4 AY 5 ARG C 45 ILE C 51 -1 SHEET 5 AY 5 THR C 58 TYR C 60 -1 SHEET 1 AZ 4 GLN D 3 SER D 7 0 SHEET 2 AZ 4 LEU D 18 SER D 25 -1 SHEET 3 AZ 4 MET D 78 MET D 83 -1 SHEET 4 AZ 4 THR D 69 ASP D 73 -1 SHEET 1 BA 5 THR D 118 VAL D 120 0 SHEET 2 BA 5 ALA D 92 GLY D 99 -1 SHEET 3 BA 5 ALA D 33 GLN D 39 -1 SHEET 4 BA 5 ARG D 45 ILE D 51 -1 SHEET 5 BA 5 THR D 58 TYR D 60 -1 SSBOND 1 CYS A 68 CYS A 97 1555 1555 2.04 SSBOND 2 CYS A 567 CYS A 820 1555 1555 2.03 SSBOND 3 CYS A 635 CYS A 669 1555 1555 2.03 SSBOND 4 CYS A 876 CYS A 1590 1555 1555 2.03 SSBOND 5 CYS A 1394 CYS A 1566 1555 1555 2.03 SSBOND 6 CYS A 1471 CYS A 1535 1555 1555 2.03 SSBOND 7 CYS A 1583 CYS A 1588 1555 1555 2.03 SSBOND 8 CYS A 1595 CYS A 1673 1555 1555 2.03 SSBOND 9 CYS A 1618 CYS A 1742 1555 1555 2.03 SSBOND 10 CYS A 1718 CYS A 1727 1555 1555 2.04 SSBOND 11 CYS B 68 CYS B 97 1555 1555 2.04 SSBOND 12 CYS B 567 CYS B 820 1555 1555 2.03 SSBOND 13 CYS B 635 CYS B 669 1555 1555 2.03 SSBOND 14 CYS B 876 CYS B 1590 1555 1555 2.03 SSBOND 15 CYS B 1394 CYS B 1566 1555 1555 2.03 SSBOND 16 CYS B 1471 CYS B 1535 1555 1555 2.03 SSBOND 17 CYS B 1583 CYS B 1588 1555 1555 2.03 SSBOND 18 CYS B 1595 CYS B 1673 1555 1555 2.03 SSBOND 19 CYS B 1618 CYS B 1742 1555 1555 2.03 SSBOND 20 CYS B 1718 CYS B 1727 1555 1555 2.04 SSBOND 21 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 22 CYS D 22 CYS D 96 1555 1555 2.04 LINK ND2 ASN A 226 C1 NAG A2001 1555 1555 1.45 LINK ND2 ASN A 862 C1 NAG A2004 1555 1555 1.44 LINK ND2 ASN B 226 C1 NAG B2001 1555 1555 1.45 LINK ND2 ASN B 862 C1 NAG B2004 1555 1555 1.44 LINK O4 NAG A2001 C1 NAG A2002 1555 1555 1.38 LINK O4 NAG A2002 C1 BMA A2003 1555 1555 1.38 LINK O4 NAG A2004 C1 NAG A2005 1555 1555 1.38 LINK O4 NAG A2005 C1 BMA A2006 1555 1555 1.37 LINK O4 NAG B2001 C1 NAG B2002 1555 1555 1.38 LINK O4 NAG B2002 C1 BMA B2003 1555 1555 1.37 LINK O4 NAG B2004 C1 NAG B2005 1555 1555 1.38 LINK O4 NAG B2005 C1 BMA B2006 1555 1555 1.37 CISPEP 1 SER A 452 PRO A 453 0 -3.35 CISPEP 2 SER B 452 PRO B 453 0 -3.26 CRYST1 131.200 89.510 231.200 90.00 97.55 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.007622 0.000000 0.001010 0.00000 SCALE2 0.000000 0.011172 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004363 0.00000