HEADER VIRAL PROTEIN/IMMUNE SYSTEM 31-DEC-24 9L9Y TITLE IMMUNE COMPLEX OF HEV E2S AND MAB 6H8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN OF MAB 6H8; COMPND 3 CHAIN: L, B; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEAVY CHAIN OF MAB 6H8; COMPND 6 CHAIN: H, A; COMPND 7 OTHER_DETAILS: PCA (PYROGLUTAMIC ACID) CAN INDEED BE REGARDED AS A COMPND 8 CYCLIZED DERIVATIVE OF GLUTAMINE (GLN). FROM A STRUCTURAL COMPND 9 PERSPECTIVE, THE SIDE CHAIN OF GLUTAMINE TERMINATES IN AN AMIDE GROUP COMPND 10 (-CONH2).; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: CAPSID PROTEIN; COMPND 13 CHAIN: C, D; COMPND 14 FRAGMENT: E2S DOMAIN; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: HEPATITIS E VIRUS; SOURCE 9 ORGANISM_COMMON: HEV; SOURCE 10 ORGANISM_TAXID: 1678143; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 561; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PTO-T7 KEYWDS IMMUNE COMPLEX, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.ZIMIN,W.GUIPING,Y.HAI,Z.QING,Z.ZIZHENG,X.NINGSHAO,L.SHAOWEI REVDAT 1 14-JAN-26 9L9Y 0 JRNL AUTH T.ZIMIN,Y.HAI,W.GUIPING,L.CHANG,Y.ZIHAO,L.JUNFEI,W.SILING, JRNL AUTH 2 Y.DONG,F.MUJIN,W.YINGBIN,G.YING,Z.JUN,L.SHAOWEI,Z.QINGBING, JRNL AUTH 3 X.NINGSHAO,Z.ZIZHENG JRNL TITL CRITICAL ROLE OF ASN490 AND MET492 ON CAPSID PROTEIN OF JRNL TITL 2 ZOONOTIC GROUP HEV IN HOST TROPISM FROM SWINE TO HUMAN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.44 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) 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) : 2.44 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.16 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 62182 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 3151 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 28.1630 - 6.9063 0.96 2472 136 0.1752 0.2132 REMARK 3 2 6.9063 - 5.4951 1.00 2556 145 0.2004 0.2103 REMARK 3 3 5.4951 - 4.8044 1.00 2555 152 0.1747 0.1871 REMARK 3 4 4.8044 - 4.3669 1.00 2588 144 0.1628 0.1715 REMARK 3 5 4.3669 - 4.0549 1.00 2559 144 0.1739 0.1977 REMARK 3 6 4.0549 - 3.8164 1.00 2565 135 0.2050 0.2489 REMARK 3 7 3.8164 - 3.6257 1.00 2543 124 0.2255 0.2367 REMARK 3 8 3.6257 - 3.4681 1.00 2615 141 0.2082 0.2082 REMARK 3 9 3.4681 - 3.3349 1.00 2540 132 0.2320 0.2547 REMARK 3 10 3.3349 - 3.2199 1.00 2589 126 0.2491 0.2910 REMARK 3 11 3.2199 - 3.1194 1.00 2593 140 0.2609 0.2947 REMARK 3 12 3.1194 - 3.0303 1.00 2572 133 0.2710 0.2907 REMARK 3 13 3.0303 - 2.9506 1.00 2589 124 0.2766 0.3265 REMARK 3 14 2.9506 - 2.8787 1.00 2574 133 0.2792 0.2993 REMARK 3 15 2.8787 - 2.8133 1.00 2543 135 0.2819 0.3027 REMARK 3 16 2.8133 - 2.7535 1.00 2582 144 0.2649 0.3172 REMARK 3 17 2.7535 - 2.6985 1.00 2529 148 0.2883 0.2769 REMARK 3 18 2.6985 - 2.6476 1.00 2580 148 0.2764 0.3300 REMARK 3 19 2.6476 - 2.6004 1.00 2581 124 0.2751 0.2983 REMARK 3 20 2.6004 - 2.5563 1.00 2540 138 0.2786 0.3006 REMARK 3 21 2.5563 - 2.5151 1.00 2612 136 0.2783 0.3389 REMARK 3 22 2.5151 - 2.4764 1.00 2620 130 0.2987 0.3671 REMARK 3 23 2.4764 - 2.4400 1.00 2534 139 0.3000 0.2884 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) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.070 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 : 0.003 8927 REMARK 3 ANGLE : 0.584 12199 REMARK 3 CHIRALITY : 0.044 1394 REMARK 3 PLANARITY : 0.003 1536 REMARK 3 DIHEDRAL : 10.947 5298 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.7992 -34.7853 0.2847 REMARK 3 T TENSOR REMARK 3 T11: 1.3297 T22: 0.8283 REMARK 3 T33: 0.6341 T12: 0.5104 REMARK 3 T13: 0.1373 T23: 0.1677 REMARK 3 L TENSOR REMARK 3 L11: 6.6008 L22: 0.7953 REMARK 3 L33: 1.3389 L12: -1.5153 REMARK 3 L13: -1.0805 L23: 0.8846 REMARK 3 S TENSOR REMARK 3 S11: -0.9565 S12: -1.1453 S13: -0.2631 REMARK 3 S21: 0.9269 S22: 0.7914 S23: 0.2151 REMARK 3 S31: -0.6006 S32: -0.3686 S33: 0.1246 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 113 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.9295 -36.4692 -9.7270 REMARK 3 T TENSOR REMARK 3 T11: 1.1480 T22: 0.8462 REMARK 3 T33: 1.3707 T12: 0.2972 REMARK 3 T13: 0.5216 T23: 0.3811 REMARK 3 L TENSOR REMARK 3 L11: 3.2629 L22: 1.9005 REMARK 3 L33: 4.4913 L12: -0.4702 REMARK 3 L13: 1.1841 L23: 0.7486 REMARK 3 S TENSOR REMARK 3 S11: -0.4223 S12: -0.4893 S13: -0.9773 REMARK 3 S21: 0.9093 S22: 0.4887 S23: 0.7043 REMARK 3 S31: 0.8737 S32: -0.3977 S33: -0.1005 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.7291 -37.0547 -22.8055 REMARK 3 T TENSOR REMARK 3 T11: 0.5823 T22: 0.3121 REMARK 3 T33: 0.4044 T12: -0.0394 REMARK 3 T13: 0.0509 T23: -0.0171 REMARK 3 L TENSOR REMARK 3 L11: 8.3884 L22: 1.5133 REMARK 3 L33: 3.9171 L12: -2.1823 REMARK 3 L13: 2.2153 L23: -0.6704 REMARK 3 S TENSOR REMARK 3 S11: -0.4630 S12: 0.6935 S13: -0.4596 REMARK 3 S21: 0.3728 S22: 0.2442 S23: 0.1221 REMARK 3 S31: -0.6636 S32: 0.3129 S33: 0.2083 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 98 THROUGH 135 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9718 -29.7075 -17.8051 REMARK 3 T TENSOR REMARK 3 T11: 0.8070 T22: 0.3879 REMARK 3 T33: 0.6184 T12: 0.1242 REMARK 3 T13: 0.2273 T23: 0.0904 REMARK 3 L TENSOR REMARK 3 L11: 3.1655 L22: 1.6524 REMARK 3 L33: 1.8129 L12: -0.7296 REMARK 3 L13: 1.5970 L23: -0.2443 REMARK 3 S TENSOR REMARK 3 S11: -0.2521 S12: -0.3447 S13: -0.3356 REMARK 3 S21: 0.6332 S22: 0.2653 S23: 0.6681 REMARK 3 S31: -0.2913 S32: -0.4251 S33: -0.0576 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 136 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.4833 -22.5950 -17.6427 REMARK 3 T TENSOR REMARK 3 T11: 0.7201 T22: 0.6740 REMARK 3 T33: 0.6662 T12: 0.2857 REMARK 3 T13: 0.1958 T23: 0.2092 REMARK 3 L TENSOR REMARK 3 L11: 4.4780 L22: 1.3202 REMARK 3 L33: 5.5005 L12: -1.5583 REMARK 3 L13: -2.4837 L23: 1.6660 REMARK 3 S TENSOR REMARK 3 S11: -0.5360 S12: -0.4493 S13: -0.4511 REMARK 3 S21: 0.7126 S22: 0.6183 S23: 0.7853 REMARK 3 S31: 0.0092 S32: -0.2802 S33: -0.0405 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.8108 -78.8885 -30.8725 REMARK 3 T TENSOR REMARK 3 T11: 1.3472 T22: 0.8483 REMARK 3 T33: 0.6384 T12: -0.5180 REMARK 3 T13: -0.1415 T23: 0.1759 REMARK 3 L TENSOR REMARK 3 L11: 6.2767 L22: 0.8265 REMARK 3 L33: 1.0399 L12: 1.4855 REMARK 3 L13: 0.8591 L23: 0.8131 REMARK 3 S TENSOR REMARK 3 S11: -0.9926 S12: 1.2482 S13: 0.2700 REMARK 3 S21: -0.9904 S22: 0.8526 S23: 0.2260 REMARK 3 S31: 0.6531 S32: -0.4360 S33: 0.1157 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.1178 -77.2364 -20.7847 REMARK 3 T TENSOR REMARK 3 T11: 1.1699 T22: 0.8908 REMARK 3 T33: 1.4046 T12: -0.3288 REMARK 3 T13: -0.5426 T23: 0.4019 REMARK 3 L TENSOR REMARK 3 L11: 3.7645 L22: 1.5739 REMARK 3 L33: 4.7184 L12: 0.1219 REMARK 3 L13: -1.0918 L23: 0.8584 REMARK 3 S TENSOR REMARK 3 S11: -0.4186 S12: 0.5735 S13: 1.1255 REMARK 3 S21: -0.8066 S22: 0.4476 S23: 0.5729 REMARK 3 S31: -0.7215 S32: -0.5213 S33: -0.1076 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.0749 -77.4963 -8.0921 REMARK 3 T TENSOR REMARK 3 T11: 0.6140 T22: 0.3253 REMARK 3 T33: 0.3988 T12: 0.0353 REMARK 3 T13: -0.0495 T23: -0.0034 REMARK 3 L TENSOR REMARK 3 L11: 7.4979 L22: 1.6057 REMARK 3 L33: 2.9400 L12: 2.0549 REMARK 3 L13: -2.7485 L23: -0.7710 REMARK 3 S TENSOR REMARK 3 S11: -0.4302 S12: -0.5110 S13: 0.3562 REMARK 3 S21: -0.3574 S22: 0.1674 S23: 0.1589 REMARK 3 S31: 0.6198 S32: 0.2910 S33: 0.2010 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.1031 -90.6543 -13.7068 REMARK 3 T TENSOR REMARK 3 T11: 0.7659 T22: 0.6731 REMARK 3 T33: 0.7575 T12: -0.3215 REMARK 3 T13: -0.2279 T23: 0.2575 REMARK 3 L TENSOR REMARK 3 L11: 4.8229 L22: 1.5642 REMARK 3 L33: 5.6978 L12: 1.1359 REMARK 3 L13: 2.0595 L23: 2.3895 REMARK 3 S TENSOR REMARK 3 S11: -0.5261 S12: 0.5279 S13: 0.5666 REMARK 3 S21: -0.8144 S22: 0.4314 S23: 0.8699 REMARK 3 S31: -0.1339 S32: -0.3655 S33: 0.1103 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 459 THROUGH 518 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.4154 -43.7866 -11.5507 REMARK 3 T TENSOR REMARK 3 T11: 0.6235 T22: 1.4116 REMARK 3 T33: 0.8317 T12: -0.3758 REMARK 3 T13: -0.2728 T23: 0.2776 REMARK 3 L TENSOR REMARK 3 L11: 2.4563 L22: 1.2023 REMARK 3 L33: 0.6715 L12: -0.0466 REMARK 3 L13: 0.0124 L23: -0.8807 REMARK 3 S TENSOR REMARK 3 S11: 0.0642 S12: -0.2201 S13: 0.5681 REMARK 3 S21: 0.7006 S22: -0.5047 S23: -1.0192 REMARK 3 S31: -1.1808 S32: 1.6500 S33: 0.1217 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 519 THROUGH 545 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.8302 -39.8174 -20.5685 REMARK 3 T TENSOR REMARK 3 T11: 0.7020 T22: 1.0985 REMARK 3 T33: 0.6037 T12: -0.3733 REMARK 3 T13: -0.2211 T23: 0.3027 REMARK 3 L TENSOR REMARK 3 L11: 3.5952 L22: 4.6007 REMARK 3 L33: 0.7329 L12: 0.8496 REMARK 3 L13: -1.1548 L23: -1.4743 REMARK 3 S TENSOR REMARK 3 S11: -0.1629 S12: 0.2120 S13: 0.5772 REMARK 3 S21: -0.0231 S22: -0.4763 S23: -0.8088 REMARK 3 S31: -0.7962 S32: 1.1302 S33: 0.4395 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 546 THROUGH 604 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.0310 -48.3337 -11.1359 REMARK 3 T TENSOR REMARK 3 T11: 0.5948 T22: 0.8049 REMARK 3 T33: 0.4256 T12: -0.1602 REMARK 3 T13: -0.1616 T23: 0.1386 REMARK 3 L TENSOR REMARK 3 L11: 3.1470 L22: 5.0990 REMARK 3 L33: 1.9443 L12: 0.5194 REMARK 3 L13: -0.8836 L23: -0.7919 REMARK 3 S TENSOR REMARK 3 S11: -0.2794 S12: 0.0315 S13: 0.3797 REMARK 3 S21: 0.5332 S22: -0.2262 S23: -0.4929 REMARK 3 S31: -0.6593 S32: 1.2513 S33: 0.3891 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 459 THROUGH 507 ) REMARK 3 ORIGIN FOR THE GROUP (A): 42.8563 -68.3527 -19.0752 REMARK 3 T TENSOR REMARK 3 T11: 0.5649 T22: 1.3125 REMARK 3 T33: 0.6860 T12: 0.2690 REMARK 3 T13: 0.1982 T23: 0.2664 REMARK 3 L TENSOR REMARK 3 L11: 2.7314 L22: 1.9712 REMARK 3 L33: 0.5384 L12: 0.0224 REMARK 3 L13: 0.0817 L23: -1.0179 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: 0.0036 S13: -0.3322 REMARK 3 S21: -0.5593 S22: -0.5637 S23: -0.9924 REMARK 3 S31: 0.9928 S32: 1.5202 S33: 0.1974 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 508 THROUGH 518 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.0770 -76.2231 -18.7802 REMARK 3 T TENSOR REMARK 3 T11: 0.8720 T22: 1.5172 REMARK 3 T33: 1.1799 T12: 0.5970 REMARK 3 T13: 0.3786 T23: 0.2843 REMARK 3 L TENSOR REMARK 3 L11: 2.2644 L22: 3.3494 REMARK 3 L33: 4.5240 L12: -0.0395 REMARK 3 L13: 0.9325 L23: -0.4945 REMARK 3 S TENSOR REMARK 3 S11: -0.0371 S12: 0.4561 S13: -0.8390 REMARK 3 S21: -0.6587 S22: -0.5250 S23: -1.0234 REMARK 3 S31: 1.0810 S32: 0.8902 S33: 0.5784 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 519 THROUGH 533 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.9790 -76.7155 -8.5763 REMARK 3 T TENSOR REMARK 3 T11: 0.7081 T22: 1.2300 REMARK 3 T33: 0.6896 T12: 0.4115 REMARK 3 T13: 0.1469 T23: 0.2838 REMARK 3 L TENSOR REMARK 3 L11: 6.3211 L22: 4.3426 REMARK 3 L33: 1.1365 L12: -0.1464 REMARK 3 L13: 0.7817 L23: -1.9491 REMARK 3 S TENSOR REMARK 3 S11: -0.1636 S12: -0.8538 S13: -0.5894 REMARK 3 S21: 0.0235 S22: -0.4391 S23: -0.8299 REMARK 3 S31: 0.8302 S32: 1.3331 S33: 0.3576 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 534 THROUGH 554 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.9134 -64.8519 -17.9096 REMARK 3 T TENSOR REMARK 3 T11: 0.4957 T22: 0.9100 REMARK 3 T33: 0.4770 T12: 0.1841 REMARK 3 T13: 0.1903 T23: 0.1644 REMARK 3 L TENSOR REMARK 3 L11: 3.2635 L22: 6.6079 REMARK 3 L33: 2.0253 L12: -0.1613 REMARK 3 L13: 1.0717 L23: -1.1910 REMARK 3 S TENSOR REMARK 3 S11: -0.3466 S12: -0.1138 S13: -0.1751 REMARK 3 S21: -0.5890 S22: -0.1954 S23: -0.7618 REMARK 3 S31: 0.6424 S32: 1.3158 S33: 0.4988 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 555 THROUGH 594 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.8230 -67.5311 -19.3543 REMARK 3 T TENSOR REMARK 3 T11: 0.6444 T22: 0.7497 REMARK 3 T33: 0.4068 T12: 0.2000 REMARK 3 T13: 0.1335 T23: 0.0986 REMARK 3 L TENSOR REMARK 3 L11: 2.8829 L22: 5.8088 REMARK 3 L33: 1.4518 L12: -0.5619 REMARK 3 L13: 0.8822 L23: -0.7727 REMARK 3 S TENSOR REMARK 3 S11: -0.3318 S12: -0.0244 S13: -0.4706 REMARK 3 S21: -0.3787 S22: -0.1479 S23: -0.1202 REMARK 3 S31: 0.9037 S32: 1.2495 S33: 0.3406 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 595 THROUGH 605 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.4795 -64.6172 -11.2688 REMARK 3 T TENSOR REMARK 3 T11: 0.5743 T22: 1.0011 REMARK 3 T33: 0.6992 T12: 0.1359 REMARK 3 T13: 0.1503 T23: 0.3107 REMARK 3 L TENSOR REMARK 3 L11: 5.2196 L22: 6.3164 REMARK 3 L33: 2.8185 L12: 0.0282 REMARK 3 L13: 1.4123 L23: 1.1518 REMARK 3 S TENSOR REMARK 3 S11: -0.2535 S12: -0.5901 S13: -0.2540 REMARK 3 S21: 0.3320 S22: -0.5989 S23: -0.9502 REMARK 3 S31: 0.5782 S32: 1.4955 S33: 0.8711 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 9L9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055284. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62284 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 11.10 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.60 REMARK 200 R MERGE FOR SHELL (I) : 0.48600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL BUFFER (PH 8.5) WITH REMARK 280 25% W/V POLYETHYLENE GLYCOL (PEG) 3350, EVAPORATION, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 98.44000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 56.83436 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 38.64100 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 98.44000 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 56.83436 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 38.64100 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 98.44000 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 56.83436 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.64100 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 113.66872 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 77.28200 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 113.66872 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 77.28200 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 113.66872 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 77.28200 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, B, A, C, 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 GLN L 1 REMARK 465 ASN L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 GLN B 1 REMARK 465 GLU B 212 REMARK 465 CYS B 213 REMARK 465 SER C 605 REMARK 465 ALA C 606 REMARK 465 ALA D 606 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 H 193 O HOH H 301 1.85 REMARK 500 O SER A 193 O HOH A 301 1.92 REMARK 500 O HOH C 715 O HOH D 729 1.94 REMARK 500 O PRO H 168 O HOH H 302 1.96 REMARK 500 O HOH C 727 O HOH C 728 1.97 REMARK 500 O HOH L 313 O HOH L 314 1.99 REMARK 500 O HOH H 321 O HOH H 331 2.03 REMARK 500 O HOH H 322 O HOH H 330 2.06 REMARK 500 O PRO D 575 O HOH D 701 2.11 REMARK 500 O HOH C 725 O HOH C 728 2.15 REMARK 500 OG1 THR H 58 O HOH H 303 2.15 REMARK 500 O HOH B 303 O HOH B 309 2.16 REMARK 500 O HOH A 329 O HOH A 332 2.16 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 THR L 50 -45.90 75.91 REMARK 500 ALA L 129 107.38 -163.46 REMARK 500 LYS L 168 -70.58 -82.23 REMARK 500 THR H 132 -174.14 -172.94 REMARK 500 SER H 173 -108.50 58.20 REMARK 500 THR B 50 -47.81 75.99 REMARK 500 ALA B 129 105.98 -163.44 REMARK 500 THR C 484 -73.67 -112.69 REMARK 500 ASN C 490 65.23 -150.52 REMARK 500 THR C 585 -162.83 -164.99 REMARK 500 THR D 484 -73.68 -114.35 REMARK 500 ASN D 490 63.33 -150.89 REMARK 500 THR D 585 -162.14 -166.28 REMARK 500 REMARK 500 REMARK: NULL DBREF 9L9Y L 1 213 PDB 9L9Y 9L9Y 1 213 DBREF 9L9Y H 1 215 PDB 9L9Y 9L9Y 1 215 DBREF 9L9Y B 1 213 PDB 9L9Y 9L9Y 1 213 DBREF 9L9Y A 1 215 PDB 9L9Y 9L9Y 1 215 DBREF 9L9Y C 459 606 UNP D3VV84 D3VV84_HEV 93 240 DBREF 9L9Y D 459 606 UNP D3VV84 D3VV84_HEV 93 240 SEQRES 1 L 213 GLN ILE PHE LEU THR GLN SER PRO ALA LEU MET SER ALA SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 L 213 SER SER VAL SER TYR MET SER TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 ARG SER SER PRO LYS PRO TRP ILE TYR LEU THR SER ASN SEQRES 5 L 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 213 PRO GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 213 SER ASN PRO PHE THR PHE GLY SER GLY THR LYS LEU GLU SEQRES 9 L 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS SEQRES 1 H 215 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 215 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA LEU GLY SEQRES 3 H 215 TYR THR PHE SER ASP TYR GLU ILE HIS TRP MET LYS GLN SEQRES 4 H 215 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE HIS SEQRES 5 H 215 PRO VAL SER ASP THR THR ALA TYR ASN GLN LYS PHE LYS SEQRES 6 H 215 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 215 ALA TYR MET GLU VAL SER SER LEU THR SER GLU ASP SER SEQRES 8 H 215 ALA VAL TYR TYR CYS THR ARG ASP TYR GLY ALA TYR TRP SEQRES 9 H 215 GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR SEQRES 10 H 215 THR ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY SEQRES 11 H 215 ASP THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL SEQRES 12 H 215 LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SEQRES 13 H 215 SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 215 VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL SEQRES 15 H 215 THR VAL THR SER SER THR TRP PRO SER GLN SER ILE THR SEQRES 16 H 215 CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP SEQRES 17 H 215 LYS LYS ILE GLU PRO ARG GLY SEQRES 1 B 213 GLN ILE PHE LEU THR GLN SER PRO ALA LEU MET SER ALA SEQRES 2 B 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 B 213 SER SER VAL SER TYR MET SER TRP TYR GLN GLN LYS PRO SEQRES 4 B 213 ARG SER SER PRO LYS PRO TRP ILE TYR LEU THR SER ASN SEQRES 5 B 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 B 213 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 B 213 PRO GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 B 213 SER ASN PRO PHE THR PHE GLY SER GLY THR LYS LEU GLU SEQRES 9 B 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 B 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 B 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 B 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 B 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 B 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 B 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 B 213 ASN ARG ASN GLU CYS SEQRES 1 A 215 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 A 215 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA LEU GLY SEQRES 3 A 215 TYR THR PHE SER ASP TYR GLU ILE HIS TRP MET LYS GLN SEQRES 4 A 215 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE HIS SEQRES 5 A 215 PRO VAL SER ASP THR THR ALA TYR ASN GLN LYS PHE LYS SEQRES 6 A 215 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 A 215 ALA TYR MET GLU VAL SER SER LEU THR SER GLU ASP SER SEQRES 8 A 215 ALA VAL TYR TYR CYS THR ARG ASP TYR GLY ALA TYR TRP SEQRES 9 A 215 GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR SEQRES 10 A 215 THR ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY SEQRES 11 A 215 ASP THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL SEQRES 12 A 215 LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SEQRES 13 A 215 SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 A 215 VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL SEQRES 15 A 215 THR VAL THR SER SER THR TRP PRO SER GLN SER ILE THR SEQRES 16 A 215 CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP SEQRES 17 A 215 LYS LYS ILE GLU PRO ARG GLY SEQRES 1 C 148 SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP VAL LEU SEQRES 2 C 148 TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN THR THR SEQRES 3 C 148 TYR GLY SER SER THR ASN PRO MET TYR VAL SER ASP THR SEQRES 4 C 148 VAL THR PHE VAL ASN VAL ALA THR GLY ALA GLN GLY VAL SEQRES 5 C 148 SER ARG SER LEU ASP TRP SER LYS VAL THR LEU ASP GLY SEQRES 6 C 148 ARG PRO LEU THR THR ILE GLN GLN TYR SER LYS THR PHE SEQRES 7 C 148 PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE TRP GLU SEQRES 8 C 148 ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN TYR ASN SEQRES 9 C 148 THR THR ALA SER ASP GLN ILE LEU ILE GLU ASN ALA PRO SEQRES 10 C 148 GLY HIS ARG VAL CYS ILE SER THR TYR THR THR ASN LEU SEQRES 11 C 148 GLY SER GLY PRO VAL SER ILE SER ALA VAL GLY VAL LEU SEQRES 12 C 148 ALA PRO HIS SER ALA SEQRES 1 D 148 SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP VAL LEU SEQRES 2 D 148 TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN THR THR SEQRES 3 D 148 TYR GLY SER SER THR ASN PRO MET TYR VAL SER ASP THR SEQRES 4 D 148 VAL THR PHE VAL ASN VAL ALA THR GLY ALA GLN GLY VAL SEQRES 5 D 148 SER ARG SER LEU ASP TRP SER LYS VAL THR LEU ASP GLY SEQRES 6 D 148 ARG PRO LEU THR THR ILE GLN GLN TYR SER LYS THR PHE SEQRES 7 D 148 PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE TRP GLU SEQRES 8 D 148 ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN TYR ASN SEQRES 9 D 148 THR THR ALA SER ASP GLN ILE LEU ILE GLU ASN ALA PRO SEQRES 10 D 148 GLY HIS ARG VAL CYS ILE SER THR TYR THR THR ASN LEU SEQRES 11 D 148 GLY SER GLY PRO VAL SER ILE SER ALA VAL GLY VAL LEU SEQRES 12 D 148 ALA PRO HIS SER ALA HET PCA H 1 8 HET PCA A 1 8 HETNAM PCA PYROGLUTAMIC ACID FORMUL 2 PCA 2(C5 H7 N O3) FORMUL 7 HOH *158(H2 O) HELIX 1 AA1 GLU L 78 ALA L 82 5 5 HELIX 2 AA2 SER L 120 THR L 125 1 6 HELIX 3 AA3 LYS L 182 HIS L 188 1 7 HELIX 4 AA4 THR H 28 TYR H 32 5 5 HELIX 5 AA5 GLN H 62 LYS H 65 5 4 HELIX 6 AA6 THR H 87 SER H 91 5 5 HELIX 7 AA7 TYR H 100 ALA H 102 5 3 HELIX 8 AA8 SER H 157 SER H 159 5 3 HELIX 9 AA9 PRO H 201 SER H 204 5 4 HELIX 10 AB1 GLU B 78 ALA B 82 5 5 HELIX 11 AB2 SER B 120 THR B 125 1 6 HELIX 12 AB3 LYS B 182 HIS B 188 1 7 HELIX 13 AB4 THR A 28 TYR A 32 5 5 HELIX 14 AB5 GLN A 62 LYS A 65 5 4 HELIX 15 AB6 THR A 87 SER A 91 5 5 HELIX 16 AB7 TYR A 100 ALA A 102 5 3 HELIX 17 AB8 SER A 157 SER A 159 5 3 HELIX 18 AB9 PRO A 201 SER A 204 5 4 HELIX 19 AC1 ASP C 515 LYS C 518 5 4 HELIX 20 AC2 ASP D 515 LYS D 518 5 4 SHEET 1 AA1 4 LEU L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA1 4 SER L 69 ILE L 74 -1 O TYR L 70 N CYS L 23 SHEET 4 AA1 4 PHE L 61 SER L 66 -1 N SER L 64 O SER L 71 SHEET 1 AA2 6 LEU L 10 ALA L 13 0 SHEET 2 AA2 6 THR L 101 ILE L 105 1 O GLU L 104 N MET L 11 SHEET 3 AA2 6 ALA L 83 GLN L 89 -1 N ALA L 83 O LEU L 103 SHEET 4 AA2 6 MET L 32 GLN L 37 -1 N SER L 33 O GLN L 88 SHEET 5 AA2 6 LYS L 44 TYR L 48 -1 O LYS L 44 N GLN L 36 SHEET 6 AA2 6 ASN L 52 LEU L 53 -1 O ASN L 52 N TYR L 48 SHEET 1 AA3 4 THR L 113 PHE L 117 0 SHEET 2 AA3 4 GLY L 128 PHE L 138 -1 O VAL L 132 N PHE L 117 SHEET 3 AA3 4 TYR L 172 THR L 181 -1 O MET L 174 N LEU L 135 SHEET 4 AA3 4 VAL L 158 TRP L 162 -1 N LEU L 159 O THR L 177 SHEET 1 AA4 4 SER L 152 ARG L 154 0 SHEET 2 AA4 4 ASN L 144 ILE L 149 -1 N TRP L 147 O ARG L 154 SHEET 3 AA4 4 SER L 190 HIS L 197 -1 O GLU L 194 N LYS L 146 SHEET 4 AA4 4 SER L 200 ASN L 209 -1 O ILE L 204 N ALA L 195 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 LEU H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA5 4 THR H 78 VAL H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA5 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA6 6 GLU H 10 VAL H 12 0 SHEET 2 AA6 6 THR H 108 VAL H 112 1 O THR H 111 N GLU H 10 SHEET 3 AA6 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 108 SHEET 4 AA6 6 ILE H 34 THR H 40 -1 N HIS H 35 O THR H 97 SHEET 5 AA6 6 GLY H 44 HIS H 52 -1 O ILE H 48 N TRP H 36 SHEET 6 AA6 6 THR H 57 TYR H 60 -1 O ALA H 59 N ALA H 50 SHEET 1 AA7 4 SER H 121 LEU H 125 0 SHEET 2 AA7 4 SER H 136 TYR H 146 -1 O LEU H 142 N TYR H 123 SHEET 3 AA7 4 LEU H 175 THR H 185 -1 O TYR H 176 N TYR H 146 SHEET 4 AA7 4 VAL H 164 THR H 166 -1 N HIS H 165 O SER H 181 SHEET 1 AA8 4 SER H 121 LEU H 125 0 SHEET 2 AA8 4 SER H 136 TYR H 146 -1 O LEU H 142 N TYR H 123 SHEET 3 AA8 4 LEU H 175 THR H 185 -1 O TYR H 176 N TYR H 146 SHEET 4 AA8 4 VAL H 170 GLN H 172 -1 N VAL H 170 O THR H 177 SHEET 1 AA9 3 THR H 152 TRP H 155 0 SHEET 2 AA9 3 THR H 195 HIS H 200 -1 O ALA H 199 N THR H 152 SHEET 3 AA9 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AB1 4 LEU B 4 SER B 7 0 SHEET 2 AB1 4 VAL B 19 ALA B 25 -1 O SER B 24 N THR B 5 SHEET 3 AB1 4 SER B 69 ILE B 74 -1 O LEU B 72 N MET B 21 SHEET 4 AB1 4 PHE B 61 SER B 66 -1 N SER B 64 O SER B 71 SHEET 1 AB2 6 LEU B 10 ALA B 13 0 SHEET 2 AB2 6 THR B 101 ILE B 105 1 O GLU B 104 N MET B 11 SHEET 3 AB2 6 ALA B 83 GLN B 89 -1 N ALA B 83 O LEU B 103 SHEET 4 AB2 6 MET B 32 GLN B 37 -1 N SER B 33 O GLN B 88 SHEET 5 AB2 6 LYS B 44 TYR B 48 -1 O LYS B 44 N GLN B 36 SHEET 6 AB2 6 ASN B 52 LEU B 53 -1 O ASN B 52 N TYR B 48 SHEET 1 AB3 4 THR B 113 PHE B 117 0 SHEET 2 AB3 4 GLY B 128 PHE B 138 -1 O VAL B 132 N PHE B 117 SHEET 3 AB3 4 TYR B 172 THR B 181 -1 O MET B 174 N LEU B 135 SHEET 4 AB3 4 VAL B 158 TRP B 162 -1 N LEU B 159 O THR B 177 SHEET 1 AB4 4 SER B 152 ARG B 154 0 SHEET 2 AB4 4 ASN B 144 ILE B 149 -1 N TRP B 147 O ARG B 154 SHEET 3 AB4 4 SER B 190 HIS B 197 -1 O GLU B 194 N LYS B 146 SHEET 4 AB4 4 SER B 200 ASN B 209 -1 O ILE B 204 N ALA B 195 SHEET 1 AB5 4 GLN A 3 GLN A 6 0 SHEET 2 AB5 4 VAL A 18 LEU A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AB5 4 THR A 78 VAL A 83 -1 O ALA A 79 N CYS A 22 SHEET 4 AB5 4 ALA A 68 ASP A 73 -1 N THR A 71 O TYR A 80 SHEET 1 AB6 6 GLU A 10 VAL A 12 0 SHEET 2 AB6 6 THR A 108 VAL A 112 1 O LEU A 109 N GLU A 10 SHEET 3 AB6 6 ALA A 92 ARG A 98 -1 N ALA A 92 O VAL A 110 SHEET 4 AB6 6 ILE A 34 THR A 40 -1 N HIS A 35 O THR A 97 SHEET 5 AB6 6 GLY A 44 HIS A 52 -1 O ILE A 48 N TRP A 36 SHEET 6 AB6 6 THR A 57 TYR A 60 -1 O ALA A 59 N ALA A 50 SHEET 1 AB7 4 SER A 121 LEU A 125 0 SHEET 2 AB7 4 SER A 136 TYR A 146 -1 O LEU A 142 N TYR A 123 SHEET 3 AB7 4 LEU A 175 THR A 185 -1 O LEU A 178 N VAL A 143 SHEET 4 AB7 4 VAL A 164 THR A 166 -1 N HIS A 165 O SER A 181 SHEET 1 AB8 4 SER A 121 LEU A 125 0 SHEET 2 AB8 4 SER A 136 TYR A 146 -1 O LEU A 142 N TYR A 123 SHEET 3 AB8 4 LEU A 175 THR A 185 -1 O LEU A 178 N VAL A 143 SHEET 4 AB8 4 VAL A 170 GLN A 172 -1 N GLN A 172 O LEU A 175 SHEET 1 AB9 3 THR A 152 TRP A 155 0 SHEET 2 AB9 3 THR A 195 HIS A 200 -1 O ASN A 197 N THR A 154 SHEET 3 AB9 3 THR A 205 LYS A 210 -1 O THR A 205 N HIS A 200 SHEET 1 AC1 3 VAL C 464 LEU C 465 0 SHEET 2 AC1 3 THR C 520 LEU C 521 1 O THR C 520 N LEU C 465 SHEET 3 AC1 3 ARG C 524 PRO C 525 -1 O ARG C 524 N LEU C 521 SHEET 1 AC2 8 GLN C 508 VAL C 510 0 SHEET 2 AC2 8 THR C 497 ASN C 502 -1 N PHE C 500 O GLY C 509 SHEET 3 AC2 8 VAL C 470 ASP C 481 -1 N TRP C 472 O VAL C 501 SHEET 4 AC2 8 MET C 492 SER C 495 -1 O MET C 492 N ASP C 481 SHEET 5 AC2 8 VAL C 579 SER C 582 -1 O ILE C 581 N TYR C 493 SHEET 6 AC2 8 GLN C 568 GLU C 572 -1 N LEU C 570 O CYS C 580 SHEET 7 AC2 8 LYS C 534 GLU C 549 -1 N PHE C 537 O ILE C 571 SHEET 8 AC2 8 THR C 528 GLN C 531 -1 N ILE C 529 O PHE C 536 SHEET 1 AC3 6 GLN C 508 VAL C 510 0 SHEET 2 AC3 6 THR C 497 ASN C 502 -1 N PHE C 500 O GLY C 509 SHEET 3 AC3 6 VAL C 470 ASP C 481 -1 N TRP C 472 O VAL C 501 SHEET 4 AC3 6 VAL C 593 LEU C 601 -1 O ILE C 595 N LEU C 475 SHEET 5 AC3 6 LYS C 534 GLU C 549 -1 N TRP C 548 O SER C 596 SHEET 6 AC3 6 THR C 528 GLN C 531 -1 N ILE C 529 O PHE C 536 SHEET 1 AC4 3 VAL D 464 LEU D 465 0 SHEET 2 AC4 3 THR D 520 LEU D 521 1 O THR D 520 N LEU D 465 SHEET 3 AC4 3 ARG D 524 PRO D 525 -1 O ARG D 524 N LEU D 521 SHEET 1 AC5 8 GLN D 508 VAL D 510 0 SHEET 2 AC5 8 THR D 497 ASN D 502 -1 N PHE D 500 O GLY D 509 SHEET 3 AC5 8 VAL D 470 ASP D 481 -1 N TRP D 472 O VAL D 501 SHEET 4 AC5 8 MET D 492 SER D 495 -1 O VAL D 494 N GLU D 479 SHEET 5 AC5 8 VAL D 579 SER D 582 -1 O ILE D 581 N TYR D 493 SHEET 6 AC5 8 GLN D 568 GLU D 572 -1 N LEU D 570 O CYS D 580 SHEET 7 AC5 8 LYS D 534 GLU D 549 -1 N PHE D 537 O ILE D 571 SHEET 8 AC5 8 THR D 528 GLN D 531 -1 N ILE D 529 O PHE D 536 SHEET 1 AC6 6 GLN D 508 VAL D 510 0 SHEET 2 AC6 6 THR D 497 ASN D 502 -1 N PHE D 500 O GLY D 509 SHEET 3 AC6 6 VAL D 470 ASP D 481 -1 N TRP D 472 O VAL D 501 SHEET 4 AC6 6 VAL D 593 LEU D 601 -1 O ILE D 595 N LEU D 475 SHEET 5 AC6 6 LYS D 534 GLU D 549 -1 N TRP D 548 O SER D 596 SHEET 6 AC6 6 THR D 528 GLN D 531 -1 N ILE D 529 O PHE D 536 SSBOND 1 CYS L 23 CYS L 87 1555 1555 2.04 SSBOND 2 CYS L 133 CYS L 193 1555 1555 2.04 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 141 CYS H 196 1555 1555 2.04 SSBOND 5 CYS B 23 CYS B 87 1555 1555 2.04 SSBOND 6 CYS B 133 CYS B 193 1555 1555 2.04 SSBOND 7 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 8 CYS A 141 CYS A 196 1555 1555 2.04 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA A 1 N VAL A 2 1555 1555 1.33 CISPEP 1 SER L 7 PRO L 8 0 -5.29 CISPEP 2 ASN L 93 PRO L 94 0 -2.42 CISPEP 3 TYR L 139 PRO L 140 0 -0.03 CISPEP 4 ASP H 131 THR H 132 0 -4.95 CISPEP 5 PHE H 147 PRO H 148 0 -2.99 CISPEP 6 GLU H 149 PRO H 150 0 1.44 CISPEP 7 TRP H 189 PRO H 190 0 3.65 CISPEP 8 SER B 7 PRO B 8 0 -5.72 CISPEP 9 SER B 55 GLY B 56 0 -5.28 CISPEP 10 ASN B 93 PRO B 94 0 -2.54 CISPEP 11 TYR B 139 PRO B 140 0 -0.13 CISPEP 12 CYS A 129 GLY A 130 0 -5.78 CISPEP 13 ASP A 131 THR A 132 0 -2.06 CISPEP 14 PHE A 147 PRO A 148 0 -3.05 CISPEP 15 GLU A 149 PRO A 150 0 0.15 CISPEP 16 TRP A 189 PRO A 190 0 4.17 CISPEP 17 GLY C 591 PRO C 592 0 -5.89 CISPEP 18 GLY D 591 PRO D 592 0 -3.28 CRYST1 196.880 196.880 115.923 90.00 90.00 120.00 H 3 18 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 0.005079 0.002932 0.000000 0.00000 SCALE2 0.000000 0.005865 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008626 0.00000