HEADER IMMUNE SYSTEM 13-MAR-19 6O9I TITLE TERNARY COMPLEX OF MOUSE ECD WITH FAB1 AND FAB2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB1 HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB1 LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ECD; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: FAB 2 HEAVY CHAIN; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: FAB2 LIGHT CHAIN; COMPND 19 CHAIN: E; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS GPCR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR X.MIN,Z.WANG REVDAT 1 22-JAN-20 6O9I 0 JRNL AUTH X.MIN,J.YIE,J.WANG,B.C.CHUNG,C.S.HUANG,H.XU,J.YANG,L.DENG, JRNL AUTH 2 J.LIN,Q.CHEN,C.M.ABBOTT,C.GUNDEL,S.A.THIBAULT,T.MENG, JRNL AUTH 3 D.L.BATES,D.J.LLOYD,M.M.VENIANT,Z.WANG JRNL TITL MOLECULAR MECHANISM OF AN ANTAGONISTIC ANTIBODY AGAINST JRNL TITL 2 GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE RECEPTOR. JRNL REF MABS 10047 2020 JRNL REFN ESSN 1942-0870 JRNL PMID 31905038 JRNL DOI 10.1080/19420862.2019.1710047 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV-2328_1692 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 28391 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.490 REMARK 3 FREE R VALUE TEST SET COUNT : 1559 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 19.7607 - 5.7391 1.00 2452 137 0.1718 0.1983 REMARK 3 2 5.7391 - 4.5739 1.00 2455 112 0.1456 0.1800 REMARK 3 3 4.5739 - 4.0012 1.00 2452 138 0.1544 0.2127 REMARK 3 4 4.0012 - 3.6378 1.00 2419 158 0.1718 0.2408 REMARK 3 5 3.6378 - 3.3785 1.00 2427 155 0.2010 0.2537 REMARK 3 6 3.3785 - 3.1801 1.00 2435 157 0.2181 0.2790 REMARK 3 7 3.1801 - 3.0215 1.00 2471 131 0.2411 0.3474 REMARK 3 8 3.0215 - 2.8904 1.00 2424 163 0.2522 0.3382 REMARK 3 9 2.8904 - 2.7794 1.00 2421 136 0.2555 0.3081 REMARK 3 10 2.7794 - 2.6837 1.00 2451 152 0.2704 0.2850 REMARK 3 11 2.6837 - 2.6000 1.00 2425 120 0.2778 0.3349 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.930 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.39 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 7555 REMARK 3 ANGLE : 0.761 10288 REMARK 3 CHIRALITY : 0.045 1139 REMARK 3 PLANARITY : 0.006 1300 REMARK 3 DIHEDRAL : 16.697 4483 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 38 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 54 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.6365 -55.0301 7.8775 REMARK 3 T TENSOR REMARK 3 T11: 0.3899 T22: 0.3178 REMARK 3 T33: 0.3039 T12: -0.0547 REMARK 3 T13: 0.0489 T23: -0.0365 REMARK 3 L TENSOR REMARK 3 L11: 1.5821 L22: 2.6363 REMARK 3 L33: 1.9487 L12: -1.1792 REMARK 3 L13: -0.1680 L23: 0.9418 REMARK 3 S TENSOR REMARK 3 S11: 0.1762 S12: -0.1726 S13: -0.0408 REMARK 3 S21: 0.2858 S22: -0.1536 S23: 0.2244 REMARK 3 S31: 0.0298 S32: -0.0408 S33: -0.0970 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 55 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.0127 -48.1877 8.0841 REMARK 3 T TENSOR REMARK 3 T11: 0.3744 T22: 0.6862 REMARK 3 T33: 0.6381 T12: -0.0290 REMARK 3 T13: 0.1534 T23: -0.1526 REMARK 3 L TENSOR REMARK 3 L11: 0.5576 L22: 3.1779 REMARK 3 L33: 0.8634 L12: 0.6522 REMARK 3 L13: -0.4728 L23: 0.5629 REMARK 3 S TENSOR REMARK 3 S11: 0.0991 S12: 0.3733 S13: -0.4366 REMARK 3 S21: -0.1873 S22: -0.4377 S23: 1.6780 REMARK 3 S31: -0.2177 S32: -0.6623 S33: 0.1458 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 69 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8617 -45.2006 14.4891 REMARK 3 T TENSOR REMARK 3 T11: 0.4313 T22: 0.4227 REMARK 3 T33: 0.3038 T12: -0.1281 REMARK 3 T13: 0.1059 T23: -0.0603 REMARK 3 L TENSOR REMARK 3 L11: 0.5272 L22: 2.0854 REMARK 3 L33: 1.9098 L12: -0.8248 REMARK 3 L13: -0.2200 L23: -0.2013 REMARK 3 S TENSOR REMARK 3 S11: -0.1630 S12: -0.2033 S13: 0.3387 REMARK 3 S21: 0.2001 S22: 0.1313 S23: -0.3315 REMARK 3 S31: -0.0219 S32: 0.3635 S33: -0.0117 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 87 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.6686 -48.5969 19.4969 REMARK 3 T TENSOR REMARK 3 T11: 0.9274 T22: 0.6469 REMARK 3 T33: 0.7344 T12: -0.1365 REMARK 3 T13: 0.2494 T23: -0.2092 REMARK 3 L TENSOR REMARK 3 L11: 2.2603 L22: 0.7098 REMARK 3 L33: 1.1523 L12: 0.9362 REMARK 3 L13: -1.4549 L23: -0.8567 REMARK 3 S TENSOR REMARK 3 S11: 0.1876 S12: 0.0827 S13: 0.0665 REMARK 3 S21: 1.3893 S22: 0.0448 S23: 0.5029 REMARK 3 S31: 0.0449 S32: -0.6943 S33: -0.1726 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.2408 -76.5139 -6.2597 REMARK 3 T TENSOR REMARK 3 T11: 0.2647 T22: 0.2995 REMARK 3 T33: 0.2071 T12: 0.0549 REMARK 3 T13: -0.0536 T23: 0.0539 REMARK 3 L TENSOR REMARK 3 L11: 1.8972 L22: 2.9734 REMARK 3 L33: 1.0682 L12: -0.0940 REMARK 3 L13: -0.3169 L23: 0.5614 REMARK 3 S TENSOR REMARK 3 S11: -0.1615 S12: -0.1505 S13: -0.0374 REMARK 3 S21: -0.3965 S22: 0.1863 S23: -0.4085 REMARK 3 S31: 0.1512 S32: 0.1950 S33: -0.0064 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.6307 -77.6993 -2.4364 REMARK 3 T TENSOR REMARK 3 T11: 0.1906 T22: 0.2083 REMARK 3 T33: 0.1709 T12: -0.0309 REMARK 3 T13: 0.0217 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 2.3370 L22: 3.6866 REMARK 3 L33: 2.1927 L12: -0.2655 REMARK 3 L13: -0.0196 L23: -1.4512 REMARK 3 S TENSOR REMARK 3 S11: 0.2231 S12: -0.2184 S13: -0.1236 REMARK 3 S21: 0.2731 S22: -0.1132 S23: 0.1508 REMARK 3 S31: 0.2033 S32: -0.2850 S33: -0.0520 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1350 -85.4655 -5.1988 REMARK 3 T TENSOR REMARK 3 T11: 0.3182 T22: 0.2753 REMARK 3 T33: 0.2216 T12: 0.0741 REMARK 3 T13: -0.0111 T23: -0.0089 REMARK 3 L TENSOR REMARK 3 L11: 1.2777 L22: 3.2384 REMARK 3 L33: 3.3683 L12: -1.3100 REMARK 3 L13: -1.4748 L23: -0.2277 REMARK 3 S TENSOR REMARK 3 S11: 0.1567 S12: -0.1828 S13: -0.2575 REMARK 3 S21: 0.5617 S22: -0.6084 S23: 0.0259 REMARK 3 S31: 0.6973 S32: -0.6432 S33: 0.3534 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9768 -77.1410 -11.9082 REMARK 3 T TENSOR REMARK 3 T11: 0.2364 T22: 0.2607 REMARK 3 T33: 0.2374 T12: 0.0265 REMARK 3 T13: -0.0345 T23: -0.0086 REMARK 3 L TENSOR REMARK 3 L11: 0.9837 L22: 0.4867 REMARK 3 L33: 1.3583 L12: -0.4130 REMARK 3 L13: -0.3818 L23: 0.6043 REMARK 3 S TENSOR REMARK 3 S11: -0.0643 S12: -0.1316 S13: 0.0368 REMARK 3 S21: -0.0588 S22: 0.2169 S23: -0.1998 REMARK 3 S31: 0.1082 S32: 0.0278 S33: -0.0937 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3411 -83.7869 -35.4797 REMARK 3 T TENSOR REMARK 3 T11: 0.1740 T22: 0.3057 REMARK 3 T33: 0.2596 T12: 0.0432 REMARK 3 T13: -0.0879 T23: 0.0144 REMARK 3 L TENSOR REMARK 3 L11: 1.4539 L22: 3.2173 REMARK 3 L33: 2.1320 L12: -0.3388 REMARK 3 L13: -0.9894 L23: -0.3968 REMARK 3 S TENSOR REMARK 3 S11: -0.0633 S12: -0.0579 S13: -0.0167 REMARK 3 S21: -0.3876 S22: 0.1131 S23: -0.1546 REMARK 3 S31: 0.2427 S32: 0.3093 S33: -0.1836 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.4548 -82.4782 -34.0961 REMARK 3 T TENSOR REMARK 3 T11: 0.1515 T22: 0.3087 REMARK 3 T33: 0.2681 T12: -0.0022 REMARK 3 T13: -0.0160 T23: 0.0088 REMARK 3 L TENSOR REMARK 3 L11: 1.6608 L22: 3.3346 REMARK 3 L33: 3.7577 L12: -1.7254 REMARK 3 L13: -0.5847 L23: 0.6065 REMARK 3 S TENSOR REMARK 3 S11: -0.0138 S12: 0.0207 S13: 0.0547 REMARK 3 S21: -0.0096 S22: 0.1902 S23: -0.0774 REMARK 3 S31: 0.0419 S32: 0.3454 S33: -0.1747 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.9971 -67.7679 -23.0477 REMARK 3 T TENSOR REMARK 3 T11: 0.2867 T22: 0.3035 REMARK 3 T33: 0.3448 T12: 0.0393 REMARK 3 T13: -0.0522 T23: -0.0159 REMARK 3 L TENSOR REMARK 3 L11: 1.1142 L22: 0.7805 REMARK 3 L33: 2.0709 L12: 0.3195 REMARK 3 L13: -0.3644 L23: -0.3728 REMARK 3 S TENSOR REMARK 3 S11: -0.0135 S12: 0.1534 S13: -0.1207 REMARK 3 S21: -0.2551 S22: 0.0085 S23: 0.3874 REMARK 3 S31: 0.4086 S32: -0.4244 S33: -0.1294 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 81 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3645 -61.3917 -14.4701 REMARK 3 T TENSOR REMARK 3 T11: 0.2046 T22: 0.1818 REMARK 3 T33: 0.2763 T12: 0.0589 REMARK 3 T13: -0.0422 T23: -0.0204 REMARK 3 L TENSOR REMARK 3 L11: 1.9770 L22: 1.5121 REMARK 3 L33: 2.7510 L12: 0.1756 REMARK 3 L13: 1.0176 L23: 0.5409 REMARK 3 S TENSOR REMARK 3 S11: 0.0489 S12: -0.0704 S13: 0.3070 REMARK 3 S21: 0.0163 S22: -0.0342 S23: 0.1423 REMARK 3 S31: -0.2922 S32: -0.2408 S33: 0.0002 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8969 -67.9031 -16.9447 REMARK 3 T TENSOR REMARK 3 T11: 0.1671 T22: 0.2278 REMARK 3 T33: 0.2998 T12: -0.0158 REMARK 3 T13: -0.0018 T23: 0.0151 REMARK 3 L TENSOR REMARK 3 L11: 0.9673 L22: 1.0767 REMARK 3 L33: 4.5570 L12: -0.8205 REMARK 3 L13: 0.4037 L23: 0.1392 REMARK 3 S TENSOR REMARK 3 S11: -0.1520 S12: 0.0932 S13: -0.0495 REMARK 3 S21: 0.1392 S22: -0.3151 S23: 0.0320 REMARK 3 S31: -0.5895 S32: -0.0749 S33: 0.4399 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9147 -70.7915 -38.1529 REMARK 3 T TENSOR REMARK 3 T11: 0.2254 T22: 0.1057 REMARK 3 T33: 0.3225 T12: 0.3121 REMARK 3 T13: -0.1844 T23: 0.2082 REMARK 3 L TENSOR REMARK 3 L11: 0.7828 L22: 1.3861 REMARK 3 L33: 1.3902 L12: -0.1497 REMARK 3 L13: 0.9969 L23: -0.1688 REMARK 3 S TENSOR REMARK 3 S11: 0.3995 S12: 0.0380 S13: 0.1655 REMARK 3 S21: -0.6894 S22: -0.7075 S23: 0.6716 REMARK 3 S31: 0.1322 S32: -0.7122 S33: -1.3118 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 120 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.8008 -89.6514 -43.4486 REMARK 3 T TENSOR REMARK 3 T11: 0.2235 T22: 0.2630 REMARK 3 T33: 0.3540 T12: 0.0089 REMARK 3 T13: -0.0295 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 0.6139 L22: 3.5879 REMARK 3 L33: 1.9373 L12: -1.4259 REMARK 3 L13: 0.4279 L23: -0.3677 REMARK 3 S TENSOR REMARK 3 S11: 0.1053 S12: -0.0976 S13: -0.1803 REMARK 3 S21: -0.2868 S22: -0.0882 S23: 0.3989 REMARK 3 S31: 0.2822 S32: -0.2584 S33: 0.0619 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 170 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.8917 -88.6794 -43.2114 REMARK 3 T TENSOR REMARK 3 T11: 0.2730 T22: 0.3148 REMARK 3 T33: 0.2440 T12: 0.0401 REMARK 3 T13: -0.1083 T23: 0.0337 REMARK 3 L TENSOR REMARK 3 L11: 2.3554 L22: 2.2087 REMARK 3 L33: 1.4607 L12: -0.5019 REMARK 3 L13: -0.8540 L23: 0.4810 REMARK 3 S TENSOR REMARK 3 S11: -0.2624 S12: 0.1301 S13: -0.4190 REMARK 3 S21: 0.0394 S22: 0.1482 S23: 0.5810 REMARK 3 S31: 0.2281 S32: 0.0473 S33: 0.0849 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 205 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.0405 -85.8406 -53.1003 REMARK 3 T TENSOR REMARK 3 T11: 0.6021 T22: 0.5185 REMARK 3 T33: 0.3167 T12: 0.0307 REMARK 3 T13: -0.1273 T23: -0.0696 REMARK 3 L TENSOR REMARK 3 L11: 1.7269 L22: 2.6800 REMARK 3 L33: 1.6993 L12: -0.2100 REMARK 3 L13: -1.0662 L23: 0.7819 REMARK 3 S TENSOR REMARK 3 S11: 0.2813 S12: 1.1710 S13: 0.4767 REMARK 3 S21: -0.5561 S22: -0.5085 S23: -0.0892 REMARK 3 S31: -0.2599 S32: -0.3140 S33: 0.1239 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6362 -48.3889 39.2856 REMARK 3 T TENSOR REMARK 3 T11: 0.7457 T22: 0.6277 REMARK 3 T33: 0.6212 T12: -0.1868 REMARK 3 T13: 0.1592 T23: 0.0120 REMARK 3 L TENSOR REMARK 3 L11: 0.6957 L22: 1.1307 REMARK 3 L33: 3.1801 L12: -0.5794 REMARK 3 L13: 0.6892 L23: 0.0523 REMARK 3 S TENSOR REMARK 3 S11: 0.4149 S12: -0.9956 S13: -0.8944 REMARK 3 S21: 0.3717 S22: -0.5046 S23: 0.2164 REMARK 3 S31: 0.6420 S32: -1.4621 S33: -0.0694 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 10 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.8810 -48.0663 45.0711 REMARK 3 T TENSOR REMARK 3 T11: 0.7074 T22: 0.6424 REMARK 3 T33: 0.5918 T12: 0.0231 REMARK 3 T13: -0.0026 T23: 0.0879 REMARK 3 L TENSOR REMARK 3 L11: 0.8035 L22: 1.6207 REMARK 3 L33: 2.2488 L12: -0.8551 REMARK 3 L13: 0.3348 L23: -0.1395 REMARK 3 S TENSOR REMARK 3 S11: 0.0537 S12: 0.0621 S13: -0.1716 REMARK 3 S21: -0.0310 S22: 0.1448 S23: -0.4322 REMARK 3 S31: 0.6479 S32: -0.0992 S33: -0.1703 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 26 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9172 -52.9951 27.4391 REMARK 3 T TENSOR REMARK 3 T11: 0.8598 T22: 0.4574 REMARK 3 T33: 0.5285 T12: -0.1898 REMARK 3 T13: 0.1198 T23: -0.1323 REMARK 3 L TENSOR REMARK 3 L11: 1.6348 L22: 0.5975 REMARK 3 L33: 0.7750 L12: 0.6246 REMARK 3 L13: -0.9833 L23: -0.6271 REMARK 3 S TENSOR REMARK 3 S11: -0.0841 S12: 0.8034 S13: -1.2848 REMARK 3 S21: -0.0000 S22: -0.0213 S23: 0.0677 REMARK 3 S31: 1.1158 S32: -0.5991 S33: 0.1023 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 34 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.2613 -36.1492 38.4514 REMARK 3 T TENSOR REMARK 3 T11: 0.7204 T22: 0.4951 REMARK 3 T33: 0.4146 T12: 0.0084 REMARK 3 T13: 0.0692 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 3.0020 L22: 0.5274 REMARK 3 L33: 2.9694 L12: -0.6909 REMARK 3 L13: -0.0053 L23: -0.4464 REMARK 3 S TENSOR REMARK 3 S11: 0.4160 S12: -0.1169 S13: 0.0277 REMARK 3 S21: 0.7411 S22: 0.1938 S23: -0.3893 REMARK 3 S31: -0.8071 S32: -0.0826 S33: -0.3541 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 45 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7357 -47.0800 32.3279 REMARK 3 T TENSOR REMARK 3 T11: 0.5571 T22: 0.4328 REMARK 3 T33: 0.5576 T12: 0.0605 REMARK 3 T13: 0.0502 T23: -0.0246 REMARK 3 L TENSOR REMARK 3 L11: 2.3599 L22: 2.3873 REMARK 3 L33: 2.8062 L12: -0.3116 REMARK 3 L13: 0.5617 L23: 0.5889 REMARK 3 S TENSOR REMARK 3 S11: 0.0304 S12: -0.0377 S13: -0.6707 REMARK 3 S21: 0.0621 S22: 0.0925 S23: -0.5768 REMARK 3 S31: 0.5733 S32: 0.4117 S33: -0.1737 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 85 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.1571 -37.3577 45.3087 REMARK 3 T TENSOR REMARK 3 T11: 0.9608 T22: 0.9296 REMARK 3 T33: 0.7078 T12: -0.1250 REMARK 3 T13: -0.0996 T23: -0.1690 REMARK 3 L TENSOR REMARK 3 L11: 2.0447 L22: 2.3480 REMARK 3 L33: 3.5031 L12: 1.8131 REMARK 3 L13: 0.7952 L23: -0.8298 REMARK 3 S TENSOR REMARK 3 S11: -0.1512 S12: 0.0362 S13: 0.4853 REMARK 3 S21: -0.9469 S22: -0.2334 S23: -0.1212 REMARK 3 S31: -0.0891 S32: 0.0293 S33: 0.1373 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 92 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.4117 -41.8018 35.2246 REMARK 3 T TENSOR REMARK 3 T11: 0.5347 T22: 0.3528 REMARK 3 T33: 0.3079 T12: -0.0460 REMARK 3 T13: 0.0961 T23: 0.0244 REMARK 3 L TENSOR REMARK 3 L11: 2.6663 L22: 0.7460 REMARK 3 L33: 2.4760 L12: -0.1178 REMARK 3 L13: 0.4173 L23: 0.6018 REMARK 3 S TENSOR REMARK 3 S11: 0.1018 S12: -0.5673 S13: -0.5073 REMARK 3 S21: 0.2756 S22: 0.0546 S23: -0.1112 REMARK 3 S31: 0.9005 S32: -0.1918 S33: -0.0728 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.1003 -35.7794 67.3014 REMARK 3 T TENSOR REMARK 3 T11: 0.7333 T22: 0.6504 REMARK 3 T33: 0.4264 T12: -0.3799 REMARK 3 T13: 0.1439 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 2.5699 L22: 3.4026 REMARK 3 L33: 2.4748 L12: -1.0787 REMARK 3 L13: 2.1891 L23: 0.4036 REMARK 3 S TENSOR REMARK 3 S11: 0.8881 S12: -0.2393 S13: 0.2145 REMARK 3 S21: 0.2223 S22: -0.6581 S23: -0.5410 REMARK 3 S31: 0.1674 S32: 0.6479 S33: 0.0826 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.0821 -17.1281 69.7612 REMARK 3 T TENSOR REMARK 3 T11: 0.8240 T22: 0.5490 REMARK 3 T33: 0.4862 T12: -0.1132 REMARK 3 T13: 0.1970 T23: -0.0549 REMARK 3 L TENSOR REMARK 3 L11: 4.4973 L22: 5.2747 REMARK 3 L33: 4.0650 L12: -1.9636 REMARK 3 L13: -0.1240 L23: 0.7041 REMARK 3 S TENSOR REMARK 3 S11: 0.2553 S12: -0.8488 S13: 0.0169 REMARK 3 S21: 0.2387 S22: 0.3654 S23: 0.2741 REMARK 3 S31: -0.4395 S32: -0.9540 S33: -0.3048 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 147 THROUGH 160 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.0712 -33.4397 63.0506 REMARK 3 T TENSOR REMARK 3 T11: 0.6527 T22: 0.6269 REMARK 3 T33: 0.4579 T12: -0.1223 REMARK 3 T13: -0.0333 T23: -0.2066 REMARK 3 L TENSOR REMARK 3 L11: 0.3781 L22: 0.9279 REMARK 3 L33: 0.6444 L12: 0.3911 REMARK 3 L13: 0.1721 L23: -0.3219 REMARK 3 S TENSOR REMARK 3 S11: 0.3212 S12: 0.4005 S13: -0.3093 REMARK 3 S21: 0.3159 S22: 0.1531 S23: -0.1150 REMARK 3 S31: 0.2317 S32: 0.2861 S33: -0.2829 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 161 THROUGH 171 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.0462 -25.5303 65.3297 REMARK 3 T TENSOR REMARK 3 T11: 0.6346 T22: 0.4485 REMARK 3 T33: 0.5463 T12: -0.0952 REMARK 3 T13: 0.0925 T23: -0.0842 REMARK 3 L TENSOR REMARK 3 L11: 0.1749 L22: 0.0720 REMARK 3 L33: 0.1751 L12: -0.1071 REMARK 3 L13: 0.0579 L23: 0.0395 REMARK 3 S TENSOR REMARK 3 S11: 0.5716 S12: -0.0751 S13: 0.0221 REMARK 3 S21: 0.3276 S22: -0.2784 S23: 0.5459 REMARK 3 S31: -0.1647 S32: -0.1214 S33: -0.2804 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 172 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9905 -30.3384 58.3423 REMARK 3 T TENSOR REMARK 3 T11: 0.4996 T22: 0.8965 REMARK 3 T33: 0.4644 T12: -0.0364 REMARK 3 T13: 0.0135 T23: -0.0857 REMARK 3 L TENSOR REMARK 3 L11: 1.3598 L22: 0.4494 REMARK 3 L33: 2.0593 L12: 0.7586 REMARK 3 L13: 0.4230 L23: -0.0061 REMARK 3 S TENSOR REMARK 3 S11: -0.1856 S12: 0.3028 S13: -0.4431 REMARK 3 S21: 0.1418 S22: 0.3412 S23: -0.3830 REMARK 3 S31: -0.3550 S32: 1.7849 S33: -0.0654 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 185 THROUGH 199 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3978 -18.3762 73.2222 REMARK 3 T TENSOR REMARK 3 T11: 0.8545 T22: 0.5680 REMARK 3 T33: 0.4635 T12: -0.1938 REMARK 3 T13: 0.2624 T23: -0.1492 REMARK 3 L TENSOR REMARK 3 L11: 1.6216 L22: 2.8552 REMARK 3 L33: 1.5373 L12: -0.7457 REMARK 3 L13: 0.7169 L23: 1.4213 REMARK 3 S TENSOR REMARK 3 S11: 0.2387 S12: -1.0549 S13: 0.2486 REMARK 3 S21: -0.7643 S22: -0.3232 S23: 1.0223 REMARK 3 S31: -0.4655 S32: -0.1623 S33: 0.3071 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 200 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7413 -36.3809 67.6031 REMARK 3 T TENSOR REMARK 3 T11: 0.7906 T22: 0.5819 REMARK 3 T33: 0.6595 T12: -0.0638 REMARK 3 T13: 0.0825 T23: -0.1487 REMARK 3 L TENSOR REMARK 3 L11: 2.9987 L22: 1.5638 REMARK 3 L33: 3.2261 L12: -0.9709 REMARK 3 L13: -1.2833 L23: 1.3054 REMARK 3 S TENSOR REMARK 3 S11: -0.3689 S12: 0.3649 S13: -0.2470 REMARK 3 S21: 0.4940 S22: 0.5467 S23: -1.0022 REMARK 3 S31: -0.4263 S32: 0.7164 S33: -0.0669 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 209 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9144 -30.8461 74.3848 REMARK 3 T TENSOR REMARK 3 T11: 0.8800 T22: 0.5450 REMARK 3 T33: 0.5026 T12: -0.0571 REMARK 3 T13: 0.2535 T23: -0.0424 REMARK 3 L TENSOR REMARK 3 L11: 0.3702 L22: 1.5957 REMARK 3 L33: 0.4546 L12: -0.6067 REMARK 3 L13: -0.1606 L23: 0.7456 REMARK 3 S TENSOR REMARK 3 S11: -0.3674 S12: -0.4917 S13: -0.1969 REMARK 3 S21: 0.1899 S22: 0.8152 S23: -0.1584 REMARK 3 S31: 0.1687 S32: 0.8778 S33: -0.3262 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.5130 -23.6717 26.0136 REMARK 3 T TENSOR REMARK 3 T11: 0.8506 T22: 0.3785 REMARK 3 T33: 0.4567 T12: -0.1342 REMARK 3 T13: 0.2336 T23: -0.0136 REMARK 3 L TENSOR REMARK 3 L11: 1.0726 L22: 1.3442 REMARK 3 L33: 2.0526 L12: 0.0551 REMARK 3 L13: -0.1185 L23: -0.0272 REMARK 3 S TENSOR REMARK 3 S11: 0.3371 S12: -0.0161 S13: 0.3617 REMARK 3 S21: -0.2724 S22: 0.0528 S23: -0.2976 REMARK 3 S31: -0.6604 S32: 0.0647 S33: -0.3317 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 38 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.8178 -29.6168 29.2805 REMARK 3 T TENSOR REMARK 3 T11: 0.5671 T22: 0.3433 REMARK 3 T33: 0.3844 T12: -0.0374 REMARK 3 T13: 0.1481 T23: 0.0257 REMARK 3 L TENSOR REMARK 3 L11: 1.1698 L22: 1.5989 REMARK 3 L33: 2.6301 L12: -0.7978 REMARK 3 L13: -0.0645 L23: 1.2429 REMARK 3 S TENSOR REMARK 3 S11: 0.0714 S12: -0.0853 S13: 0.1877 REMARK 3 S21: -0.1500 S22: -0.0384 S23: 0.0890 REMARK 3 S31: -0.5092 S32: -0.1938 S33: -0.0196 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 108 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7157 -14.9131 45.9235 REMARK 3 T TENSOR REMARK 3 T11: 1.0168 T22: 0.5007 REMARK 3 T33: 0.5928 T12: 0.0883 REMARK 3 T13: -0.0256 T23: -0.0607 REMARK 3 L TENSOR REMARK 3 L11: 1.3214 L22: -0.0068 REMARK 3 L33: 0.7314 L12: 0.0365 REMARK 3 L13: -0.3897 L23: 0.1202 REMARK 3 S TENSOR REMARK 3 S11: 0.1180 S12: 0.0200 S13: 0.4708 REMARK 3 S21: 0.9365 S22: -0.0992 S23: -0.5782 REMARK 3 S31: -1.2723 S32: -0.2514 S33: 0.1440 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 120 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.6600 -16.7687 62.3513 REMARK 3 T TENSOR REMARK 3 T11: 1.1053 T22: 0.7487 REMARK 3 T33: 0.4327 T12: -0.4079 REMARK 3 T13: 0.0908 T23: -0.2300 REMARK 3 L TENSOR REMARK 3 L11: 2.2395 L22: 1.6901 REMARK 3 L33: 2.0756 L12: 0.5300 REMARK 3 L13: -0.8202 L23: -0.3135 REMARK 3 S TENSOR REMARK 3 S11: 0.4595 S12: 0.0072 S13: -0.2902 REMARK 3 S21: 0.3778 S22: 0.0517 S23: -0.0063 REMARK 3 S31: -0.5598 S32: 0.8695 S33: -0.3693 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 156 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.7105 -19.1847 53.8285 REMARK 3 T TENSOR REMARK 3 T11: 0.7181 T22: 0.5639 REMARK 3 T33: 0.4644 T12: -0.0625 REMARK 3 T13: 0.2204 T23: -0.1084 REMARK 3 L TENSOR REMARK 3 L11: 2.2830 L22: 2.1698 REMARK 3 L33: 1.4991 L12: -0.3976 REMARK 3 L13: 0.7022 L23: -0.3748 REMARK 3 S TENSOR REMARK 3 S11: -0.9178 S12: -0.0721 S13: 0.0942 REMARK 3 S21: 0.1145 S22: 0.2827 S23: -0.0776 REMARK 3 S31: 0.1219 S32: -0.0853 S33: 0.4053 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 181 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.1594 -9.4650 61.5263 REMARK 3 T TENSOR REMARK 3 T11: 1.4803 T22: 0.7942 REMARK 3 T33: 0.4942 T12: -0.5066 REMARK 3 T13: 0.0162 T23: -0.0756 REMARK 3 L TENSOR REMARK 3 L11: 0.5604 L22: 1.0351 REMARK 3 L33: 0.5924 L12: -0.0917 REMARK 3 L13: -0.1814 L23: 0.8037 REMARK 3 S TENSOR REMARK 3 S11: -0.1614 S12: 0.4904 S13: 0.1274 REMARK 3 S21: 0.0812 S22: -0.0557 S23: -0.1119 REMARK 3 S31: -0.8330 S32: 0.9852 S33: 0.0018 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 6O9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-19. REMARK 100 THE DEPOSITION ID IS D_1000240265. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-FEB-16 REMARK 200 TEMPERATURE (KELVIN) : 77 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.29 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28394 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 19.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.19200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.80 REMARK 200 R MERGE FOR SHELL (I) : 0.96700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 5.5, 0.2 M MGCL2 REMARK 280 AND 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 43660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 APPLY THE FOLLOWING TO CHAINS: D, E REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -6.70502 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -43.16231 REMARK 350 BIOMT3 2 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 A 136 REMARK 465 THR A 137 REMARK 465 CYS A 220 REMARK 465 GLY A 221 REMARK 465 CYS A 222 REMARK 465 LYS A 223 REMARK 465 PRO A 224 REMARK 465 CYS A 225 REMARK 465 ASN B 218 REMARK 465 GLU B 219 REMARK 465 CYS B 220 REMARK 465 MET C -27 REMARK 465 GLY C -26 REMARK 465 SER C -25 REMARK 465 SER C -24 REMARK 465 HIS C -23 REMARK 465 HIS C -22 REMARK 465 HIS C -21 REMARK 465 HIS C -20 REMARK 465 HIS C -19 REMARK 465 HIS C -18 REMARK 465 SER C -17 REMARK 465 SER C -16 REMARK 465 GLY C -15 REMARK 465 LEU C -14 REMARK 465 VAL C -13 REMARK 465 PRO C -12 REMARK 465 ARG C -11 REMARK 465 GLY C -10 REMARK 465 SER C -9 REMARK 465 HIS C -8 REMARK 465 MET C -7 REMARK 465 GLU C -6 REMARK 465 THR C -5 REMARK 465 ASP C -4 REMARK 465 SER C -3 REMARK 465 GLU C -2 REMARK 465 GLY C -1 REMARK 465 GLN C 0 REMARK 465 THR C 1 REMARK 465 THR C 2 REMARK 465 THR C 3 REMARK 465 GLY D 8 REMARK 465 GLY D 133 REMARK 465 SER D 134 REMARK 465 ALA D 135 REMARK 465 ALA D 136 REMARK 465 GLN D 137 REMARK 465 THR D 138 REMARK 465 ASN D 139 REMARK 465 GLN D 177 REMARK 465 SER D 178 REMARK 465 ARG D 219 REMARK 465 ASP D 220 REMARK 465 CYS D 221 REMARK 465 GLY D 222 REMARK 465 CYS D 223 REMARK 465 LYS D 224 REMARK 465 PRO D 225 REMARK 465 CYS D 226 REMARK 465 ASP E 157 REMARK 465 GLY E 158 REMARK 465 SER E 159 REMARK 465 GLU E 160 REMARK 465 ARG E 161 REMARK 465 THR E 186 REMARK 465 LEU E 187 REMARK 465 THR E 188 REMARK 465 LYS E 189 REMARK 465 ASP E 190 REMARK 465 GLU E 191 REMARK 465 TYR E 192 REMARK 465 GLU E 193 REMARK 465 THR E 206 REMARK 465 ARG E 217 REMARK 465 ASN E 218 REMARK 465 GLU E 219 REMARK 465 CYS E 220 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 OG SER A 195 O HOH A 401 1.90 REMARK 500 O THR E 208 O HOH E 401 1.92 REMARK 500 O HOH B 465 O HOH B 468 1.97 REMARK 500 O HOH B 426 O HOH B 455 1.98 REMARK 500 NZ LYS D 38 OE1 GLU D 89 2.00 REMARK 500 O VAL A 157 O HOH A 402 2.02 REMARK 500 O ILE E 156 O HOH E 402 2.03 REMARK 500 OD2 ASP E 1 O HOH E 403 2.08 REMARK 500 NE2 GLN A 39 O HOH A 403 2.08 REMARK 500 OE1 GLN D 43 O HOH D 401 2.09 REMARK 500 O HOH A 465 O HOH A 466 2.11 REMARK 500 OG1 THR B 186 O HOH B 401 2.12 REMARK 500 O2 EDO A 301 O HOH A 404 2.13 REMARK 500 O HOH B 411 O HOH B 447 2.15 REMARK 500 O HOH E 422 O HOH E 424 2.16 REMARK 500 OE2 GLU E 111 OH TYR E 179 2.16 REMARK 500 N GLN E 6 O HOH E 404 2.17 REMARK 500 OG SER E 14 OD1 ASP E 17 2.17 REMARK 500 O LYS B 113 O HOH B 402 2.17 REMARK 500 O PRO A 172 O HOH A 405 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU D 89 CD GLU D 89 OE1 -0.068 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 VAL A 48 -60.74 -106.23 REMARK 500 VAL A 64 -20.42 -143.90 REMARK 500 ALA A 106 -46.81 -132.47 REMARK 500 ALA A 134 127.20 -171.52 REMARK 500 SER A 177 49.98 36.70 REMARK 500 ALA B 57 -38.69 70.46 REMARK 500 LEU B 89 109.64 -55.19 REMARK 500 PRO B 147 -179.41 -61.71 REMARK 500 MET C 38 -1.59 63.26 REMARK 500 GLN C 99 -91.25 -85.26 REMARK 500 THR D 103 -169.79 -129.97 REMARK 500 THR D 122 107.46 -48.34 REMARK 500 TYR E 37 74.33 -108.67 REMARK 500 VAL E 56 -59.84 75.85 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 466 DISTANCE = 6.19 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 301 DBREF 6O9I A 1 225 PDB 6O9I 6O9I 1 225 DBREF 6O9I B 1 220 PDB 6O9I 6O9I 1 220 DBREF 6O9I C -27 109 PDB 6O9I 6O9I -27 109 DBREF 6O9I D 1 226 PDB 6O9I 6O9I 1 226 DBREF 6O9I E 1 220 PDB 6O9I 6O9I 1 220 SEQRES 1 A 225 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 225 PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 225 PHE THR PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 225 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 A 225 SER GLY SER SER THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 A 225 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 A 225 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 A 225 ALA MET TYR TYR CYS ALA ARG GLY LYS TYR PRO THR TRP SEQRES 9 A 225 ILE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 A 225 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 A 225 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 A 225 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 225 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 A 225 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 A 225 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 A 225 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 A 225 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 18 A 225 CYS LYS PRO CYS SEQRES 1 B 220 ASP ILE VAL MET THR GLN SER PRO SER SER LEU THR VAL SEQRES 2 B 220 THR ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 B 220 GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 B 220 THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 B 220 LEU ILE SER TRP ALA SER THR ARG ASP SER GLY VAL PRO SEQRES 6 B 220 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 B 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 B 220 TYR TYR CYS GLN ASN ASP TYR SER TYR PRO LEU THR PHE SEQRES 9 B 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 B 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 B 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 B 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 B 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 B 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 B 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 B 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 B 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 C 137 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 C 137 LEU VAL PRO ARG GLY SER HIS MET GLU THR ASP SER GLU SEQRES 3 C 137 GLY GLN THR THR THR GLY GLU LEU TYR GLN ARG TRP GLU SEQRES 4 C 137 HIS TYR GLY GLN GLU CYS GLN LYS MET LEU GLU THR THR SEQRES 5 C 137 GLU PRO PRO SER GLY LEU ALA CYS ASN GLY SER PHE ASP SEQRES 6 C 137 MET TYR ALA CYS TRP ASN TYR THR ALA ALA ASN THR THR SEQRES 7 C 137 ALA ARG VAL SER CYS PRO TRP TYR LEU PRO TRP PHE ARG SEQRES 8 C 137 GLN VAL SER ALA GLY PHE VAL PHE ARG GLN CYS GLY SER SEQRES 9 C 137 ASP GLY GLN TRP GLY SER TRP ARG ASP HIS THR GLN CYS SEQRES 10 C 137 GLU ASN PRO GLU LYS ASN GLY ALA PHE GLN ASP GLN THR SEQRES 11 C 137 LEU ILE LEU GLU ARG LEU GLN SEQRES 1 D 226 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 D 226 PRO GLY ALA SER VAL LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 D 226 TYR THR PHE THR SER ASN TRP MET HIS TRP VAL LYS GLN SEQRES 4 D 226 ARG PRO ARG GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 D 226 PRO SER ASN GLY ARG SER ASN TYR ASN GLU LYS PHE LYS SEQRES 6 D 226 THR LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 D 226 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 D 226 ALA VAL TYR TYR CYS ALA ARG PHE TYR TYR GLY THR SER SEQRES 9 D 226 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL ALA VAL SEQRES 10 D 226 SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU SEQRES 11 D 226 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR SEQRES 12 D 226 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 D 226 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 D 226 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 D 226 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SEQRES 16 D 226 SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 D 226 SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 18 D 226 GLY CYS LYS PRO CYS SEQRES 1 E 220 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 E 220 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 E 220 GLN SER LEU VAL HIS SER ASN GLY ASP THR TYR LEU HIS SEQRES 4 E 220 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 E 220 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 E 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 E 220 LYS ILE SER ARG VAL GLU ALA ALA ASP LEU GLY VAL TYR SEQRES 8 E 220 PHE CYS SER GLN SER THR HIS VAL PRO PRO PHE THR PHE SEQRES 9 E 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA SEQRES 10 E 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 E 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 E 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 E 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 E 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 E 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 E 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 E 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS HET EDO A 301 4 HET EDO B 301 4 HET EDO D 301 4 HET EDO D 302 4 HET EDO E 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 6 EDO 5(C2 H6 O2) FORMUL 11 HOH *200(H2 O) HELIX 1 AA1 THR A 28 PHE A 32 5 5 HELIX 2 AA2 ASN A 74 LYS A 76 5 3 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 SER A 161 SER A 163 5 3 HELIX 5 AA5 GLN B 85 LEU B 89 5 5 HELIX 6 AA6 SER B 127 GLY B 134 1 8 HELIX 7 AA7 LYS B 189 ARG B 194 1 6 HELIX 8 AA8 LEU C 6 THR C 23 1 18 HELIX 9 AA9 HIS C 86 GLU C 90 5 5 HELIX 10 AB1 GLN C 99 GLU C 106 1 8 HELIX 11 AB2 ARG C 107 GLN C 109 5 3 HELIX 12 AB3 THR D 28 ASN D 32 5 5 HELIX 13 AB4 GLU D 62 LYS D 65 5 4 HELIX 14 AB5 THR D 87 SER D 91 5 5 HELIX 15 AB6 SER D 162 SER D 164 5 3 HELIX 16 AB7 PRO D 206 SER D 209 5 4 HELIX 17 AB8 SER E 127 GLY E 134 1 8 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 ARG A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA1 4 THR A 69 ASP A 73 -1 N SER A 71 O PHE A 80 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AA2 6 ALA A 92 LYS A 100 -1 N TYR A 94 O THR A 112 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O ILE A 51 N MET A 34 SHEET 6 AA2 6 ILE A 58 TYR A 60 -1 O TYR A 59 N TYR A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AA3 4 ALA A 92 LYS A 100 -1 N TYR A 94 O THR A 112 SHEET 4 AA3 4 THR A 103 TRP A 108 -1 O ALA A 106 N ARG A 98 SHEET 1 AA4 4 SER A 125 LEU A 129 0 SHEET 2 AA4 4 MET A 140 TYR A 150 -1 O LYS A 148 N SER A 125 SHEET 3 AA4 4 LEU A 179 PRO A 189 -1 O TYR A 180 N TYR A 150 SHEET 4 AA4 4 VAL A 168 THR A 170 -1 N HIS A 169 O SER A 185 SHEET 1 AA5 4 SER A 125 LEU A 129 0 SHEET 2 AA5 4 MET A 140 TYR A 150 -1 O LYS A 148 N SER A 125 SHEET 3 AA5 4 LEU A 179 PRO A 189 -1 O TYR A 180 N TYR A 150 SHEET 4 AA5 4 VAL A 174 GLN A 176 -1 N VAL A 174 O THR A 181 SHEET 1 AA6 3 THR A 156 TRP A 159 0 SHEET 2 AA6 3 THR A 199 HIS A 204 -1 O ASN A 201 N THR A 158 SHEET 3 AA6 3 THR A 209 LYS A 214 -1 O THR A 209 N HIS A 204 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA7 4 ASP B 76 ILE B 81 -1 O ILE B 81 N VAL B 19 SHEET 4 AA7 4 PHE B 68 SER B 73 -1 N THR B 69 O THR B 80 SHEET 1 AA8 6 SER B 10 THR B 14 0 SHEET 2 AA8 6 THR B 108 LYS B 113 1 O GLU B 111 N LEU B 11 SHEET 3 AA8 6 ALA B 90 ASN B 96 -1 N ALA B 90 O LEU B 110 SHEET 4 AA8 6 LEU B 39 GLN B 44 -1 N TYR B 42 O TYR B 93 SHEET 5 AA8 6 LYS B 51 SER B 55 -1 O LYS B 51 N GLN B 43 SHEET 6 AA8 6 THR B 59 ARG B 60 -1 O THR B 59 N SER B 55 SHEET 1 AA9 4 SER B 10 THR B 14 0 SHEET 2 AA9 4 THR B 108 LYS B 113 1 O GLU B 111 N LEU B 11 SHEET 3 AA9 4 ALA B 90 ASN B 96 -1 N ALA B 90 O LEU B 110 SHEET 4 AA9 4 THR B 103 PHE B 104 -1 O THR B 103 N ASN B 96 SHEET 1 AB1 2 LEU B 30 ASN B 31 0 SHEET 2 AB1 2 LYS B 36 ASN B 37 -1 O LYS B 36 N ASN B 31 SHEET 1 AB2 4 THR B 120 PHE B 124 0 SHEET 2 AB2 4 GLY B 135 PHE B 145 -1 O PHE B 141 N SER B 122 SHEET 3 AB2 4 TYR B 179 THR B 188 -1 O LEU B 185 N VAL B 138 SHEET 4 AB2 4 VAL B 165 TRP B 169 -1 N SER B 168 O SER B 182 SHEET 1 AB3 4 SER B 159 ARG B 161 0 SHEET 2 AB3 4 ASN B 151 ILE B 156 -1 N TRP B 154 O ARG B 161 SHEET 3 AB3 4 SER B 197 THR B 203 -1 O GLU B 201 N LYS B 153 SHEET 4 AB3 4 ILE B 211 ASN B 216 -1 O ILE B 211 N ALA B 202 SHEET 1 AB4 2 ALA C 31 CYS C 32 0 SHEET 2 AB4 2 THR C 45 ALA C 46 -1 O THR C 45 N CYS C 32 SHEET 1 AB5 2 SER C 35 PHE C 36 0 SHEET 2 AB5 2 CYS C 41 TRP C 42 -1 O TRP C 42 N SER C 35 SHEET 1 AB6 3 THR C 49 SER C 54 0 SHEET 2 AB6 3 PHE C 69 CYS C 74 -1 O VAL C 70 N VAL C 53 SHEET 3 AB6 3 TRP C 80 ASP C 85 -1 O GLY C 81 N GLN C 73 SHEET 1 AB7 4 GLN D 3 GLN D 5 0 SHEET 2 AB7 4 VAL D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AB7 4 THR D 78 LEU D 83 -1 O ALA D 79 N CYS D 22 SHEET 4 AB7 4 ALA D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AB8 6 GLU D 10 VAL D 12 0 SHEET 2 AB8 6 THR D 113 VAL D 117 1 O LEU D 114 N GLU D 10 SHEET 3 AB8 6 ALA D 92 PHE D 99 -1 N ALA D 92 O VAL D 115 SHEET 4 AB8 6 MET D 34 GLN D 39 -1 N GLN D 39 O VAL D 93 SHEET 5 AB8 6 LEU D 45 ILE D 51 -1 O ILE D 48 N TRP D 36 SHEET 6 AB8 6 SER D 58 TYR D 60 -1 O ASN D 59 N GLU D 50 SHEET 1 AB9 4 GLU D 10 VAL D 12 0 SHEET 2 AB9 4 THR D 113 VAL D 117 1 O LEU D 114 N GLU D 10 SHEET 3 AB9 4 ALA D 92 PHE D 99 -1 N ALA D 92 O VAL D 115 SHEET 4 AB9 4 PHE D 106 TRP D 109 -1 O TYR D 108 N ARG D 98 SHEET 1 AC1 4 SER D 126 LEU D 130 0 SHEET 2 AC1 4 MET D 141 TYR D 151 -1 O GLY D 145 N LEU D 130 SHEET 3 AC1 4 TYR D 181 PRO D 190 -1 O VAL D 189 N VAL D 142 SHEET 4 AC1 4 VAL D 169 THR D 171 -1 N HIS D 170 O SER D 186 SHEET 1 AC2 3 THR D 157 TRP D 160 0 SHEET 2 AC2 3 THR D 200 HIS D 205 -1 O ASN D 202 N THR D 159 SHEET 3 AC2 3 THR D 210 LYS D 215 -1 O LYS D 214 N CYS D 201 SHEET 1 AC3 4 MET E 4 THR E 7 0 SHEET 2 AC3 4 ALA E 19 SER E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AC3 4 ASP E 75 ILE E 80 -1 O LEU E 78 N ILE E 21 SHEET 4 AC3 4 PHE E 67 SER E 72 -1 N SER E 68 O LYS E 79 SHEET 1 AC4 6 SER E 10 VAL E 13 0 SHEET 2 AC4 6 THR E 108 ILE E 112 1 O LYS E 109 N LEU E 11 SHEET 3 AC4 6 GLY E 89 GLN E 95 -1 N GLY E 89 O LEU E 110 SHEET 4 AC4 6 LEU E 38 GLN E 43 -1 N HIS E 39 O SER E 94 SHEET 5 AC4 6 LYS E 50 TYR E 54 -1 O ILE E 53 N TRP E 40 SHEET 6 AC4 6 ASN E 58 ARG E 59 -1 O ASN E 58 N TYR E 54 SHEET 1 AC5 4 SER E 10 VAL E 13 0 SHEET 2 AC5 4 THR E 108 ILE E 112 1 O LYS E 109 N LEU E 11 SHEET 3 AC5 4 GLY E 89 GLN E 95 -1 N GLY E 89 O LEU E 110 SHEET 4 AC5 4 THR E 103 PHE E 104 -1 O THR E 103 N GLN E 95 SHEET 1 AC6 4 THR E 120 PHE E 124 0 SHEET 2 AC6 4 VAL E 139 PHE E 145 -1 O PHE E 141 N SER E 122 SHEET 3 AC6 4 TYR E 179 THR E 184 -1 O TYR E 179 N PHE E 145 SHEET 4 AC6 4 LEU E 166 TRP E 169 -1 N SER E 168 O SER E 182 SHEET 1 AC7 3 ASN E 151 LYS E 155 0 SHEET 2 AC7 3 TYR E 198 THR E 203 -1 O GLU E 201 N LYS E 153 SHEET 3 AC7 3 ILE E 211 PHE E 215 -1 O ILE E 211 N ALA E 202 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 145 CYS A 200 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 94 1555 1555 2.03 SSBOND 4 CYS B 140 CYS B 200 1555 1555 2.04 SSBOND 5 CYS C 17 CYS C 41 1555 1555 2.04 SSBOND 6 CYS C 32 CYS C 74 1555 1555 2.03 SSBOND 7 CYS C 55 CYS C 89 1555 1555 2.03 SSBOND 8 CYS D 22 CYS D 96 1555 1555 2.03 SSBOND 9 CYS D 146 CYS D 201 1555 1555 2.03 SSBOND 10 CYS E 23 CYS E 93 1555 1555 2.04 SSBOND 11 CYS E 140 CYS E 200 1555 1555 2.03 CISPEP 1 TYR A 101 PRO A 102 0 3.11 CISPEP 2 PHE A 151 PRO A 152 0 -2.48 CISPEP 3 GLU A 153 PRO A 154 0 -0.10 CISPEP 4 TRP A 193 PRO A 194 0 2.66 CISPEP 5 SER B 7 PRO B 8 0 -3.83 CISPEP 6 TYR B 100 PRO B 101 0 -0.98 CISPEP 7 TYR B 146 PRO B 147 0 0.37 CISPEP 8 PHE D 152 PRO D 153 0 -5.19 CISPEP 9 GLU D 154 PRO D 155 0 3.50 CISPEP 10 TRP D 194 PRO D 195 0 1.13 CISPEP 11 THR E 7 PRO E 8 0 -2.61 CISPEP 12 VAL E 99 PRO E 100 0 -2.60 CISPEP 13 PRO E 100 PRO E 101 0 -2.01 CISPEP 14 TYR E 146 PRO E 147 0 1.02 SITE 1 AC1 5 TYR A 59 HOH A 404 VAL E 30 HIS E 31 SITE 2 AC1 5 SER E 32 SITE 1 AC2 2 TYR B 98 HIS C 12 SITE 1 AC3 2 HOH E 406 HOH E 417 CRYST1 41.430 43.680 133.820 87.86 88.38 81.17 P 1 1 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 0.024137 -0.003750 -0.000558 0.00000 SCALE2 0.000000 0.023168 -0.000776 0.00000 SCALE3 0.000000 0.000000 0.007480 0.00000