HEADER SIGNALING PROTEIN/IMMUNE SYSTEM 30-JUN-22 8DJG TITLE ADGRL3-LECTIN DOMAIN IN COMPLEX WITH AN ACTIVATING SYNTHETIC ANTIBODY TITLE 2 FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: SAB HEAVY CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SAB LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ISOFORM 2 OF ADHESION G PROTEIN-COUPLED RECEPTOR L3; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: CALCIUM-INDEPENDENT ALPHA-LATROTOXIN RECEPTOR 3,CIRL-3, COMPND 13 LATROPHILIN-3,LECTOMEDIN-3; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 8 ORGANISM_TAXID: 32630; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: ADGRL3, KIAA0768, LEC3, LPHN3; SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS ADHESION GPCR, LECTIN DOMAIN, SAB, SIGNALING PROTEIN, SIGNALING KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.P.KORDON,S.J.BANDEKAR,D.ARAC REVDAT 1 15-FEB-23 8DJG 0 JRNL AUTH S.P.KORDON,P.DUTKA,J.M.ADAMSKA,S.J.BANDEKAR,K.LEON,B.ADAMS, JRNL AUTH 2 J.LI,D.ARAC,A.A.KOSSIAKOFF JRNL TITL ISOFORM- AND LIGAND-SPECIFIC MODULATION OF THE ADHESION GPCR JRNL TITL 2 ADGRL3/LATROPHILIN3 BY A SYNTHETIC BINDER JRNL REF NAT COMMUN 2023 JRNL REFN ESSN 2041-1723 JRNL DOI 10.1038/S41467-023-36312-7 REMARK 2 REMARK 2 RESOLUTION. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.51 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 38700 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.239 REMARK 3 R VALUE (WORKING SET) : 0.237 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 3521 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 47.5100 - 7.7400 1.00 2812 122 0.2019 0.2001 REMARK 3 2 7.7400 - 6.1500 1.00 2797 138 0.2173 0.2356 REMARK 3 3 6.1500 - 5.3700 1.00 2821 137 0.2138 0.2588 REMARK 3 4 5.3700 - 4.8800 1.00 2751 153 0.1825 0.1763 REMARK 3 5 4.8800 - 4.5300 1.00 2790 132 0.1718 0.2065 REMARK 3 6 4.5300 - 4.2600 1.00 2810 128 0.1854 0.2815 REMARK 3 7 4.2600 - 4.0500 1.00 2813 129 0.2146 0.2659 REMARK 3 8 4.0500 - 3.8700 1.00 2786 157 0.2268 0.3140 REMARK 3 9 3.8700 - 3.7200 1.00 2793 128 0.2523 0.2815 REMARK 3 10 3.7200 - 3.6000 1.00 2814 150 0.2555 0.2890 REMARK 3 11 3.6000 - 3.4800 1.00 2801 143 0.2549 0.3370 REMARK 3 12 3.4800 - 3.3800 1.00 2788 130 0.2910 0.3633 REMARK 3 13 3.3800 - 3.3000 1.00 2782 176 0.2953 0.3547 REMARK 3 14 3.3000 - 3.2100 1.00 2786 143 0.3170 0.3316 REMARK 3 15 3.2100 - 3.1400 1.00 2713 158 0.2951 0.3366 REMARK 3 16 3.1400 - 3.0800 1.00 2817 136 0.3143 0.3848 REMARK 3 17 3.0700 - 3.0100 1.00 2814 157 0.3347 0.3767 REMARK 3 18 3.0100 - 2.9600 1.00 2759 124 0.3394 0.3598 REMARK 3 19 2.9600 - 2.9000 1.00 2823 140 0.3531 0.4249 REMARK 3 20 2.9000 - 2.8500 1.00 2798 137 0.3906 0.4266 REMARK 3 21 2.8500 - 2.8100 1.00 2778 160 0.4018 0.3994 REMARK 3 22 2.8100 - 2.7700 1.00 2819 122 0.4006 0.4572 REMARK 3 23 2.7700 - 2.7200 1.00 2726 133 0.3724 0.4454 REMARK 3 24 2.7200 - 2.6900 1.00 2819 155 0.3747 0.3919 REMARK 3 25 2.6900 - 2.6500 1.00 2771 133 0.3851 0.3883 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) : 0.440 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.100 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 80.04 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 104.6 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 : 0.012 8268 REMARK 3 ANGLE : 1.563 11240 REMARK 3 CHIRALITY : 0.097 1256 REMARK 3 PLANARITY : 0.009 1443 REMARK 3 DIHEDRAL : 13.000 2982 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 29 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 31 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.0909 -0.0703 15.4694 REMARK 3 T TENSOR REMARK 3 T11: 0.6445 T22: 0.5685 REMARK 3 T33: 0.7735 T12: -0.1406 REMARK 3 T13: -0.0595 T23: 0.0726 REMARK 3 L TENSOR REMARK 3 L11: 5.0135 L22: 7.8597 REMARK 3 L33: 4.2681 L12: -0.5094 REMARK 3 L13: -0.1678 L23: -2.4522 REMARK 3 S TENSOR REMARK 3 S11: 0.1195 S12: 0.1396 S13: 0.6044 REMARK 3 S21: 0.5796 S22: -0.1036 S23: -0.8216 REMARK 3 S31: -0.2769 S32: 0.3467 S33: -0.0313 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9636 -2.7772 19.6335 REMARK 3 T TENSOR REMARK 3 T11: 1.1704 T22: 0.7498 REMARK 3 T33: 0.5637 T12: -0.2020 REMARK 3 T13: -0.0580 T23: 0.0767 REMARK 3 L TENSOR REMARK 3 L11: 3.7556 L22: 4.2883 REMARK 3 L33: 2.7136 L12: -0.2274 REMARK 3 L13: 1.4015 L23: -1.5266 REMARK 3 S TENSOR REMARK 3 S11: 0.3308 S12: -0.3493 S13: 0.3894 REMARK 3 S21: 0.7898 S22: 0.1901 S23: 0.1503 REMARK 3 S31: 0.2913 S32: -0.3739 S33: -0.5739 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 132 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.2186 -29.4846 22.7668 REMARK 3 T TENSOR REMARK 3 T11: 1.3461 T22: 1.4053 REMARK 3 T33: 0.5997 T12: -0.6860 REMARK 3 T13: 0.1035 T23: 0.1395 REMARK 3 L TENSOR REMARK 3 L11: 3.4713 L22: 0.6235 REMARK 3 L33: 7.5421 L12: -0.6003 REMARK 3 L13: 0.3611 L23: 2.0321 REMARK 3 S TENSOR REMARK 3 S11: -0.8849 S12: 0.6124 S13: 0.1880 REMARK 3 S21: -1.9473 S22: 0.3186 S23: -0.9606 REMARK 3 S31: -2.9126 S32: 1.3347 S33: 0.2743 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.6381 -33.4347 19.4914 REMARK 3 T TENSOR REMARK 3 T11: 1.1057 T22: 2.1874 REMARK 3 T33: 0.8513 T12: -0.9257 REMARK 3 T13: 0.6960 T23: -0.2346 REMARK 3 L TENSOR REMARK 3 L11: 0.9182 L22: 3.1167 REMARK 3 L33: 2.4661 L12: -0.6682 REMARK 3 L13: 1.3462 L23: -0.4361 REMARK 3 S TENSOR REMARK 3 S11: -0.0939 S12: 1.3307 S13: 0.4988 REMARK 3 S21: -1.1096 S22: 0.3855 S23: -2.3808 REMARK 3 S31: -1.0079 S32: 2.6005 S33: -0.0794 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.0566 -20.8876 11.3678 REMARK 3 T TENSOR REMARK 3 T11: 1.5664 T22: 0.8583 REMARK 3 T33: 0.6381 T12: -0.2638 REMARK 3 T13: -0.4487 T23: 0.2827 REMARK 3 L TENSOR REMARK 3 L11: 3.7145 L22: 7.5963 REMARK 3 L33: 1.8690 L12: 2.2128 REMARK 3 L13: -0.6401 L23: 2.3900 REMARK 3 S TENSOR REMARK 3 S11: 0.3502 S12: 0.3465 S13: -0.1577 REMARK 3 S21: 0.2624 S22: 0.2999 S23: 1.8953 REMARK 3 S31: 0.6917 S32: -0.3581 S33: -0.4125 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5688 -22.2248 11.7649 REMARK 3 T TENSOR REMARK 3 T11: 1.0216 T22: 0.8124 REMARK 3 T33: 0.5643 T12: -0.1407 REMARK 3 T13: -0.2706 T23: 0.0438 REMARK 3 L TENSOR REMARK 3 L11: 3.1186 L22: 5.9656 REMARK 3 L33: 1.4681 L12: -2.8049 REMARK 3 L13: 1.1001 L23: -3.2731 REMARK 3 S TENSOR REMARK 3 S11: 0.4006 S12: 0.3061 S13: -0.0553 REMARK 3 S21: -1.1644 S22: 0.2039 S23: 0.6458 REMARK 3 S31: 0.1728 S32: 0.2078 S33: -0.5130 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 130 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.9674 -40.8085 28.4030 REMARK 3 T TENSOR REMARK 3 T11: 0.3544 T22: 0.6316 REMARK 3 T33: 0.5197 T12: -0.0245 REMARK 3 T13: -0.0547 T23: 0.0342 REMARK 3 L TENSOR REMARK 3 L11: 3.8746 L22: 8.5719 REMARK 3 L33: 7.5068 L12: 1.0633 REMARK 3 L13: -0.7547 L23: 3.0862 REMARK 3 S TENSOR REMARK 3 S11: -0.2825 S12: -0.0610 S13: -0.2747 REMARK 3 S21: -0.6377 S22: 0.2197 S23: -0.0957 REMARK 3 S31: -0.1510 S32: 0.6616 S33: 0.1216 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.7751 -16.8492 49.5445 REMARK 3 T TENSOR REMARK 3 T11: 0.4922 T22: 0.6235 REMARK 3 T33: 1.1043 T12: 0.0237 REMARK 3 T13: -0.2849 T23: -0.1117 REMARK 3 L TENSOR REMARK 3 L11: 2.4200 L22: 2.1268 REMARK 3 L33: 4.2961 L12: -1.1187 REMARK 3 L13: -1.6974 L23: 0.6896 REMARK 3 S TENSOR REMARK 3 S11: -0.4395 S12: -0.2421 S13: 0.5418 REMARK 3 S21: 0.3797 S22: 0.3719 S23: 0.3195 REMARK 3 S31: -0.4647 S32: -0.3569 S33: -0.1743 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2099 -14.3197 54.0262 REMARK 3 T TENSOR REMARK 3 T11: 0.7425 T22: 0.5585 REMARK 3 T33: 1.1095 T12: 0.0612 REMARK 3 T13: -0.2926 T23: -0.1649 REMARK 3 L TENSOR REMARK 3 L11: 3.1991 L22: 4.3957 REMARK 3 L33: 4.3329 L12: -1.2867 REMARK 3 L13: 2.4581 L23: -1.9911 REMARK 3 S TENSOR REMARK 3 S11: -0.6111 S12: -0.3254 S13: 1.1672 REMARK 3 S21: 0.9168 S22: 0.2759 S23: -0.9003 REMARK 3 S31: -0.9962 S32: 0.2865 S33: 0.3263 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 87 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.1026 -19.7399 48.1562 REMARK 3 T TENSOR REMARK 3 T11: 0.5051 T22: 0.4577 REMARK 3 T33: 1.0223 T12: 0.0146 REMARK 3 T13: -0.0449 T23: -0.1225 REMARK 3 L TENSOR REMARK 3 L11: 4.6937 L22: 3.4332 REMARK 3 L33: 5.0170 L12: -1.2440 REMARK 3 L13: 2.0165 L23: 0.4174 REMARK 3 S TENSOR REMARK 3 S11: -0.0208 S12: 0.1958 S13: 0.7545 REMARK 3 S21: 0.1921 S22: 0.0104 S23: -0.1029 REMARK 3 S31: -0.2524 S32: 0.1460 S33: -0.0542 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 132 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.2184 -38.7835 22.8735 REMARK 3 T TENSOR REMARK 3 T11: 0.7454 T22: 0.8640 REMARK 3 T33: 1.2252 T12: -0.0151 REMARK 3 T13: -0.2121 T23: 0.0537 REMARK 3 L TENSOR REMARK 3 L11: 6.8369 L22: 2.7552 REMARK 3 L33: 5.4833 L12: -0.9226 REMARK 3 L13: 0.0177 L23: -3.8228 REMARK 3 S TENSOR REMARK 3 S11: -0.8621 S12: -0.2428 S13: -0.4054 REMARK 3 S21: -1.0154 S22: 0.8560 S23: 2.5898 REMARK 3 S31: 0.3635 S32: -0.6425 S33: 0.0556 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 156 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0684 -30.6506 32.5362 REMARK 3 T TENSOR REMARK 3 T11: 0.6162 T22: 0.8194 REMARK 3 T33: 1.1176 T12: 0.0371 REMARK 3 T13: -0.0873 T23: 0.3233 REMARK 3 L TENSOR REMARK 3 L11: 2.5783 L22: 1.7788 REMARK 3 L33: 2.4531 L12: -1.1137 REMARK 3 L13: -2.1869 L23: 1.6866 REMARK 3 S TENSOR REMARK 3 S11: -0.2816 S12: 0.1228 S13: 0.2891 REMARK 3 S21: 0.5598 S22: 0.5175 S23: 0.5081 REMARK 3 S31: -0.0436 S32: -0.6427 S33: -0.2126 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 190 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.0957 -39.1567 30.9000 REMARK 3 T TENSOR REMARK 3 T11: 0.7457 T22: 0.8758 REMARK 3 T33: 1.3248 T12: -0.1241 REMARK 3 T13: 0.0010 T23: 0.2772 REMARK 3 L TENSOR REMARK 3 L11: 7.4079 L22: 7.6731 REMARK 3 L33: 8.5367 L12: 1.0101 REMARK 3 L13: -0.8846 L23: 1.8853 REMARK 3 S TENSOR REMARK 3 S11: 0.3640 S12: -0.1778 S13: -1.7545 REMARK 3 S21: 1.0691 S22: -0.2033 S23: 0.7218 REMARK 3 S31: 1.6264 S32: -1.3175 S33: -0.1684 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 216 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.4341 -35.0236 26.4859 REMARK 3 T TENSOR REMARK 3 T11: 0.6963 T22: 1.1625 REMARK 3 T33: 1.4275 T12: 0.0314 REMARK 3 T13: -0.0337 T23: 0.1376 REMARK 3 L TENSOR REMARK 3 L11: 3.0877 L22: 2.9336 REMARK 3 L33: 6.0224 L12: -0.2650 REMARK 3 L13: 0.1726 L23: -0.6524 REMARK 3 S TENSOR REMARK 3 S11: 0.4518 S12: 0.8248 S13: 0.8773 REMARK 3 S21: -0.2415 S22: -0.1453 S23: -0.4894 REMARK 3 S31: -0.7434 S32: -1.4817 S33: -0.0948 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 6 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6544 -33.6329 45.0758 REMARK 3 T TENSOR REMARK 3 T11: 0.5798 T22: 0.4849 REMARK 3 T33: 0.7156 T12: -0.0299 REMARK 3 T13: -0.0817 T23: 0.0094 REMARK 3 L TENSOR REMARK 3 L11: 6.2397 L22: 5.8002 REMARK 3 L33: 5.7230 L12: -2.5597 REMARK 3 L13: 0.7998 L23: 2.5668 REMARK 3 S TENSOR REMARK 3 S11: -0.1430 S12: 0.0305 S13: 1.1320 REMARK 3 S21: 0.0051 S22: 0.2040 S23: -0.4030 REMARK 3 S31: -0.6923 S32: 0.6135 S33: -0.0743 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 50 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1759 -35.5084 41.2869 REMARK 3 T TENSOR REMARK 3 T11: 0.3362 T22: 0.3794 REMARK 3 T33: 0.6892 T12: -0.0674 REMARK 3 T13: -0.0238 T23: 0.0546 REMARK 3 L TENSOR REMARK 3 L11: 2.3205 L22: 2.9293 REMARK 3 L33: 4.1341 L12: -0.9390 REMARK 3 L13: 1.4179 L23: -0.0311 REMARK 3 S TENSOR REMARK 3 S11: -0.2255 S12: 0.2286 S13: 0.7292 REMARK 3 S21: 0.0868 S22: 0.1231 S23: -0.0583 REMARK 3 S31: -0.1543 S32: 0.3019 S33: 0.1055 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.2674 -36.1787 17.3662 REMARK 3 T TENSOR REMARK 3 T11: 0.8811 T22: 0.6646 REMARK 3 T33: 1.0867 T12: -0.2507 REMARK 3 T13: -0.4744 T23: 0.1128 REMARK 3 L TENSOR REMARK 3 L11: 2.5568 L22: 3.2084 REMARK 3 L33: 2.8010 L12: -1.4978 REMARK 3 L13: -0.6822 L23: 0.1263 REMARK 3 S TENSOR REMARK 3 S11: -0.0166 S12: 0.6200 S13: -0.2609 REMARK 3 S21: -0.8784 S22: 0.0582 S23: 0.9765 REMARK 3 S31: -0.2115 S32: -0.0073 S33: -0.0621 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 29 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.7379 -27.6923 81.3272 REMARK 3 T TENSOR REMARK 3 T11: 1.0895 T22: 0.8519 REMARK 3 T33: 1.5482 T12: -0.0361 REMARK 3 T13: 0.1133 T23: -0.3549 REMARK 3 L TENSOR REMARK 3 L11: 3.1350 L22: 7.8621 REMARK 3 L33: 6.3127 L12: 0.6485 REMARK 3 L13: 0.7412 L23: -6.7398 REMARK 3 S TENSOR REMARK 3 S11: -0.8771 S12: 0.3716 S13: -1.9690 REMARK 3 S21: 1.2905 S22: -0.4070 S23: -1.9715 REMARK 3 S31: 1.0629 S32: -0.2903 S33: 1.0693 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 37 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0319 -28.6171 84.8488 REMARK 3 T TENSOR REMARK 3 T11: 0.9013 T22: 0.9032 REMARK 3 T33: 1.6096 T12: -0.0503 REMARK 3 T13: -0.0035 T23: -0.2622 REMARK 3 L TENSOR REMARK 3 L11: 7.8468 L22: 8.4229 REMARK 3 L33: 3.1800 L12: 0.3173 REMARK 3 L13: -1.3574 L23: -4.6899 REMARK 3 S TENSOR REMARK 3 S11: -1.1387 S12: -0.5833 S13: -2.3318 REMARK 3 S21: -0.2438 S22: 0.0731 S23: -0.1805 REMARK 3 S31: 0.9696 S32: -1.6016 S33: 0.8461 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 50 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5450 -16.8505 77.5943 REMARK 3 T TENSOR REMARK 3 T11: 0.8020 T22: 0.7442 REMARK 3 T33: 1.0981 T12: -0.0904 REMARK 3 T13: -0.1226 T23: -0.2830 REMARK 3 L TENSOR REMARK 3 L11: 1.9258 L22: 2.8750 REMARK 3 L33: 5.7297 L12: -0.9251 REMARK 3 L13: -0.0874 L23: -0.2650 REMARK 3 S TENSOR REMARK 3 S11: 0.0786 S12: 0.0884 S13: -0.3731 REMARK 3 S21: -0.3497 S22: -0.2312 S23: -0.0165 REMARK 3 S31: 0.3851 S32: -0.0340 S33: 0.1115 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 92 THROUGH 100 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3766 -24.9633 90.2551 REMARK 3 T TENSOR REMARK 3 T11: 0.8606 T22: 1.2828 REMARK 3 T33: 1.3660 T12: -0.1826 REMARK 3 T13: 0.0929 T23: -0.2269 REMARK 3 L TENSOR REMARK 3 L11: 4.6246 L22: 4.8121 REMARK 3 L33: 9.1704 L12: 1.2468 REMARK 3 L13: 2.8646 L23: -0.2035 REMARK 3 S TENSOR REMARK 3 S11: 0.0704 S12: -1.1310 S13: -1.1731 REMARK 3 S21: 0.6328 S22: -0.5676 S23: 1.2320 REMARK 3 S31: 0.4630 S32: -2.1504 S33: 0.6285 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 101 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9043 -12.3679 75.0998 REMARK 3 T TENSOR REMARK 3 T11: 0.9001 T22: 0.8760 REMARK 3 T33: 1.3102 T12: 0.1445 REMARK 3 T13: -0.5213 T23: -0.5350 REMARK 3 L TENSOR REMARK 3 L11: 3.9925 L22: 7.6428 REMARK 3 L33: 8.0939 L12: 5.5123 REMARK 3 L13: -5.6714 L23: -7.8516 REMARK 3 S TENSOR REMARK 3 S11: 0.6438 S12: 0.2590 S13: 0.7910 REMARK 3 S21: 0.1263 S22: 0.7326 S23: 1.6426 REMARK 3 S31: -1.7550 S32: -0.2655 S33: 0.5920 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 116 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3571 -25.6684 88.1475 REMARK 3 T TENSOR REMARK 3 T11: 0.7033 T22: 0.8652 REMARK 3 T33: 1.4731 T12: -0.0337 REMARK 3 T13: -0.1951 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 2.9376 L22: 7.1703 REMARK 3 L33: 2.4526 L12: -0.0195 REMARK 3 L13: -0.4925 L23: -4.1290 REMARK 3 S TENSOR REMARK 3 S11: -0.1959 S12: -0.6069 S13: -1.6493 REMARK 3 S21: 0.4944 S22: -0.3122 S23: -1.0416 REMARK 3 S31: -0.3207 S32: 1.1581 S33: 0.4177 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 29 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.9065 10.5550 -9.0164 REMARK 3 T TENSOR REMARK 3 T11: 1.1562 T22: 0.9711 REMARK 3 T33: 1.0856 T12: -0.2236 REMARK 3 T13: -0.1086 T23: 0.3883 REMARK 3 L TENSOR REMARK 3 L11: 6.8049 L22: 3.0205 REMARK 3 L33: 2.9300 L12: -1.5282 REMARK 3 L13: 3.4754 L23: -2.5072 REMARK 3 S TENSOR REMARK 3 S11: 0.1363 S12: 0.7999 S13: -0.6811 REMARK 3 S21: 0.2039 S22: -0.0331 S23: 1.2602 REMARK 3 S31: 1.8031 S32: -0.4998 S33: -0.0097 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 45 THROUGH 69 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1274 12.7987 -6.1885 REMARK 3 T TENSOR REMARK 3 T11: 1.0935 T22: 1.1840 REMARK 3 T33: 1.5742 T12: -0.2555 REMARK 3 T13: 0.2514 T23: 0.8957 REMARK 3 L TENSOR REMARK 3 L11: 5.6512 L22: 2.1587 REMARK 3 L33: 0.3562 L12: -0.4502 REMARK 3 L13: 1.1296 L23: 0.4343 REMARK 3 S TENSOR REMARK 3 S11: 0.3816 S12: 0.6384 S13: -0.3820 REMARK 3 S21: -0.6340 S22: 1.4961 S23: 1.4288 REMARK 3 S31: 1.0905 S32: -1.9790 S33: 0.5138 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 70 THROUGH 80 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.9889 12.6804 8.5019 REMARK 3 T TENSOR REMARK 3 T11: 1.0450 T22: 1.4504 REMARK 3 T33: 1.6145 T12: -0.0096 REMARK 3 T13: 0.4368 T23: 0.4151 REMARK 3 L TENSOR REMARK 3 L11: 2.4290 L22: 3.8516 REMARK 3 L33: 3.5080 L12: -2.9474 REMARK 3 L13: 2.8681 L23: -3.2746 REMARK 3 S TENSOR REMARK 3 S11: -0.0315 S12: -0.6945 S13: 0.4998 REMARK 3 S21: 0.4965 S22: 0.1049 S23: -0.0917 REMARK 3 S31: -0.8487 S32: -1.2889 S33: -0.4790 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 81 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.3590 24.0578 -7.4952 REMARK 3 T TENSOR REMARK 3 T11: 1.2623 T22: 1.2958 REMARK 3 T33: 2.1432 T12: 0.1403 REMARK 3 T13: 0.2491 T23: 0.9585 REMARK 3 L TENSOR REMARK 3 L11: 6.3813 L22: 3.3904 REMARK 3 L33: 7.6640 L12: -3.9840 REMARK 3 L13: -3.8608 L23: 4.5964 REMARK 3 S TENSOR REMARK 3 S11: 1.0777 S12: 1.2539 S13: 1.3993 REMARK 3 S21: 0.3057 S22: 0.3458 S23: 1.2492 REMARK 3 S31: -3.3816 S32: -0.8409 S33: -0.5826 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 92 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6553 17.8455 -2.5201 REMARK 3 T TENSOR REMARK 3 T11: 0.8811 T22: 0.9614 REMARK 3 T33: 0.9875 T12: 0.1925 REMARK 3 T13: 0.1615 T23: 0.2646 REMARK 3 L TENSOR REMARK 3 L11: 6.5851 L22: 8.2005 REMARK 3 L33: 3.3028 L12: 4.1175 REMARK 3 L13: -0.6533 L23: 0.1913 REMARK 3 S TENSOR REMARK 3 S11: 1.1794 S12: 0.1663 S13: 1.2898 REMARK 3 S21: 0.8548 S22: -0.2285 S23: 0.1156 REMARK 3 S31: -1.3888 S32: -0.1420 S33: -0.9933 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 116 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9994 17.3905 -15.7693 REMARK 3 T TENSOR REMARK 3 T11: 0.9062 T22: 1.3458 REMARK 3 T33: 1.3326 T12: 0.1051 REMARK 3 T13: 0.0897 T23: 0.5793 REMARK 3 L TENSOR REMARK 3 L11: 3.7932 L22: 3.4604 REMARK 3 L33: 6.2792 L12: -1.2304 REMARK 3 L13: 3.8407 L23: 1.4551 REMARK 3 S TENSOR REMARK 3 S11: 0.1095 S12: 0.6991 S13: -0.5941 REMARK 3 S21: -0.2877 S22: -0.8049 S23: 0.6320 REMARK 3 S31: -0.3115 S32: 0.5923 S33: 0.1249 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 8DJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-22. REMARK 100 THE DEPOSITION ID IS D_1000266795. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUN-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56710 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330 REMARK 200 RESOLUTION RANGE LOW (A) : 47.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.03800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 7.31000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: 6VHH, 4XWO REMARK 200 REMARK 200 REMARK: TETRAGONAL BIPYRAMIDS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 150 MM AMMONIUM REMARK 280 SULFATE, 20% PEG 4000, PH 4.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 296K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.89950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.52900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.92450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.52900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.89950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.92450 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24350 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 141 REMARK 465 SER A 142 REMARK 465 THR A 143 REMARK 465 SER A 144 REMARK 465 GLY A 145 REMARK 465 GLY A 146 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 THR A 231 REMARK 465 HIS A 232 REMARK 465 THR A 233 REMARK 465 SER B 1 REMARK 465 ASP B 2 REMARK 465 ILE B 3 REMARK 465 GLN B 4 REMARK 465 MET B 5 REMARK 465 GLN B 28 REMARK 465 SER B 29 REMARK 465 VAL B 30 REMARK 465 GLU C 1 REMARK 465 ILE C 2 REMARK 465 SER C 3 REMARK 465 LYS C 141 REMARK 465 SER C 142 REMARK 465 ASP C 229 REMARK 465 LYS C 230 REMARK 465 THR C 231 REMARK 465 HIS C 232 REMARK 465 THR C 233 REMARK 465 SER D 1 REMARK 465 ASP D 2 REMARK 465 ILE D 3 REMARK 465 GLN D 4 REMARK 465 MET D 5 REMARK 465 PRO E 24 REMARK 465 ILE E 25 REMARK 465 PRO E 26 REMARK 465 MET E 27 REMARK 465 ALA E 28 REMARK 465 HIS E 127 REMARK 465 HIS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 HIS E 132 REMARK 465 PRO F 24 REMARK 465 ILE F 25 REMARK 465 PRO F 26 REMARK 465 MET F 27 REMARK 465 ALA F 28 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS D 195 CA - CB - SG ANGL. DEV. = 9.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 34 33.67 -98.47 REMARK 500 ALA A 95 155.50 176.71 REMARK 500 MET A 109 43.68 38.69 REMARK 500 ASP A 156 72.42 60.40 REMARK 500 ALA B 52 -40.91 71.91 REMARK 500 ALA B 85 -164.07 -163.52 REMARK 500 THR B 94 -128.05 44.54 REMARK 500 ASN B 139 69.74 66.21 REMARK 500 THR B 173 -164.06 -102.62 REMARK 500 LYS B 191 -54.94 -131.84 REMARK 500 TYR C 34 49.86 -91.66 REMARK 500 ALA C 95 164.64 178.76 REMARK 500 ASP C 220 75.99 -115.62 REMARK 500 SER D 31 -122.52 45.95 REMARK 500 ALA D 33 43.50 -80.26 REMARK 500 ALA D 52 -40.72 72.29 REMARK 500 ALA D 85 -165.34 -164.43 REMARK 500 LEU D 96 139.79 -174.35 REMARK 500 ASN D 139 68.15 63.02 REMARK 500 GLU D 144 99.75 -66.94 REMARK 500 ASP D 152 47.52 38.04 REMARK 500 GLU D 214 -131.38 45.85 REMARK 500 CYS E 66 78.71 56.67 REMARK 500 CYS E 110 80.82 -155.03 REMARK 500 SER F 38 -6.59 78.47 REMARK 500 THR F 48 65.36 -105.58 REMARK 500 CYS F 66 76.86 63.64 REMARK 500 SER F 68 -167.64 -160.18 REMARK 500 VAL F 105 -73.39 -115.51 REMARK 500 PRO F 107 -156.00 -84.07 REMARK 500 REMARK 500 REMARK: NULL DBREF 8DJG A 1 233 PDB 8DJG 8DJG 1 233 DBREF 8DJG B 1 215 PDB 8DJG 8DJG 1 215 DBREF 8DJG C 1 233 PDB 8DJG 8DJG 1 233 DBREF 8DJG D 1 215 PDB 8DJG 8DJG 1 215 DBREF 8DJG E 24 126 UNP Q9HAR2 AGRL3_HUMAN 24 126 DBREF 8DJG F 24 126 UNP Q9HAR2 AGRL3_HUMAN 24 126 SEQADV 8DJG HIS E 127 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS E 128 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS E 129 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS E 130 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS E 131 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS E 132 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 127 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 128 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 129 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 130 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 131 UNP Q9HAR2 EXPRESSION TAG SEQADV 8DJG HIS F 132 UNP Q9HAR2 EXPRESSION TAG SEQRES 1 A 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 A 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 A 233 ALA SER GLY PHE ASN ILE TYR TYR SER SER ILE HIS TRP SEQRES 4 A 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 A 233 TYR ILE SER PRO TYR SER GLY SER THR SER TYR ALA ASP SEQRES 6 A 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 A 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 A 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TYR LYS TYR SEQRES 9 A 233 GLY GLN GLY HIS MET GLY ALA PHE ASP TYR TRP GLY GLN SEQRES 10 A 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 B 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 B 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 B 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 B 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 B 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 B 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 B 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 B 215 SER ASN THR GLU LEU VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 C 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 C 233 ALA SER GLY PHE ASN ILE TYR TYR SER SER ILE HIS TRP SEQRES 4 C 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 C 233 TYR ILE SER PRO TYR SER GLY SER THR SER TYR ALA ASP SEQRES 6 C 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 C 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 C 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TYR LYS TYR SEQRES 9 C 233 GLY GLN GLY HIS MET GLY ALA PHE ASP TYR TRP GLY GLN SEQRES 10 C 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 C 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 C 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 C 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 C 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 C 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 C 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 C 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 C 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 D 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 D 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 D 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 D 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 D 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 D 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 D 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 D 215 SER ASN THR GLU LEU VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 109 PRO ILE PRO MET ALA VAL VAL ARG ARG GLU LEU SER CYS SEQRES 2 E 109 GLU SER TYR PRO ILE GLU LEU ARG CYS PRO GLY THR ASP SEQRES 3 E 109 VAL ILE MET ILE GLU SER ALA ASN TYR GLY ARG THR ASP SEQRES 4 E 109 ASP LYS ILE CYS ASP SER ASP PRO ALA GLN MET GLU ASN SEQRES 5 E 109 ILE ARG CYS TYR LEU PRO ASP ALA TYR LYS ILE MET SER SEQRES 6 E 109 GLN ARG CYS ASN ASN ARG THR GLN CYS ALA VAL VAL ALA SEQRES 7 E 109 GLY PRO ASP VAL PHE PRO ASP PRO CYS PRO GLY THR TYR SEQRES 8 E 109 LYS TYR LEU GLU VAL GLN TYR GLU CYS VAL PRO TYR HIS SEQRES 9 E 109 HIS HIS HIS HIS HIS SEQRES 1 F 109 PRO ILE PRO MET ALA VAL VAL ARG ARG GLU LEU SER CYS SEQRES 2 F 109 GLU SER TYR PRO ILE GLU LEU ARG CYS PRO GLY THR ASP SEQRES 3 F 109 VAL ILE MET ILE GLU SER ALA ASN TYR GLY ARG THR ASP SEQRES 4 F 109 ASP LYS ILE CYS ASP SER ASP PRO ALA GLN MET GLU ASN SEQRES 5 F 109 ILE ARG CYS TYR LEU PRO ASP ALA TYR LYS ILE MET SER SEQRES 6 F 109 GLN ARG CYS ASN ASN ARG THR GLN CYS ALA VAL VAL ALA SEQRES 7 F 109 GLY PRO ASP VAL PHE PRO ASP PRO CYS PRO GLY THR TYR SEQRES 8 F 109 LYS TYR LEU GLU VAL GLN TYR GLU CYS VAL PRO TYR HIS SEQRES 9 F 109 HIS HIS HIS HIS HIS HET SO4 A 301 5 HET SO4 C 301 5 HET GOL D 301 6 HET GOL D 302 6 HET PEG D 303 7 HET SO4 D 304 5 HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 SO4 3(O4 S 2-) FORMUL 9 GOL 2(C3 H8 O3) FORMUL 11 PEG C4 H10 O3 FORMUL 13 HOH *7(H2 O) HELIX 1 AA1 ASN A 31 TYR A 33 5 3 HELIX 2 AA2 THR A 77 LYS A 79 5 3 HELIX 3 AA3 ARG A 90 THR A 94 5 5 HELIX 4 AA4 SER A 168 ALA A 170 5 3 HELIX 5 AA5 GLN B 80 PHE B 84 5 5 HELIX 6 AA6 SER B 122 GLY B 129 1 8 HELIX 7 AA7 LYS B 184 GLU B 188 1 5 HELIX 8 AA8 ASN C 31 SER C 35 5 5 HELIX 9 AA9 ARG C 90 THR C 94 5 5 HELIX 10 AB1 SER C 168 ALA C 170 5 3 HELIX 11 AB2 SER C 199 LEU C 201 5 3 HELIX 12 AB3 LYS C 213 ASN C 216 5 4 HELIX 13 AB4 GLN D 80 PHE D 84 5 5 HELIX 14 AB5 SER D 122 SER D 128 1 7 HELIX 15 AB6 LYS D 184 GLU D 188 1 5 HELIX 16 AB7 ASP E 69 GLU E 74 5 6 HELIX 17 AB8 ASP E 82 ASN E 92 1 11 HELIX 18 AB9 ASP F 69 GLU F 74 5 6 HELIX 19 AC1 PRO F 81 ASN F 92 1 12 SHEET 1 AA1 4 GLN A 6 SER A 10 0 SHEET 2 AA1 4 SER A 20 SER A 28 -1 O SER A 24 N SER A 10 SHEET 3 AA1 4 THR A 81 ASN A 87 -1 O ALA A 82 N CYS A 25 SHEET 4 AA1 4 PHE A 71 ASP A 76 -1 N SER A 74 O TYR A 83 SHEET 1 AA2 6 GLY A 13 VAL A 15 0 SHEET 2 AA2 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 15 SHEET 3 AA2 6 ALA A 95 LYS A 103 -1 N TYR A 97 O THR A 119 SHEET 4 AA2 6 SER A 35 GLN A 42 -1 N VAL A 40 O TYR A 98 SHEET 5 AA2 6 LEU A 48 ILE A 54 -1 O GLU A 49 N ARG A 41 SHEET 6 AA2 6 THR A 61 TYR A 63 -1 O SER A 62 N TYR A 53 SHEET 1 AA3 4 SER A 132 LEU A 136 0 SHEET 2 AA3 4 ALA A 148 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA3 4 TYR A 188 VAL A 196 -1 O VAL A 196 N ALA A 148 SHEET 4 AA3 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AA4 4 SER A 132 LEU A 136 0 SHEET 2 AA4 4 ALA A 148 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA4 4 TYR A 188 VAL A 196 -1 O VAL A 196 N ALA A 148 SHEET 4 AA4 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AA5 3 THR A 163 TRP A 166 0 SHEET 2 AA5 3 ILE A 207 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AA5 3 THR A 217 LYS A 222 -1 O VAL A 219 N VAL A 210 SHEET 1 AA6 6 SER B 10 ALA B 14 0 SHEET 2 AA6 6 THR B 103 ILE B 107 1 O LYS B 104 N SER B 10 SHEET 3 AA6 6 THR B 86 SER B 92 -1 N TYR B 87 O THR B 103 SHEET 4 AA6 6 VAL B 34 GLN B 39 -1 N TYR B 37 O TYR B 88 SHEET 5 AA6 6 LYS B 46 TYR B 50 -1 O ILE B 49 N TRP B 36 SHEET 6 AA6 6 SER B 54 LEU B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AA7 4 SER B 10 ALA B 14 0 SHEET 2 AA7 4 THR B 103 ILE B 107 1 O LYS B 104 N SER B 10 SHEET 3 AA7 4 THR B 86 SER B 92 -1 N TYR B 87 O THR B 103 SHEET 4 AA7 4 VAL B 97 PHE B 99 -1 O THR B 98 N GLN B 91 SHEET 1 AA8 7 PHE B 63 SER B 68 0 SHEET 2 AA8 7 ASP B 71 ILE B 76 -1 O THR B 75 N SER B 64 SHEET 3 AA8 7 VAL B 20 THR B 23 -1 N ILE B 22 O LEU B 74 SHEET 4 AA8 7 LEU D 155 SER D 157 1 O SER D 157 N THR B 23 SHEET 5 AA8 7 ALA D 145 VAL D 151 -1 N TRP D 149 O GLN D 156 SHEET 6 AA8 7 VAL D 192 HIS D 199 -1 O GLU D 196 N GLN D 148 SHEET 7 AA8 7 VAL D 206 ASN D 211 -1 O PHE D 210 N TYR D 193 SHEET 1 AA9 4 SER B 115 PHE B 119 0 SHEET 2 AA9 4 THR B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AA9 4 TYR B 174 SER B 183 -1 O LEU B 182 N ALA B 131 SHEET 4 AA9 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AB1 7 VAL B 206 ASN B 211 0 SHEET 2 AB1 7 VAL B 192 THR B 198 -1 N VAL B 197 O VAL B 206 SHEET 3 AB1 7 LYS B 146 VAL B 151 -1 N GLN B 148 O GLU B 196 SHEET 4 AB1 7 ALA B 154 SER B 157 -1 O GLN B 156 N TRP B 149 SHEET 5 AB1 7 ARG D 19 THR D 23 1 O ARG D 19 N LEU B 155 SHEET 6 AB1 7 ASP D 71 ILE D 76 -1 O LEU D 74 N ILE D 22 SHEET 7 AB1 7 PHE D 63 SER D 68 -1 N SER D 68 O ASP D 71 SHEET 1 AB2 4 GLN C 6 SER C 10 0 SHEET 2 AB2 4 LEU C 21 SER C 28 -1 O SER C 24 N SER C 10 SHEET 3 AB2 4 THR C 81 MET C 86 -1 O MET C 86 N LEU C 21 SHEET 4 AB2 4 PHE C 71 ASP C 76 -1 N ASP C 76 O THR C 81 SHEET 1 AB3 6 LEU C 14 VAL C 15 0 SHEET 2 AB3 6 THR C 119 VAL C 123 1 O THR C 122 N VAL C 15 SHEET 3 AB3 6 ALA C 95 ALA C 100 -1 N ALA C 95 O VAL C 121 SHEET 4 AB3 6 ILE C 37 GLN C 42 -1 N VAL C 40 O TYR C 98 SHEET 5 AB3 6 LEU C 48 ILE C 54 -1 O VAL C 51 N TRP C 39 SHEET 6 AB3 6 THR C 61 TYR C 63 -1 O SER C 62 N TYR C 53 SHEET 1 AB4 4 SER C 132 LEU C 136 0 SHEET 2 AB4 4 THR C 147 TYR C 157 -1 O LYS C 155 N SER C 132 SHEET 3 AB4 4 TYR C 188 PRO C 197 -1 O VAL C 196 N ALA C 148 SHEET 4 AB4 4 VAL C 175 THR C 177 -1 N HIS C 176 O VAL C 193 SHEET 1 AB5 4 SER C 132 LEU C 136 0 SHEET 2 AB5 4 THR C 147 TYR C 157 -1 O LYS C 155 N SER C 132 SHEET 3 AB5 4 TYR C 188 PRO C 197 -1 O VAL C 196 N ALA C 148 SHEET 4 AB5 4 VAL C 181 LEU C 182 -1 N VAL C 181 O SER C 189 SHEET 1 AB6 3 THR C 163 TRP C 166 0 SHEET 2 AB6 3 CYS C 208 HIS C 212 -1 O ASN C 209 N SER C 165 SHEET 3 AB6 3 THR C 217 VAL C 219 -1 O VAL C 219 N VAL C 210 SHEET 1 AB7 6 SER D 10 ALA D 14 0 SHEET 2 AB7 6 THR D 103 ILE D 107 1 O LYS D 104 N SER D 10 SHEET 3 AB7 6 THR D 86 SER D 92 -1 N TYR D 87 O THR D 103 SHEET 4 AB7 6 VAL D 34 GLN D 39 -1 N TYR D 37 O TYR D 88 SHEET 5 AB7 6 LYS D 46 TYR D 50 -1 O LYS D 46 N GLN D 38 SHEET 6 AB7 6 SER D 54 LEU D 55 -1 O SER D 54 N TYR D 50 SHEET 1 AB8 4 SER D 10 ALA D 14 0 SHEET 2 AB8 4 THR D 103 ILE D 107 1 O LYS D 104 N SER D 10 SHEET 3 AB8 4 THR D 86 SER D 92 -1 N TYR D 87 O THR D 103 SHEET 4 AB8 4 VAL D 97 PHE D 99 -1 O THR D 98 N GLN D 91 SHEET 1 AB9 4 SER D 115 PHE D 119 0 SHEET 2 AB9 4 THR D 130 PHE D 140 -1 O ASN D 138 N SER D 115 SHEET 3 AB9 4 TYR D 174 SER D 183 -1 O LEU D 180 N VAL D 133 SHEET 4 AB9 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AC1 3 ARG E 31 CYS E 36 0 SHEET 2 AC1 3 TYR E 116 VAL E 124 -1 O TYR E 121 N ARG E 31 SHEET 3 AC1 3 VAL E 50 GLY E 59 -1 N VAL E 50 O VAL E 124 SHEET 1 AC2 2 PRO E 40 ARG E 44 0 SHEET 2 AC2 2 GLN E 96 VAL E 100 -1 O VAL E 99 N ILE E 41 SHEET 1 AC3 3 VAL F 30 CYS F 36 0 SHEET 2 AC3 3 TYR F 116 VAL F 124 -1 O TYR F 121 N ARG F 31 SHEET 3 AC3 3 VAL F 50 GLY F 59 -1 N VAL F 50 O VAL F 124 SHEET 1 AC4 2 PRO F 40 ARG F 44 0 SHEET 2 AC4 2 GLN F 96 VAL F 100 -1 O VAL F 99 N ILE F 41 SSBOND 1 CYS A 25 CYS A 99 1555 1555 2.04 SSBOND 2 CYS A 152 CYS A 208 1555 1555 2.03 SSBOND 3 CYS A 228 CYS B 215 1555 1555 2.08 SSBOND 4 CYS B 24 CYS B 89 1555 1555 2.04 SSBOND 5 CYS B 135 CYS B 195 1555 1555 2.04 SSBOND 6 CYS C 25 CYS C 99 1555 1555 2.07 SSBOND 7 CYS C 152 CYS C 208 1555 1555 2.02 SSBOND 8 CYS C 228 CYS D 215 1555 1555 2.23 SSBOND 9 CYS D 24 CYS D 89 1555 1555 2.04 SSBOND 10 CYS D 135 CYS D 195 1555 1555 2.03 SSBOND 11 CYS E 36 CYS E 66 1555 1555 2.03 SSBOND 12 CYS E 45 CYS E 123 1555 1555 2.02 SSBOND 13 CYS E 78 CYS E 110 1555 1555 2.03 SSBOND 14 CYS E 91 CYS E 97 1555 1555 2.02 SSBOND 15 CYS F 36 CYS F 66 1555 1555 2.03 SSBOND 16 CYS F 45 CYS F 123 1555 1555 2.02 SSBOND 17 CYS F 78 CYS F 110 1555 1555 2.01 SSBOND 18 CYS F 91 CYS F 97 1555 1555 2.02 CISPEP 1 PHE A 158 PRO A 159 0 -11.74 CISPEP 2 GLU A 160 PRO A 161 0 -5.08 CISPEP 3 TYR B 141 PRO B 142 0 15.52 CISPEP 4 PHE C 158 PRO C 159 0 -18.35 CISPEP 5 GLU C 160 PRO C 161 0 7.59 CISPEP 6 TYR D 141 PRO D 142 0 1.96 CRYST1 81.799 97.849 163.058 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012225 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010220 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006133 0.00000