HEADER IMMUNE SYSTEM 23-JUN-25 9P8X TITLE CRYSTAL STRUCTURE OF GITR IN COMPLEX WITH LIGAND-NON-COMPETITIVE AB#1 TITLE 2 FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: AB#1-FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: AB#1-FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 18; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: ACTIVATION-INDUCIBLE TNFR FAMILY RECEPTOR,GLUCOCORTICOID- COMPND 13 INDUCED TNFR-RELATED PROTEIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: TNFRSF18, AITR, GITR, UNQ319/PRO364; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS GITR, GITRL, GLUCOCORTICOID-INDUCED TNF RECEPTOR, TNFRSF18, TNFR, KEYWDS 2 TNF, TUMOR NECROSIS FACTOR RECEPTOR, ANTIBODY, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.-S.HUANG,L.MOSYAK,Z.MABEN REVDAT 1 31-DEC-25 9P8X 0 JRNL AUTH J.YAN,J.MIN-DEBARTOLO,C.S.HUANG,M.N.SHARIF,L.LI,S.FISH, JRNL AUTH 2 C.DOWER,D.MURPHY,T.ANDREYEVA,H.LIU,X.HAN,W.ZHENG,J.H.OOI, JRNL AUTH 3 J.EDMONDS,T.CHEN,Z.MABEN,C.R.STEVENS,P.GOIHBERG, JRNL AUTH 4 M.NOCULA-LUGOWSKA,S.M.EVANS,L.MOSYAK,K.KELLEHER,C.DICKINSON, JRNL AUTH 5 M.HEGEN,A.WINKLER,F.KARLSSON JRNL TITL LIGAND NON-COMPETITIVE GITR ANTIBODY PREVENTS FORMATION OF JRNL TITL 2 THE OBLIGATORY SIGNAL-TRIGGERING GITRL: GITR STOICHIOMETRY. JRNL REF SCI REP 2025 JRNL REFN ESSN 2045-2322 JRNL PMID 41413164 JRNL DOI 10.1038/S41598-025-32541-6 REMARK 2 REMARK 2 RESOLUTION. 2.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 18744 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.590 REMARK 3 FREE R VALUE TEST SET COUNT : 860 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 44.7600 - 5.1900 1.00 3381 181 0.1982 0.2311 REMARK 3 2 5.1900 - 4.1200 1.00 3187 157 0.1785 0.2157 REMARK 3 3 4.1200 - 3.6000 0.83 2624 132 0.2243 0.2869 REMARK 3 4 3.6000 - 3.2700 0.79 2473 122 0.2633 0.3512 REMARK 3 5 3.2700 - 3.0400 1.00 3113 137 0.2771 0.3164 REMARK 3 6 3.0400 - 2.8600 1.00 3106 131 0.2875 0.3287 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) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.420 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 76.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 4307 REMARK 3 ANGLE : 0.781 5857 REMARK 3 CHIRALITY : 0.047 651 REMARK 3 PLANARITY : 0.007 751 REMARK 3 DIHEDRAL : 5.146 591 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.3724 52.7562 -12.0951 REMARK 3 T TENSOR REMARK 3 T11: 1.0115 T22: 1.5310 REMARK 3 T33: 1.2889 T12: 0.0676 REMARK 3 T13: 0.0329 T23: 0.7073 REMARK 3 L TENSOR REMARK 3 L11: 7.5809 L22: 1.4881 REMARK 3 L33: 4.3588 L12: -0.8002 REMARK 3 L13: 2.3845 L23: -1.0285 REMARK 3 S TENSOR REMARK 3 S11: -0.3081 S12: 2.0452 S13: 2.4858 REMARK 3 S21: -0.6538 S22: 0.1687 S23: 0.8449 REMARK 3 S31: -0.8108 S32: -1.0524 S33: -0.1009 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 158 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.5037 48.6760 -9.5806 REMARK 3 T TENSOR REMARK 3 T11: 0.9984 T22: 1.1396 REMARK 3 T33: 0.9678 T12: -0.0722 REMARK 3 T13: 0.1117 T23: 0.3938 REMARK 3 L TENSOR REMARK 3 L11: 1.1742 L22: 5.2832 REMARK 3 L33: 3.1411 L12: 1.0484 REMARK 3 L13: 0.6419 L23: -0.7862 REMARK 3 S TENSOR REMARK 3 S11: -0.3355 S12: 0.8590 S13: 1.0948 REMARK 3 S21: -0.7269 S22: 0.7542 S23: 0.3831 REMARK 3 S31: -0.4743 S32: -1.0488 S33: -0.5185 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 189 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.0503 58.4663 -15.7135 REMARK 3 T TENSOR REMARK 3 T11: 1.3472 T22: 1.4719 REMARK 3 T33: 1.4948 T12: -0.0284 REMARK 3 T13: 0.0451 T23: 1.0221 REMARK 3 L TENSOR REMARK 3 L11: 4.8642 L22: 3.3867 REMARK 3 L33: 4.7552 L12: -1.8343 REMARK 3 L13: 4.3830 L23: -0.1852 REMARK 3 S TENSOR REMARK 3 S11: 0.0028 S12: 1.6980 S13: 0.8114 REMARK 3 S21: -0.9948 S22: 0.7274 S23: -0.4407 REMARK 3 S31: -0.6528 S32: -0.1713 S33: 0.8926 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9347 5.2644 19.4195 REMARK 3 T TENSOR REMARK 3 T11: 1.4384 T22: 0.9221 REMARK 3 T33: 1.6932 T12: 0.2718 REMARK 3 T13: -0.0213 T23: -0.0050 REMARK 3 L TENSOR REMARK 3 L11: 8.5586 L22: 8.1620 REMARK 3 L33: 4.5411 L12: -4.7972 REMARK 3 L13: 2.7009 L23: -0.6271 REMARK 3 S TENSOR REMARK 3 S11: 0.8428 S12: -0.1767 S13: -0.9485 REMARK 3 S21: 1.1271 S22: 0.1579 S23: -2.3775 REMARK 3 S31: -0.0027 S32: 1.4055 S33: -0.9670 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.5640 -10.2608 25.1500 REMARK 3 T TENSOR REMARK 3 T11: 2.6511 T22: 1.6240 REMARK 3 T33: 3.2935 T12: 0.3825 REMARK 3 T13: -0.1536 T23: 0.3308 REMARK 3 L TENSOR REMARK 3 L11: 0.3214 L22: 4.0494 REMARK 3 L33: 0.9547 L12: -0.9588 REMARK 3 L13: -0.4410 L23: 1.8824 REMARK 3 S TENSOR REMARK 3 S11: 0.1129 S12: -1.1160 S13: -3.6476 REMARK 3 S21: 3.1410 S22: 1.5220 S23: -1.3319 REMARK 3 S31: 1.7282 S32: 0.5432 S33: -0.7663 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.7698 1.9556 25.9886 REMARK 3 T TENSOR REMARK 3 T11: 1.8414 T22: 1.9714 REMARK 3 T33: 1.8419 T12: 1.5616 REMARK 3 T13: 0.2866 T23: 0.5702 REMARK 3 L TENSOR REMARK 3 L11: 1.4969 L22: 4.7217 REMARK 3 L33: 1.3322 L12: -1.0778 REMARK 3 L13: -0.8707 L23: 1.9230 REMARK 3 S TENSOR REMARK 3 S11: -0.7874 S12: -1.1001 S13: -0.6741 REMARK 3 S21: 1.3513 S22: 0.5129 S23: -0.6200 REMARK 3 S31: 0.8790 S32: 0.5809 S33: -1.0398 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.8836 10.9915 28.6565 REMARK 3 T TENSOR REMARK 3 T11: 1.0345 T22: 0.8490 REMARK 3 T33: 1.4039 T12: 0.2999 REMARK 3 T13: 0.2090 T23: 0.4550 REMARK 3 L TENSOR REMARK 3 L11: 4.8282 L22: 5.6741 REMARK 3 L33: 8.1578 L12: -0.5530 REMARK 3 L13: 1.4661 L23: 2.9125 REMARK 3 S TENSOR REMARK 3 S11: -0.4480 S12: -1.2216 S13: -1.4960 REMARK 3 S21: 1.3994 S22: -0.5423 S23: -0.3349 REMARK 3 S31: 1.1294 S32: -0.1570 S33: 0.3495 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.4029 7.3703 34.1048 REMARK 3 T TENSOR REMARK 3 T11: 1.7131 T22: 1.3621 REMARK 3 T33: 1.0911 T12: 0.0015 REMARK 3 T13: 0.2407 T23: 0.4838 REMARK 3 L TENSOR REMARK 3 L11: 4.5088 L22: 2.3411 REMARK 3 L33: 3.2743 L12: -0.0378 REMARK 3 L13: 1.9691 L23: 1.7966 REMARK 3 S TENSOR REMARK 3 S11: 0.1379 S12: -1.0174 S13: -1.5478 REMARK 3 S21: 2.0709 S22: 0.1946 S23: 0.1191 REMARK 3 S31: 1.3581 S32: -1.5346 S33: 0.4352 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 115 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.4631 19.0735 41.1014 REMARK 3 T TENSOR REMARK 3 T11: 1.1696 T22: 3.1001 REMARK 3 T33: 2.4226 T12: 0.5526 REMARK 3 T13: -0.8663 T23: 1.1935 REMARK 3 L TENSOR REMARK 3 L11: 2.8732 L22: 6.2375 REMARK 3 L33: 8.5517 L12: -4.0193 REMARK 3 L13: -2.3300 L23: 1.3086 REMARK 3 S TENSOR REMARK 3 S11: -0.3508 S12: -1.6026 S13: 0.2626 REMARK 3 S21: 1.0009 S22: -0.1917 S23: -3.8846 REMARK 3 S31: -1.2885 S32: 3.1430 S33: 1.9730 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.6928 23.7979 8.4734 REMARK 3 T TENSOR REMARK 3 T11: 0.7563 T22: 0.4801 REMARK 3 T33: 0.5307 T12: -0.0489 REMARK 3 T13: 0.0702 T23: 0.0220 REMARK 3 L TENSOR REMARK 3 L11: 2.7126 L22: 5.8454 REMARK 3 L33: 5.0208 L12: -2.9096 REMARK 3 L13: 1.8696 L23: -1.6718 REMARK 3 S TENSOR REMARK 3 S11: 0.2124 S12: 0.8413 S13: -1.0050 REMARK 3 S21: -0.4207 S22: -0.6082 S23: 0.4161 REMARK 3 S31: 0.8860 S32: -0.2177 S33: 0.4377 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.4030 23.1372 20.0308 REMARK 3 T TENSOR REMARK 3 T11: 0.4650 T22: 0.3762 REMARK 3 T33: 0.3729 T12: -0.0053 REMARK 3 T13: 0.0841 T23: 0.0836 REMARK 3 L TENSOR REMARK 3 L11: 8.1640 L22: 5.7670 REMARK 3 L33: 5.5786 L12: -2.0688 REMARK 3 L13: 0.6166 L23: -1.0046 REMARK 3 S TENSOR REMARK 3 S11: -0.3262 S12: -0.2572 S13: -0.5425 REMARK 3 S21: 0.3154 S22: 0.0424 S23: 0.0050 REMARK 3 S31: 0.5201 S32: -0.2662 S33: 0.3426 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.8369 26.3942 16.4494 REMARK 3 T TENSOR REMARK 3 T11: 0.4517 T22: 0.5120 REMARK 3 T33: 0.4369 T12: 0.0360 REMARK 3 T13: 0.0529 T23: 0.1123 REMARK 3 L TENSOR REMARK 3 L11: 4.5174 L22: 7.0903 REMARK 3 L33: 6.2871 L12: -2.9647 REMARK 3 L13: 1.5006 L23: -2.8919 REMARK 3 S TENSOR REMARK 3 S11: -0.0915 S12: 0.0030 S13: -0.2778 REMARK 3 S21: -0.0120 S22: -0.3535 S23: -0.2244 REMARK 3 S31: 0.5210 S32: 0.5689 S33: 0.4409 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 121 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.3631 40.3776 -14.9833 REMARK 3 T TENSOR REMARK 3 T11: 0.9339 T22: 1.9887 REMARK 3 T33: 0.7627 T12: -0.1916 REMARK 3 T13: 0.0355 T23: 0.3033 REMARK 3 L TENSOR REMARK 3 L11: 2.6075 L22: 1.9093 REMARK 3 L33: 8.4178 L12: 0.0430 REMARK 3 L13: -4.6859 L23: -0.5469 REMARK 3 S TENSOR REMARK 3 S11: -0.4710 S12: 2.9544 S13: 0.6585 REMARK 3 S21: -0.7851 S22: 0.6001 S23: -0.2937 REMARK 3 S31: 0.0117 S32: -0.8854 S33: -0.2033 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 164 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.4558 38.2564 -10.1580 REMARK 3 T TENSOR REMARK 3 T11: 0.7501 T22: 1.1250 REMARK 3 T33: 0.6321 T12: -0.0358 REMARK 3 T13: 0.0209 T23: 0.0200 REMARK 3 L TENSOR REMARK 3 L11: 2.2791 L22: 2.8658 REMARK 3 L33: 5.8358 L12: 2.2096 REMARK 3 L13: -0.6617 L23: 0.4701 REMARK 3 S TENSOR REMARK 3 S11: -0.4451 S12: 2.3545 S13: -0.3688 REMARK 3 S21: -0.1826 S22: -0.2312 S23: 0.1054 REMARK 3 S31: -0.1961 S32: -0.7386 S33: 0.5978 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 187 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.1145 39.0475 -24.0689 REMARK 3 T TENSOR REMARK 3 T11: 1.1690 T22: 2.2798 REMARK 3 T33: 0.8694 T12: -0.2495 REMARK 3 T13: 0.5399 T23: -0.1473 REMARK 3 L TENSOR REMARK 3 L11: 1.8541 L22: 1.5527 REMARK 3 L33: 5.5512 L12: -1.4214 REMARK 3 L13: -2.9409 L23: 1.5817 REMARK 3 S TENSOR REMARK 3 S11: 0.2146 S12: 2.2232 S13: -0.7261 REMARK 3 S21: -1.3011 S22: 0.4750 S23: -0.4398 REMARK 3 S31: 0.3029 S32: -0.9346 S33: 0.3132 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 204 THROUGH 225 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.7963 34.9700 -20.1209 REMARK 3 T TENSOR REMARK 3 T11: 1.2404 T22: 2.3403 REMARK 3 T33: 0.8614 T12: -0.5308 REMARK 3 T13: 0.0296 T23: -0.4457 REMARK 3 L TENSOR REMARK 3 L11: 7.4281 L22: 1.9174 REMARK 3 L33: 5.5307 L12: -2.9651 REMARK 3 L13: -1.4406 L23: 1.4111 REMARK 3 S TENSOR REMARK 3 S11: -1.2494 S12: 2.0622 S13: -0.2503 REMARK 3 S21: -0.8073 S22: -0.2169 S23: -0.1948 REMARK 3 S31: 0.3355 S32: 0.9419 S33: 1.1301 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.7481 32.6128 16.2817 REMARK 3 T TENSOR REMARK 3 T11: 0.4281 T22: 0.5638 REMARK 3 T33: 0.6165 T12: 0.0918 REMARK 3 T13: -0.0564 T23: 0.0699 REMARK 3 L TENSOR REMARK 3 L11: 3.9238 L22: 4.7111 REMARK 3 L33: 5.2663 L12: 1.9235 REMARK 3 L13: -1.4705 L23: -1.4358 REMARK 3 S TENSOR REMARK 3 S11: -0.1950 S12: -0.3162 S13: -0.2494 REMARK 3 S21: 0.0671 S22: -0.0622 S23: -0.9040 REMARK 3 S31: 0.1896 S32: 0.7951 S33: 0.3129 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 89 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.8315 38.6498 11.0378 REMARK 3 T TENSOR REMARK 3 T11: 0.6364 T22: 0.6101 REMARK 3 T33: 0.6206 T12: 0.0493 REMARK 3 T13: 0.0682 T23: 0.0478 REMARK 3 L TENSOR REMARK 3 L11: 3.3974 L22: 1.3883 REMARK 3 L33: 3.1034 L12: 1.5811 REMARK 3 L13: -3.2396 L23: -1.1548 REMARK 3 S TENSOR REMARK 3 S11: -0.1106 S12: -0.0686 S13: 0.3138 REMARK 3 S21: -0.1339 S22: 0.0480 S23: -0.2302 REMARK 3 S31: 0.0052 S32: 0.0197 S33: -0.4486 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 9P8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000296775. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 17-ID 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18744 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.860 REMARK 200 RESOLUTION RANGE LOW (A) : 44.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.01810 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.1900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.96 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.26920 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.580 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG20,000, AND 100 MM SODIUM REMARK 280 ACETATE PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.22133 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 146.44267 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.83200 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 183.05333 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.61067 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.22133 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 146.44267 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 183.05333 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 109.83200 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.61067 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN A 26 REMARK 465 ARG A 27 REMARK 465 PRO A 28 REMARK 465 THR A 29 REMARK 465 GLY A 30 REMARK 465 GLY A 31 REMARK 465 ARG A 59 REMARK 465 ASP A 60 REMARK 465 TYR A 61 REMARK 465 PRO A 62 REMARK 465 GLY A 63 REMARK 465 GLU A 64 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 OD1 ASP A 83 OG1 THR A 87 2.12 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 CYS H 22 102.65 -163.02 REMARK 500 SER H 85 70.51 50.36 REMARK 500 LYS H 138 56.16 -98.11 REMARK 500 SER H 224 -74.41 -67.03 REMARK 500 TYR L 31 112.94 -162.51 REMARK 500 ILE L 50 -59.47 68.53 REMARK 500 ALA L 83 -172.77 -170.69 REMARK 500 ASN L 137 68.81 29.26 REMARK 500 ASN L 151 -5.53 69.91 REMARK 500 LYS L 189 -2.76 70.47 REMARK 500 CYS A 34 177.25 64.79 REMARK 500 THR A 55 -174.01 60.76 REMARK 500 CYS A 66 -163.73 63.23 REMARK 500 HIS A 92 86.78 -155.57 REMARK 500 ASN A 146 -152.85 -143.17 REMARK 500 REMARK 500 REMARK: NULL DBREF 9P8X H 1 225 PDB 9P8X 9P8X 1 225 DBREF 9P8X L 1 213 PDB 9P8X 9P8X 1 213 DBREF 9P8X A 26 155 UNP Q9Y5U5 TNR18_HUMAN 26 155 SEQADV 9P8X SER A 57 UNP Q9Y5U5 CYS 57 CONFLICT SEQRES 1 H 225 GLN ILE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 225 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 225 TYR THR PHE THR ASP TYR TYR ILE ASN TRP VAL LYS GLN SEQRES 4 H 225 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR SEQRES 5 H 225 PRO GLY SER GLY ASN THR LYS TYR ASN GLU LYS PHE ARG SEQRES 6 H 225 GLY LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 225 ALA ALA MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 225 ALA VAL TYR PHE CYS VAL ARG TRP SER THR THR SER PRO SEQRES 9 H 225 PHE GLY GLY TYR PHE ASP VAL TRP GLY THR GLY THR THR SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS SEQRES 1 L 213 GLU ILE LEU LEU THR GLN SER PRO ALA ILE ILE ALA ALA SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 L 213 SER SER VAL SER TYR MET ASN TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 GLY SER SER PRO LYS ILE TRP ILE TYR GLY ILE SER ASN SEQRES 5 L 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER PHE SER PHE THR ILE ASN SER MET GLU SEQRES 7 L 213 ALA GLU ASP VAL ALA THR TYR TYR CYS GLN GLN ARG ASN SEQRES 8 L 213 ASN TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 L 213 LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 A 130 GLN ARG PRO THR GLY GLY PRO GLY CYS GLY PRO GLY ARG SEQRES 2 A 130 LEU LEU LEU GLY THR GLY THR ASP ALA ARG CYS CYS ARG SEQRES 3 A 130 VAL HIS THR THR ARG SER CYS ARG ASP TYR PRO GLY GLU SEQRES 4 A 130 GLU CYS CYS SER GLU TRP ASP CYS MET CYS VAL GLN PRO SEQRES 5 A 130 GLU PHE HIS CYS GLY ASP PRO CYS CYS THR THR CYS ARG SEQRES 6 A 130 HIS HIS PRO CYS PRO PRO GLY GLN GLY VAL GLN SER GLN SEQRES 7 A 130 GLY LYS PHE SER PHE GLY PHE GLN CYS ILE ASP CYS ALA SEQRES 8 A 130 SER GLY THR PHE SER GLY GLY HIS GLU GLY HIS CYS LYS SEQRES 9 A 130 PRO TRP THR ASP CYS THR GLN PHE GLY PHE LEU THR VAL SEQRES 10 A 130 PHE PRO GLY ASN LYS THR HIS ASN ALA VAL CYS VAL PRO HET ACT H 301 4 HET NAG A 201 14 HETNAM ACT ACETATE ION HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 ACT C2 H3 O2 1- FORMUL 5 NAG C8 H15 N O6 FORMUL 6 HOH *29(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 GLU H 62 ARG H 65 5 4 HELIX 3 AA3 THR H 87 SER H 91 5 5 HELIX 4 AA4 GLU L 78 VAL L 82 5 5 HELIX 5 AA5 SER L 120 GLY L 127 1 8 HELIX 6 AA6 LYS L 182 LYS L 189 1 8 HELIX 7 AA7 THR A 43 ASP A 46 5 4 HELIX 8 AA8 ASP A 133 GLY A 138 5 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N THR H 71 O ALA H 80 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA2 6 ALA H 92 TRP H 99 -1 N TYR H 94 O THR H 116 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N ASN H 35 O VAL H 97 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O LYS H 59 N TRP H 50 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA3 4 ALA H 92 TRP H 99 -1 N TYR H 94 O THR H 116 SHEET 4 AA3 4 PHE H 109 TRP H 112 -1 O VAL H 111 N ARG H 98 SHEET 1 AA4 4 SER H 129 LEU H 133 0 SHEET 2 AA4 4 ALA H 145 TYR H 154 -1 O GLY H 148 N LEU H 133 SHEET 3 AA4 4 TYR H 185 VAL H 193 -1 O VAL H 193 N ALA H 145 SHEET 4 AA4 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AA5 4 SER H 129 LEU H 133 0 SHEET 2 AA5 4 ALA H 145 TYR H 154 -1 O GLY H 148 N LEU H 133 SHEET 3 AA5 4 TYR H 185 VAL H 193 -1 O VAL H 193 N ALA H 145 SHEET 4 AA5 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AA6 3 THR H 160 TRP H 163 0 SHEET 2 AA6 3 ILE H 204 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AA6 3 THR H 214 LYS H 219 -1 O THR H 214 N HIS H 209 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 VAL L 19 VAL L 29 -1 O SER L 24 N THR L 5 SHEET 3 AA7 3 PHE L 61 ILE L 74 -1 O PHE L 72 N ILE L 21 SHEET 1 AA8 6 ILE L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 101 LEU L 105 1 O GLU L 104 N ILE L 11 SHEET 3 AA8 6 ALA L 83 GLN L 89 -1 N ALA L 83 O LEU L 103 SHEET 4 AA8 6 MET L 32 GLN L 37 -1 N GLN L 37 O THR L 84 SHEET 5 AA8 6 LYS L 44 TYR L 48 -1 O TRP L 46 N TRP L 34 SHEET 6 AA8 6 ASN L 52 LEU L 53 -1 O ASN L 52 N TYR L 48 SHEET 1 AA9 4 ILE L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 101 LEU L 105 1 O GLU L 104 N ILE L 11 SHEET 3 AA9 4 ALA L 83 GLN L 89 -1 N ALA L 83 O LEU L 103 SHEET 4 AA9 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 89 SHEET 1 AB1 4 SER L 113 PHE L 117 0 SHEET 2 AB1 4 THR L 128 PHE L 138 -1 O VAL L 132 N PHE L 117 SHEET 3 AB1 4 TYR L 172 SER L 181 -1 O LEU L 180 N ALA L 129 SHEET 4 AB1 4 SER L 158 VAL L 162 -1 N GLN L 159 O THR L 177 SHEET 1 AB2 4 ALA L 152 LEU L 153 0 SHEET 2 AB2 4 ALA L 143 VAL L 149 -1 N VAL L 149 O ALA L 152 SHEET 3 AB2 4 VAL L 190 HIS L 197 -1 O GLU L 194 N GLN L 146 SHEET 4 AB2 4 VAL L 204 THR L 205 -1 O VAL L 204 N VAL L 195 SHEET 1 AB3 4 ALA L 152 LEU L 153 0 SHEET 2 AB3 4 ALA L 143 VAL L 149 -1 N VAL L 149 O ALA L 152 SHEET 3 AB3 4 VAL L 190 HIS L 197 -1 O GLU L 194 N GLN L 146 SHEET 4 AB3 4 PHE L 208 ASN L 209 -1 O PHE L 208 N TYR L 191 SHEET 1 AB4 3 LEU A 39 LEU A 41 0 SHEET 2 AB4 3 ARG A 48 VAL A 52 -1 O ARG A 48 N LEU A 41 SHEET 3 AB4 3 GLU A 69 CYS A 74 -1 O MET A 73 N CYS A 49 SHEET 1 AB5 2 PHE A 79 CYS A 81 0 SHEET 2 AB5 2 CYS A 89 HIS A 91 -1 O ARG A 90 N HIS A 80 SHEET 1 AB6 2 GLN A 98 GLY A 104 0 SHEET 2 AB6 2 PHE A 108 ASP A 114 -1 O ILE A 113 N GLY A 99 SHEET 1 AB7 2 THR A 119 PHE A 120 0 SHEET 2 AB7 2 LYS A 129 PRO A 130 -1 O LYS A 129 N PHE A 120 SHEET 1 AB8 2 LEU A 140 PHE A 143 0 SHEET 2 AB8 2 VAL A 152 VAL A 154 -1 O VAL A 154 N LEU A 140 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 3 CYS H 225 CYS L 213 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 87 1555 1555 2.05 SSBOND 5 CYS L 133 CYS L 193 1555 1555 2.04 SSBOND 6 CYS A 34 CYS A 49 1555 1555 2.03 SSBOND 7 CYS A 50 CYS A 72 1555 1555 2.03 SSBOND 8 CYS A 58 CYS A 66 1555 1555 2.03 SSBOND 9 CYS A 67 CYS A 85 1555 1555 2.03 SSBOND 10 CYS A 74 CYS A 89 1555 1555 2.03 SSBOND 11 CYS A 81 CYS A 86 1555 1555 2.03 SSBOND 12 CYS A 94 CYS A 112 1555 1555 2.04 SSBOND 13 CYS A 115 CYS A 128 1555 1555 2.03 SSBOND 14 CYS A 134 CYS A 153 1555 1555 2.03 LINK ND2 ASN A 146 C1 NAG A 201 1555 1555 1.44 CISPEP 1 PHE H 155 PRO H 156 0 -3.63 CISPEP 2 GLU H 157 PRO H 158 0 6.50 CISPEP 3 SER L 7 PRO L 8 0 1.78 CISPEP 4 TYR L 93 PRO L 94 0 6.53 CISPEP 5 TYR L 139 PRO L 140 0 4.52 CRYST1 113.198 113.198 219.664 90.00 90.00 120.00 P 61 2 2 12 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 0.008834 0.005100 0.000000 0.00000 SCALE2 0.000000 0.010201 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004552 0.00000