HEADER ALLERGEN/IMMUNE SYSTEM 14-AUG-25 9Q1L TITLE CRYSTAL STRUCTURE OF THE WALNUT ALLERGEN JUG R 2 BOUND TO THE HUMAN- TITLE 2 DERIVED FAB 6D12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 6D12 FAB LIGHT CHAIN; COMPND 3 CHAIN: B, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 6D12 FAB HEAVY CHAIN; COMPND 7 CHAIN: A, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: VICILIN JUG R 2.0102 HAIRPININ ALPHA 4; COMPND 11 CHAIN: C, F; COMPND 12 SYNONYM: 7S GLOBULIN,7S SEED STORAGE PROTEIN,ALLERGEN JUG R 2,VICILIN COMPND 13 JUG R 2,VICILIN-LIKE JUG R 2; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES; COMPND 16 OTHER_DETAILS: JUG R 2.0102 HAIRPININ ALPHA 4 (S236I, E245D) IS THE COMPND 17 SAME AS JUG R 2.0101 HAIRPININ ALPHA 1 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 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: JUGLANS REGIA; SOURCE 14 ORGANISM_COMMON: PERSIAN WALNUT; SOURCE 15 ORGANISM_TAXID: 51240; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS WALNUT, ALLERGEN, ANTIBODY BINDING, FAB, VICILIN, ALPHA-HAIRPININ KEYWDS 2 DOMAINS, SEED STORAGE PROTEIN, ALLERGEN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.C.PEDERSEN,I.R.LYTLE,G.A.MUELLER,D.C.CROOTE REVDAT 1 21-JAN-26 9Q1L 0 JRNL AUTH G.O.LEIGHTON,T.M.COSEY,E.R.DE DIAVOUKANA,I.R.LYTLE, JRNL AUTH 2 A.C.Y.FOO,L.C.PEDERSEN,S.A.GABEL,R.M.PETROVICH,M.SHI, JRNL AUTH 3 V.ARUVA,P.CREEKS,J.J.W.WONG,J.ZHANG,R.S.PEEBLES JR., JRNL AUTH 4 D.CROOTE,S.A.SMITH,G.A.MUELLER JRNL TITL POLYMERIC ALPHA-HAIRPININ ALLERGENS INDUCE A FUNCTIONAL JRNL TITL 2 RESPONSE VIA A SINGLE ANTIBODY. JRNL REF ALLERGY 2025 JRNL REFN ESSN 1398-9995 JRNL PMID 41476027 JRNL DOI 10.1111/ALL.70201 REMARK 2 REMARK 2 RESOLUTION. 1.56 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) : 1.56 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.41 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 144159 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.168 REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.370 REMARK 3 FREE R VALUE TEST SET COUNT : 1980 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 42.4100 - 3.7600 0.97 10453 145 0.1610 0.1838 REMARK 3 2 3.7600 - 2.9800 1.00 10477 146 0.1570 0.2066 REMARK 3 3 2.9800 - 2.6100 0.99 10414 146 0.1635 0.1755 REMARK 3 4 2.6100 - 2.3700 0.99 10350 145 0.1673 0.1940 REMARK 3 5 2.3700 - 2.2000 0.96 10047 139 0.1597 0.1857 REMARK 3 6 2.2000 - 2.0700 0.99 10268 143 0.1609 0.1939 REMARK 3 7 2.0700 - 1.9600 0.99 10329 145 0.1628 0.1787 REMARK 3 8 1.9600 - 1.8800 0.99 10358 145 0.1597 0.1937 REMARK 3 9 1.8800 - 1.8100 0.99 10245 142 0.1675 0.1857 REMARK 3 10 1.8100 - 1.7400 0.99 10234 143 0.1860 0.2116 REMARK 3 11 1.7400 - 1.6900 0.97 10058 135 0.2075 0.2434 REMARK 3 12 1.6900 - 1.6400 0.95 9814 139 0.2108 0.2288 REMARK 3 13 1.6400 - 1.6000 0.97 9977 141 0.2214 0.2616 REMARK 3 14 1.6000 - 1.5600 0.88 9155 126 0.2400 0.2481 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.150 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.590 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.54 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 : 0.005 7598 REMARK 3 ANGLE : 0.876 10382 REMARK 3 CHIRALITY : 0.054 1183 REMARK 3 PLANARITY : 0.006 1354 REMARK 3 DIHEDRAL : 14.309 2723 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 34 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.5662 -15.1830 -56.7457 REMARK 3 T TENSOR REMARK 3 T11: 0.1462 T22: 0.2009 REMARK 3 T33: 0.1678 T12: 0.0403 REMARK 3 T13: 0.0012 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 1.1211 L22: 1.8724 REMARK 3 L33: 2.1154 L12: 1.2916 REMARK 3 L13: 1.4739 L23: 1.3746 REMARK 3 S TENSOR REMARK 3 S11: 0.1023 S12: 0.1710 S13: -0.1166 REMARK 3 S21: 0.1792 S22: 0.0645 S23: -0.1030 REMARK 3 S31: 0.1995 S32: 0.3339 S33: -0.1309 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9194 -7.8071 -60.4110 REMARK 3 T TENSOR REMARK 3 T11: 0.0850 T22: 0.1037 REMARK 3 T33: 0.0885 T12: 0.0127 REMARK 3 T13: 0.0153 T23: -0.0055 REMARK 3 L TENSOR REMARK 3 L11: 2.6819 L22: 1.2060 REMARK 3 L33: 1.8492 L12: 0.5589 REMARK 3 L13: 0.5458 L23: 0.3074 REMARK 3 S TENSOR REMARK 3 S11: -0.0006 S12: 0.1022 S13: -0.0048 REMARK 3 S21: -0.0354 S22: 0.0102 S23: -0.1122 REMARK 3 S31: -0.0033 S32: 0.2428 S33: -0.0119 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 121 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.0970 -8.1317 -43.6551 REMARK 3 T TENSOR REMARK 3 T11: 0.1223 T22: 0.1788 REMARK 3 T33: 0.1865 T12: 0.0158 REMARK 3 T13: -0.0232 T23: -0.0187 REMARK 3 L TENSOR REMARK 3 L11: 5.5694 L22: 2.6727 REMARK 3 L33: 7.5185 L12: 3.8553 REMARK 3 L13: 6.4706 L23: 4.4719 REMARK 3 S TENSOR REMARK 3 S11: -0.0053 S12: 0.2452 S13: -0.0952 REMARK 3 S21: 0.0038 S22: 0.2143 S23: -0.0933 REMARK 3 S31: 0.0270 S32: 0.3062 S33: -0.2056 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9731 4.8898 -18.4044 REMARK 3 T TENSOR REMARK 3 T11: 0.2079 T22: 0.1956 REMARK 3 T33: 0.1529 T12: 0.0236 REMARK 3 T13: -0.0604 T23: -0.0461 REMARK 3 L TENSOR REMARK 3 L11: 8.8907 L22: 2.7202 REMARK 3 L33: 6.5833 L12: -1.9377 REMARK 3 L13: -3.0656 L23: 1.5163 REMARK 3 S TENSOR REMARK 3 S11: -0.1320 S12: -0.6846 S13: 0.4237 REMARK 3 S21: 0.2257 S22: 0.2191 S23: -0.0850 REMARK 3 S31: -0.3500 S32: 0.0222 S33: -0.0822 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.5258 -5.0453 -25.9579 REMARK 3 T TENSOR REMARK 3 T11: 0.1409 T22: 0.1554 REMARK 3 T33: 0.1365 T12: -0.0232 REMARK 3 T13: -0.0387 T23: -0.0235 REMARK 3 L TENSOR REMARK 3 L11: 3.3112 L22: 1.2769 REMARK 3 L33: 4.8317 L12: -0.7164 REMARK 3 L13: -3.2720 L23: 0.1064 REMARK 3 S TENSOR REMARK 3 S11: -0.1616 S12: -0.0678 S13: -0.0901 REMARK 3 S21: 0.1935 S22: 0.0655 S23: -0.1113 REMARK 3 S31: 0.2577 S32: -0.1097 S33: 0.1216 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 170 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.3034 -5.3357 -29.7720 REMARK 3 T TENSOR REMARK 3 T11: 0.1183 T22: 0.0936 REMARK 3 T33: 0.1317 T12: 0.0080 REMARK 3 T13: -0.0259 T23: -0.0203 REMARK 3 L TENSOR REMARK 3 L11: 1.5522 L22: 0.9797 REMARK 3 L33: 7.2785 L12: 0.0930 REMARK 3 L13: -0.6361 L23: -0.6364 REMARK 3 S TENSOR REMARK 3 S11: 0.0311 S12: 0.0254 S13: -0.0291 REMARK 3 S21: 0.0901 S22: 0.1906 S23: -0.0205 REMARK 3 S31: 0.3205 S32: -0.1024 S33: -0.1780 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 194 THROUGH 232 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9145 -2.8360 -16.5474 REMARK 3 T TENSOR REMARK 3 T11: 0.2303 T22: 0.1992 REMARK 3 T33: 0.1622 T12: 0.0390 REMARK 3 T13: -0.0647 T23: -0.0201 REMARK 3 L TENSOR REMARK 3 L11: 1.4415 L22: 1.2356 REMARK 3 L33: 4.9803 L12: -0.2621 REMARK 3 L13: -0.8368 L23: 1.0214 REMARK 3 S TENSOR REMARK 3 S11: -0.1163 S12: -0.3004 S13: 0.0527 REMARK 3 S21: 0.2739 S22: 0.2001 S23: -0.1415 REMARK 3 S31: 0.1936 S32: 0.1508 S33: -0.0775 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.3305 0.9998 -44.1027 REMARK 3 T TENSOR REMARK 3 T11: 0.0794 T22: 0.0949 REMARK 3 T33: 0.1340 T12: -0.0242 REMARK 3 T13: 0.0505 T23: -0.0654 REMARK 3 L TENSOR REMARK 3 L11: 2.2017 L22: 3.7493 REMARK 3 L33: 6.3250 L12: 0.4961 REMARK 3 L13: -0.3901 L23: -1.2611 REMARK 3 S TENSOR REMARK 3 S11: -0.0257 S12: -0.1140 S13: -0.0502 REMARK 3 S21: 0.0824 S22: -0.2708 S23: -0.0214 REMARK 3 S31: -0.0853 S32: -0.2820 S33: -0.0694 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 78 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.5215 -0.6353 -55.6837 REMARK 3 T TENSOR REMARK 3 T11: 0.0993 T22: 0.0772 REMARK 3 T33: 0.1273 T12: -0.0133 REMARK 3 T13: 0.0187 T23: -0.0094 REMARK 3 L TENSOR REMARK 3 L11: 2.5659 L22: 1.4686 REMARK 3 L33: 3.2396 L12: -0.0047 REMARK 3 L13: 0.2894 L23: 1.3080 REMARK 3 S TENSOR REMARK 3 S11: 0.0277 S12: 0.1087 S13: 0.1515 REMARK 3 S21: -0.1067 S22: -0.0475 S23: 0.1421 REMARK 3 S31: -0.1866 S32: -0.0389 S33: 0.0150 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.1662 -5.9709 -54.3878 REMARK 3 T TENSOR REMARK 3 T11: 0.0942 T22: 0.1615 REMARK 3 T33: 0.1858 T12: -0.0091 REMARK 3 T13: -0.0152 T23: -0.0456 REMARK 3 L TENSOR REMARK 3 L11: 3.0257 L22: 0.9528 REMARK 3 L33: 4.1629 L12: 0.8624 REMARK 3 L13: -0.2414 L23: 0.7928 REMARK 3 S TENSOR REMARK 3 S11: -0.0753 S12: 0.1788 S13: 0.1337 REMARK 3 S21: 0.0422 S22: -0.2780 S23: 0.2441 REMARK 3 S31: 0.0582 S32: -0.3517 S33: 0.1836 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 98 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.4192 -3.0565 -47.8493 REMARK 3 T TENSOR REMARK 3 T11: 0.1068 T22: 0.1262 REMARK 3 T33: 0.1408 T12: -0.0270 REMARK 3 T13: 0.0365 T23: -0.0711 REMARK 3 L TENSOR REMARK 3 L11: 3.1382 L22: 2.7310 REMARK 3 L33: 4.9433 L12: 0.3904 REMARK 3 L13: 0.3472 L23: -0.9747 REMARK 3 S TENSOR REMARK 3 S11: 0.0781 S12: 0.0532 S13: 0.1246 REMARK 3 S21: 0.1395 S22: -0.2267 S23: 0.2560 REMARK 3 S31: -0.0350 S32: -0.4053 S33: 0.1026 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7748 -0.4193 -58.8016 REMARK 3 T TENSOR REMARK 3 T11: 0.1114 T22: 0.0820 REMARK 3 T33: 0.1256 T12: 0.0055 REMARK 3 T13: 0.0155 T23: -0.0000 REMARK 3 L TENSOR REMARK 3 L11: 1.9391 L22: 2.0394 REMARK 3 L33: 5.5547 L12: 0.4671 REMARK 3 L13: -1.0473 L23: 0.6762 REMARK 3 S TENSOR REMARK 3 S11: 0.0767 S12: 0.1348 S13: 0.1414 REMARK 3 S21: -0.1735 S22: 0.0245 S23: -0.0048 REMARK 3 S31: -0.4695 S32: 0.0773 S33: -0.0801 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.7228 -2.4548 -32.4709 REMARK 3 T TENSOR REMARK 3 T11: 0.1524 T22: 0.1200 REMARK 3 T33: 0.1381 T12: -0.0416 REMARK 3 T13: 0.0144 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 1.2166 L22: 3.8410 REMARK 3 L33: 1.1793 L12: 1.5718 REMARK 3 L13: -0.1906 L23: 0.7866 REMARK 3 S TENSOR REMARK 3 S11: 0.0782 S12: -0.0656 S13: -0.0040 REMARK 3 S21: 0.3854 S22: -0.0660 S23: 0.0479 REMARK 3 S31: 0.6198 S32: -0.3391 S33: -0.0189 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.4952 7.2950 -24.7673 REMARK 3 T TENSOR REMARK 3 T11: 0.1777 T22: 0.2062 REMARK 3 T33: 0.1770 T12: -0.0433 REMARK 3 T13: -0.0298 T23: -0.0296 REMARK 3 L TENSOR REMARK 3 L11: 5.4340 L22: 2.1937 REMARK 3 L33: 2.1671 L12: 0.5033 REMARK 3 L13: -0.2063 L23: -0.0889 REMARK 3 S TENSOR REMARK 3 S11: 0.0671 S12: -0.4235 S13: 0.2677 REMARK 3 S21: 0.1396 S22: -0.0228 S23: -0.3517 REMARK 3 S31: -0.1959 S32: 0.4433 S33: 0.0505 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4274 3.4746 -32.3546 REMARK 3 T TENSOR REMARK 3 T11: 0.1113 T22: 0.0921 REMARK 3 T33: 0.0922 T12: -0.0046 REMARK 3 T13: -0.0043 T23: -0.0017 REMARK 3 L TENSOR REMARK 3 L11: 3.5806 L22: 1.8063 REMARK 3 L33: 1.8592 L12: -0.3285 REMARK 3 L13: 0.1159 L23: -0.0343 REMARK 3 S TENSOR REMARK 3 S11: -0.0241 S12: 0.0621 S13: 0.0576 REMARK 3 S21: 0.0496 S22: -0.0010 S23: -0.0659 REMARK 3 S31: -0.0445 S32: 0.1585 S33: 0.0249 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.6748 7.3959 -29.6072 REMARK 3 T TENSOR REMARK 3 T11: 0.1768 T22: 0.1982 REMARK 3 T33: 0.1767 T12: -0.0688 REMARK 3 T13: -0.0152 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 4.6131 L22: 3.3821 REMARK 3 L33: 2.2644 L12: 0.9902 REMARK 3 L13: -0.1152 L23: -0.1165 REMARK 3 S TENSOR REMARK 3 S11: -0.0617 S12: -0.0351 S13: 0.4736 REMARK 3 S21: 0.0010 S22: 0.0566 S23: -0.2426 REMARK 3 S31: -0.3151 S32: 0.4955 S33: -0.0169 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 244 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4609 13.9583 -28.3144 REMARK 3 T TENSOR REMARK 3 T11: 0.2244 T22: 0.1216 REMARK 3 T33: 0.2775 T12: -0.0357 REMARK 3 T13: -0.0241 T23: -0.0493 REMARK 3 L TENSOR REMARK 3 L11: 4.5058 L22: 2.9058 REMARK 3 L33: 2.2675 L12: 1.7651 REMARK 3 L13: 0.5694 L23: 0.2951 REMARK 3 S TENSOR REMARK 3 S11: -0.0738 S12: -0.1043 S13: 0.7819 REMARK 3 S21: 0.3455 S22: 0.1029 S23: -0.0540 REMARK 3 S31: -0.3978 S32: 0.2247 S33: 0.0488 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 14 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.9049 -2.3508 -76.9517 REMARK 3 T TENSOR REMARK 3 T11: 0.2129 T22: 0.3156 REMARK 3 T33: 0.2004 T12: -0.0309 REMARK 3 T13: -0.0374 T23: 0.0202 REMARK 3 L TENSOR REMARK 3 L11: 5.4488 L22: 6.8680 REMARK 3 L33: 3.4698 L12: -2.2399 REMARK 3 L13: 2.7852 L23: -4.6183 REMARK 3 S TENSOR REMARK 3 S11: -0.1857 S12: 0.6813 S13: 0.4527 REMARK 3 S21: -0.3590 S22: -0.0038 S23: -0.0981 REMARK 3 S31: -0.0478 S32: 0.1260 S33: 0.2136 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 33 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.4584 -9.2342 -81.7343 REMARK 3 T TENSOR REMARK 3 T11: 0.2097 T22: 0.4203 REMARK 3 T33: 0.1626 T12: -0.0027 REMARK 3 T13: 0.0262 T23: -0.0124 REMARK 3 L TENSOR REMARK 3 L11: 2.0388 L22: 4.5730 REMARK 3 L33: 6.8602 L12: -0.6773 REMARK 3 L13: 2.4847 L23: -2.9581 REMARK 3 S TENSOR REMARK 3 S11: 0.0808 S12: 0.7646 S13: 0.1070 REMARK 3 S21: -0.5234 S22: 0.0937 S23: -0.0495 REMARK 3 S31: 0.1757 S32: 0.1068 S33: -0.0941 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 20 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.2266 13.8378 3.2788 REMARK 3 T TENSOR REMARK 3 T11: 0.2402 T22: 0.2570 REMARK 3 T33: 0.1550 T12: -0.0101 REMARK 3 T13: -0.0170 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 3.1955 L22: 2.1435 REMARK 3 L33: 2.7188 L12: 0.8590 REMARK 3 L13: 0.4505 L23: -0.9843 REMARK 3 S TENSOR REMARK 3 S11: 0.0769 S12: -0.5618 S13: -0.0352 REMARK 3 S21: 0.3083 S22: -0.0614 S23: 0.0976 REMARK 3 S31: -0.3201 S32: -0.1122 S33: -0.0412 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 45 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.9768 2.1847 2.1449 REMARK 3 T TENSOR REMARK 3 T11: 0.1946 T22: 0.2220 REMARK 3 T33: 0.1986 T12: -0.0248 REMARK 3 T13: -0.0355 T23: 0.0925 REMARK 3 L TENSOR REMARK 3 L11: 2.5444 L22: 1.9158 REMARK 3 L33: 2.6731 L12: 0.6693 REMARK 3 L13: -0.0596 L23: -0.9939 REMARK 3 S TENSOR REMARK 3 S11: 0.1082 S12: -0.4817 S13: -0.3920 REMARK 3 S21: 0.1277 S22: -0.0452 S23: -0.1200 REMARK 3 S31: 0.1056 S32: -0.0210 S33: -0.0262 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 89 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.3296 6.9560 0.8693 REMARK 3 T TENSOR REMARK 3 T11: 0.1825 T22: 0.2275 REMARK 3 T33: 0.1281 T12: -0.0221 REMARK 3 T13: -0.0226 T23: 0.0658 REMARK 3 L TENSOR REMARK 3 L11: 2.4863 L22: 1.9397 REMARK 3 L33: 2.9708 L12: 0.7700 REMARK 3 L13: -0.5363 L23: -1.5975 REMARK 3 S TENSOR REMARK 3 S11: 0.1021 S12: -0.4415 S13: -0.1634 REMARK 3 S21: 0.2208 S22: 0.0782 S23: 0.0681 REMARK 3 S31: -0.0550 S32: -0.1613 S33: -0.0351 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 121 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0475 21.2560 -11.7183 REMARK 3 T TENSOR REMARK 3 T11: 0.1886 T22: 0.1498 REMARK 3 T33: 0.2073 T12: -0.0326 REMARK 3 T13: -0.0731 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 3.8716 L22: 5.8326 REMARK 3 L33: 7.6296 L12: 4.6557 REMARK 3 L13: -4.8836 L23: -5.3539 REMARK 3 S TENSOR REMARK 3 S11: 0.1024 S12: -0.3446 S13: -0.1388 REMARK 3 S21: 0.3327 S22: -0.3989 S23: -0.2733 REMARK 3 S31: -0.5292 S32: 0.3740 S33: 0.1973 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 133 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.5711 21.8160 -38.3903 REMARK 3 T TENSOR REMARK 3 T11: 0.1176 T22: 0.1037 REMARK 3 T33: 0.1459 T12: -0.0156 REMARK 3 T13: 0.0140 T23: -0.0150 REMARK 3 L TENSOR REMARK 3 L11: 6.0053 L22: 2.8276 REMARK 3 L33: 7.0261 L12: 3.1176 REMARK 3 L13: 6.0054 L23: 2.3762 REMARK 3 S TENSOR REMARK 3 S11: -0.0513 S12: 0.4523 S13: -0.3811 REMARK 3 S21: -0.1425 S22: 0.1763 S23: -0.1391 REMARK 3 S31: -0.0440 S32: 0.1412 S33: -0.1091 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 148 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2228 25.8986 -24.6076 REMARK 3 T TENSOR REMARK 3 T11: 0.1702 T22: 0.0799 REMARK 3 T33: 0.1292 T12: -0.0260 REMARK 3 T13: -0.0026 T23: -0.0103 REMARK 3 L TENSOR REMARK 3 L11: 3.1010 L22: 0.7784 REMARK 3 L33: 3.2936 L12: -1.1864 REMARK 3 L13: 1.9577 L23: -1.2106 REMARK 3 S TENSOR REMARK 3 S11: -0.0527 S12: -0.1352 S13: 0.0493 REMARK 3 S21: 0.1839 S22: 0.0199 S23: -0.0587 REMARK 3 S31: -0.2659 S32: -0.0886 S33: 0.0271 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 194 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.1836 31.1268 -32.6874 REMARK 3 T TENSOR REMARK 3 T11: 0.1523 T22: 0.0611 REMARK 3 T33: 0.1504 T12: 0.0007 REMARK 3 T13: -0.0135 T23: -0.0078 REMARK 3 L TENSOR REMARK 3 L11: 2.6189 L22: 2.2046 REMARK 3 L33: 2.0032 L12: 1.1518 REMARK 3 L13: 0.8476 L23: 0.0080 REMARK 3 S TENSOR REMARK 3 S11: -0.1724 S12: 0.0288 S13: 0.2913 REMARK 3 S21: 0.0956 S22: 0.0490 S23: 0.0272 REMARK 3 S31: -0.3534 S32: -0.0609 S33: 0.1477 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 224 THROUGH 233 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.9207 31.0128 -40.8277 REMARK 3 T TENSOR REMARK 3 T11: 0.1521 T22: 0.2010 REMARK 3 T33: 0.1674 T12: -0.0543 REMARK 3 T13: 0.0047 T23: -0.0136 REMARK 3 L TENSOR REMARK 3 L11: 3.5344 L22: 5.4546 REMARK 3 L33: 1.4477 L12: 2.8235 REMARK 3 L13: 1.9145 L23: 1.6521 REMARK 3 S TENSOR REMARK 3 S11: -0.2312 S12: 0.7440 S13: -0.0961 REMARK 3 S21: -0.4094 S22: 0.3048 S23: -0.2485 REMARK 3 S31: -0.3058 S32: 0.6269 S33: -0.1799 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 20 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.5290 -3.1625 -16.4405 REMARK 3 T TENSOR REMARK 3 T11: 0.2334 T22: 0.1924 REMARK 3 T33: 0.3290 T12: -0.0764 REMARK 3 T13: -0.0935 T23: -0.0504 REMARK 3 L TENSOR REMARK 3 L11: 3.3565 L22: 5.2658 REMARK 3 L33: 4.0133 L12: -3.3439 REMARK 3 L13: 0.4934 L23: -0.8348 REMARK 3 S TENSOR REMARK 3 S11: 0.4080 S12: 0.5269 S13: -0.5240 REMARK 3 S21: -0.1073 S22: -0.2242 S23: -0.1237 REMARK 3 S31: 0.4399 S32: -0.0697 S33: -0.1627 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 37 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.1044 -6.8399 -4.6652 REMARK 3 T TENSOR REMARK 3 T11: 0.3269 T22: 0.3375 REMARK 3 T33: 0.5227 T12: -0.1155 REMARK 3 T13: -0.1169 T23: 0.1864 REMARK 3 L TENSOR REMARK 3 L11: 1.6475 L22: 1.3623 REMARK 3 L33: 3.6865 L12: 0.2571 REMARK 3 L13: 0.7690 L23: -0.6804 REMARK 3 S TENSOR REMARK 3 S11: 0.2688 S12: -0.4327 S13: -0.9122 REMARK 3 S21: 0.1750 S22: 0.0542 S23: -0.0807 REMARK 3 S31: 0.6594 S32: -0.4579 S33: -0.2147 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 95 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.5367 -0.4095 -14.2690 REMARK 3 T TENSOR REMARK 3 T11: 0.1947 T22: 0.1246 REMARK 3 T33: 0.2624 T12: -0.0532 REMARK 3 T13: -0.0439 T23: 0.0161 REMARK 3 L TENSOR REMARK 3 L11: 1.4746 L22: 0.9080 REMARK 3 L33: 2.1913 L12: 0.1999 REMARK 3 L13: 0.1862 L23: -0.8139 REMARK 3 S TENSOR REMARK 3 S11: 0.0605 S12: -0.1909 S13: -0.3744 REMARK 3 S21: 0.0060 S22: 0.0982 S23: -0.0665 REMARK 3 S31: 0.2960 S32: -0.2871 S33: -0.0760 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 165 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.7891 12.8505 -29.7776 REMARK 3 T TENSOR REMARK 3 T11: 0.1174 T22: 0.0780 REMARK 3 T33: 0.1110 T12: -0.0230 REMARK 3 T13: 0.0015 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 3.3110 L22: 1.3284 REMARK 3 L33: 1.4349 L12: -0.2414 REMARK 3 L13: -0.3773 L23: 0.1202 REMARK 3 S TENSOR REMARK 3 S11: -0.0227 S12: -0.1202 S13: -0.0418 REMARK 3 S21: -0.0515 S22: 0.0364 S23: -0.1403 REMARK 3 S31: 0.0867 S32: -0.0709 S33: -0.0291 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 221 THROUGH 246 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.6824 6.8901 -37.1077 REMARK 3 T TENSOR REMARK 3 T11: 0.1671 T22: 0.1106 REMARK 3 T33: 0.1761 T12: -0.0336 REMARK 3 T13: 0.0076 T23: -0.0167 REMARK 3 L TENSOR REMARK 3 L11: 7.5358 L22: 2.1956 REMARK 3 L33: 3.9018 L12: 1.0992 REMARK 3 L13: -3.0332 L23: 0.3685 REMARK 3 S TENSOR REMARK 3 S11: -0.0700 S12: 0.5822 S13: -0.2334 REMARK 3 S21: -0.2906 S22: 0.1512 S23: 0.0136 REMARK 3 S31: 0.0865 S32: -0.3769 S33: 0.0216 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 15 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.7118 -19.3025 12.0350 REMARK 3 T TENSOR REMARK 3 T11: 0.5410 T22: 0.7810 REMARK 3 T33: 0.8014 T12: -0.2427 REMARK 3 T13: -0.3094 T23: 0.4983 REMARK 3 L TENSOR REMARK 3 L11: 2.1854 L22: 3.6274 REMARK 3 L33: 4.2603 L12: -1.2072 REMARK 3 L13: 2.3075 L23: -2.9796 REMARK 3 S TENSOR REMARK 3 S11: 0.7429 S12: -0.0786 S13: -0.9938 REMARK 3 S21: -0.2755 S22: 0.1632 S23: 0.4995 REMARK 3 S31: 0.9450 S32: -0.4646 S33: 0.2302 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 33 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.7194 -17.2173 20.3151 REMARK 3 T TENSOR REMARK 3 T11: 0.3568 T22: 0.6881 REMARK 3 T33: 0.6017 T12: -0.0733 REMARK 3 T13: -0.0546 T23: 0.3658 REMARK 3 L TENSOR REMARK 3 L11: 1.8645 L22: 7.1427 REMARK 3 L33: 3.4871 L12: -3.6450 REMARK 3 L13: 2.5622 L23: -4.9321 REMARK 3 S TENSOR REMARK 3 S11: -0.1224 S12: 0.0096 S13: -0.3085 REMARK 3 S21: 0.2306 S22: 0.7951 S23: 0.7914 REMARK 3 S31: -0.2022 S32: -0.5375 S33: -0.5333 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 9Q1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298922. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-OCT-22 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 : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145193 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11800 REMARK 200 FOR THE DATA SET : 5.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.69200 REMARK 200 FOR SHELL : 1.500 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 (%): 49.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE, 20% PEG 4000, 5% REMARK 280 ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 24.75400 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, D, 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 APPLY THE FOLLOWING TO CHAINS: B, A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 CYS B 214 REMARK 465 SER A 28 REMARK 465 LEU A 29 REMARK 465 SER A 30 REMARK 465 SER A 138 REMARK 465 LYS A 139 REMARK 465 SER A 140 REMARK 465 THR A 141 REMARK 465 SER A 142 REMARK 465 GLY A 143 REMARK 465 SER A 225 REMARK 465 CYS A 226 REMARK 465 ASP A 227 REMARK 465 LYS A 228 REMARK 465 THR A 229 REMARK 465 HIS A 230 REMARK 465 GLY C 206 REMARK 465 MET C 207 REMARK 465 ARG C 208 REMARK 465 ARG C 247 REMARK 465 SER C 248 REMARK 465 GLN C 249 REMARK 465 GLU C 250 REMARK 465 GLU C 251 REMARK 465 ARG C 252 REMARK 465 SER D 138 REMARK 465 LYS D 139 REMARK 465 SER D 140 REMARK 465 THR D 141 REMARK 465 SER D 142 REMARK 465 ASP D 227 REMARK 465 LYS D 228 REMARK 465 THR D 229 REMARK 465 HIS D 230 REMARK 465 GLY F 206 REMARK 465 MET F 207 REMARK 465 ARG F 208 REMARK 465 ASP F 209 REMARK 465 GLN F 249 REMARK 465 GLU F 250 REMARK 465 GLU F 251 REMARK 465 ARG F 252 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS B 42 CE NZ REMARK 470 GLN B 100 CD OE1 NE2 REMARK 470 GLU B 123 CG CD OE1 OE2 REMARK 470 LYS B 126 CG CD CE NZ REMARK 470 LYS B 145 CD CE NZ REMARK 470 LYS B 169 NZ REMARK 470 LYS B 183 NZ REMARK 470 GLU B 213 CD OE1 OE2 REMARK 470 GLN A 1 CG CD OE1 NE2 REMARK 470 ASP A 27 CG OD1 OD2 REMARK 470 SER A 31 OG REMARK 470 LYS A 45 CD CE NZ REMARK 470 LYS A 83 CE NZ REMARK 470 THR A 201 OG1 CG2 REMARK 470 LYS A 216 CE NZ REMARK 470 LYS A 224 CD CE NZ REMARK 470 ASP C 209 CG OD1 OD2 REMARK 470 ARG C 211 CD NE CZ NH1 NH2 REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 ARG C 215 CD NE CZ NH1 NH2 REMARK 470 GLU C 239 CG CD OE1 OE2 REMARK 470 GLN E 3 CG CD OE1 NE2 REMARK 470 LYS E 107 CD CE NZ REMARK 470 LYS E 126 CG CD CE NZ REMARK 470 ARG E 142 CZ NH1 NH2 REMARK 470 LYS E 169 CG CD CE NZ REMARK 470 LYS E 188 CE NZ REMARK 470 CYS E 214 SG REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 SER D 25 OG REMARK 470 ASP D 27 CG OD1 OD2 REMARK 470 LYS D 66 CD CE NZ REMARK 470 SER D 76 OG REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 115 CD OE1 NE2 REMARK 470 SER D 137 OG REMARK 470 LYS D 211 CE NZ REMARK 470 LYS D 216 CE NZ REMARK 470 ARG D 220 CZ NH1 NH2 REMARK 470 LYS D 224 CG CD CE NZ REMARK 470 CYS D 226 SG REMARK 470 ARG F 211 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 212 CG CD OE1 OE2 REMARK 470 ARG F 215 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 219 CG CD OE1 OE2 REMARK 470 ARG F 237 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 241 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 243 CG CD OE1 OE2 REMARK 470 GLU F 244 CG CD OE1 OE2 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 SER B 30 -128.30 54.53 REMARK 500 ALA B 51 -37.88 76.33 REMARK 500 ASN B 152 -8.94 81.29 REMARK 500 SER A 15 -3.51 78.71 REMARK 500 THR A 104 -73.93 -107.25 REMARK 500 THR A 105 -84.60 -101.48 REMARK 500 ASP A 154 73.43 67.84 REMARK 500 SER E 30 -126.51 54.22 REMARK 500 ALA E 51 -35.85 77.13 REMARK 500 ALA E 84 170.51 178.98 REMARK 500 ASN E 138 71.00 53.70 REMARK 500 ASN E 152 -1.67 75.69 REMARK 500 SER D 15 -11.11 81.65 REMARK 500 SER D 25 58.46 -90.91 REMARK 500 THR D 105 -78.65 -121.74 REMARK 500 ASP D 154 68.85 65.95 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 647 DISTANCE = 6.69 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 EDO E 301 DBREF 9Q1L B 1 214 PDB 9Q1L 9Q1L 1 214 DBREF 9Q1L A 1 230 PDB 9Q1L 9Q1L 1 230 DBREF 9Q1L C 208 252 UNP Q9SEW4 VCL2_JUGRE 12 56 DBREF 9Q1L E 1 214 PDB 9Q1L 9Q1L 1 214 DBREF 9Q1L D 1 230 PDB 9Q1L 9Q1L 1 230 DBREF 9Q1L F 208 252 UNP Q9SEW4 VCL2_JUGRE 12 56 SEQADV 9Q1L GLY C 206 UNP Q9SEW4 EXPRESSION TAG SEQADV 9Q1L MET C 207 UNP Q9SEW4 EXPRESSION TAG SEQADV 9Q1L GLY F 206 UNP Q9SEW4 EXPRESSION TAG SEQADV 9Q1L MET F 207 UNP Q9SEW4 EXPRESSION TAG SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO PRO SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY VAL ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 B 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR PHE THR ILE THR SER LEU SEQRES 7 B 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 ASP THR VAL PRO LEU THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 230 GLN VAL GLN LEU LEU GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 230 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 230 ASP SER LEU SER SER GLY SER TYR PHE TRP SER TRP ILE SEQRES 4 A 230 ARG GLN PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 A 230 MET HIS SER SER GLY SER SER ASN TYR ASN PRO SER LEU SEQRES 6 A 230 LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS ARG SEQRES 7 A 230 GLN PHE SER LEU LYS LEU ARG SER VAL THR ALA THR ASP SEQRES 8 A 230 THR ALA VAL TYR TYR CYS ALA ARG ALA ASP CYS SER THR SEQRES 9 A 230 THR SER CYS TYR THR TYR HIS ILE TRP GLY GLN GLY THR SEQRES 10 A 230 MET VAL ILE VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 A 230 GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 C 47 GLY MET ARG ASP PRO ARG GLU GLN TYR ARG GLN CYS GLN SEQRES 2 C 47 GLU TYR CYS ARG ARG GLN GLY GLN GLY GLN ARG GLN GLN SEQRES 3 C 47 GLN GLN CYS GLN ILE ARG CYS GLU GLU ARG LEU GLU GLU SEQRES 4 C 47 ASP GLN ARG SER GLN GLU GLU ARG SEQRES 1 E 214 ASP ILE GLN MET THR GLN SER PRO PRO SER LEU SER ALA SEQRES 2 E 214 SER VAL GLY VAL ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 E 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 E 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 E 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER GLY THR ASP PHE THR PHE THR ILE THR SER LEU SEQRES 7 E 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 E 214 ASP THR VAL PRO LEU THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 E 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 E 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 E 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 E 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 E 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 E 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 E 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 E 214 PHE ASN ARG GLY GLU CYS SEQRES 1 D 230 GLN VAL GLN LEU LEU GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 D 230 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 D 230 ASP SER LEU SER SER GLY SER TYR PHE TRP SER TRP ILE SEQRES 4 D 230 ARG GLN PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 D 230 MET HIS SER SER GLY SER SER ASN TYR ASN PRO SER LEU SEQRES 6 D 230 LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS ARG SEQRES 7 D 230 GLN PHE SER LEU LYS LEU ARG SER VAL THR ALA THR ASP SEQRES 8 D 230 THR ALA VAL TYR TYR CYS ALA ARG ALA ASP CYS SER THR SEQRES 9 D 230 THR SER CYS TYR THR TYR HIS ILE TRP GLY GLN GLY THR SEQRES 10 D 230 MET VAL ILE VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 D 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 D 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 D 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 D 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 D 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 D 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 D 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 D 230 GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 F 47 GLY MET ARG ASP PRO ARG GLU GLN TYR ARG GLN CYS GLN SEQRES 2 F 47 GLU TYR CYS ARG ARG GLN GLY GLN GLY GLN ARG GLN GLN SEQRES 3 F 47 GLN GLN CYS GLN ILE ARG CYS GLU GLU ARG LEU GLU GLU SEQRES 4 F 47 ASP GLN ARG SER GLN GLU GLU ARG HET EDO B 301 10 HET EDO B 302 10 HET EDO B 303 10 HET EDO A 301 10 HET EDO A 302 10 HET EDO A 303 10 HET EDO A 304 10 HET EDO E 301 6 HET EDO E 302 10 HET EDO E 303 10 HET EDO E 304 10 HET CL E 305 1 HET EDO D 301 10 HET EDO D 302 10 HETNAM EDO 1,2-ETHANEDIOL HETNAM CL CHLORIDE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 7 EDO 13(C2 H6 O2) FORMUL 18 CL CL 1- FORMUL 21 HOH *981(H2 O) HELIX 1 AA1 GLN B 79 VAL B 83 5 5 HELIX 2 AA2 SER B 121 SER B 127 1 7 HELIX 3 AA3 LYS B 183 GLU B 187 1 5 HELIX 4 AA4 PRO A 63 LYS A 66 5 4 HELIX 5 AA5 THR A 75 LYS A 77 5 3 HELIX 6 AA6 THR A 88 THR A 92 5 5 HELIX 7 AA7 SER A 166 ALA A 168 5 3 HELIX 8 AA8 SER A 197 LEU A 199 5 3 HELIX 9 AA9 LYS A 211 ASN A 214 5 4 HELIX 10 AB1 PRO C 210 GLY C 225 1 16 HELIX 11 AB2 GLY C 227 GLN C 246 1 20 HELIX 12 AB3 GLN E 79 VAL E 83 5 5 HELIX 13 AB4 SER E 121 SER E 127 1 7 HELIX 14 AB5 LYS E 183 GLU E 187 1 5 HELIX 15 AB6 ASP D 27 SER D 31 5 5 HELIX 16 AB7 THR D 88 THR D 92 5 5 HELIX 17 AB8 SER D 166 ALA D 168 5 3 HELIX 18 AB9 SER D 197 THR D 201 5 5 HELIX 19 AC1 LYS D 211 ASN D 214 5 4 HELIX 20 AC2 ARG F 211 GLY F 225 1 15 HELIX 21 AC3 GLY F 227 ARG F 247 1 21 SHEET 1 AA1 4 MET B 4 SER B 7 0 SHEET 2 AA1 4 VAL B 19 ALA B 25 -1 O GLN B 24 N THR B 5 SHEET 3 AA1 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21 SHEET 4 AA1 4 PHE B 62 GLY B 66 -1 N SER B 63 O THR B 74 SHEET 1 AA2 6 SER B 10 SER B 14 0 SHEET 2 AA2 6 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA2 6 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA2 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA2 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA2 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA3 4 SER B 10 SER B 14 0 SHEET 2 AA3 4 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA3 4 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA3 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA4 4 SER B 114 PHE B 118 0 SHEET 2 AA4 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AA4 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AA4 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AA5 4 ALA B 153 LEU B 154 0 SHEET 2 AA5 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AA5 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AA5 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AA6 4 LEU A 4 SER A 7 0 SHEET 2 AA6 4 LEU A 18 VAL A 24 -1 O THR A 21 N SER A 7 SHEET 3 AA6 4 GLN A 79 LEU A 84 -1 O PHE A 80 N CYS A 22 SHEET 4 AA6 4 VAL A 69 ASP A 74 -1 N ASP A 74 O GLN A 79 SHEET 1 AA7 6 LEU A 11 VAL A 12 0 SHEET 2 AA7 6 THR A 117 VAL A 121 1 O ILE A 120 N VAL A 12 SHEET 3 AA7 6 ALA A 93 ASP A 101 -1 N TYR A 95 O THR A 117 SHEET 4 AA7 6 TYR A 34 GLN A 41 -1 N ILE A 39 O TYR A 96 SHEET 5 AA7 6 GLU A 48 HIS A 54 -1 O GLU A 48 N ARG A 40 SHEET 6 AA7 6 SER A 59 TYR A 61 -1 O ASN A 60 N HIS A 52 SHEET 1 AA8 4 LEU A 11 VAL A 12 0 SHEET 2 AA8 4 THR A 117 VAL A 121 1 O ILE A 120 N VAL A 12 SHEET 3 AA8 4 ALA A 93 ASP A 101 -1 N TYR A 95 O THR A 117 SHEET 4 AA8 4 ILE A 112 TRP A 113 -1 O ILE A 112 N ARG A 99 SHEET 1 AA9 4 SER A 130 LEU A 134 0 SHEET 2 AA9 4 THR A 145 TYR A 155 -1 O GLY A 149 N LEU A 134 SHEET 3 AA9 4 TYR A 186 PRO A 195 -1 O LEU A 188 N VAL A 152 SHEET 4 AA9 4 VAL A 173 THR A 175 -1 N HIS A 174 O VAL A 191 SHEET 1 AB1 4 SER A 130 LEU A 134 0 SHEET 2 AB1 4 THR A 145 TYR A 155 -1 O GLY A 149 N LEU A 134 SHEET 3 AB1 4 TYR A 186 PRO A 195 -1 O LEU A 188 N VAL A 152 SHEET 4 AB1 4 VAL A 179 LEU A 180 -1 N VAL A 179 O SER A 187 SHEET 1 AB2 3 THR A 161 TRP A 164 0 SHEET 2 AB2 3 ILE A 205 HIS A 210 -1 O ASN A 207 N SER A 163 SHEET 3 AB2 3 THR A 215 ARG A 220 -1 O VAL A 217 N VAL A 208 SHEET 1 AB3 4 MET E 4 SER E 7 0 SHEET 2 AB3 4 VAL E 19 ALA E 25 -1 O GLN E 24 N THR E 5 SHEET 3 AB3 4 ASP E 70 ILE E 75 -1 O PHE E 73 N ILE E 21 SHEET 4 AB3 4 PHE E 62 GLY E 66 -1 N SER E 63 O THR E 74 SHEET 1 AB4 6 SER E 10 SER E 14 0 SHEET 2 AB4 6 THR E 102 LYS E 107 1 O GLU E 105 N LEU E 11 SHEET 3 AB4 6 ALA E 84 GLN E 90 -1 N ALA E 84 O LEU E 104 SHEET 4 AB4 6 LEU E 33 GLN E 38 -1 N TYR E 36 O TYR E 87 SHEET 5 AB4 6 LYS E 45 TYR E 49 -1 O ILE E 48 N TRP E 35 SHEET 6 AB4 6 ASN E 53 LEU E 54 -1 O ASN E 53 N TYR E 49 SHEET 1 AB5 4 SER E 10 SER E 14 0 SHEET 2 AB5 4 THR E 102 LYS E 107 1 O GLU E 105 N LEU E 11 SHEET 3 AB5 4 ALA E 84 GLN E 90 -1 N ALA E 84 O LEU E 104 SHEET 4 AB5 4 THR E 97 PHE E 98 -1 O THR E 97 N GLN E 90 SHEET 1 AB6 4 SER E 114 PHE E 118 0 SHEET 2 AB6 4 THR E 129 PHE E 139 -1 O LEU E 135 N PHE E 116 SHEET 3 AB6 4 TYR E 173 SER E 182 -1 O LEU E 181 N ALA E 130 SHEET 4 AB6 4 SER E 159 VAL E 163 -1 N GLN E 160 O THR E 178 SHEET 1 AB7 4 ALA E 153 LEU E 154 0 SHEET 2 AB7 4 LYS E 145 VAL E 150 -1 N VAL E 150 O ALA E 153 SHEET 3 AB7 4 VAL E 191 THR E 197 -1 O GLU E 195 N GLN E 147 SHEET 4 AB7 4 VAL E 205 ASN E 210 -1 O VAL E 205 N VAL E 196 SHEET 1 AB8 4 LEU D 4 SER D 7 0 SHEET 2 AB8 4 LEU D 18 VAL D 24 -1 O THR D 23 N LEU D 5 SHEET 3 AB8 4 GLN D 79 LEU D 84 -1 O LEU D 84 N LEU D 18 SHEET 4 AB8 4 VAL D 69 ASP D 74 -1 N SER D 72 O SER D 81 SHEET 1 AB9 6 LEU D 11 VAL D 12 0 SHEET 2 AB9 6 THR D 117 VAL D 121 1 O ILE D 120 N VAL D 12 SHEET 3 AB9 6 ALA D 93 ASP D 101 -1 N TYR D 95 O THR D 117 SHEET 4 AB9 6 TYR D 34 GLN D 41 -1 N ILE D 39 O TYR D 96 SHEET 5 AB9 6 GLU D 48 HIS D 54 -1 O GLU D 48 N ARG D 40 SHEET 6 AB9 6 SER D 59 TYR D 61 -1 O ASN D 60 N HIS D 52 SHEET 1 AC1 4 LEU D 11 VAL D 12 0 SHEET 2 AC1 4 THR D 117 VAL D 121 1 O ILE D 120 N VAL D 12 SHEET 3 AC1 4 ALA D 93 ASP D 101 -1 N TYR D 95 O THR D 117 SHEET 4 AC1 4 TYR D 110 TRP D 113 -1 O ILE D 112 N ARG D 99 SHEET 1 AC2 4 SER D 130 LEU D 134 0 SHEET 2 AC2 4 THR D 145 TYR D 155 -1 O LYS D 153 N SER D 130 SHEET 3 AC2 4 TYR D 186 PRO D 195 -1 O LEU D 188 N VAL D 152 SHEET 4 AC2 4 VAL D 173 THR D 175 -1 N HIS D 174 O VAL D 191 SHEET 1 AC3 4 SER D 130 LEU D 134 0 SHEET 2 AC3 4 THR D 145 TYR D 155 -1 O LYS D 153 N SER D 130 SHEET 3 AC3 4 TYR D 186 PRO D 195 -1 O LEU D 188 N VAL D 152 SHEET 4 AC3 4 VAL D 179 LEU D 180 -1 N VAL D 179 O SER D 187 SHEET 1 AC4 3 THR D 161 TRP D 164 0 SHEET 2 AC4 3 ILE D 205 HIS D 210 -1 O ASN D 207 N SER D 163 SHEET 3 AC4 3 THR D 215 ARG D 220 -1 O VAL D 217 N VAL D 208 SSBOND 1 CYS B 23 CYS B 88 1555 1555 2.07 SSBOND 2 CYS B 134 CYS B 194 1555 1555 2.05 SSBOND 3 CYS A 22 CYS A 97 1555 1555 2.09 SSBOND 4 CYS A 102 CYS A 107 1555 1555 2.05 SSBOND 5 CYS A 150 CYS A 206 1555 1555 2.04 SSBOND 6 CYS C 217 CYS C 238 1555 1555 2.04 SSBOND 7 CYS C 221 CYS C 234 1555 1555 2.03 SSBOND 8 CYS E 23 CYS E 88 1555 1555 2.06 SSBOND 9 CYS E 134 CYS E 194 1555 1555 2.06 SSBOND 10 CYS D 22 CYS D 97 1555 1555 2.05 SSBOND 11 CYS D 102 CYS D 107 1555 1555 2.04 SSBOND 12 CYS D 150 CYS D 206 1555 1555 2.04 SSBOND 13 CYS F 217 CYS F 238 1555 1555 2.03 SSBOND 14 CYS F 221 CYS F 234 1555 1555 2.06 CISPEP 1 SER B 7 PRO B 8 0 -4.67 CISPEP 2 VAL B 94 PRO B 95 0 -1.04 CISPEP 3 TYR B 140 PRO B 141 0 1.60 CISPEP 4 PHE A 156 PRO A 157 0 -4.17 CISPEP 5 GLU A 158 PRO A 159 0 1.83 CISPEP 6 SER E 7 PRO E 8 0 -6.26 CISPEP 7 VAL E 94 PRO E 95 0 0.39 CISPEP 8 TYR E 140 PRO E 141 0 1.03 CISPEP 9 PHE D 156 PRO D 157 0 -6.60 CISPEP 10 GLU D 158 PRO D 159 0 0.90 CRYST1 98.541 49.508 111.093 90.00 104.73 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010148 0.000000 0.002668 0.00000 SCALE2 0.000000 0.020199 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009307 0.00000