HEADER IMMUNE SYSTEM 08-NOV-23 8UX6 TITLE STRUCTURE OF FAB201 WITH A T. PARVA SPOROZOITE NEUTRALIZING B CELL TITLE 2 EPITOPE OF P67 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB201 LIGHT CHAIN; COMPND 3 CHAIN: C, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB201 HEAVY CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: P67 PROTEIN; COMPND 11 CHAIN: E, F; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: XP_763305.1 RESIDUES 572-612 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 17 MOL_ID: 3; SOURCE 18 SYNTHETIC: YES; SOURCE 19 ORGANISM_SCIENTIFIC: THEILERIA PARVA STRAIN MUGUGA; SOURCE 20 ORGANISM_TAXID: 333668 KEYWDS NEUTRALIZING ANTIBODY, PROTOZOAN, SPOROZOITE, CELL INVASION, KEYWDS 2 IMMUNITY, WEST COAST FEVER, CATTLE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.U.SINGER,A.GOPALSAMY,F.A.FELLOUSE,S.MIERSCH,S.S.SIDHU REVDAT 1 16-OCT-24 8UX6 0 JRNL AUTH S.MIERSCH,A.U.SINGER,C.CHEN,A.GOPALSAMY,L.DA COSTA, JRNL AUTH 2 A.LACASTA,H.CHEGE,N.CHEGE,F.SICHERI,V.NENE,S.S.SIDHU JRNL TITL MOLECULAR CHARACTERIZATION OF A NOVEL CONFORMATIONAL JRNL TITL 2 SPOROZOITE NEUTRALIZING B CELL EPITOPE IN P67 OF THEILERIA JRNL TITL 3 PARVA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.00 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3 REMARK 3 NUMBER OF REFLECTIONS : 54787 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.270 REMARK 3 FREE R VALUE TEST SET COUNT : 1792 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.5200 - 4.6800 0.89 4173 137 0.1968 0.2116 REMARK 3 2 4.6800 - 3.7300 0.94 4375 151 0.1705 0.2028 REMARK 3 3 3.7300 - 3.2600 0.79 3660 128 0.1896 0.2375 REMARK 3 4 3.2600 - 2.9600 0.89 4158 135 0.2130 0.2760 REMARK 3 5 2.9600 - 2.7500 0.91 4222 150 0.2113 0.2507 REMARK 3 6 2.7500 - 2.5900 0.92 4270 137 0.2248 0.2913 REMARK 3 7 2.5900 - 2.4600 0.78 3632 131 0.2228 0.2895 REMARK 3 8 2.4600 - 2.3500 0.82 3869 124 0.2353 0.2845 REMARK 3 9 2.3500 - 2.2600 0.87 4018 136 0.2249 0.2967 REMARK 3 10 2.2600 - 2.1800 0.89 4146 140 0.2268 0.2896 REMARK 3 11 2.1800 - 2.1100 0.89 4153 145 0.2334 0.3482 REMARK 3 12 2.1100 - 2.0500 0.89 4120 134 0.2318 0.2859 REMARK 3 13 2.0500 - 2.0000 0.89 4199 144 0.2373 0.2960 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) : 0.257 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.705 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.19 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.35 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 : 0.008 6826 REMARK 3 ANGLE : 0.943 9283 REMARK 3 CHIRALITY : 0.056 1064 REMARK 3 PLANARITY : 0.008 1181 REMARK 3 DIHEDRAL : 16.154 2379 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.2985 9.9825 30.9863 REMARK 3 T TENSOR REMARK 3 T11: 0.3293 T22: 0.4142 REMARK 3 T33: 0.2060 T12: -0.0925 REMARK 3 T13: 0.0400 T23: -0.0880 REMARK 3 L TENSOR REMARK 3 L11: 1.4135 L22: 2.9436 REMARK 3 L33: 5.2168 L12: -0.4631 REMARK 3 L13: 0.3172 L23: 0.7371 REMARK 3 S TENSOR REMARK 3 S11: 0.0458 S12: -0.4380 S13: 0.2586 REMARK 3 S21: 0.3448 S22: 0.0356 S23: -0.1304 REMARK 3 S31: -0.1111 S32: 0.2579 S33: -0.0899 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 107 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.6733 26.6505 18.7543 REMARK 3 T TENSOR REMARK 3 T11: 0.2164 T22: 0.2726 REMARK 3 T33: 0.4101 T12: -0.0220 REMARK 3 T13: 0.0472 T23: -0.0371 REMARK 3 L TENSOR REMARK 3 L11: 0.3497 L22: 4.2637 REMARK 3 L33: 1.1781 L12: 1.3415 REMARK 3 L13: -0.0617 L23: -0.4785 REMARK 3 S TENSOR REMARK 3 S11: 0.2806 S12: -0.1323 S13: 0.2826 REMARK 3 S21: 0.5086 S22: -0.2528 S23: 0.0352 REMARK 3 S31: -0.2773 S32: 0.0530 S33: -0.0086 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 149 THROUGH 233 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0083 42.6019 15.7618 REMARK 3 T TENSOR REMARK 3 T11: 0.3467 T22: 0.2668 REMARK 3 T33: 0.5514 T12: -0.1213 REMARK 3 T13: 0.0788 T23: -0.0772 REMARK 3 L TENSOR REMARK 3 L11: 1.6012 L22: 5.2838 REMARK 3 L33: 6.5691 L12: -0.1575 REMARK 3 L13: -0.1663 L23: -3.4626 REMARK 3 S TENSOR REMARK 3 S11: 0.1719 S12: -0.1447 S13: 0.1946 REMARK 3 S21: 0.4746 S22: -0.1837 S23: 0.3216 REMARK 3 S31: -0.4678 S32: -0.2145 S33: -0.0257 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1113 17.2343 53.0803 REMARK 3 T TENSOR REMARK 3 T11: 0.3050 T22: 0.4839 REMARK 3 T33: 0.2556 T12: 0.0949 REMARK 3 T13: -0.0162 T23: -0.1294 REMARK 3 L TENSOR REMARK 3 L11: 1.0293 L22: 2.7948 REMARK 3 L33: 5.2018 L12: -0.6367 REMARK 3 L13: -0.0791 L23: 0.8030 REMARK 3 S TENSOR REMARK 3 S11: 0.1850 S12: 0.6478 S13: -0.1893 REMARK 3 S21: -0.3381 S22: -0.2863 S23: 0.1540 REMARK 3 S31: 0.0661 S32: -0.1406 S33: 0.0698 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 183 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.8663 49.3440 46.1203 REMARK 3 T TENSOR REMARK 3 T11: 0.6554 T22: 0.8511 REMARK 3 T33: 0.4694 T12: 0.2807 REMARK 3 T13: -0.0025 T23: 0.2484 REMARK 3 L TENSOR REMARK 3 L11: 1.2431 L22: 1.6150 REMARK 3 L33: 1.3198 L12: -0.9504 REMARK 3 L13: 0.1645 L23: -0.5048 REMARK 3 S TENSOR REMARK 3 S11: 0.1626 S12: 0.9305 S13: 0.6038 REMARK 3 S21: -0.4231 S22: -0.3231 S23: -0.0409 REMARK 3 S31: -0.0891 S32: 0.2897 S33: 0.1204 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 231 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3352 51.9422 43.9339 REMARK 3 T TENSOR REMARK 3 T11: 0.6504 T22: 0.8574 REMARK 3 T33: 0.4666 T12: 0.2450 REMARK 3 T13: 0.1146 T23: 0.2593 REMARK 3 L TENSOR REMARK 3 L11: 2.6664 L22: 3.1358 REMARK 3 L33: 4.7101 L12: -0.1131 REMARK 3 L13: 1.2445 L23: -0.4677 REMARK 3 S TENSOR REMARK 3 S11: 0.1926 S12: 1.0834 S13: 0.4233 REMARK 3 S21: -0.7891 S22: -0.3314 S23: -0.3957 REMARK 3 S31: -0.7781 S32: 0.2600 S33: 0.1173 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7943 26.0849 76.9375 REMARK 3 T TENSOR REMARK 3 T11: 0.1795 T22: 0.1766 REMARK 3 T33: 0.1871 T12: 0.0401 REMARK 3 T13: 0.0108 T23: -0.0438 REMARK 3 L TENSOR REMARK 3 L11: 4.1201 L22: 8.9835 REMARK 3 L33: 1.8176 L12: 4.1183 REMARK 3 L13: 0.2001 L23: -0.2413 REMARK 3 S TENSOR REMARK 3 S11: 0.1479 S12: 0.0432 S13: 0.2043 REMARK 3 S21: 0.2036 S22: -0.2242 S23: 0.3581 REMARK 3 S31: 0.0993 S32: -0.1732 S33: 0.0795 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.1460 25.5872 74.4655 REMARK 3 T TENSOR REMARK 3 T11: 0.1307 T22: 0.1729 REMARK 3 T33: 0.1944 T12: 0.0286 REMARK 3 T13: -0.0028 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 2.6564 L22: 2.9621 REMARK 3 L33: 2.6601 L12: -0.1387 REMARK 3 L13: -0.0741 L23: -0.0310 REMARK 3 S TENSOR REMARK 3 S11: 0.0266 S12: 0.1881 S13: -0.0243 REMARK 3 S21: -0.1331 S22: -0.0607 S23: -0.2005 REMARK 3 S31: 0.0862 S32: 0.1351 S33: 0.0517 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3340 30.0261 69.4802 REMARK 3 T TENSOR REMARK 3 T11: 0.1874 T22: 0.2349 REMARK 3 T33: 0.1615 T12: 0.0547 REMARK 3 T13: -0.0421 T23: -0.0007 REMARK 3 L TENSOR REMARK 3 L11: 2.0346 L22: 3.3623 REMARK 3 L33: 1.3738 L12: -1.1037 REMARK 3 L13: -0.8247 L23: 0.2791 REMARK 3 S TENSOR REMARK 3 S11: 0.0859 S12: 0.3480 S13: -0.0166 REMARK 3 S21: -0.1335 S22: -0.1898 S23: 0.2761 REMARK 3 S31: 0.0317 S32: -0.0328 S33: 0.1071 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9425 48.1927 57.2614 REMARK 3 T TENSOR REMARK 3 T11: 0.3455 T22: 0.7752 REMARK 3 T33: 0.4066 T12: 0.1893 REMARK 3 T13: 0.0527 T23: 0.1998 REMARK 3 L TENSOR REMARK 3 L11: 2.5691 L22: 1.7126 REMARK 3 L33: 4.5854 L12: -0.7809 REMARK 3 L13: 2.2879 L23: -0.6501 REMARK 3 S TENSOR REMARK 3 S11: 0.1386 S12: 0.9728 S13: 0.4973 REMARK 3 S21: -0.2027 S22: -0.0508 S23: 0.1529 REMARK 3 S31: -0.2079 S32: -0.5718 S33: 0.0009 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 210 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9954 49.4796 66.0506 REMARK 3 T TENSOR REMARK 3 T11: 0.3391 T22: 0.5807 REMARK 3 T33: 0.3279 T12: 0.1849 REMARK 3 T13: 0.0212 T23: 0.1101 REMARK 3 L TENSOR REMARK 3 L11: 8.4397 L22: 1.1965 REMARK 3 L33: 7.6739 L12: -1.9961 REMARK 3 L13: 8.0121 L23: -2.0387 REMARK 3 S TENSOR REMARK 3 S11: 0.2498 S12: 0.2718 S13: 0.3926 REMARK 3 S21: -0.1628 S22: -0.2722 S23: -0.1057 REMARK 3 S31: -0.3031 S32: -0.8885 S33: -0.0368 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.1880 7.3116 3.3764 REMARK 3 T TENSOR REMARK 3 T11: 0.1580 T22: 0.1500 REMARK 3 T33: 0.1993 T12: -0.0280 REMARK 3 T13: 0.0628 T23: -0.0216 REMARK 3 L TENSOR REMARK 3 L11: 3.6234 L22: 5.5097 REMARK 3 L33: 8.9619 L12: -1.2081 REMARK 3 L13: 4.2751 L23: -4.6149 REMARK 3 S TENSOR REMARK 3 S11: 0.1221 S12: 0.3373 S13: 0.0724 REMARK 3 S21: 0.0190 S22: -0.1628 S23: -0.1505 REMARK 3 S31: -0.1566 S32: 0.5488 S33: 0.1025 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 19 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.5055 -3.6090 8.0370 REMARK 3 T TENSOR REMARK 3 T11: 0.2190 T22: 0.1227 REMARK 3 T33: 0.2044 T12: 0.0002 REMARK 3 T13: 0.0200 T23: -0.0345 REMARK 3 L TENSOR REMARK 3 L11: 4.5013 L22: 4.4564 REMARK 3 L33: 6.1772 L12: -1.7006 REMARK 3 L13: 1.4459 L23: -3.3386 REMARK 3 S TENSOR REMARK 3 S11: 0.2030 S12: -0.1173 S13: -0.1168 REMARK 3 S21: 0.0295 S22: -0.2547 S23: 0.1879 REMARK 3 S31: 0.1019 S32: 0.0595 S33: 0.0059 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 38 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.6316 3.2347 11.2914 REMARK 3 T TENSOR REMARK 3 T11: 0.1560 T22: 0.1371 REMARK 3 T33: 0.1802 T12: -0.0191 REMARK 3 T13: 0.0391 T23: -0.0037 REMARK 3 L TENSOR REMARK 3 L11: 3.5170 L22: 2.5949 REMARK 3 L33: 3.1205 L12: 0.1678 REMARK 3 L13: -0.4011 L23: -0.6038 REMARK 3 S TENSOR REMARK 3 S11: 0.1259 S12: -0.2030 S13: 0.2375 REMARK 3 S21: 0.3001 S22: -0.0593 S23: 0.3168 REMARK 3 S31: -0.2259 S32: -0.1298 S33: -0.0499 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6641 3.1180 2.9148 REMARK 3 T TENSOR REMARK 3 T11: 0.1448 T22: 0.1105 REMARK 3 T33: 0.1764 T12: -0.0400 REMARK 3 T13: 0.0106 T23: -0.0152 REMARK 3 L TENSOR REMARK 3 L11: 3.3953 L22: 0.9216 REMARK 3 L33: 2.7687 L12: 0.8427 REMARK 3 L13: 0.4096 L23: -1.2978 REMARK 3 S TENSOR REMARK 3 S11: 0.0328 S12: 0.0817 S13: -0.0225 REMARK 3 S21: 0.0145 S22: -0.0879 S23: 0.3647 REMARK 3 S31: 0.0272 S32: 0.0175 S33: 0.0658 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 100 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5275 3.3225 15.4892 REMARK 3 T TENSOR REMARK 3 T11: 0.1983 T22: 0.1705 REMARK 3 T33: 0.1489 T12: -0.0475 REMARK 3 T13: 0.0039 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 4.4517 L22: 3.7768 REMARK 3 L33: 4.6947 L12: 0.5983 REMARK 3 L13: -1.3086 L23: -1.1039 REMARK 3 S TENSOR REMARK 3 S11: -0.0900 S12: -0.4631 S13: -0.2070 REMARK 3 S21: -0.0811 S22: -0.2252 S23: -0.1335 REMARK 3 S31: 0.1347 S32: 0.3740 S33: 0.2840 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 122 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1906 20.6768 -1.3488 REMARK 3 T TENSOR REMARK 3 T11: 0.2546 T22: 0.1452 REMARK 3 T33: 0.3446 T12: -0.0298 REMARK 3 T13: 0.0069 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 5.4447 L22: 3.8762 REMARK 3 L33: 2.7915 L12: 3.8122 REMARK 3 L13: -2.1779 L23: -0.4389 REMARK 3 S TENSOR REMARK 3 S11: -0.0094 S12: 0.4515 S13: 0.6347 REMARK 3 S21: -0.3294 S22: 0.3510 S23: 0.1598 REMARK 3 S31: 0.0630 S32: -0.0861 S33: -0.2776 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 135 THROUGH 160 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.1702 35.8264 6.2739 REMARK 3 T TENSOR REMARK 3 T11: 0.3583 T22: 0.2405 REMARK 3 T33: 0.6991 T12: -0.0815 REMARK 3 T13: 0.1397 T23: -0.1310 REMARK 3 L TENSOR REMARK 3 L11: 3.6440 L22: 3.6746 REMARK 3 L33: 4.2574 L12: 3.0336 REMARK 3 L13: 2.5536 L23: 2.1254 REMARK 3 S TENSOR REMARK 3 S11: 0.0159 S12: -0.4272 S13: 1.0317 REMARK 3 S21: -0.3353 S22: -0.0019 S23: -0.2707 REMARK 3 S31: -0.7686 S32: 0.0814 S33: 0.0592 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 161 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.1171 25.2974 8.9428 REMARK 3 T TENSOR REMARK 3 T11: 0.3839 T22: 0.2929 REMARK 3 T33: 0.5525 T12: -0.0669 REMARK 3 T13: -0.0354 T23: -0.0514 REMARK 3 L TENSOR REMARK 3 L11: 1.7333 L22: 1.4559 REMARK 3 L33: 2.0756 L12: -0.0297 REMARK 3 L13: 0.2564 L23: 0.7864 REMARK 3 S TENSOR REMARK 3 S11: 0.1446 S12: -0.1068 S13: -0.4700 REMARK 3 S21: 0.1157 S22: 0.2469 S23: -0.6194 REMARK 3 S31: 0.2420 S32: 0.3202 S33: -0.3556 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 181 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.9831 30.8910 5.7031 REMARK 3 T TENSOR REMARK 3 T11: 0.2622 T22: 0.2804 REMARK 3 T33: 0.6024 T12: -0.0836 REMARK 3 T13: 0.0781 T23: -0.0844 REMARK 3 L TENSOR REMARK 3 L11: 1.0438 L22: 2.5604 REMARK 3 L33: 3.3367 L12: 1.3012 REMARK 3 L13: 1.7413 L23: 1.3585 REMARK 3 S TENSOR REMARK 3 S11: 0.1498 S12: 0.0104 S13: 0.2165 REMARK 3 S21: 0.0238 S22: 0.1659 S23: -0.5935 REMARK 3 S31: -0.1350 S32: 0.3999 S33: -0.2500 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.0967 8.6969 72.1844 REMARK 3 T TENSOR REMARK 3 T11: 0.6921 T22: 0.3002 REMARK 3 T33: 0.4396 T12: 0.1817 REMARK 3 T13: 0.0138 T23: -0.0169 REMARK 3 L TENSOR REMARK 3 L11: 3.4576 L22: 6.7314 REMARK 3 L33: 6.7546 L12: 2.0131 REMARK 3 L13: -0.4225 L23: 5.8678 REMARK 3 S TENSOR REMARK 3 S11: 0.0503 S12: -0.2517 S13: -0.4973 REMARK 3 S21: 1.2623 S22: 0.3429 S23: 0.5776 REMARK 3 S31: 1.2127 S32: 0.3768 S33: -0.3572 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 21 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2094 4.3391 65.1293 REMARK 3 T TENSOR REMARK 3 T11: 0.7491 T22: 0.3273 REMARK 3 T33: 0.4000 T12: -0.0610 REMARK 3 T13: 0.0152 T23: -0.2197 REMARK 3 L TENSOR REMARK 3 L11: 7.0153 L22: 7.7799 REMARK 3 L33: 6.5471 L12: -5.1685 REMARK 3 L13: -3.4435 L23: 0.6612 REMARK 3 S TENSOR REMARK 3 S11: -0.2653 S12: 1.3542 S13: -1.8616 REMARK 3 S21: 0.3960 S22: 0.4460 S23: 0.0613 REMARK 3 S31: 1.3943 S32: 0.2710 S33: -0.1321 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 0 THROUGH 5 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.6902 -8.7123 19.7645 REMARK 3 T TENSOR REMARK 3 T11: 0.5415 T22: 0.2949 REMARK 3 T33: 0.4475 T12: -0.1414 REMARK 3 T13: 0.0588 T23: 0.0833 REMARK 3 L TENSOR REMARK 3 L11: 3.3150 L22: 5.8230 REMARK 3 L33: 8.5848 L12: 3.9677 REMARK 3 L13: -4.5070 L23: -3.8066 REMARK 3 S TENSOR REMARK 3 S11: -0.4695 S12: -0.1705 S13: -0.6591 REMARK 3 S21: 0.0518 S22: 0.6186 S23: 1.4088 REMARK 3 S31: 1.0625 S32: -0.7289 S33: -0.0845 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 6 THROUGH 19 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.1110 -8.3107 28.1189 REMARK 3 T TENSOR REMARK 3 T11: 0.6487 T22: 0.4285 REMARK 3 T33: 0.2708 T12: -0.0774 REMARK 3 T13: 0.0070 T23: 0.0527 REMARK 3 L TENSOR REMARK 3 L11: 3.1076 L22: 5.1572 REMARK 3 L33: 4.3912 L12: 2.5382 REMARK 3 L13: -3.0113 L23: -1.6884 REMARK 3 S TENSOR REMARK 3 S11: 0.3418 S12: -1.4668 S13: -1.0682 REMARK 3 S21: 0.9255 S22: -0.2475 S23: -0.1503 REMARK 3 S31: 0.3314 S32: 0.2218 S33: 0.0051 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 8UX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-23. REMARK 100 THE DEPOSITION ID IS D_1000278869. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-OCT-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979180 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54860 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 83.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.3 REMARK 200 DATA REDUNDANCY : 2.200 REMARK 200 R MERGE (I) : 0.06800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.24100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 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 (%): 47.92 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG6000, 0.1 M HEPES PH 7.0 AND REMARK 280 0.2 M CALCIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 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: 7820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19790 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 TOTAL BURIED SURFACE AREA: 5800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 CYS C 234 REMARK 465 GLY C 235 REMARK 465 GLY C 236 REMARK 465 GLY A 232 REMARK 465 GLU A 233 REMARK 465 CYS A 234 REMARK 465 GLY A 235 REMARK 465 GLY A 236 REMARK 465 SER B 0 REMARK 465 SER B 142 REMARK 465 SER B 143 REMARK 465 LYS B 144 REMARK 465 SER B 145 REMARK 465 THR B 146 REMARK 465 SER B 147 REMARK 465 GLY B 148 REMARK 465 GLY B 149 REMARK 465 LYS B 229 REMARK 465 SER B 230 REMARK 465 CYS B 231 REMARK 465 SER D 0 REMARK 465 SER D 143 REMARK 465 LYS D 144 REMARK 465 SER D 145 REMARK 465 THR D 146 REMARK 465 SER D 147 REMARK 465 GLY D 148 REMARK 465 LYS D 229 REMARK 465 SER D 230 REMARK 465 CYS D 231 REMARK 465 GLY E -5 REMARK 465 THR E -4 REMARK 465 GLY E -3 REMARK 465 GLY E -2 REMARK 465 GLY E -1 REMARK 465 SER E 0 REMARK 465 LEU E 1 REMARK 465 PRO E 22 REMARK 465 SER E 23 REMARK 465 ASP E 24 REMARK 465 GLY E 25 REMARK 465 GLU E 26 REMARK 465 LEU E 27 REMARK 465 GLY E 28 REMARK 465 LEU E 29 REMARK 465 GLY E 30 REMARK 465 ASP E 31 REMARK 465 LEU E 32 REMARK 465 SER E 33 REMARK 465 ASP E 34 REMARK 465 PRO E 35 REMARK 465 GLY F -7 REMARK 465 THR F -6 REMARK 465 GLY F -5 REMARK 465 GLY F -4 REMARK 465 GLY F -3 REMARK 465 SER F -2 REMARK 465 LEU F -1 REMARK 465 PRO F 20 REMARK 465 SER F 21 REMARK 465 ASP F 22 REMARK 465 GLY F 23 REMARK 465 GLU F 24 REMARK 465 LEU F 25 REMARK 465 GLY F 26 REMARK 465 LEU F 27 REMARK 465 GLY F 28 REMARK 465 ASP F 29 REMARK 465 LEU F 30 REMARK 465 SER F 31 REMARK 465 ASP F 32 REMARK 465 PRO F 33 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 VAL C 15 CG1 CG2 REMARK 470 ARG C 24 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 27 CG CD OE1 NE2 REMARK 470 LYS C 45 NZ REMARK 470 GLN C 120 CG CD OE1 NE2 REMARK 470 LYS C 127 NZ REMARK 470 LYS C 146 CD CE NZ REMARK 470 ARG C 162 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 165 CG CD CE NZ REMARK 470 LEU C 174 CG CD1 CD2 REMARK 470 LYS C 210 CG CD CE NZ REMARK 470 GLN A 3 CD OE1 NE2 REMARK 470 SER A 12 OG REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 27 CG CD OE1 NE2 REMARK 470 LYS A 51 CE NZ REMARK 470 GLN A 95 CG CD OE1 NE2 REMARK 470 PHE A 99 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 127 CE NZ REMARK 470 ARG A 128 NE CZ NH1 NH2 REMARK 470 LYS A 146 CD CE NZ REMARK 470 LYS A 165 CG CD CE NZ REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 VAL A 170 CG1 CG2 REMARK 470 LEU A 174 CG CD1 CD2 REMARK 470 SER A 176 OG REMARK 470 GLU A 185 OE1 OE2 REMARK 470 LYS A 189 CG CD CE NZ REMARK 470 LEU A 199 CG CD1 CD2 REMARK 470 LEU A 201 CG CD1 CD2 REMARK 470 LYS A 203 CG CD CE NZ REMARK 470 ASP A 205 CG OD1 OD2 REMARK 470 GLU A 207 CD OE1 OE2 REMARK 470 LYS A 208 CG CD CE NZ REMARK 470 HIS A 209 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 210 CG CD CE NZ REMARK 470 GLU A 215 CG CD OE1 OE2 REMARK 470 SER A 223 OG REMARK 470 ASN A 230 CG OD1 ND2 REMARK 470 ARG A 231 CZ NH1 NH2 REMARK 470 LYS B 48 CE NZ REMARK 470 LEU B 204 CG CD1 CD2 REMARK 470 LYS B 221 CD CE NZ REMARK 470 LYS B 225 CG CD CE NZ REMARK 470 LYS D 48 CD CE NZ REMARK 470 LYS D 72 NZ REMARK 470 SER D 142 OG REMARK 470 SER D 201 OG REMARK 470 LYS D 216 CG CD CE NZ REMARK 470 LYS D 221 CG CD CE NZ REMARK 470 LYS D 225 CE NZ REMARK 470 GLU D 227 CG CD OE1 OE2 REMARK 470 ARG E 2 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 12 CD CE NZ REMARK 470 LYS E 13 CG CD CE NZ REMARK 470 GLU E 17 CG CD OE1 OE2 REMARK 470 LYS E 20 CG CD CE NZ REMARK 470 ASP E 21 CG OD1 OD2 REMARK 470 ARG F 0 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 7 CD OE1 OE2 REMARK 470 LYS F 11 CG CD CE NZ REMARK 470 LYS F 18 CD CE NZ REMARK 470 ASP F 19 CG OD1 OD2 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 OH TYR B 117 C1 PEG B 304 1.38 REMARK 500 REMARK 500 REMARK: NULL 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 PRO D 200 N - CD - CG ANGL. DEV. = -13.7 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 SER C 36 -126.70 53.62 REMARK 500 ALA C 57 -43.31 70.75 REMARK 500 SER C 65 12.59 -141.79 REMARK 500 ALA C 100 -177.56 -176.47 REMARK 500 ASN C 158 79.49 52.06 REMARK 500 ASN C 178 11.73 -145.02 REMARK 500 SER A 36 -129.00 54.80 REMARK 500 ALA A 57 -39.34 67.29 REMARK 500 SER A 65 16.08 -142.46 REMARK 500 ASN A 158 70.50 58.48 REMARK 500 LYS A 210 -60.63 -107.31 REMARK 500 ALA B 100 171.06 178.08 REMARK 500 ASP B 159 62.66 75.83 REMARK 500 THR B 175 -33.17 -134.15 REMARK 500 SER B 202 7.92 -63.71 REMARK 500 THR B 206 -76.43 -85.28 REMARK 500 ALA D 100 166.15 178.73 REMARK 500 ASP D 159 60.31 72.40 REMARK 500 THR D 175 -32.17 -132.71 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 C 507 DISTANCE = 5.94 ANGSTROMS REMARK 525 HOH C 508 DISTANCE = 6.27 ANGSTROMS REMARK 525 HOH C 509 DISTANCE = 6.32 ANGSTROMS REMARK 525 HOH C 510 DISTANCE = 8.55 ANGSTROMS REMARK 525 HOH A 475 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH B 535 DISTANCE = 6.20 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 305 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER C 36 O REMARK 620 2 GLY C 84 O 106.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 306 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER C 93 OG REMARK 620 2 HOH C 461 O 66.3 REMARK 620 3 HOH C 484 O 120.8 59.5 REMARK 620 4 HOH C 492 O 109.7 140.0 126.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 304 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 178 OD1 REMARK 620 2 SER C 179 OG 99.4 REMARK 620 3 HOH C 446 O 138.4 109.9 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D 305 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH C 474 O REMARK 620 2 TYR D 113 OH 99.3 REMARK 620 3 HOH D 524 O 122.7 107.2 REMARK 620 4 ASP F 3 OD1 92.1 128.6 107.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 304 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ILE A 116 O REMARK 620 2 HOH A 445 O 104.5 REMARK 620 3 HOH B 428 O 88.0 131.9 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 305 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 462 O REMARK 620 2 HOH A 471 O 63.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D 306 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B 474 O REMARK 620 2 ASP D 81 OD2 128.2 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D 307 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR D 65 O REMARK 620 2 HOH D 479 O 70.5 REMARK 620 N 1 DBREF 8UX6 C 1 236 PDB 8UX6 8UX6 1 236 DBREF 8UX6 A 1 236 PDB 8UX6 8UX6 1 236 DBREF 8UX6 B 0 231 PDB 8UX6 8UX6 0 231 DBREF 8UX6 D 0 231 PDB 8UX6 8UX6 0 231 DBREF 8UX6 E -5 35 UNP Q27040 Q27040_THEPA 572 612 DBREF 8UX6 F -7 33 UNP Q27040 Q27040_THEPA 572 612 SEQRES 1 C 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 C 216 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 C 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 C 216 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 216 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 C 216 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 C 216 TYR TYR ALA PRO ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 C 216 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 216 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 C 216 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 216 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 216 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 216 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 216 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 216 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 216 PHE ASN ARG GLY GLU CYS GLY GLY SEQRES 1 A 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 216 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 A 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 A 216 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 216 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 216 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 A 216 TYR TYR ALA PRO ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 A 216 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 216 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 A 216 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 216 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 216 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 216 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 216 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 216 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 216 PHE ASN ARG GLY GLU CYS GLY GLY SEQRES 1 B 221 SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 B 221 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 B 221 GLY PHE ASN ILE SER SER SER SER ILE HIS TRP VAL ARG SEQRES 4 B 221 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SEQRES 5 B 221 SER PRO TYR TYR SER SER THR SER TYR ALA ASP SER VAL SEQRES 6 B 221 LYS GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN SEQRES 7 B 221 THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP SEQRES 8 B 221 THR ALA VAL TYR TYR CYS ALA ARG GLY PRO GLY TYR ALA SEQRES 9 B 221 MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 B 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 B 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 B 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 B 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 B 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 B 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 B 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 D 221 SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 D 221 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 D 221 GLY PHE ASN ILE SER SER SER SER ILE HIS TRP VAL ARG SEQRES 4 D 221 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SEQRES 5 D 221 SER PRO TYR TYR SER SER THR SER TYR ALA ASP SER VAL SEQRES 6 D 221 LYS GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN SEQRES 7 D 221 THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP SEQRES 8 D 221 THR ALA VAL TYR TYR CYS ALA ARG GLY PRO GLY TYR ALA SEQRES 9 D 221 MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 D 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 D 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 D 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 D 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 D 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 D 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 D 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 D 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 E 41 GLY THR GLY GLY GLY SER LEU ARG GLY LEU ASP LEU SER SEQRES 2 E 41 GLU GLU GLU VAL LYS LYS ILE LEU ASP GLU ILE VAL LYS SEQRES 3 E 41 ASP PRO SER ASP GLY GLU LEU GLY LEU GLY ASP LEU SER SEQRES 4 E 41 ASP PRO SEQRES 1 F 41 GLY THR GLY GLY GLY SER LEU ARG GLY LEU ASP LEU SER SEQRES 2 F 41 GLU GLU GLU VAL LYS LYS ILE LEU ASP GLU ILE VAL LYS SEQRES 3 F 41 ASP PRO SER ASP GLY GLU LEU GLY LEU GLY ASP LEU SER SEQRES 4 F 41 ASP PRO HET EDO C 301 4 HET EPE C 302 15 HET PEG C 303 7 HET NA C 304 1 HET CA C 305 1 HET CA C 306 1 HET EDO C 307 4 HET EDO C 308 4 HET EDO C 309 4 HET EDO C 310 4 HET PEG A 301 7 HET EPE A 302 15 HET EDO A 303 4 HET NA A 304 1 HET CA A 305 1 HET EDO A 306 4 HET EDO A 307 4 HET EDO B 301 4 HET NA B 302 1 HET EDO B 303 4 HET PEG B 304 14 HET CL B 305 1 HET PEG D 301 7 HET PEG D 302 7 HET PEG D 303 7 HET PEG D 304 7 HET NA D 305 1 HET NA D 306 1 HET NA D 307 1 HET EDO D 308 8 HET EDO D 309 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM NA SODIUM ION HETNAM CA CALCIUM ION HETNAM CL CHLORIDE ION HETSYN EDO ETHYLENE GLYCOL HETSYN EPE HEPES FORMUL 7 EDO 12(C2 H6 O2) FORMUL 8 EPE 2(C8 H18 N2 O4 S) FORMUL 9 PEG 7(C4 H10 O3) FORMUL 10 NA 6(NA 1+) FORMUL 11 CA 3(CA 2+) FORMUL 28 CL CL 1- FORMUL 38 HOH *487(H2 O) HELIX 1 AA1 GLN C 95 PHE C 99 5 5 HELIX 2 AA2 SER C 141 GLY C 148 1 8 HELIX 3 AA3 LYS C 203 GLU C 207 1 5 HELIX 4 AA4 GLN A 95 PHE A 99 5 5 HELIX 5 AA5 SER A 141 GLY A 148 1 8 HELIX 6 AA6 LYS A 203 LYS A 208 1 6 HELIX 7 AA7 ASN B 29 SER B 37 5 5 HELIX 8 AA8 ASP B 69 LYS B 72 5 4 HELIX 9 AA9 THR B 82 LYS B 84 5 3 HELIX 10 AB1 ARG B 95 THR B 99 5 5 HELIX 11 AB2 SER B 171 ALA B 173 5 3 HELIX 12 AB3 PRO B 200 LEU B 204 5 5 HELIX 13 AB4 LYS B 216 ASN B 219 5 4 HELIX 14 AB5 ASN D 29 SER D 37 5 5 HELIX 15 AB6 ASP D 69 LYS D 72 5 4 HELIX 16 AB7 THR D 82 LYS D 84 5 3 HELIX 17 AB8 ARG D 95 THR D 99 5 5 HELIX 18 AB9 SER D 202 LEU D 204 5 3 HELIX 19 AC1 LYS D 216 ASN D 219 5 4 HELIX 20 AC2 SER E 7 ASP E 21 1 15 HELIX 21 AC3 SER F 5 ASP F 19 1 15 SHEET 1 AA1 4 MET C 4 SER C 7 0 SHEET 2 AA1 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AA1 4 ASP C 86 ILE C 91 -1 O PHE C 87 N CYS C 23 SHEET 4 AA1 4 PHE C 76 SER C 83 -1 N SER C 79 O THR C 88 SHEET 1 AA2 6 SER C 10 ALA C 13 0 SHEET 2 AA2 6 THR C 122 ILE C 126 1 O GLU C 125 N LEU C 11 SHEET 3 AA2 6 ALA C 100 GLN C 106 -1 N ALA C 100 O VAL C 124 SHEET 4 AA2 6 VAL C 39 GLN C 44 -1 N GLN C 44 O THR C 101 SHEET 5 AA2 6 LYS C 51 TYR C 55 -1 O LEU C 53 N TRP C 41 SHEET 6 AA2 6 SER C 66 LEU C 67 -1 O SER C 66 N TYR C 55 SHEET 1 AA3 4 SER C 10 ALA C 13 0 SHEET 2 AA3 4 THR C 122 ILE C 126 1 O GLU C 125 N LEU C 11 SHEET 3 AA3 4 ALA C 100 GLN C 106 -1 N ALA C 100 O VAL C 124 SHEET 4 AA3 4 THR C 117 PHE C 118 -1 O THR C 117 N GLN C 106 SHEET 1 AA4 4 SER C 134 PHE C 138 0 SHEET 2 AA4 4 THR C 149 PHE C 159 -1 O LEU C 155 N PHE C 136 SHEET 3 AA4 4 TYR C 193 SER C 202 -1 O LEU C 199 N VAL C 152 SHEET 4 AA4 4 SER C 179 VAL C 183 -1 N SER C 182 O SER C 196 SHEET 1 AA5 4 ALA C 173 LEU C 174 0 SHEET 2 AA5 4 LYS C 165 VAL C 170 -1 N VAL C 170 O ALA C 173 SHEET 3 AA5 4 VAL C 211 THR C 217 -1 O GLU C 215 N GLN C 167 SHEET 4 AA5 4 VAL C 225 ASN C 230 -1 O VAL C 225 N VAL C 216 SHEET 1 AA6 4 MET A 4 SER A 7 0 SHEET 2 AA6 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA6 4 ASP A 86 ILE A 91 -1 O LEU A 89 N ILE A 21 SHEET 4 AA6 4 PHE A 76 SER A 83 -1 N SER A 77 O THR A 90 SHEET 1 AA7 6 SER A 10 ALA A 13 0 SHEET 2 AA7 6 THR A 122 ILE A 126 1 O GLU A 125 N LEU A 11 SHEET 3 AA7 6 ALA A 100 GLN A 106 -1 N TYR A 102 O THR A 122 SHEET 4 AA7 6 VAL A 39 GLN A 44 -1 N GLN A 44 O THR A 101 SHEET 5 AA7 6 LYS A 51 TYR A 55 -1 O LEU A 53 N TRP A 41 SHEET 6 AA7 6 SER A 66 LEU A 67 -1 O SER A 66 N TYR A 55 SHEET 1 AA8 4 SER A 10 ALA A 13 0 SHEET 2 AA8 4 THR A 122 ILE A 126 1 O GLU A 125 N LEU A 11 SHEET 3 AA8 4 ALA A 100 GLN A 106 -1 N TYR A 102 O THR A 122 SHEET 4 AA8 4 THR A 117 PHE A 118 -1 O THR A 117 N GLN A 106 SHEET 1 AA9 4 SER A 134 PHE A 138 0 SHEET 2 AA9 4 THR A 149 PHE A 159 -1 O LEU A 155 N PHE A 136 SHEET 3 AA9 4 TYR A 193 SER A 202 -1 O LEU A 195 N LEU A 156 SHEET 4 AA9 4 SER A 179 VAL A 183 -1 N SER A 182 O SER A 196 SHEET 1 AB1 4 ALA A 173 LEU A 174 0 SHEET 2 AB1 4 LYS A 165 VAL A 170 -1 N VAL A 170 O ALA A 173 SHEET 3 AB1 4 VAL A 211 THR A 217 -1 O THR A 217 N LYS A 165 SHEET 4 AB1 4 VAL A 225 ASN A 230 -1 O VAL A 225 N VAL A 216 SHEET 1 AB2 4 GLN B 3 SER B 7 0 SHEET 2 AB2 4 LEU B 19 SER B 26 -1 O SER B 22 N SER B 7 SHEET 3 AB2 4 THR B 86 MET B 91 -1 O MET B 91 N LEU B 19 SHEET 4 AB2 4 PHE B 76 ASP B 81 -1 N THR B 77 O GLN B 90 SHEET 1 AB3 6 LEU B 12 VAL B 13 0 SHEET 2 AB3 6 THR B 122 VAL B 126 1 O THR B 125 N VAL B 13 SHEET 3 AB3 6 ALA B 100 GLY B 107 -1 N ALA B 100 O VAL B 124 SHEET 4 AB3 6 SER B 38 GLN B 44 -1 N VAL B 42 O TYR B 103 SHEET 5 AB3 6 LEU B 50 SER B 57 -1 O ALA B 54 N TRP B 41 SHEET 6 AB3 6 SER B 64 TYR B 67 -1 O SER B 64 N SER B 57 SHEET 1 AB4 4 LEU B 12 VAL B 13 0 SHEET 2 AB4 4 THR B 122 VAL B 126 1 O THR B 125 N VAL B 13 SHEET 3 AB4 4 ALA B 100 GLY B 107 -1 N ALA B 100 O VAL B 124 SHEET 4 AB4 4 TYR B 117 TRP B 118 -1 O TYR B 117 N ARG B 106 SHEET 1 AB5 4 SER B 135 LEU B 139 0 SHEET 2 AB5 4 ALA B 151 TYR B 160 -1 O LEU B 156 N PHE B 137 SHEET 3 AB5 4 TYR B 191 VAL B 199 -1 O VAL B 199 N ALA B 151 SHEET 4 AB5 4 VAL B 178 THR B 180 -1 N HIS B 179 O VAL B 196 SHEET 1 AB6 4 SER B 135 LEU B 139 0 SHEET 2 AB6 4 ALA B 151 TYR B 160 -1 O LEU B 156 N PHE B 137 SHEET 3 AB6 4 TYR B 191 VAL B 199 -1 O VAL B 199 N ALA B 151 SHEET 4 AB6 4 VAL B 184 LEU B 185 -1 N VAL B 184 O SER B 192 SHEET 1 AB7 3 THR B 166 TRP B 169 0 SHEET 2 AB7 3 ILE B 210 HIS B 215 -1 O ASN B 214 N THR B 166 SHEET 3 AB7 3 THR B 220 LYS B 225 -1 O VAL B 222 N VAL B 213 SHEET 1 AB8 4 GLN D 3 SER D 7 0 SHEET 2 AB8 4 LEU D 19 SER D 26 -1 O SER D 22 N SER D 7 SHEET 3 AB8 4 THR D 86 MET D 91 -1 O MET D 91 N LEU D 19 SHEET 4 AB8 4 PHE D 76 ASP D 81 -1 N THR D 77 O GLN D 90 SHEET 1 AB9 6 GLY D 11 VAL D 13 0 SHEET 2 AB9 6 THR D 122 VAL D 126 1 O THR D 125 N VAL D 13 SHEET 3 AB9 6 ALA D 100 GLY D 107 -1 N ALA D 100 O VAL D 124 SHEET 4 AB9 6 SER D 38 GLN D 44 -1 N VAL D 42 O TYR D 103 SHEET 5 AB9 6 LEU D 50 SER D 57 -1 O VAL D 53 N TRP D 41 SHEET 6 AB9 6 SER D 64 TYR D 67 -1 O SER D 64 N SER D 57 SHEET 1 AC1 4 GLY D 11 VAL D 13 0 SHEET 2 AC1 4 THR D 122 VAL D 126 1 O THR D 125 N VAL D 13 SHEET 3 AC1 4 ALA D 100 GLY D 107 -1 N ALA D 100 O VAL D 124 SHEET 4 AC1 4 TYR D 117 TRP D 118 -1 O TYR D 117 N ARG D 106 SHEET 1 AC2 4 SER D 135 LEU D 139 0 SHEET 2 AC2 4 THR D 150 TYR D 160 -1 O LYS D 158 N SER D 135 SHEET 3 AC2 4 TYR D 191 PRO D 200 -1 O VAL D 199 N ALA D 151 SHEET 4 AC2 4 VAL D 178 THR D 180 -1 N HIS D 179 O VAL D 196 SHEET 1 AC3 4 SER D 135 LEU D 139 0 SHEET 2 AC3 4 THR D 150 TYR D 160 -1 O LYS D 158 N SER D 135 SHEET 3 AC3 4 TYR D 191 PRO D 200 -1 O VAL D 199 N ALA D 151 SHEET 4 AC3 4 VAL D 184 LEU D 185 -1 N VAL D 184 O SER D 192 SHEET 1 AC4 3 THR D 166 TRP D 169 0 SHEET 2 AC4 3 ILE D 210 HIS D 215 -1 O ASN D 212 N SER D 168 SHEET 3 AC4 3 THR D 220 LYS D 225 -1 O VAL D 222 N VAL D 213 SSBOND 1 CYS C 23 CYS C 104 1555 1555 2.09 SSBOND 2 CYS C 154 CYS C 214 1555 1555 2.06 SSBOND 3 CYS A 23 CYS A 104 1555 1555 2.08 SSBOND 4 CYS A 154 CYS A 214 1555 1555 2.05 SSBOND 5 CYS B 23 CYS B 104 1555 1555 2.08 SSBOND 6 CYS B 155 CYS B 211 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 104 1555 1555 2.09 SSBOND 8 CYS D 155 CYS D 211 1555 1555 2.06 LINK O SER C 36 CA CA C 305 1555 1555 2.75 LINK O GLY C 84 CA CA C 305 1555 1555 2.93 LINK OG SER C 93 CA CA C 306 1555 1555 2.36 LINK OD1 ASN C 178 NA NA C 304 1555 1555 3.01 LINK OG SER C 179 NA NA C 304 1555 1555 2.64 LINK NA NA C 304 O HOH C 446 1555 1555 2.54 LINK CA CA C 306 O HOH C 461 1555 1555 2.88 LINK CA CA C 306 O HOH C 484 1555 1555 2.42 LINK CA CA C 306 O HOH C 492 1555 1555 2.42 LINK O HOH C 474 NA NA D 305 1555 1555 2.74 LINK O ILE A 116 NA NA A 304 1555 1555 2.83 LINK NA NA A 304 O HOH A 445 1555 1555 2.53 LINK NA NA A 304 O HOH B 428 1555 1555 2.80 LINK CA CA A 305 O HOH A 462 1555 1555 2.81 LINK CA CA A 305 O HOH A 471 1555 1555 2.27 LINK OE2 GLU B 97 NA NA B 302 1555 1555 2.21 LINK O HOH B 474 NA NA D 306 1654 1555 2.91 LINK O THR D 65 NA NA D 307 1555 1555 2.57 LINK OD2 ASP D 81 NA NA D 306 1555 1555 2.67 LINK OH TYR D 113 NA NA D 305 1555 1555 2.52 LINK NA NA D 305 O HOH D 524 1555 1555 2.78 LINK NA NA D 305 OD1 ASP F 3 1555 1555 2.92 LINK NA NA D 307 O HOH D 479 1555 1555 2.90 CISPEP 1 SER C 7 PRO C 8 0 -8.58 CISPEP 2 ALA C 114 PRO C 115 0 2.78 CISPEP 3 TYR C 160 PRO C 161 0 6.05 CISPEP 4 SER A 7 PRO A 8 0 -8.69 CISPEP 5 ALA A 114 PRO A 115 0 1.93 CISPEP 6 TYR A 160 PRO A 161 0 7.19 CISPEP 7 PHE B 161 PRO B 162 0 -8.97 CISPEP 8 GLU B 163 PRO B 164 0 -2.40 CISPEP 9 PHE D 161 PRO D 162 0 -4.57 CISPEP 10 GLU D 163 PRO D 164 0 0.71 CRYST1 39.010 75.560 90.591 69.26 77.60 76.08 P 1 2 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 0.025634 -0.006353 -0.003808 0.00000 SCALE2 0.000000 0.013635 -0.004590 0.00000 SCALE3 0.000000 0.000000 0.011926 0.00000