HEADER VIRAL PROTEIN 07-APR-25 9QT3 TITLE STRUCTURE OF VACCINIA VIRUS A26 (RESIDUES 1-397) IN COMPLEX WITH FAB TITLE 2 8M2110 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOP PROTEIN OPG153; COMPND 3 CHAIN: A, E, I, M; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN OF FAB 8M2110; COMPND 7 CHAIN: B, F, J, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN OF FAB 8M2110; COMPND 11 CHAIN: C, G, K, O; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ANTI-FAB VHH; COMPND 15 CHAIN: D, H, L, P; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS WESTERN RESERVE; SOURCE 3 ORGANISM_TAXID: 696871; SOURCE 4 GENE: OPG153, VACWR149, A26L; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 21 ORGANISM_TAXID: 9844; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS VACCINIA VIRUS MPOX VIRUS ORTHOPOXVIRUS NEUTRALIZING ANTIBODY, VIRAL KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.GUARDADO-CALVO,L.BATTINI REVDAT 1 19-NOV-25 9QT3 0 JRNL AUTH P.GUARDADO-CALVO,L.BATTINI JRNL TITL STRUCTURE OF VACCINIA VIRUS A26 (RESIDUES 1-397) IN COMPLEX JRNL TITL 2 WITH FAB 8M2110 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 223523 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 11388 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 39.0800 - 8.9800 0.99 7051 355 0.1722 0.2080 REMARK 3 2 8.9800 - 7.1400 1.00 7027 450 0.1718 0.1914 REMARK 3 3 7.1400 - 6.2400 1.00 7062 383 0.1981 0.2188 REMARK 3 4 6.2400 - 5.6700 1.00 7045 396 0.1874 0.2196 REMARK 3 5 5.6700 - 5.2700 1.00 7099 390 0.1665 0.1933 REMARK 3 6 5.2700 - 4.9600 1.00 7101 304 0.1495 0.1678 REMARK 3 7 4.9600 - 4.7100 1.00 7103 396 0.1345 0.1694 REMARK 3 8 4.7100 - 4.5000 1.00 7072 383 0.1407 0.1674 REMARK 3 9 4.5000 - 4.3300 1.00 7043 428 0.1412 0.1835 REMARK 3 10 4.3300 - 4.1800 1.00 7029 408 0.1489 0.1871 REMARK 3 11 4.1800 - 4.0500 1.00 7070 363 0.1617 0.1918 REMARK 3 12 4.0500 - 3.9400 1.00 7132 386 0.1756 0.2137 REMARK 3 13 3.9300 - 3.8300 1.00 6988 408 0.1849 0.2236 REMARK 3 14 3.8300 - 3.7400 1.00 7062 376 0.1951 0.2321 REMARK 3 15 3.7400 - 3.6500 1.00 7154 350 0.1966 0.2487 REMARK 3 16 3.6500 - 3.5800 1.00 7079 350 0.2077 0.2610 REMARK 3 17 3.5800 - 3.5000 1.00 6959 364 0.2213 0.2766 REMARK 3 18 3.5000 - 3.4400 1.00 7202 364 0.2329 0.2533 REMARK 3 19 3.4400 - 3.3800 1.00 7133 392 0.2627 0.2889 REMARK 3 20 3.3800 - 3.3200 1.00 6889 435 0.2589 0.3063 REMARK 3 21 3.3200 - 3.2700 1.00 7209 348 0.2580 0.2963 REMARK 3 22 3.2700 - 3.2200 1.00 6941 422 0.2589 0.3084 REMARK 3 23 3.2200 - 3.1700 1.00 7121 420 0.2668 0.3155 REMARK 3 24 3.1700 - 3.1200 1.00 7103 304 0.2736 0.2896 REMARK 3 25 3.1200 - 3.0800 1.00 7075 399 0.2859 0.3407 REMARK 3 26 3.0800 - 3.0400 1.00 7040 370 0.2993 0.3358 REMARK 3 27 3.0400 - 3.0000 1.00 7166 328 0.3050 0.3372 REMARK 3 28 3.0000 - 2.9700 1.00 7137 324 0.2874 0.3206 REMARK 3 29 2.9700 - 2.9300 1.00 7048 452 0.2969 0.3150 REMARK 3 30 2.9300 - 2.9000 1.00 6995 340 0.3070 0.3559 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) : 0.334 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.940 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.97 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.92 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 : 0.002 28934 REMARK 3 ANGLE : 0.503 39234 REMARK 3 CHIRALITY : 0.042 4285 REMARK 3 PLANARITY : 0.004 5022 REMARK 3 DIHEDRAL : 12.138 10430 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 15 THROUGH 364) REMARK 3 ORIGIN FOR THE GROUP (A): -53.9905 -17.9445 61.1179 REMARK 3 T TENSOR REMARK 3 T11: 0.3207 T22: 0.2558 REMARK 3 T33: 0.2676 T12: -0.0475 REMARK 3 T13: -0.0060 T23: -0.0566 REMARK 3 L TENSOR REMARK 3 L11: 0.5080 L22: 1.2714 REMARK 3 L33: 1.0069 L12: -0.1345 REMARK 3 L13: -0.0727 L23: 0.0298 REMARK 3 S TENSOR REMARK 3 S11: 0.0153 S12: 0.0640 S13: -0.0739 REMARK 3 S21: -0.0528 S22: -0.0268 S23: 0.0638 REMARK 3 S31: 0.1073 S32: -0.0695 S33: 0.0499 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 20 THROUGH 244) REMARK 3 ORIGIN FOR THE GROUP (A): -85.3227 2.9248 87.8680 REMARK 3 T TENSOR REMARK 3 T11: 0.2784 T22: 0.3590 REMARK 3 T33: 0.3289 T12: -0.0074 REMARK 3 T13: -0.0585 T23: -0.0737 REMARK 3 L TENSOR REMARK 3 L11: 0.6385 L22: 0.5023 REMARK 3 L33: 0.4177 L12: -0.1759 REMARK 3 L13: -0.1780 L23: 0.2859 REMARK 3 S TENSOR REMARK 3 S11: -0.0537 S12: 0.1780 S13: 0.0600 REMARK 3 S21: -0.1726 S22: -0.0569 S23: 0.1544 REMARK 3 S31: -0.0234 S32: -0.2402 S33: 0.0366 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 20 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): -77.5335 17.4630 96.7638 REMARK 3 T TENSOR REMARK 3 T11: 0.2439 T22: 0.2571 REMARK 3 T33: 0.3126 T12: 0.0475 REMARK 3 T13: -0.0077 T23: -0.0576 REMARK 3 L TENSOR REMARK 3 L11: 0.7252 L22: 0.9735 REMARK 3 L33: 0.4632 L12: -0.2452 REMARK 3 L13: 0.0622 L23: 0.0238 REMARK 3 S TENSOR REMARK 3 S11: -0.0423 S12: -0.0056 S13: 0.0921 REMARK 3 S21: 0.0050 S22: 0.0050 S23: 0.2384 REMARK 3 S31: -0.0864 S32: -0.1957 S33: 0.0005 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 2 THROUGH 113) REMARK 3 ORIGIN FOR THE GROUP (A): -67.7089 42.5437 106.0353 REMARK 3 T TENSOR REMARK 3 T11: 0.4497 T22: 0.3157 REMARK 3 T33: 0.4126 T12: 0.1190 REMARK 3 T13: -0.0689 T23: -0.0733 REMARK 3 L TENSOR REMARK 3 L11: 1.6800 L22: 1.5235 REMARK 3 L33: 0.8990 L12: -0.0166 REMARK 3 L13: 0.0140 L23: 0.5817 REMARK 3 S TENSOR REMARK 3 S11: -0.0448 S12: -0.1591 S13: 0.1284 REMARK 3 S21: 0.1585 S22: 0.0996 S23: -0.0026 REMARK 3 S31: -0.2161 S32: 0.0633 S33: -0.0061 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 15 THROUGH 364) REMARK 3 ORIGIN FOR THE GROUP (A): -34.3132 28.8793 97.1773 REMARK 3 T TENSOR REMARK 3 T11: 0.3065 T22: 0.1903 REMARK 3 T33: 0.2615 T12: -0.0243 REMARK 3 T13: 0.0277 T23: -0.0657 REMARK 3 L TENSOR REMARK 3 L11: 0.9714 L22: 0.7707 REMARK 3 L33: 0.9224 L12: 0.1894 REMARK 3 L13: 0.1013 L23: 0.0638 REMARK 3 S TENSOR REMARK 3 S11: -0.0167 S12: -0.0428 S13: 0.0577 REMARK 3 S21: -0.0128 S22: 0.0444 S23: -0.0728 REMARK 3 S31: -0.1485 S32: 0.0636 S33: -0.0042 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 20 THROUGH 244) REMARK 3 ORIGIN FOR THE GROUP (A): -58.5627 39.8250 59.4258 REMARK 3 T TENSOR REMARK 3 T11: 0.4024 T22: 0.2835 REMARK 3 T33: 0.3574 T12: 0.0255 REMARK 3 T13: 0.0080 T23: -0.0098 REMARK 3 L TENSOR REMARK 3 L11: 0.2065 L22: 0.3402 REMARK 3 L33: 0.7699 L12: -0.0521 REMARK 3 L13: 0.2764 L23: 0.0728 REMARK 3 S TENSOR REMARK 3 S11: -0.0503 S12: 0.0808 S13: 0.0750 REMARK 3 S21: 0.1173 S22: -0.0466 S23: 0.1433 REMARK 3 S31: -0.1605 S32: -0.0768 S33: -0.0158 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'G' AND RESID 20 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): -64.5519 24.2265 50.9520 REMARK 3 T TENSOR REMARK 3 T11: 0.2710 T22: 0.2861 REMARK 3 T33: 0.3177 T12: 0.0100 REMARK 3 T13: -0.0044 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 1.2404 L22: 0.4877 REMARK 3 L33: 0.4997 L12: -0.0522 REMARK 3 L13: 0.4629 L23: 0.2194 REMARK 3 S TENSOR REMARK 3 S11: -0.0382 S12: 0.0966 S13: 0.1998 REMARK 3 S21: 0.0005 S22: -0.0703 S23: 0.1597 REMARK 3 S31: -0.0806 S32: -0.1358 S33: -0.0045 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 2 THROUGH 113) REMARK 3 ORIGIN FOR THE GROUP (A): -77.9120 1.5032 40.7057 REMARK 3 T TENSOR REMARK 3 T11: 0.3481 T22: 0.5282 REMARK 3 T33: 0.5393 T12: 0.0133 REMARK 3 T13: -0.0394 T23: -0.1936 REMARK 3 L TENSOR REMARK 3 L11: 1.1895 L22: 1.7016 REMARK 3 L33: 0.5390 L12: -0.3565 REMARK 3 L13: 0.5028 L23: 0.1790 REMARK 3 S TENSOR REMARK 3 S11: 0.0699 S12: 0.3197 S13: -0.3267 REMARK 3 S21: -0.1394 S22: -0.1659 S23: 0.3736 REMARK 3 S31: 0.1196 S32: -0.0712 S33: 0.0280 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN 'I' AND RESID 15 THROUGH 364) REMARK 3 ORIGIN FOR THE GROUP (A): -38.0299 -3.6617 6.5077 REMARK 3 T TENSOR REMARK 3 T11: 0.4402 T22: 0.4872 REMARK 3 T33: 0.3829 T12: -0.1532 REMARK 3 T13: -0.0024 T23: -0.1215 REMARK 3 L TENSOR REMARK 3 L11: 1.5702 L22: 0.9708 REMARK 3 L33: 1.6997 L12: 0.0116 REMARK 3 L13: -0.0603 L23: -0.0180 REMARK 3 S TENSOR REMARK 3 S11: -0.0125 S12: 0.3442 S13: -0.4005 REMARK 3 S21: -0.1151 S22: 0.0315 S23: 0.1219 REMARK 3 S31: 0.3402 S32: -0.3084 S33: 0.0279 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN 'J' AND RESID 20 THROUGH 244) REMARK 3 ORIGIN FOR THE GROUP (A): -43.4184 36.9455 27.2509 REMARK 3 T TENSOR REMARK 3 T11: 0.3598 T22: 0.4258 REMARK 3 T33: 0.3097 T12: -0.0232 REMARK 3 T13: -0.0181 T23: 0.0869 REMARK 3 L TENSOR REMARK 3 L11: 0.8449 L22: 0.5301 REMARK 3 L33: 0.5224 L12: -0.0160 REMARK 3 L13: 0.0101 L23: 0.0831 REMARK 3 S TENSOR REMARK 3 S11: -0.0927 S12: 0.3506 S13: 0.1459 REMARK 3 S21: -0.1630 S22: 0.0068 S23: -0.0506 REMARK 3 S31: -0.1284 S32: -0.0639 S33: -0.0203 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN 'K' AND RESID 20 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): -30.2682 39.4832 40.3187 REMARK 3 T TENSOR REMARK 3 T11: 0.3748 T22: 0.2847 REMARK 3 T33: 0.3883 T12: -0.0334 REMARK 3 T13: -0.0224 T23: 0.0375 REMARK 3 L TENSOR REMARK 3 L11: 0.7315 L22: 0.3783 REMARK 3 L33: 0.4938 L12: 0.0889 REMARK 3 L13: -0.0107 L23: 0.1352 REMARK 3 S TENSOR REMARK 3 S11: -0.0664 S12: 0.1160 S13: 0.2926 REMARK 3 S21: -0.0430 S22: 0.0475 S23: 0.0286 REMARK 3 S31: -0.1477 S32: -0.0137 S33: -0.0209 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 2 THROUGH 113) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5855 45.9927 56.2209 REMARK 3 T TENSOR REMARK 3 T11: 0.4124 T22: 0.2491 REMARK 3 T33: 0.3444 T12: -0.0583 REMARK 3 T13: 0.0350 T23: -0.0754 REMARK 3 L TENSOR REMARK 3 L11: 1.4529 L22: 1.4686 REMARK 3 L33: 1.1774 L12: 0.0760 REMARK 3 L13: 0.4878 L23: -0.1294 REMARK 3 S TENSOR REMARK 3 S11: 0.0271 S12: -0.0933 S13: 0.1729 REMARK 3 S21: 0.0902 S22: 0.0737 S23: 0.0980 REMARK 3 S31: 0.0051 S32: 0.0277 S33: -0.0231 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN 'M' AND RESID 15 THROUGH 364) REMARK 3 ORIGIN FOR THE GROUP (A): -0.5721 9.7026 55.0097 REMARK 3 T TENSOR REMARK 3 T11: 0.2738 T22: 0.2197 REMARK 3 T33: 0.2161 T12: -0.0111 REMARK 3 T13: -0.0052 T23: -0.0234 REMARK 3 L TENSOR REMARK 3 L11: 0.9863 L22: 1.0502 REMARK 3 L33: 0.9116 L12: -0.1541 REMARK 3 L13: -0.1195 L23: 0.0516 REMARK 3 S TENSOR REMARK 3 S11: -0.0308 S12: -0.0348 S13: -0.0708 REMARK 3 S21: 0.1539 S22: 0.0131 S23: -0.1450 REMARK 3 S31: 0.0079 S32: 0.1165 S33: 0.0271 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN 'N' AND RESID 20 THROUGH 244) REMARK 3 ORIGIN FOR THE GROUP (A): 6.1269 31.4054 16.2218 REMARK 3 T TENSOR REMARK 3 T11: 0.3868 T22: 0.3235 REMARK 3 T33: 0.3117 T12: 0.0011 REMARK 3 T13: 0.0768 T23: -0.0480 REMARK 3 L TENSOR REMARK 3 L11: 0.5569 L22: 0.2824 REMARK 3 L33: 1.0492 L12: 0.2731 REMARK 3 L13: -0.0175 L23: -0.2885 REMARK 3 S TENSOR REMARK 3 S11: 0.0011 S12: -0.0496 S13: 0.0863 REMARK 3 S21: 0.0304 S22: -0.0350 S23: -0.0491 REMARK 3 S31: -0.2772 S32: 0.0497 S33: 0.0236 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN 'O' AND RESID 20 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5125 27.5320 3.3156 REMARK 3 T TENSOR REMARK 3 T11: 0.3822 T22: 0.3704 REMARK 3 T33: 0.3349 T12: -0.0090 REMARK 3 T13: 0.0286 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 0.5292 L22: 0.1944 REMARK 3 L33: 1.2244 L12: 0.0193 REMARK 3 L13: 0.2146 L23: -0.0737 REMARK 3 S TENSOR REMARK 3 S11: -0.0416 S12: 0.1137 S13: 0.2079 REMARK 3 S21: -0.1111 S22: 0.0420 S23: 0.0546 REMARK 3 S31: -0.1864 S32: -0.0367 S33: 0.0065 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN 'P' AND RESID 2 THROUGH 113) REMARK 3 ORIGIN FOR THE GROUP (A): -26.4838 23.4885 -16.6867 REMARK 3 T TENSOR REMARK 3 T11: 0.5208 T22: 0.6683 REMARK 3 T33: 0.4227 T12: 0.0084 REMARK 3 T13: -0.0236 T23: 0.1223 REMARK 3 L TENSOR REMARK 3 L11: 1.4400 L22: 1.0244 REMARK 3 L33: 1.6255 L12: 0.6061 REMARK 3 L13: 0.5026 L23: 0.2516 REMARK 3 S TENSOR REMARK 3 S11: -0.0073 S12: 0.4277 S13: 0.4026 REMARK 3 S21: -0.0662 S22: 0.0709 S23: -0.1087 REMARK 3 S31: 0.0960 S32: -0.3931 S33: -0.0035 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 4 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 15 through 321 or REMARK 3 resid 327 through 364)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 15 through 321 or REMARK 3 resid 327 through 364)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "I" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "M" and (resid 15 through 321 or REMARK 3 resid 327 through 364)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "F" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "J" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "N" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "G" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "K" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "O" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "P" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9QT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292146951. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-OCT-24 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 : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.978565 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 : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 223523 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 39.080 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 18.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 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) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350, 0.2 M AMMONIUM REMARK 280 CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 421.87467 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 210.93733 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 210.93733 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 421.87467 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASN A 3 REMARK 465 ILE A 4 REMARK 465 ILE A 5 REMARK 465 ASN A 6 REMARK 465 LEU A 7 REMARK 465 TRP A 8 REMARK 465 ASN A 9 REMARK 465 GLY A 10 REMARK 465 ILE A 11 REMARK 465 VAL A 12 REMARK 465 PRO A 13 REMARK 465 THR A 14 REMARK 465 THR A 323 REMARK 465 ASP A 324 REMARK 465 VAL A 325 REMARK 465 GLN A 326 REMARK 465 ILE A 365 REMARK 465 GLU A 366 REMARK 465 VAL A 367 REMARK 465 GLU A 368 REMARK 465 ASP A 369 REMARK 465 ASP A 370 REMARK 465 VAL A 371 REMARK 465 ILE A 372 REMARK 465 ASP A 373 REMARK 465 ASP A 374 REMARK 465 ASP A 375 REMARK 465 ASP A 376 REMARK 465 TYR A 377 REMARK 465 ASN A 378 REMARK 465 PRO A 379 REMARK 465 LYS A 380 REMARK 465 PRO A 381 REMARK 465 THR A 382 REMARK 465 PRO A 383 REMARK 465 ILE A 384 REMARK 465 PRO A 385 REMARK 465 GLU A 386 REMARK 465 PRO A 387 REMARK 465 HIS A 388 REMARK 465 PRO A 389 REMARK 465 ARG A 390 REMARK 465 PRO A 391 REMARK 465 PRO A 392 REMARK 465 PHE A 393 REMARK 465 PRO A 394 REMARK 465 ARG A 395 REMARK 465 HIS A 396 REMARK 465 GLU A 397 REMARK 465 GLY A 398 REMARK 465 SER A 399 REMARK 465 GLY A 400 REMARK 465 LEU A 401 REMARK 465 VAL A 402 REMARK 465 PRO A 403 REMARK 465 ARG A 404 REMARK 465 ILE A 405 REMARK 465 GLY A 406 REMARK 465 SER A 407 REMARK 465 GLY A 408 REMARK 465 SER A 409 REMARK 465 ALA A 410 REMARK 465 GLY A 411 REMARK 465 TRP A 412 REMARK 465 SER A 413 REMARK 465 HIS A 414 REMARK 465 PRO A 415 REMARK 465 GLN A 416 REMARK 465 PHE A 417 REMARK 465 GLU A 418 REMARK 465 LYS A 419 REMARK 465 GLY A 420 REMARK 465 GLY A 421 REMARK 465 GLY A 422 REMARK 465 SER A 423 REMARK 465 GLY A 424 REMARK 465 GLY A 425 REMARK 465 GLY A 426 REMARK 465 SER A 427 REMARK 465 GLY A 428 REMARK 465 GLY A 429 REMARK 465 GLY A 430 REMARK 465 SER A 431 REMARK 465 TRP A 432 REMARK 465 SER A 433 REMARK 465 HIS A 434 REMARK 465 PRO A 435 REMARK 465 GLN A 436 REMARK 465 PHE A 437 REMARK 465 GLU A 438 REMARK 465 LYS A 439 REMARK 465 GLY A 440 REMARK 465 THR A 441 REMARK 465 GLY A 442 REMARK 465 GLY A 443 REMARK 465 LEU A 444 REMARK 465 ASN A 445 REMARK 465 ASP A 446 REMARK 465 ILE A 447 REMARK 465 PHE A 448 REMARK 465 GLU A 449 REMARK 465 ALA A 450 REMARK 465 GLN A 451 REMARK 465 LYS A 452 REMARK 465 ILE A 453 REMARK 465 GLU A 454 REMARK 465 TRP A 455 REMARK 465 HIS A 456 REMARK 465 GLU A 457 REMARK 465 SER B 159 REMARK 465 LYS B 160 REMARK 465 SER B 161 REMARK 465 THR B 162 REMARK 465 SER B 163 REMARK 465 GLY B 164 REMARK 465 CYS C 233 REMARK 465 GLY D -1 REMARK 465 SER D 0 REMARK 465 GLN D 1 REMARK 465 MET E 1 REMARK 465 ALA E 2 REMARK 465 ASN E 3 REMARK 465 ILE E 4 REMARK 465 ILE E 5 REMARK 465 ASN E 6 REMARK 465 LEU E 7 REMARK 465 TRP E 8 REMARK 465 ASN E 9 REMARK 465 GLY E 10 REMARK 465 ILE E 11 REMARK 465 VAL E 12 REMARK 465 PRO E 13 REMARK 465 THR E 14 REMARK 465 THR E 323 REMARK 465 ASP E 324 REMARK 465 VAL E 325 REMARK 465 GLN E 326 REMARK 465 ILE E 365 REMARK 465 GLU E 366 REMARK 465 VAL E 367 REMARK 465 GLU E 368 REMARK 465 ASP E 369 REMARK 465 ASP E 370 REMARK 465 VAL E 371 REMARK 465 ILE E 372 REMARK 465 ASP E 373 REMARK 465 ASP E 374 REMARK 465 ASP E 375 REMARK 465 ASP E 376 REMARK 465 TYR E 377 REMARK 465 ASN E 378 REMARK 465 PRO E 379 REMARK 465 LYS E 380 REMARK 465 PRO E 381 REMARK 465 THR E 382 REMARK 465 PRO E 383 REMARK 465 ILE E 384 REMARK 465 PRO E 385 REMARK 465 GLU E 386 REMARK 465 PRO E 387 REMARK 465 HIS E 388 REMARK 465 PRO E 389 REMARK 465 ARG E 390 REMARK 465 PRO E 391 REMARK 465 PRO E 392 REMARK 465 PHE E 393 REMARK 465 PRO E 394 REMARK 465 ARG E 395 REMARK 465 HIS E 396 REMARK 465 GLU E 397 REMARK 465 GLY E 398 REMARK 465 SER E 399 REMARK 465 GLY E 400 REMARK 465 LEU E 401 REMARK 465 VAL E 402 REMARK 465 PRO E 403 REMARK 465 ARG E 404 REMARK 465 ILE E 405 REMARK 465 GLY E 406 REMARK 465 SER E 407 REMARK 465 GLY E 408 REMARK 465 SER E 409 REMARK 465 ALA E 410 REMARK 465 GLY E 411 REMARK 465 TRP E 412 REMARK 465 SER E 413 REMARK 465 HIS E 414 REMARK 465 PRO E 415 REMARK 465 GLN E 416 REMARK 465 PHE E 417 REMARK 465 GLU E 418 REMARK 465 LYS E 419 REMARK 465 GLY E 420 REMARK 465 GLY E 421 REMARK 465 GLY E 422 REMARK 465 SER E 423 REMARK 465 GLY E 424 REMARK 465 GLY E 425 REMARK 465 GLY E 426 REMARK 465 SER E 427 REMARK 465 GLY E 428 REMARK 465 GLY E 429 REMARK 465 GLY E 430 REMARK 465 SER E 431 REMARK 465 TRP E 432 REMARK 465 SER E 433 REMARK 465 HIS E 434 REMARK 465 PRO E 435 REMARK 465 GLN E 436 REMARK 465 PHE E 437 REMARK 465 GLU E 438 REMARK 465 LYS E 439 REMARK 465 GLY E 440 REMARK 465 THR E 441 REMARK 465 GLY E 442 REMARK 465 GLY E 443 REMARK 465 LEU E 444 REMARK 465 ASN E 445 REMARK 465 ASP E 446 REMARK 465 ILE E 447 REMARK 465 PHE E 448 REMARK 465 GLU E 449 REMARK 465 ALA E 450 REMARK 465 GLN E 451 REMARK 465 LYS E 452 REMARK 465 ILE E 453 REMARK 465 GLU E 454 REMARK 465 TRP E 455 REMARK 465 HIS E 456 REMARK 465 GLU E 457 REMARK 465 SER F 159 REMARK 465 LYS F 160 REMARK 465 SER F 161 REMARK 465 THR F 162 REMARK 465 SER F 163 REMARK 465 GLY F 164 REMARK 465 CYS G 233 REMARK 465 GLY H -1 REMARK 465 SER H 0 REMARK 465 GLN H 1 REMARK 465 MET I 1 REMARK 465 ALA I 2 REMARK 465 ASN I 3 REMARK 465 ILE I 4 REMARK 465 ILE I 5 REMARK 465 ASN I 6 REMARK 465 LEU I 7 REMARK 465 TRP I 8 REMARK 465 ASN I 9 REMARK 465 GLY I 10 REMARK 465 ILE I 11 REMARK 465 VAL I 12 REMARK 465 PRO I 13 REMARK 465 THR I 14 REMARK 465 SER I 322 REMARK 465 THR I 323 REMARK 465 ASP I 324 REMARK 465 VAL I 325 REMARK 465 GLN I 326 REMARK 465 ILE I 365 REMARK 465 GLU I 366 REMARK 465 VAL I 367 REMARK 465 GLU I 368 REMARK 465 ASP I 369 REMARK 465 ASP I 370 REMARK 465 VAL I 371 REMARK 465 ILE I 372 REMARK 465 ASP I 373 REMARK 465 ASP I 374 REMARK 465 ASP I 375 REMARK 465 ASP I 376 REMARK 465 TYR I 377 REMARK 465 ASN I 378 REMARK 465 PRO I 379 REMARK 465 LYS I 380 REMARK 465 PRO I 381 REMARK 465 THR I 382 REMARK 465 PRO I 383 REMARK 465 ILE I 384 REMARK 465 PRO I 385 REMARK 465 GLU I 386 REMARK 465 PRO I 387 REMARK 465 HIS I 388 REMARK 465 PRO I 389 REMARK 465 ARG I 390 REMARK 465 PRO I 391 REMARK 465 PRO I 392 REMARK 465 PHE I 393 REMARK 465 PRO I 394 REMARK 465 ARG I 395 REMARK 465 HIS I 396 REMARK 465 GLU I 397 REMARK 465 GLY I 398 REMARK 465 SER I 399 REMARK 465 GLY I 400 REMARK 465 LEU I 401 REMARK 465 VAL I 402 REMARK 465 PRO I 403 REMARK 465 ARG I 404 REMARK 465 ILE I 405 REMARK 465 GLY I 406 REMARK 465 SER I 407 REMARK 465 GLY I 408 REMARK 465 SER I 409 REMARK 465 ALA I 410 REMARK 465 GLY I 411 REMARK 465 TRP I 412 REMARK 465 SER I 413 REMARK 465 HIS I 414 REMARK 465 PRO I 415 REMARK 465 GLN I 416 REMARK 465 PHE I 417 REMARK 465 GLU I 418 REMARK 465 LYS I 419 REMARK 465 GLY I 420 REMARK 465 GLY I 421 REMARK 465 GLY I 422 REMARK 465 SER I 423 REMARK 465 GLY I 424 REMARK 465 GLY I 425 REMARK 465 GLY I 426 REMARK 465 SER I 427 REMARK 465 GLY I 428 REMARK 465 GLY I 429 REMARK 465 GLY I 430 REMARK 465 SER I 431 REMARK 465 TRP I 432 REMARK 465 SER I 433 REMARK 465 HIS I 434 REMARK 465 PRO I 435 REMARK 465 GLN I 436 REMARK 465 PHE I 437 REMARK 465 GLU I 438 REMARK 465 LYS I 439 REMARK 465 GLY I 440 REMARK 465 THR I 441 REMARK 465 GLY I 442 REMARK 465 GLY I 443 REMARK 465 LEU I 444 REMARK 465 ASN I 445 REMARK 465 ASP I 446 REMARK 465 ILE I 447 REMARK 465 PHE I 448 REMARK 465 GLU I 449 REMARK 465 ALA I 450 REMARK 465 GLN I 451 REMARK 465 LYS I 452 REMARK 465 ILE I 453 REMARK 465 GLU I 454 REMARK 465 TRP I 455 REMARK 465 HIS I 456 REMARK 465 GLU I 457 REMARK 465 SER J 159 REMARK 465 LYS J 160 REMARK 465 SER J 161 REMARK 465 THR J 162 REMARK 465 SER J 163 REMARK 465 GLY J 164 REMARK 465 CYS K 233 REMARK 465 GLY L -1 REMARK 465 SER L 0 REMARK 465 GLN L 1 REMARK 465 MET M 1 REMARK 465 ALA M 2 REMARK 465 ASN M 3 REMARK 465 ILE M 4 REMARK 465 ILE M 5 REMARK 465 ASN M 6 REMARK 465 LEU M 7 REMARK 465 TRP M 8 REMARK 465 ASN M 9 REMARK 465 GLY M 10 REMARK 465 ILE M 11 REMARK 465 VAL M 12 REMARK 465 PRO M 13 REMARK 465 THR M 14 REMARK 465 ILE M 365 REMARK 465 GLU M 366 REMARK 465 VAL M 367 REMARK 465 GLU M 368 REMARK 465 ASP M 369 REMARK 465 ASP M 370 REMARK 465 VAL M 371 REMARK 465 ILE M 372 REMARK 465 ASP M 373 REMARK 465 ASP M 374 REMARK 465 ASP M 375 REMARK 465 ASP M 376 REMARK 465 TYR M 377 REMARK 465 ASN M 378 REMARK 465 PRO M 379 REMARK 465 LYS M 380 REMARK 465 PRO M 381 REMARK 465 THR M 382 REMARK 465 PRO M 383 REMARK 465 ILE M 384 REMARK 465 PRO M 385 REMARK 465 GLU M 386 REMARK 465 PRO M 387 REMARK 465 HIS M 388 REMARK 465 PRO M 389 REMARK 465 ARG M 390 REMARK 465 PRO M 391 REMARK 465 PRO M 392 REMARK 465 PHE M 393 REMARK 465 PRO M 394 REMARK 465 ARG M 395 REMARK 465 HIS M 396 REMARK 465 GLU M 397 REMARK 465 GLY M 398 REMARK 465 SER M 399 REMARK 465 GLY M 400 REMARK 465 LEU M 401 REMARK 465 VAL M 402 REMARK 465 PRO M 403 REMARK 465 ARG M 404 REMARK 465 ILE M 405 REMARK 465 GLY M 406 REMARK 465 SER M 407 REMARK 465 GLY M 408 REMARK 465 SER M 409 REMARK 465 ALA M 410 REMARK 465 GLY M 411 REMARK 465 TRP M 412 REMARK 465 SER M 413 REMARK 465 HIS M 414 REMARK 465 PRO M 415 REMARK 465 GLN M 416 REMARK 465 PHE M 417 REMARK 465 GLU M 418 REMARK 465 LYS M 419 REMARK 465 GLY M 420 REMARK 465 GLY M 421 REMARK 465 GLY M 422 REMARK 465 SER M 423 REMARK 465 GLY M 424 REMARK 465 GLY M 425 REMARK 465 GLY M 426 REMARK 465 SER M 427 REMARK 465 GLY M 428 REMARK 465 GLY M 429 REMARK 465 GLY M 430 REMARK 465 SER M 431 REMARK 465 TRP M 432 REMARK 465 SER M 433 REMARK 465 HIS M 434 REMARK 465 PRO M 435 REMARK 465 GLN M 436 REMARK 465 PHE M 437 REMARK 465 GLU M 438 REMARK 465 LYS M 439 REMARK 465 GLY M 440 REMARK 465 THR M 441 REMARK 465 GLY M 442 REMARK 465 GLY M 443 REMARK 465 LEU M 444 REMARK 465 ASN M 445 REMARK 465 ASP M 446 REMARK 465 ILE M 447 REMARK 465 PHE M 448 REMARK 465 GLU M 449 REMARK 465 ALA M 450 REMARK 465 GLN M 451 REMARK 465 LYS M 452 REMARK 465 ILE M 453 REMARK 465 GLU M 454 REMARK 465 TRP M 455 REMARK 465 HIS M 456 REMARK 465 GLU M 457 REMARK 465 SER N 159 REMARK 465 LYS N 160 REMARK 465 SER N 161 REMARK 465 THR N 162 REMARK 465 SER N 163 REMARK 465 GLY N 164 REMARK 465 CYS O 233 REMARK 465 GLY P -1 REMARK 465 SER P 0 REMARK 465 GLN P 1 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 LYS A 70 66.37 -152.14 REMARK 500 ASN A 233 -120.13 59.39 REMARK 500 SER B 34 -5.53 69.42 REMARK 500 LYS B 62 -169.11 -112.89 REMARK 500 SER B 123 45.45 -147.94 REMARK 500 ASP B 175 78.28 61.62 REMARK 500 SER C 49 -126.23 57.51 REMARK 500 ALA C 70 -32.98 71.24 REMARK 500 SER C 71 -3.65 -140.17 REMARK 500 ASN C 157 80.29 50.21 REMARK 500 PRO C 160 -177.14 -69.93 REMARK 500 LYS E 70 62.95 -152.28 REMARK 500 ASN E 192 14.41 59.52 REMARK 500 ASN E 233 -120.88 58.99 REMARK 500 ASP E 267 -159.97 -81.05 REMARK 500 ASP E 321 -15.97 -143.66 REMARK 500 SER F 34 -6.41 69.65 REMARK 500 LYS F 62 -169.36 -112.85 REMARK 500 SER F 84 -13.35 65.76 REMARK 500 SER F 123 45.24 -148.25 REMARK 500 ASP F 175 78.60 61.51 REMARK 500 SER G 49 -126.25 57.36 REMARK 500 ALA G 70 -33.20 71.04 REMARK 500 SER G 71 -2.42 -140.90 REMARK 500 ASN G 157 79.70 50.74 REMARK 500 PRO G 160 -175.92 -69.81 REMARK 500 LYS I 70 66.38 -152.11 REMARK 500 ASN I 233 -120.65 59.75 REMARK 500 SER J 34 -6.17 69.10 REMARK 500 LYS J 62 -169.83 -112.55 REMARK 500 LEU J 82 48.93 -106.47 REMARK 500 SER J 123 45.57 -147.60 REMARK 500 ASP J 175 78.55 61.94 REMARK 500 SER K 49 -126.16 57.08 REMARK 500 ALA K 70 -33.53 71.28 REMARK 500 SER K 71 -3.43 -140.70 REMARK 500 ASN K 157 80.64 51.10 REMARK 500 LYS M 70 63.75 -151.99 REMARK 500 ASN M 233 -120.80 59.72 REMARK 500 ASN M 320 -134.91 -126.08 REMARK 500 ASP M 321 24.56 -142.29 REMARK 500 ASP M 324 85.77 -69.20 REMARK 500 VAL M 325 68.02 -60.12 REMARK 500 GLN M 326 -32.40 -174.76 REMARK 500 SER N 34 -6.69 68.40 REMARK 500 LYS N 62 -169.69 -112.48 REMARK 500 LEU N 82 50.57 -108.12 REMARK 500 LYS N 83 -76.87 -74.58 REMARK 500 SER N 123 45.77 -148.33 REMARK 500 ASP N 175 78.73 62.33 REMARK 500 REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 9QT3 A 1 397 UNP P24758 PG153_VACCW 1 397 DBREF 9QT3 B 20 244 PDB 9QT3 9QT3 20 244 DBREF 9QT3 C 20 233 PDB 9QT3 9QT3 20 233 DBREF 9QT3 D -1 113 PDB 9QT3 9QT3 -1 113 DBREF 9QT3 E 1 397 UNP P24758 PG153_VACCW 1 397 DBREF 9QT3 F 20 244 PDB 9QT3 9QT3 20 244 DBREF 9QT3 G 20 233 PDB 9QT3 9QT3 20 233 DBREF 9QT3 H -1 113 PDB 9QT3 9QT3 -1 113 DBREF 9QT3 I 1 397 UNP P24758 PG153_VACCW 1 397 DBREF 9QT3 J 20 244 PDB 9QT3 9QT3 20 244 DBREF 9QT3 K 20 233 PDB 9QT3 9QT3 20 233 DBREF 9QT3 L -1 113 PDB 9QT3 9QT3 -1 113 DBREF 9QT3 M 1 397 UNP P24758 PG153_VACCW 1 397 DBREF 9QT3 N 20 244 PDB 9QT3 9QT3 20 244 DBREF 9QT3 O 20 233 PDB 9QT3 9QT3 20 233 DBREF 9QT3 P -1 113 PDB 9QT3 9QT3 -1 113 SEQADV 9QT3 GLY A 398 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 399 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 400 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU A 401 UNP P24758 EXPRESSION TAG SEQADV 9QT3 VAL A 402 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO A 403 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ARG A 404 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE A 405 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 406 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 407 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 408 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 409 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA A 410 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 411 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP A 412 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 413 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS A 414 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO A 415 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN A 416 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE A 417 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU A 418 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS A 419 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 420 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 421 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 422 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 423 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 424 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 425 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 426 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 427 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 428 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 429 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 430 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 431 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP A 432 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER A 433 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS A 434 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO A 435 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN A 436 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE A 437 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU A 438 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS A 439 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 440 UNP P24758 EXPRESSION TAG SEQADV 9QT3 THR A 441 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 442 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY A 443 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU A 444 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASN A 445 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASP A 446 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE A 447 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE A 448 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU A 449 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA A 450 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN A 451 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS A 452 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE A 453 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU A 454 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP A 455 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS A 456 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU A 457 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 398 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 399 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 400 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU E 401 UNP P24758 EXPRESSION TAG SEQADV 9QT3 VAL E 402 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO E 403 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ARG E 404 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE E 405 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 406 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 407 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 408 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 409 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA E 410 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 411 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP E 412 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 413 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS E 414 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO E 415 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN E 416 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE E 417 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU E 418 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS E 419 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 420 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 421 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 422 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 423 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 424 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 425 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 426 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 427 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 428 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 429 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 430 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 431 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP E 432 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER E 433 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS E 434 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO E 435 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN E 436 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE E 437 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU E 438 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS E 439 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 440 UNP P24758 EXPRESSION TAG SEQADV 9QT3 THR E 441 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 442 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY E 443 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU E 444 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASN E 445 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASP E 446 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE E 447 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE E 448 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU E 449 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA E 450 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN E 451 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS E 452 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE E 453 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU E 454 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP E 455 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS E 456 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU E 457 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 398 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 399 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 400 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU I 401 UNP P24758 EXPRESSION TAG SEQADV 9QT3 VAL I 402 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO I 403 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ARG I 404 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE I 405 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 406 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 407 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 408 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 409 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA I 410 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 411 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP I 412 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 413 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS I 414 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO I 415 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN I 416 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE I 417 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU I 418 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS I 419 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 420 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 421 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 422 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 423 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 424 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 425 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 426 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 427 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 428 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 429 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 430 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 431 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP I 432 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER I 433 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS I 434 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO I 435 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN I 436 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE I 437 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU I 438 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS I 439 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 440 UNP P24758 EXPRESSION TAG SEQADV 9QT3 THR I 441 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 442 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY I 443 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU I 444 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASN I 445 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASP I 446 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE I 447 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE I 448 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU I 449 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA I 450 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN I 451 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS I 452 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE I 453 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU I 454 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP I 455 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS I 456 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU I 457 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 398 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 399 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 400 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU M 401 UNP P24758 EXPRESSION TAG SEQADV 9QT3 VAL M 402 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO M 403 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ARG M 404 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE M 405 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 406 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 407 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 408 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 409 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA M 410 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 411 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP M 412 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 413 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS M 414 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO M 415 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN M 416 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE M 417 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU M 418 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS M 419 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 420 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 421 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 422 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 423 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 424 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 425 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 426 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 427 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 428 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 429 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 430 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 431 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP M 432 UNP P24758 EXPRESSION TAG SEQADV 9QT3 SER M 433 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS M 434 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PRO M 435 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN M 436 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE M 437 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU M 438 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS M 439 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 440 UNP P24758 EXPRESSION TAG SEQADV 9QT3 THR M 441 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 442 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLY M 443 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LEU M 444 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASN M 445 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ASP M 446 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE M 447 UNP P24758 EXPRESSION TAG SEQADV 9QT3 PHE M 448 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU M 449 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ALA M 450 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLN M 451 UNP P24758 EXPRESSION TAG SEQADV 9QT3 LYS M 452 UNP P24758 EXPRESSION TAG SEQADV 9QT3 ILE M 453 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU M 454 UNP P24758 EXPRESSION TAG SEQADV 9QT3 TRP M 455 UNP P24758 EXPRESSION TAG SEQADV 9QT3 HIS M 456 UNP P24758 EXPRESSION TAG SEQADV 9QT3 GLU M 457 UNP P24758 EXPRESSION TAG SEQRES 1 A 457 MET ALA ASN ILE ILE ASN LEU TRP ASN GLY ILE VAL PRO SEQRES 2 A 457 THR VAL GLN ASP VAL ASN VAL ALA SER ILE THR ALA PHE SEQRES 3 A 457 LYS SER MET ILE ASP GLU THR TRP ASP LYS LYS ILE GLU SEQRES 4 A 457 ALA ASN THR CYS ILE SER ARG LYS HIS ARG ASN ILE ILE SEQRES 5 A 457 HIS GLU VAL ILE ARG ASP PHE MET LYS ALA TYR PRO LYS SEQRES 6 A 457 MET ASP GLU ASN LYS LYS SER PRO LEU GLY ALA PRO MET SEQRES 7 A 457 GLN TRP LEU THR GLN TYR TYR ILE LEU LYS ASN GLU TYR SEQRES 8 A 457 HIS LYS THR MET LEU ALA TYR ASP ASN GLY SER LEU ASN SEQRES 9 A 457 THR LYS PHE LYS THR LEU ASN ILE TYR MET ILE THR ASN SEQRES 10 A 457 VAL GLY GLN TYR ILE LEU TYR ILE VAL PHE CYS ILE ILE SEQRES 11 A 457 SER GLY LYS ASN HIS ASP GLY THR PRO TYR ILE TYR ASP SEQRES 12 A 457 SER GLU ILE THR SER ASN ASP LYS ASN PHE ILE ASN GLU SEQRES 13 A 457 ARG ILE LYS TYR ALA CYS LYS GLN ILE LEU HIS GLY GLN SEQRES 14 A 457 LEU THR ILE ALA LEU ARG ILE ARG ASN LYS PHE MET PHE SEQRES 15 A 457 ILE GLY SER PRO MET TYR LEU TRP PHE ASN VAL ASN GLY SEQRES 16 A 457 SER GLN VAL TYR HIS ASP ILE TYR ASP ARG ASN ALA GLY SEQRES 17 A 457 PHE HIS ASN LYS GLU ILE GLY ARG LEU LEU TYR ALA PHE SEQRES 18 A 457 MET TYR TYR LEU SER ILE SER GLY ARG PHE LEU ASN ASP SEQRES 19 A 457 PHE ALA LEU LEU LYS PHE THR TYR LEU GLY GLU SER TRP SEQRES 20 A 457 THR PHE SER LEU SER VAL PRO GLU TYR ILE LEU TYR GLY SEQRES 21 A 457 LEU GLY TYR SER VAL PHE ASP THR ILE GLU LYS PHE SER SEQRES 22 A 457 ASN ASP ALA ILE LEU VAL TYR ILE ARG THR ASN ASN ARG SEQRES 23 A 457 ASN GLY TYR ASP TYR VAL GLU PHE ASN LYS LYS GLY ILE SEQRES 24 A 457 ALA LYS VAL THR GLU ASP LYS PRO ASP ASN ASP LYS ARG SEQRES 25 A 457 ILE HIS ALA ILE ARG LEU ILE ASN ASP SER THR ASP VAL SEQRES 26 A 457 GLN HIS ILE HIS PHE GLY PHE ARG ASN MET VAL ILE ILE SEQRES 27 A 457 ASP ASN GLU CYS ALA ASN ILE GLN SER SER ALA GLU ASN SEQRES 28 A 457 ALA THR ASP THR GLY HIS HIS GLN ASP SER LYS ILE ASN SEQRES 29 A 457 ILE GLU VAL GLU ASP ASP VAL ILE ASP ASP ASP ASP TYR SEQRES 30 A 457 ASN PRO LYS PRO THR PRO ILE PRO GLU PRO HIS PRO ARG SEQRES 31 A 457 PRO PRO PHE PRO ARG HIS GLU GLY SER GLY LEU VAL PRO SEQRES 32 A 457 ARG ILE GLY SER GLY SER ALA GLY TRP SER HIS PRO GLN SEQRES 33 A 457 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SEQRES 34 A 457 GLY SER TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLY SEQRES 35 A 457 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 36 A 457 HIS GLU SEQRES 1 B 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 B 225 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 B 225 GLY SER ILE SER THR TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 B 225 PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY LEU MET TYR SEQRES 5 B 225 ASN SER GLY SER PRO ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 B 225 ARG VAL THR MET SER GLY ASP THR SER LYS ASN GLN PHE SEQRES 7 B 225 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 B 225 VAL TYR TYR CYS ALA ARG LEU ARG TYR ASP PHE TRP SER SEQRES 9 B 225 GLY SER LYS GLY ARG TYR TYR MET ASP VAL TRP GLY LYS SEQRES 10 B 225 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 B 225 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 B 225 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 B 225 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 B 225 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 B 225 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 B 225 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 B 225 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 B 225 LYS VAL GLU PRO SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 C 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 C 214 PRO GLY GLN ALA PRO LYS LEU LEU ILE HIS ASP ALA SER SEQRES 5 C 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR PHE THR VAL SER SER LEU SEQRES 7 C 214 GLN ALA GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 C 214 TYR ASN LEU PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 C 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS SEQRES 1 D 123 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 D 123 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 D 123 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 4 D 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 D 123 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 6 D 123 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 7 D 123 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 D 123 ASP THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR SEQRES 9 D 123 PHE TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 D 123 GLN VAL THR VAL SER SER SEQRES 1 E 457 MET ALA ASN ILE ILE ASN LEU TRP ASN GLY ILE VAL PRO SEQRES 2 E 457 THR VAL GLN ASP VAL ASN VAL ALA SER ILE THR ALA PHE SEQRES 3 E 457 LYS SER MET ILE ASP GLU THR TRP ASP LYS LYS ILE GLU SEQRES 4 E 457 ALA ASN THR CYS ILE SER ARG LYS HIS ARG ASN ILE ILE SEQRES 5 E 457 HIS GLU VAL ILE ARG ASP PHE MET LYS ALA TYR PRO LYS SEQRES 6 E 457 MET ASP GLU ASN LYS LYS SER PRO LEU GLY ALA PRO MET SEQRES 7 E 457 GLN TRP LEU THR GLN TYR TYR ILE LEU LYS ASN GLU TYR SEQRES 8 E 457 HIS LYS THR MET LEU ALA TYR ASP ASN GLY SER LEU ASN SEQRES 9 E 457 THR LYS PHE LYS THR LEU ASN ILE TYR MET ILE THR ASN SEQRES 10 E 457 VAL GLY GLN TYR ILE LEU TYR ILE VAL PHE CYS ILE ILE SEQRES 11 E 457 SER GLY LYS ASN HIS ASP GLY THR PRO TYR ILE TYR ASP SEQRES 12 E 457 SER GLU ILE THR SER ASN ASP LYS ASN PHE ILE ASN GLU SEQRES 13 E 457 ARG ILE LYS TYR ALA CYS LYS GLN ILE LEU HIS GLY GLN SEQRES 14 E 457 LEU THR ILE ALA LEU ARG ILE ARG ASN LYS PHE MET PHE SEQRES 15 E 457 ILE GLY SER PRO MET TYR LEU TRP PHE ASN VAL ASN GLY SEQRES 16 E 457 SER GLN VAL TYR HIS ASP ILE TYR ASP ARG ASN ALA GLY SEQRES 17 E 457 PHE HIS ASN LYS GLU ILE GLY ARG LEU LEU TYR ALA PHE SEQRES 18 E 457 MET TYR TYR LEU SER ILE SER GLY ARG PHE LEU ASN ASP SEQRES 19 E 457 PHE ALA LEU LEU LYS PHE THR TYR LEU GLY GLU SER TRP SEQRES 20 E 457 THR PHE SER LEU SER VAL PRO GLU TYR ILE LEU TYR GLY SEQRES 21 E 457 LEU GLY TYR SER VAL PHE ASP THR ILE GLU LYS PHE SER SEQRES 22 E 457 ASN ASP ALA ILE LEU VAL TYR ILE ARG THR ASN ASN ARG SEQRES 23 E 457 ASN GLY TYR ASP TYR VAL GLU PHE ASN LYS LYS GLY ILE SEQRES 24 E 457 ALA LYS VAL THR GLU ASP LYS PRO ASP ASN ASP LYS ARG SEQRES 25 E 457 ILE HIS ALA ILE ARG LEU ILE ASN ASP SER THR ASP VAL SEQRES 26 E 457 GLN HIS ILE HIS PHE GLY PHE ARG ASN MET VAL ILE ILE SEQRES 27 E 457 ASP ASN GLU CYS ALA ASN ILE GLN SER SER ALA GLU ASN SEQRES 28 E 457 ALA THR ASP THR GLY HIS HIS GLN ASP SER LYS ILE ASN SEQRES 29 E 457 ILE GLU VAL GLU ASP ASP VAL ILE ASP ASP ASP ASP TYR SEQRES 30 E 457 ASN PRO LYS PRO THR PRO ILE PRO GLU PRO HIS PRO ARG SEQRES 31 E 457 PRO PRO PHE PRO ARG HIS GLU GLY SER GLY LEU VAL PRO SEQRES 32 E 457 ARG ILE GLY SER GLY SER ALA GLY TRP SER HIS PRO GLN SEQRES 33 E 457 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SEQRES 34 E 457 GLY SER TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLY SEQRES 35 E 457 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 36 E 457 HIS GLU SEQRES 1 F 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 F 225 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 F 225 GLY SER ILE SER THR TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 F 225 PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY LEU MET TYR SEQRES 5 F 225 ASN SER GLY SER PRO ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 F 225 ARG VAL THR MET SER GLY ASP THR SER LYS ASN GLN PHE SEQRES 7 F 225 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 F 225 VAL TYR TYR CYS ALA ARG LEU ARG TYR ASP PHE TRP SER SEQRES 9 F 225 GLY SER LYS GLY ARG TYR TYR MET ASP VAL TRP GLY LYS SEQRES 10 F 225 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 F 225 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 F 225 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 F 225 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 F 225 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 F 225 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 F 225 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 F 225 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 F 225 LYS VAL GLU PRO SEQRES 1 G 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 G 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 G 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 G 214 PRO GLY GLN ALA PRO LYS LEU LEU ILE HIS ASP ALA SER SEQRES 5 G 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 G 214 GLY SER GLY THR ASP PHE THR PHE THR VAL SER SER LEU SEQRES 7 G 214 GLN ALA GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 G 214 TYR ASN LEU PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 G 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 G 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 G 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 G 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 G 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 G 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 G 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 G 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 G 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 123 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 H 123 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 123 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 4 H 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 H 123 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 6 H 123 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 7 H 123 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 H 123 ASP THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR SEQRES 9 H 123 PHE TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 123 GLN VAL THR VAL SER SER SEQRES 1 I 457 MET ALA ASN ILE ILE ASN LEU TRP ASN GLY ILE VAL PRO SEQRES 2 I 457 THR VAL GLN ASP VAL ASN VAL ALA SER ILE THR ALA PHE SEQRES 3 I 457 LYS SER MET ILE ASP GLU THR TRP ASP LYS LYS ILE GLU SEQRES 4 I 457 ALA ASN THR CYS ILE SER ARG LYS HIS ARG ASN ILE ILE SEQRES 5 I 457 HIS GLU VAL ILE ARG ASP PHE MET LYS ALA TYR PRO LYS SEQRES 6 I 457 MET ASP GLU ASN LYS LYS SER PRO LEU GLY ALA PRO MET SEQRES 7 I 457 GLN TRP LEU THR GLN TYR TYR ILE LEU LYS ASN GLU TYR SEQRES 8 I 457 HIS LYS THR MET LEU ALA TYR ASP ASN GLY SER LEU ASN SEQRES 9 I 457 THR LYS PHE LYS THR LEU ASN ILE TYR MET ILE THR ASN SEQRES 10 I 457 VAL GLY GLN TYR ILE LEU TYR ILE VAL PHE CYS ILE ILE SEQRES 11 I 457 SER GLY LYS ASN HIS ASP GLY THR PRO TYR ILE TYR ASP SEQRES 12 I 457 SER GLU ILE THR SER ASN ASP LYS ASN PHE ILE ASN GLU SEQRES 13 I 457 ARG ILE LYS TYR ALA CYS LYS GLN ILE LEU HIS GLY GLN SEQRES 14 I 457 LEU THR ILE ALA LEU ARG ILE ARG ASN LYS PHE MET PHE SEQRES 15 I 457 ILE GLY SER PRO MET TYR LEU TRP PHE ASN VAL ASN GLY SEQRES 16 I 457 SER GLN VAL TYR HIS ASP ILE TYR ASP ARG ASN ALA GLY SEQRES 17 I 457 PHE HIS ASN LYS GLU ILE GLY ARG LEU LEU TYR ALA PHE SEQRES 18 I 457 MET TYR TYR LEU SER ILE SER GLY ARG PHE LEU ASN ASP SEQRES 19 I 457 PHE ALA LEU LEU LYS PHE THR TYR LEU GLY GLU SER TRP SEQRES 20 I 457 THR PHE SER LEU SER VAL PRO GLU TYR ILE LEU TYR GLY SEQRES 21 I 457 LEU GLY TYR SER VAL PHE ASP THR ILE GLU LYS PHE SER SEQRES 22 I 457 ASN ASP ALA ILE LEU VAL TYR ILE ARG THR ASN ASN ARG SEQRES 23 I 457 ASN GLY TYR ASP TYR VAL GLU PHE ASN LYS LYS GLY ILE SEQRES 24 I 457 ALA LYS VAL THR GLU ASP LYS PRO ASP ASN ASP LYS ARG SEQRES 25 I 457 ILE HIS ALA ILE ARG LEU ILE ASN ASP SER THR ASP VAL SEQRES 26 I 457 GLN HIS ILE HIS PHE GLY PHE ARG ASN MET VAL ILE ILE SEQRES 27 I 457 ASP ASN GLU CYS ALA ASN ILE GLN SER SER ALA GLU ASN SEQRES 28 I 457 ALA THR ASP THR GLY HIS HIS GLN ASP SER LYS ILE ASN SEQRES 29 I 457 ILE GLU VAL GLU ASP ASP VAL ILE ASP ASP ASP ASP TYR SEQRES 30 I 457 ASN PRO LYS PRO THR PRO ILE PRO GLU PRO HIS PRO ARG SEQRES 31 I 457 PRO PRO PHE PRO ARG HIS GLU GLY SER GLY LEU VAL PRO SEQRES 32 I 457 ARG ILE GLY SER GLY SER ALA GLY TRP SER HIS PRO GLN SEQRES 33 I 457 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SEQRES 34 I 457 GLY SER TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLY SEQRES 35 I 457 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 36 I 457 HIS GLU SEQRES 1 J 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 J 225 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 J 225 GLY SER ILE SER THR TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 J 225 PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY LEU MET TYR SEQRES 5 J 225 ASN SER GLY SER PRO ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 J 225 ARG VAL THR MET SER GLY ASP THR SER LYS ASN GLN PHE SEQRES 7 J 225 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 J 225 VAL TYR TYR CYS ALA ARG LEU ARG TYR ASP PHE TRP SER SEQRES 9 J 225 GLY SER LYS GLY ARG TYR TYR MET ASP VAL TRP GLY LYS SEQRES 10 J 225 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 J 225 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 J 225 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 J 225 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 J 225 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 J 225 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 J 225 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 J 225 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 J 225 LYS VAL GLU PRO SEQRES 1 K 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 K 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 K 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 K 214 PRO GLY GLN ALA PRO LYS LEU LEU ILE HIS ASP ALA SER SEQRES 5 K 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 214 GLY SER GLY THR ASP PHE THR PHE THR VAL SER SER LEU SEQRES 7 K 214 GLN ALA GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 K 214 TYR ASN LEU PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 K 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 K 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 K 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 K 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 K 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 K 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 K 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 K 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 K 214 PHE ASN ARG GLY GLU CYS SEQRES 1 L 123 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 L 123 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 L 123 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 4 L 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 L 123 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 6 L 123 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 7 L 123 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 L 123 ASP THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR SEQRES 9 L 123 PHE TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 L 123 GLN VAL THR VAL SER SER SEQRES 1 M 457 MET ALA ASN ILE ILE ASN LEU TRP ASN GLY ILE VAL PRO SEQRES 2 M 457 THR VAL GLN ASP VAL ASN VAL ALA SER ILE THR ALA PHE SEQRES 3 M 457 LYS SER MET ILE ASP GLU THR TRP ASP LYS LYS ILE GLU SEQRES 4 M 457 ALA ASN THR CYS ILE SER ARG LYS HIS ARG ASN ILE ILE SEQRES 5 M 457 HIS GLU VAL ILE ARG ASP PHE MET LYS ALA TYR PRO LYS SEQRES 6 M 457 MET ASP GLU ASN LYS LYS SER PRO LEU GLY ALA PRO MET SEQRES 7 M 457 GLN TRP LEU THR GLN TYR TYR ILE LEU LYS ASN GLU TYR SEQRES 8 M 457 HIS LYS THR MET LEU ALA TYR ASP ASN GLY SER LEU ASN SEQRES 9 M 457 THR LYS PHE LYS THR LEU ASN ILE TYR MET ILE THR ASN SEQRES 10 M 457 VAL GLY GLN TYR ILE LEU TYR ILE VAL PHE CYS ILE ILE SEQRES 11 M 457 SER GLY LYS ASN HIS ASP GLY THR PRO TYR ILE TYR ASP SEQRES 12 M 457 SER GLU ILE THR SER ASN ASP LYS ASN PHE ILE ASN GLU SEQRES 13 M 457 ARG ILE LYS TYR ALA CYS LYS GLN ILE LEU HIS GLY GLN SEQRES 14 M 457 LEU THR ILE ALA LEU ARG ILE ARG ASN LYS PHE MET PHE SEQRES 15 M 457 ILE GLY SER PRO MET TYR LEU TRP PHE ASN VAL ASN GLY SEQRES 16 M 457 SER GLN VAL TYR HIS ASP ILE TYR ASP ARG ASN ALA GLY SEQRES 17 M 457 PHE HIS ASN LYS GLU ILE GLY ARG LEU LEU TYR ALA PHE SEQRES 18 M 457 MET TYR TYR LEU SER ILE SER GLY ARG PHE LEU ASN ASP SEQRES 19 M 457 PHE ALA LEU LEU LYS PHE THR TYR LEU GLY GLU SER TRP SEQRES 20 M 457 THR PHE SER LEU SER VAL PRO GLU TYR ILE LEU TYR GLY SEQRES 21 M 457 LEU GLY TYR SER VAL PHE ASP THR ILE GLU LYS PHE SER SEQRES 22 M 457 ASN ASP ALA ILE LEU VAL TYR ILE ARG THR ASN ASN ARG SEQRES 23 M 457 ASN GLY TYR ASP TYR VAL GLU PHE ASN LYS LYS GLY ILE SEQRES 24 M 457 ALA LYS VAL THR GLU ASP LYS PRO ASP ASN ASP LYS ARG SEQRES 25 M 457 ILE HIS ALA ILE ARG LEU ILE ASN ASP SER THR ASP VAL SEQRES 26 M 457 GLN HIS ILE HIS PHE GLY PHE ARG ASN MET VAL ILE ILE SEQRES 27 M 457 ASP ASN GLU CYS ALA ASN ILE GLN SER SER ALA GLU ASN SEQRES 28 M 457 ALA THR ASP THR GLY HIS HIS GLN ASP SER LYS ILE ASN SEQRES 29 M 457 ILE GLU VAL GLU ASP ASP VAL ILE ASP ASP ASP ASP TYR SEQRES 30 M 457 ASN PRO LYS PRO THR PRO ILE PRO GLU PRO HIS PRO ARG SEQRES 31 M 457 PRO PRO PHE PRO ARG HIS GLU GLY SER GLY LEU VAL PRO SEQRES 32 M 457 ARG ILE GLY SER GLY SER ALA GLY TRP SER HIS PRO GLN SEQRES 33 M 457 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SEQRES 34 M 457 GLY SER TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLY SEQRES 35 M 457 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 36 M 457 HIS GLU SEQRES 1 N 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 N 225 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 N 225 GLY SER ILE SER THR TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 N 225 PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY LEU MET TYR SEQRES 5 N 225 ASN SER GLY SER PRO ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 N 225 ARG VAL THR MET SER GLY ASP THR SER LYS ASN GLN PHE SEQRES 7 N 225 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 N 225 VAL TYR TYR CYS ALA ARG LEU ARG TYR ASP PHE TRP SER SEQRES 9 N 225 GLY SER LYS GLY ARG TYR TYR MET ASP VAL TRP GLY LYS SEQRES 10 N 225 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 N 225 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 N 225 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 N 225 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 N 225 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 N 225 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 N 225 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 N 225 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 N 225 LYS VAL GLU PRO SEQRES 1 O 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 O 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 O 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 O 214 PRO GLY GLN ALA PRO LYS LEU LEU ILE HIS ASP ALA SER SEQRES 5 O 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 O 214 GLY SER GLY THR ASP PHE THR PHE THR VAL SER SER LEU SEQRES 7 O 214 GLN ALA GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 O 214 TYR ASN LEU PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 O 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 O 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 O 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 O 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 O 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 O 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 O 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 O 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 O 214 PHE ASN ARG GLY GLU CYS SEQRES 1 P 123 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 P 123 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 P 123 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 4 P 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 P 123 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 6 P 123 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 7 P 123 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 P 123 ASP THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR SEQRES 9 P 123 PHE TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 P 123 GLN VAL THR VAL SER SER FORMUL 17 HOH *433(H2 O) HELIX 1 AA1 ASN A 19 TRP A 34 1 16 HELIX 2 AA2 SER A 45 TYR A 63 1 19 HELIX 3 AA3 PRO A 77 LEU A 81 5 5 HELIX 4 AA4 THR A 82 LYS A 88 1 7 HELIX 5 AA5 ASN A 89 LYS A 108 1 20 HELIX 6 AA6 ASN A 117 GLY A 132 1 16 HELIX 7 AA7 TYR A 142 ILE A 146 5 5 HELIX 8 AA8 ASP A 150 ARG A 177 1 28 HELIX 9 AA9 PRO A 186 PHE A 191 5 6 HELIX 10 AB1 ASN A 194 ASP A 204 1 11 HELIX 11 AB2 ASN A 206 ASN A 211 5 6 HELIX 12 AB3 GLY A 215 SER A 228 1 14 HELIX 13 AB4 LEU A 232 ALA A 236 5 5 HELIX 14 AB5 PRO A 254 GLY A 262 1 9 HELIX 15 AB6 HIS A 327 GLY A 331 5 5 HELIX 16 AB7 PHE A 332 ILE A 337 1 6 HELIX 17 AB8 GLU A 341 ILE A 345 5 5 HELIX 18 AB9 GLY A 356 ASP A 360 5 5 HELIX 19 AC1 PRO B 80 LYS B 83 5 4 HELIX 20 AC2 THR B 105 THR B 109 5 5 HELIX 21 AC3 SER B 187 ALA B 189 5 3 HELIX 22 AC4 SER B 218 LEU B 220 5 3 HELIX 23 AC5 LYS B 232 ASN B 235 5 4 HELIX 24 AC6 GLN C 98 ILE C 102 5 5 HELIX 25 AC7 SER C 140 LYS C 145 1 6 HELIX 26 AC8 LYS C 202 LYS C 207 1 6 HELIX 27 AC9 THR D 28 TYR D 32 5 5 HELIX 28 AD1 LYS D 83 THR D 87 5 5 HELIX 29 AD2 ASN E 19 TRP E 34 1 16 HELIX 30 AD3 SER E 45 TYR E 63 1 19 HELIX 31 AD4 PRO E 77 LEU E 81 5 5 HELIX 32 AD5 THR E 82 LEU E 87 1 6 HELIX 33 AD6 ASN E 89 LYS E 108 1 20 HELIX 34 AD7 ASN E 117 SER E 131 1 15 HELIX 35 AD8 TYR E 142 ILE E 146 5 5 HELIX 36 AD9 ASP E 150 ARG E 177 1 28 HELIX 37 AE1 PRO E 186 PHE E 191 5 6 HELIX 38 AE2 ASN E 194 ASP E 204 1 11 HELIX 39 AE3 ARG E 205 ASN E 211 5 7 HELIX 40 AE4 GLY E 215 SER E 228 1 14 HELIX 41 AE5 LEU E 232 ALA E 236 5 5 HELIX 42 AE6 PRO E 254 GLY E 262 1 9 HELIX 43 AE7 HIS E 327 GLY E 331 5 5 HELIX 44 AE8 PHE E 332 ILE E 337 1 6 HELIX 45 AE9 GLU E 341 ILE E 345 5 5 HELIX 46 AF1 GLY E 356 ASP E 360 5 5 HELIX 47 AF2 THR F 105 THR F 109 5 5 HELIX 48 AF3 SER F 187 ALA F 189 5 3 HELIX 49 AF4 SER F 218 LEU F 220 5 3 HELIX 50 AF5 LYS F 232 ASN F 235 5 4 HELIX 51 AF6 GLN G 98 ILE G 102 5 5 HELIX 52 AF7 SER G 140 LYS G 145 1 6 HELIX 53 AF8 LYS G 202 LYS G 207 1 6 HELIX 54 AF9 THR H 28 TYR H 32 5 5 HELIX 55 AG1 ASP H 61 GLN H 64 5 4 HELIX 56 AG2 LYS H 83 THR H 87 5 5 HELIX 57 AG3 ASN I 19 TRP I 34 1 16 HELIX 58 AG4 SER I 45 TYR I 63 1 19 HELIX 59 AG5 PRO I 77 LEU I 81 5 5 HELIX 60 AG6 THR I 82 LEU I 87 1 6 HELIX 61 AG7 ASN I 89 LYS I 108 1 20 HELIX 62 AG8 ASN I 117 ILE I 130 1 14 HELIX 63 AG9 TYR I 142 ILE I 146 5 5 HELIX 64 AH1 ASP I 150 ARG I 177 1 28 HELIX 65 AH2 PRO I 186 PHE I 191 5 6 HELIX 66 AH3 ASN I 194 ASP I 204 1 11 HELIX 67 AH4 ASN I 206 ASN I 211 5 6 HELIX 68 AH5 GLY I 215 SER I 228 1 14 HELIX 69 AH6 LEU I 232 ALA I 236 5 5 HELIX 70 AH7 PRO I 254 GLY I 262 1 9 HELIX 71 AH8 HIS I 327 GLY I 331 5 5 HELIX 72 AH9 PHE I 332 ILE I 337 1 6 HELIX 73 AI1 GLU I 341 ILE I 345 5 5 HELIX 74 AI2 GLY I 356 ASP I 360 5 5 HELIX 75 AI3 PRO J 80 LYS J 83 5 4 HELIX 76 AI4 THR J 105 THR J 109 5 5 HELIX 77 AI5 SER J 187 ALA J 189 5 3 HELIX 78 AI6 SER J 218 LEU J 220 5 3 HELIX 79 AI7 LYS J 232 ASN J 235 5 4 HELIX 80 AI8 GLN K 98 ILE K 102 5 5 HELIX 81 AI9 SER K 140 LYS K 145 1 6 HELIX 82 AJ1 LYS K 202 LYS K 207 1 6 HELIX 83 AJ2 THR L 28 TYR L 32 5 5 HELIX 84 AJ3 ASP L 61 GLN L 64 5 4 HELIX 85 AJ4 LYS L 83 THR L 87 5 5 HELIX 86 AJ5 ASN M 19 TRP M 34 1 16 HELIX 87 AJ6 SER M 45 TYR M 63 1 19 HELIX 88 AJ7 PRO M 77 LEU M 81 5 5 HELIX 89 AJ8 THR M 82 LYS M 88 1 7 HELIX 90 AJ9 ASN M 89 LYS M 108 1 20 HELIX 91 AK1 THR M 109 LEU M 110 5 2 HELIX 92 AK2 ASN M 111 ILE M 115 5 5 HELIX 93 AK3 ASN M 117 GLY M 132 1 16 HELIX 94 AK4 TYR M 142 ILE M 146 5 5 HELIX 95 AK5 ASP M 150 ARG M 177 1 28 HELIX 96 AK6 PRO M 186 PHE M 191 5 6 HELIX 97 AK7 ASN M 194 ASP M 204 1 11 HELIX 98 AK8 ARG M 205 ASN M 211 5 7 HELIX 99 AK9 GLY M 215 SER M 228 1 14 HELIX 100 AL1 LEU M 232 ALA M 236 5 5 HELIX 101 AL2 PRO M 254 GLY M 262 1 9 HELIX 102 AL3 ILE M 328 GLY M 331 5 4 HELIX 103 AL4 PHE M 332 ILE M 337 1 6 HELIX 104 AL5 GLU M 341 ILE M 345 5 5 HELIX 105 AL6 GLY M 356 ASP M 360 5 5 HELIX 106 AL7 PRO N 80 LYS N 83 5 4 HELIX 107 AL8 THR N 105 THR N 109 5 5 HELIX 108 AL9 SER N 187 ALA N 189 5 3 HELIX 109 AM1 SER N 218 LEU N 220 5 3 HELIX 110 AM2 LYS N 232 ASN N 235 5 4 HELIX 111 AM3 GLN O 98 ILE O 102 5 5 HELIX 112 AM4 SER O 140 LYS O 145 1 6 HELIX 113 AM5 LYS O 202 LYS O 207 1 6 HELIX 114 AM6 THR P 28 TYR P 32 5 5 HELIX 115 AM7 ASP P 61 GLN P 64 5 4 HELIX 116 AM8 LYS P 83 THR P 87 5 5 SHEET 1 AA1 4 GLU A 245 PHE A 249 0 SHEET 2 AA1 4 LEU A 238 TYR A 242 -1 N PHE A 240 O TRP A 247 SHEET 3 AA1 4 THR A 268 LYS A 271 -1 O THR A 268 N THR A 241 SHEET 4 AA1 4 GLY A 298 ALA A 300 -1 O ALA A 300 N ILE A 269 SHEET 1 AA2 4 ARG A 312 ILE A 319 0 SHEET 2 AA2 4 ALA A 276 THR A 283 -1 N ILE A 281 O ILE A 313 SHEET 3 AA2 4 TYR A 289 PHE A 294 -1 O VAL A 292 N VAL A 279 SHEET 4 AA2 4 SER A 361 LYS A 362 1 O SER A 361 N TYR A 291 SHEET 1 AA3 4 GLN B 22 SER B 26 0 SHEET 2 AA3 4 LEU B 37 SER B 44 -1 O THR B 40 N SER B 26 SHEET 3 AA3 4 GLN B 96 LEU B 101 -1 O LEU B 101 N LEU B 37 SHEET 4 AA3 4 VAL B 86 ASP B 91 -1 N ASP B 91 O GLN B 96 SHEET 1 AA4 6 LEU B 30 VAL B 31 0 SHEET 2 AA4 6 THR B 138 VAL B 142 1 O THR B 141 N VAL B 31 SHEET 3 AA4 6 ALA B 110 ASP B 120 -1 N TYR B 112 O THR B 138 SHEET 4 AA4 6 TYR B 52 GLN B 58 -1 N ILE B 56 O TYR B 113 SHEET 5 AA4 6 GLU B 65 MET B 70 -1 O GLU B 65 N ARG B 57 SHEET 6 AA4 6 PRO B 76 TYR B 78 -1 O ASN B 77 N LEU B 69 SHEET 1 AA5 4 LEU B 30 VAL B 31 0 SHEET 2 AA5 4 THR B 138 VAL B 142 1 O THR B 141 N VAL B 31 SHEET 3 AA5 4 ALA B 110 ASP B 120 -1 N TYR B 112 O THR B 138 SHEET 4 AA5 4 ARG B 128 TRP B 134 -1 O VAL B 133 N ARG B 116 SHEET 1 AA6 4 SER B 151 LEU B 155 0 SHEET 2 AA6 4 THR B 166 TYR B 176 -1 O GLY B 170 N LEU B 155 SHEET 3 AA6 4 TYR B 207 PRO B 216 -1 O TYR B 207 N TYR B 176 SHEET 4 AA6 4 VAL B 194 THR B 196 -1 N HIS B 195 O VAL B 212 SHEET 1 AA7 4 SER B 151 LEU B 155 0 SHEET 2 AA7 4 THR B 166 TYR B 176 -1 O GLY B 170 N LEU B 155 SHEET 3 AA7 4 TYR B 207 PRO B 216 -1 O TYR B 207 N TYR B 176 SHEET 4 AA7 4 VAL B 200 LEU B 201 -1 N VAL B 200 O SER B 208 SHEET 1 AA8 3 THR B 182 TRP B 185 0 SHEET 2 AA8 3 TYR B 225 HIS B 231 -1 O ASN B 228 N SER B 184 SHEET 3 AA8 3 THR B 236 VAL B 242 -1 O THR B 236 N HIS B 231 SHEET 1 AA9 4 MET C 23 SER C 26 0 SHEET 2 AA9 4 VAL C 38 ALA C 44 -1 O GLN C 43 N THR C 24 SHEET 3 AA9 4 ASP C 89 VAL C 94 -1 O PHE C 92 N ILE C 40 SHEET 4 AA9 4 PHE C 81 GLY C 85 -1 N SER C 82 O THR C 93 SHEET 1 AB1 6 SER C 29 SER C 33 0 SHEET 2 AB1 6 THR C 121 LYS C 126 1 O ASP C 124 N LEU C 30 SHEET 3 AB1 6 ALA C 103 GLN C 109 -1 N TYR C 105 O THR C 121 SHEET 4 AB1 6 LEU C 52 GLN C 57 -1 N TYR C 55 O TYR C 106 SHEET 5 AB1 6 LYS C 64 HIS C 68 -1 O LYS C 64 N GLN C 56 SHEET 6 AB1 6 ASN C 72 LEU C 73 -1 O ASN C 72 N HIS C 68 SHEET 1 AB2 4 SER C 29 SER C 33 0 SHEET 2 AB2 4 THR C 121 LYS C 126 1 O ASP C 124 N LEU C 30 SHEET 3 AB2 4 ALA C 103 GLN C 109 -1 N TYR C 105 O THR C 121 SHEET 4 AB2 4 THR C 116 PHE C 117 -1 O THR C 116 N GLN C 109 SHEET 1 AB3 4 SER C 133 PHE C 137 0 SHEET 2 AB3 4 THR C 148 PHE C 158 -1 O LEU C 154 N PHE C 135 SHEET 3 AB3 4 TYR C 192 SER C 201 -1 O LEU C 200 N ALA C 149 SHEET 4 AB3 4 SER C 178 VAL C 182 -1 N GLN C 179 O THR C 197 SHEET 1 AB4 3 LYS C 164 VAL C 169 0 SHEET 2 AB4 3 VAL C 210 THR C 216 -1 O GLU C 214 N GLN C 166 SHEET 3 AB4 3 VAL C 224 ASN C 229 -1 O VAL C 224 N VAL C 215 SHEET 1 AB5 4 GLN D 3 SER D 7 0 SHEET 2 AB5 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AB5 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AB5 4 PHE D 67 ASP D 72 -1 N ASP D 72 O THR D 77 SHEET 1 AB6 6 GLY D 10 VAL D 12 0 SHEET 2 AB6 6 THR D 107 VAL D 111 1 O THR D 110 N GLY D 10 SHEET 3 AB6 6 ALA D 88 ASP D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AB6 6 ALA D 33 GLN D 39 -1 N PHE D 37 O TYR D 91 SHEET 5 AB6 6 GLU D 46 ALA D 51 -1 O ALA D 51 N MET D 34 SHEET 6 AB6 6 ALA D 57 TYR D 59 -1 O PHE D 58 N VAL D 50 SHEET 1 AB7 4 GLY D 10 VAL D 12 0 SHEET 2 AB7 4 THR D 107 VAL D 111 1 O THR D 110 N GLY D 10 SHEET 3 AB7 4 ALA D 88 ASP D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AB7 4 TYR D 100D TRP D 103 -1 O TYR D 102 N ILE D 94 SHEET 1 AB8 4 GLU E 245 PHE E 249 0 SHEET 2 AB8 4 LEU E 238 TYR E 242 -1 N PHE E 240 O TRP E 247 SHEET 3 AB8 4 THR E 268 LYS E 271 -1 O THR E 268 N THR E 241 SHEET 4 AB8 4 GLY E 298 ILE E 299 -1 O GLY E 298 N LYS E 271 SHEET 1 AB9 4 ARG E 312 ILE E 319 0 SHEET 2 AB9 4 ALA E 276 THR E 283 -1 N ALA E 276 O ILE E 319 SHEET 3 AB9 4 TYR E 289 PHE E 294 -1 O VAL E 292 N VAL E 279 SHEET 4 AB9 4 SER E 361 LYS E 362 1 O SER E 361 N TYR E 291 SHEET 1 AC1 4 GLN F 22 SER F 26 0 SHEET 2 AC1 4 LEU F 37 SER F 44 -1 O SER F 42 N GLN F 24 SHEET 3 AC1 4 GLN F 96 LEU F 101 -1 O LEU F 101 N LEU F 37 SHEET 4 AC1 4 VAL F 86 ASP F 91 -1 N ASP F 91 O GLN F 96 SHEET 1 AC2 6 LEU F 30 VAL F 31 0 SHEET 2 AC2 6 THR F 138 VAL F 142 1 O THR F 141 N VAL F 31 SHEET 3 AC2 6 ALA F 110 ASP F 120 -1 N TYR F 112 O THR F 138 SHEET 4 AC2 6 TYR F 52 GLN F 58 -1 N ILE F 56 O TYR F 113 SHEET 5 AC2 6 GLU F 65 MET F 70 -1 O ILE F 67 N TRP F 55 SHEET 6 AC2 6 PRO F 76 TYR F 78 -1 O ASN F 77 N LEU F 69 SHEET 1 AC3 4 LEU F 30 VAL F 31 0 SHEET 2 AC3 4 THR F 138 VAL F 142 1 O THR F 141 N VAL F 31 SHEET 3 AC3 4 ALA F 110 ASP F 120 -1 N TYR F 112 O THR F 138 SHEET 4 AC3 4 ARG F 128 TRP F 134 -1 O TYR F 130 N ARG F 118 SHEET 1 AC4 4 SER F 151 LEU F 155 0 SHEET 2 AC4 4 THR F 166 TYR F 176 -1 O GLY F 170 N LEU F 155 SHEET 3 AC4 4 TYR F 207 PRO F 216 -1 O TYR F 207 N TYR F 176 SHEET 4 AC4 4 VAL F 194 THR F 196 -1 N HIS F 195 O VAL F 212 SHEET 1 AC5 4 SER F 151 LEU F 155 0 SHEET 2 AC5 4 THR F 166 TYR F 176 -1 O GLY F 170 N LEU F 155 SHEET 3 AC5 4 TYR F 207 PRO F 216 -1 O TYR F 207 N TYR F 176 SHEET 4 AC5 4 VAL F 200 LEU F 201 -1 N VAL F 200 O SER F 208 SHEET 1 AC6 3 THR F 182 TRP F 185 0 SHEET 2 AC6 3 TYR F 225 HIS F 231 -1 O ASN F 228 N SER F 184 SHEET 3 AC6 3 THR F 236 VAL F 242 -1 O THR F 236 N HIS F 231 SHEET 1 AC7 4 MET G 23 SER G 26 0 SHEET 2 AC7 4 VAL G 38 ALA G 44 -1 O GLN G 43 N THR G 24 SHEET 3 AC7 4 ASP G 89 VAL G 94 -1 O PHE G 92 N ILE G 40 SHEET 4 AC7 4 PHE G 81 GLY G 85 -1 N SER G 82 O THR G 93 SHEET 1 AC8 6 SER G 29 SER G 33 0 SHEET 2 AC8 6 THR G 121 LYS G 126 1 O LYS G 126 N ALA G 32 SHEET 3 AC8 6 ALA G 103 GLN G 109 -1 N TYR G 105 O THR G 121 SHEET 4 AC8 6 LEU G 52 GLN G 57 -1 N TYR G 55 O TYR G 106 SHEET 5 AC8 6 LYS G 64 HIS G 68 -1 O LYS G 64 N GLN G 56 SHEET 6 AC8 6 ASN G 72 LEU G 73 -1 O ASN G 72 N HIS G 68 SHEET 1 AC9 4 SER G 29 SER G 33 0 SHEET 2 AC9 4 THR G 121 LYS G 126 1 O LYS G 126 N ALA G 32 SHEET 3 AC9 4 ALA G 103 GLN G 109 -1 N TYR G 105 O THR G 121 SHEET 4 AC9 4 THR G 116 PHE G 117 -1 O THR G 116 N GLN G 109 SHEET 1 AD1 4 SER G 133 PHE G 137 0 SHEET 2 AD1 4 THR G 148 PHE G 158 -1 O LEU G 154 N PHE G 135 SHEET 3 AD1 4 TYR G 192 SER G 201 -1 O LEU G 200 N ALA G 149 SHEET 4 AD1 4 SER G 178 VAL G 182 -1 N GLN G 179 O THR G 197 SHEET 1 AD2 3 LYS G 164 VAL G 169 0 SHEET 2 AD2 3 VAL G 210 THR G 216 -1 O ALA G 212 N LYS G 168 SHEET 3 AD2 3 VAL G 224 ASN G 229 -1 O VAL G 224 N VAL G 215 SHEET 1 AD3 4 GLN H 3 SER H 7 0 SHEET 2 AD3 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AD3 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AD3 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AD4 6 GLY H 10 VAL H 12 0 SHEET 2 AD4 6 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AD4 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AD4 6 ALA H 33 GLN H 39 -1 N PHE H 37 O TYR H 91 SHEET 5 AD4 6 ARG H 45 ALA H 51 -1 O ALA H 51 N MET H 34 SHEET 6 AD4 6 ALA H 57 TYR H 59 -1 O PHE H 58 N VAL H 50 SHEET 1 AD5 4 GLY H 10 VAL H 12 0 SHEET 2 AD5 4 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AD5 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AD5 4 TYR H 100D TRP H 103 -1 O TYR H 102 N ILE H 94 SHEET 1 AD6 4 GLU I 245 PHE I 249 0 SHEET 2 AD6 4 LEU I 238 TYR I 242 -1 N PHE I 240 O TRP I 247 SHEET 3 AD6 4 THR I 268 LYS I 271 -1 O THR I 268 N THR I 241 SHEET 4 AD6 4 GLY I 298 ILE I 299 -1 O GLY I 298 N LYS I 271 SHEET 1 AD7 4 ARG I 312 ILE I 319 0 SHEET 2 AD7 4 ALA I 276 THR I 283 -1 N LEU I 278 O ARG I 317 SHEET 3 AD7 4 TYR I 289 PHE I 294 -1 O VAL I 292 N VAL I 279 SHEET 4 AD7 4 SER I 361 LYS I 362 1 O SER I 361 N TYR I 291 SHEET 1 AD8 4 GLN J 22 SER J 26 0 SHEET 2 AD8 4 LEU J 37 SER J 44 -1 O THR J 40 N SER J 26 SHEET 3 AD8 4 GLN J 96 LEU J 101 -1 O LEU J 101 N LEU J 37 SHEET 4 AD8 4 VAL J 86 ASP J 91 -1 N ASP J 91 O GLN J 96 SHEET 1 AD9 6 LEU J 30 VAL J 31 0 SHEET 2 AD9 6 THR J 138 VAL J 142 1 O THR J 141 N VAL J 31 SHEET 3 AD9 6 ALA J 110 ASP J 120 -1 N TYR J 112 O THR J 138 SHEET 4 AD9 6 TYR J 52 GLN J 58 -1 N ILE J 56 O TYR J 113 SHEET 5 AD9 6 GLU J 65 MET J 70 -1 O ILE J 67 N TRP J 55 SHEET 6 AD9 6 PRO J 76 TYR J 78 -1 O ASN J 77 N LEU J 69 SHEET 1 AE1 4 LEU J 30 VAL J 31 0 SHEET 2 AE1 4 THR J 138 VAL J 142 1 O THR J 141 N VAL J 31 SHEET 3 AE1 4 ALA J 110 ASP J 120 -1 N TYR J 112 O THR J 138 SHEET 4 AE1 4 ARG J 128 TRP J 134 -1 O TYR J 130 N ARG J 118 SHEET 1 AE2 4 SER J 151 LEU J 155 0 SHEET 2 AE2 4 THR J 166 TYR J 176 -1 O GLY J 170 N LEU J 155 SHEET 3 AE2 4 TYR J 207 PRO J 216 -1 O TYR J 207 N TYR J 176 SHEET 4 AE2 4 VAL J 194 THR J 196 -1 N HIS J 195 O VAL J 212 SHEET 1 AE3 4 SER J 151 LEU J 155 0 SHEET 2 AE3 4 THR J 166 TYR J 176 -1 O GLY J 170 N LEU J 155 SHEET 3 AE3 4 TYR J 207 PRO J 216 -1 O TYR J 207 N TYR J 176 SHEET 4 AE3 4 VAL J 200 LEU J 201 -1 N VAL J 200 O SER J 208 SHEET 1 AE4 3 THR J 182 TRP J 185 0 SHEET 2 AE4 3 TYR J 225 HIS J 231 -1 O ASN J 228 N SER J 184 SHEET 3 AE4 3 THR J 236 VAL J 242 -1 O VAL J 238 N VAL J 229 SHEET 1 AE5 4 MET K 23 SER K 26 0 SHEET 2 AE5 4 VAL K 38 ALA K 44 -1 O GLN K 43 N THR K 24 SHEET 3 AE5 4 ASP K 89 VAL K 94 -1 O PHE K 92 N ILE K 40 SHEET 4 AE5 4 PHE K 81 GLY K 85 -1 N SER K 82 O THR K 93 SHEET 1 AE6 6 SER K 29 SER K 33 0 SHEET 2 AE6 6 THR K 121 LYS K 126 1 O ASP K 124 N LEU K 30 SHEET 3 AE6 6 ALA K 103 GLN K 109 -1 N TYR K 105 O THR K 121 SHEET 4 AE6 6 LEU K 52 GLN K 57 -1 N TYR K 55 O TYR K 106 SHEET 5 AE6 6 LYS K 64 HIS K 68 -1 O LYS K 64 N GLN K 56 SHEET 6 AE6 6 ASN K 72 LEU K 73 -1 O ASN K 72 N HIS K 68 SHEET 1 AE7 4 SER K 29 SER K 33 0 SHEET 2 AE7 4 THR K 121 LYS K 126 1 O ASP K 124 N LEU K 30 SHEET 3 AE7 4 ALA K 103 GLN K 109 -1 N TYR K 105 O THR K 121 SHEET 4 AE7 4 THR K 116 PHE K 117 -1 O THR K 116 N GLN K 109 SHEET 1 AE8 4 SER K 133 PHE K 137 0 SHEET 2 AE8 4 THR K 148 PHE K 158 -1 O LEU K 154 N PHE K 135 SHEET 3 AE8 4 TYR K 192 SER K 201 -1 O LEU K 200 N ALA K 149 SHEET 4 AE8 4 SER K 178 VAL K 182 -1 N GLN K 179 O THR K 197 SHEET 1 AE9 3 LYS K 164 VAL K 169 0 SHEET 2 AE9 3 VAL K 210 THR K 216 -1 O GLU K 214 N GLN K 166 SHEET 3 AE9 3 VAL K 224 ASN K 229 -1 O VAL K 224 N VAL K 215 SHEET 1 AF1 4 GLN L 3 SER L 7 0 SHEET 2 AF1 4 LEU L 18 SER L 25 -1 O SER L 21 N SER L 7 SHEET 3 AF1 4 THR L 77 MET L 82 -1 O MET L 82 N LEU L 18 SHEET 4 AF1 4 PHE L 67 ASP L 72 -1 N ASP L 72 O THR L 77 SHEET 1 AF2 6 GLY L 10 VAL L 12 0 SHEET 2 AF2 6 THR L 107 VAL L 111 1 O THR L 110 N GLY L 10 SHEET 3 AF2 6 ALA L 88 ASP L 95 -1 N TYR L 90 O THR L 107 SHEET 4 AF2 6 ALA L 33 GLN L 39 -1 N PHE L 37 O TYR L 91 SHEET 5 AF2 6 GLU L 46 ALA L 51 -1 O ALA L 49 N TRP L 36 SHEET 6 AF2 6 ALA L 57 TYR L 59 -1 O PHE L 58 N VAL L 50 SHEET 1 AF3 4 GLY L 10 VAL L 12 0 SHEET 2 AF3 4 THR L 107 VAL L 111 1 O THR L 110 N GLY L 10 SHEET 3 AF3 4 ALA L 88 ASP L 95 -1 N TYR L 90 O THR L 107 SHEET 4 AF3 4 TYR L 100D TRP L 103 -1 O TYR L 102 N ILE L 94 SHEET 1 AF4 4 GLU M 245 PHE M 249 0 SHEET 2 AF4 4 LEU M 238 TYR M 242 -1 N PHE M 240 O TRP M 247 SHEET 3 AF4 4 THR M 268 LYS M 271 -1 O THR M 268 N THR M 241 SHEET 4 AF4 4 GLY M 298 ILE M 299 -1 O GLY M 298 N LYS M 271 SHEET 1 AF5 4 ARG M 312 ILE M 319 0 SHEET 2 AF5 4 ALA M 276 THR M 283 -1 N LEU M 278 O ARG M 317 SHEET 3 AF5 4 TYR M 289 PHE M 294 -1 O VAL M 292 N VAL M 279 SHEET 4 AF5 4 SER M 361 LYS M 362 1 O SER M 361 N TYR M 291 SHEET 1 AF6 4 GLN N 22 SER N 26 0 SHEET 2 AF6 4 LEU N 37 SER N 44 -1 O SER N 42 N GLN N 24 SHEET 3 AF6 4 GLN N 96 LEU N 101 -1 O LEU N 101 N LEU N 37 SHEET 4 AF6 4 VAL N 86 ASP N 91 -1 N ASP N 91 O GLN N 96 SHEET 1 AF7 6 LEU N 30 VAL N 31 0 SHEET 2 AF7 6 THR N 138 VAL N 142 1 O THR N 141 N VAL N 31 SHEET 3 AF7 6 ALA N 110 ASP N 120 -1 N TYR N 112 O THR N 138 SHEET 4 AF7 6 TYR N 52 GLN N 58 -1 N ILE N 56 O TYR N 113 SHEET 5 AF7 6 GLU N 65 MET N 70 -1 O ILE N 67 N TRP N 55 SHEET 6 AF7 6 PRO N 76 TYR N 78 -1 O ASN N 77 N LEU N 69 SHEET 1 AF8 4 LEU N 30 VAL N 31 0 SHEET 2 AF8 4 THR N 138 VAL N 142 1 O THR N 141 N VAL N 31 SHEET 3 AF8 4 ALA N 110 ASP N 120 -1 N TYR N 112 O THR N 138 SHEET 4 AF8 4 ARG N 128 TRP N 134 -1 O VAL N 133 N ARG N 116 SHEET 1 AF9 4 SER N 151 LEU N 155 0 SHEET 2 AF9 4 THR N 166 TYR N 176 -1 O LEU N 172 N PHE N 153 SHEET 3 AF9 4 TYR N 207 PRO N 216 -1 O VAL N 215 N ALA N 167 SHEET 4 AF9 4 VAL N 194 THR N 196 -1 N HIS N 195 O VAL N 212 SHEET 1 AG1 4 SER N 151 LEU N 155 0 SHEET 2 AG1 4 THR N 166 TYR N 176 -1 O LEU N 172 N PHE N 153 SHEET 3 AG1 4 TYR N 207 PRO N 216 -1 O VAL N 215 N ALA N 167 SHEET 4 AG1 4 VAL N 200 LEU N 201 -1 N VAL N 200 O SER N 208 SHEET 1 AG2 3 THR N 182 TRP N 185 0 SHEET 2 AG2 3 TYR N 225 HIS N 231 -1 O ASN N 228 N SER N 184 SHEET 3 AG2 3 THR N 236 VAL N 242 -1 O THR N 236 N HIS N 231 SHEET 1 AG3 4 MET O 23 SER O 26 0 SHEET 2 AG3 4 VAL O 38 ALA O 44 -1 O GLN O 43 N THR O 24 SHEET 3 AG3 4 ASP O 89 VAL O 94 -1 O PHE O 92 N ILE O 40 SHEET 4 AG3 4 PHE O 81 GLY O 85 -1 N SER O 82 O THR O 93 SHEET 1 AG4 6 SER O 29 ALA O 32 0 SHEET 2 AG4 6 THR O 121 ILE O 125 1 O ASP O 124 N LEU O 30 SHEET 3 AG4 6 ALA O 103 GLN O 109 -1 N TYR O 105 O THR O 121 SHEET 4 AG4 6 LEU O 52 GLN O 57 -1 N TYR O 55 O TYR O 106 SHEET 5 AG4 6 LYS O 64 HIS O 68 -1 O LYS O 64 N GLN O 56 SHEET 6 AG4 6 ASN O 72 LEU O 73 -1 O ASN O 72 N HIS O 68 SHEET 1 AG5 4 SER O 29 ALA O 32 0 SHEET 2 AG5 4 THR O 121 ILE O 125 1 O ASP O 124 N LEU O 30 SHEET 3 AG5 4 ALA O 103 GLN O 109 -1 N TYR O 105 O THR O 121 SHEET 4 AG5 4 THR O 116 PHE O 117 -1 O THR O 116 N GLN O 109 SHEET 1 AG6 4 SER O 133 PHE O 137 0 SHEET 2 AG6 4 THR O 148 PHE O 158 -1 O LEU O 154 N PHE O 135 SHEET 3 AG6 4 TYR O 192 SER O 201 -1 O LEU O 200 N ALA O 149 SHEET 4 AG6 4 SER O 178 VAL O 182 -1 N SER O 181 O SER O 195 SHEET 1 AG7 3 LYS O 164 VAL O 169 0 SHEET 2 AG7 3 VAL O 210 THR O 216 -1 O GLU O 214 N GLN O 166 SHEET 3 AG7 3 VAL O 224 ASN O 229 -1 O VAL O 224 N VAL O 215 SHEET 1 AG8 4 GLN P 3 SER P 7 0 SHEET 2 AG8 4 LEU P 18 SER P 25 -1 O SER P 21 N SER P 7 SHEET 3 AG8 4 THR P 77 MET P 82 -1 O MET P 82 N LEU P 18 SHEET 4 AG8 4 PHE P 67 ASP P 72 -1 N ASP P 72 O THR P 77 SHEET 1 AG9 6 GLY P 10 VAL P 12 0 SHEET 2 AG9 6 THR P 107 VAL P 111 1 O THR P 110 N GLY P 10 SHEET 3 AG9 6 ALA P 88 ASP P 95 -1 N TYR P 90 O THR P 107 SHEET 4 AG9 6 ALA P 33 GLN P 39 -1 N PHE P 37 O TYR P 91 SHEET 5 AG9 6 ARG P 45 ALA P 51 -1 O ALA P 49 N TRP P 36 SHEET 6 AG9 6 ALA P 57 TYR P 59 -1 O PHE P 58 N VAL P 50 SHEET 1 AH1 4 GLY P 10 VAL P 12 0 SHEET 2 AH1 4 THR P 107 VAL P 111 1 O THR P 110 N GLY P 10 SHEET 3 AH1 4 ALA P 88 ASP P 95 -1 N TYR P 90 O THR P 107 SHEET 4 AH1 4 TYR P 100D TRP P 103 -1 O TYR P 102 N ILE P 94 SSBOND 1 CYS A 43 CYS A 342 1555 1555 2.03 SSBOND 2 CYS B 41 CYS B 114 1555 1555 2.04 SSBOND 3 CYS B 171 CYS B 227 1555 1555 2.03 SSBOND 4 CYS C 42 CYS C 107 1555 1555 2.03 SSBOND 5 CYS C 153 CYS C 213 1555 1555 2.04 SSBOND 6 CYS E 43 CYS E 342 1555 1555 2.04 SSBOND 7 CYS F 41 CYS F 114 1555 1555 2.04 SSBOND 8 CYS F 171 CYS F 227 1555 1555 2.03 SSBOND 9 CYS G 42 CYS G 107 1555 1555 2.04 SSBOND 10 CYS G 153 CYS G 213 1555 1555 2.03 SSBOND 11 CYS I 43 CYS I 342 1555 1555 2.03 SSBOND 12 CYS J 41 CYS J 114 1555 1555 2.04 SSBOND 13 CYS J 171 CYS J 227 1555 1555 2.03 SSBOND 14 CYS K 42 CYS K 107 1555 1555 2.04 SSBOND 15 CYS K 153 CYS K 213 1555 1555 2.03 SSBOND 16 CYS M 43 CYS M 342 1555 1555 2.04 SSBOND 17 CYS N 41 CYS N 114 1555 1555 2.03 SSBOND 18 CYS N 171 CYS N 227 1555 1555 2.03 SSBOND 19 CYS O 42 CYS O 107 1555 1555 2.04 SSBOND 20 CYS O 153 CYS O 213 1555 1555 2.03 CISPEP 1 PHE B 177 PRO B 178 0 -5.19 CISPEP 2 GLU B 179 PRO B 180 0 -2.22 CISPEP 3 SER C 26 PRO C 27 0 -3.18 CISPEP 4 LEU C 113 PRO C 114 0 2.15 CISPEP 5 TYR C 159 PRO C 160 0 1.84 CISPEP 6 PHE F 177 PRO F 178 0 -5.35 CISPEP 7 GLU F 179 PRO F 180 0 -1.44 CISPEP 8 SER G 26 PRO G 27 0 -3.00 CISPEP 9 LEU G 113 PRO G 114 0 2.15 CISPEP 10 TYR G 159 PRO G 160 0 1.79 CISPEP 11 PHE J 177 PRO J 178 0 -5.59 CISPEP 12 GLU J 179 PRO J 180 0 -1.82 CISPEP 13 SER K 26 PRO K 27 0 -2.58 CISPEP 14 LEU K 113 PRO K 114 0 2.10 CISPEP 15 TYR K 159 PRO K 160 0 1.25 CISPEP 16 PHE N 177 PRO N 178 0 -3.98 CISPEP 17 GLU N 179 PRO N 180 0 -3.42 CISPEP 18 SER O 26 PRO O 27 0 -2.66 CISPEP 19 LEU O 113 PRO O 114 0 2.43 CISPEP 20 TYR O 159 PRO O 160 0 0.47 CRYST1 119.405 119.405 632.812 90.00 90.00 120.00 P 32 2 1 24 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 0.008375 0.004835 0.000000 0.00000 SCALE2 0.000000 0.009670 0.000000 0.00000 SCALE3 0.000000 0.000000 0.001580 0.00000 MTRIX1 1 0.448781 -0.843905 0.293972 -43.19305 1 MTRIX2 1 -0.842950 -0.508982 -0.174277 -15.11464 1 MTRIX3 1 0.296700 -0.169591 -0.939791 167.59109 1 MTRIX1 2 0.465709 0.833811 -0.296436 20.15177 1 MTRIX2 2 -0.850400 0.514348 0.110751 -47.11521 1 MTRIX3 2 0.244816 0.200511 0.948610 -34.60501 1 MTRIX1 3 -0.548897 -0.789790 0.273758 -61.30441 1 MTRIX2 3 -0.795303 0.392631 -0.461881 2.05708 1 MTRIX3 3 0.257304 -0.471246 -0.843636 112.19326 1 MTRIX1 4 0.464713 -0.839107 0.282740 -41.30105 1 MTRIX2 4 -0.837840 -0.520007 -0.166184 -15.53878 1 MTRIX3 4 0.286473 -0.159662 -0.944691 167.34185 1 MTRIX1 5 0.464382 0.835459 -0.293869 19.58221 1 MTRIX2 5 -0.837791 0.521992 0.160097 -50.13131 1 MTRIX3 5 0.287152 0.171854 0.942343 -31.55176 1 MTRIX1 6 -0.475841 -0.824385 0.306538 -58.99609 1 MTRIX2 6 -0.860720 0.364769 -0.355113 -11.89518 1 MTRIX3 6 0.180934 -0.432820 -0.883136 110.52495 1 MTRIX1 7 0.462166 -0.839425 0.285951 -41.72967 1 MTRIX2 7 -0.837791 -0.519010 -0.169511 -15.26430 1 MTRIX3 7 0.290703 -0.161225 -0.943132 167.56955 1 MTRIX1 8 0.458762 0.835754 -0.301750 19.90321 1 MTRIX2 8 -0.836812 0.520568 0.169574 -50.89653 1 MTRIX3 8 0.298804 0.174714 0.938185 -30.34653 1 MTRIX1 9 -0.467315 -0.801045 0.374089 -64.95158 1 MTRIX2 9 -0.873116 0.351697 -0.337606 -13.63718 1 MTRIX3 9 0.138871 -0.484392 -0.863759 106.12004 1 MTRIX1 10 0.474070 -0.823312 0.312113 -43.88115 1 MTRIX2 10 -0.831685 -0.535091 -0.148250 -16.32780 1 MTRIX3 10 0.289065 -0.189299 -0.938407 167.83521 1 MTRIX1 11 0.455031 0.841000 -0.292686 18.48176 1 MTRIX2 11 -0.834763 0.517297 0.188613 -52.53452 1 MTRIX3 11 0.310029 0.158498 0.937422 -28.92700 1 MTRIX1 12 -0.396432 -0.814573 0.423452 -63.57396 1 MTRIX2 12 -0.909834 0.286967 -0.299754 -18.54110 1 MTRIX3 12 0.122654 -0.504103 -0.854889 103.71175 1