HEADER IMMUNE SYSTEM 24-DEC-24 9HV2 TITLE CRYSTAL STRUCTURE OF TRI-SPECIFIC FMDV MAB-34 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_TAXID: 9913; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 9 ORGANISM_TAXID: 9913; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS FOOT-AND-MOUTH DISEASE VIRUS, CATTLE ANTIBODY, CROSS-REACTIVE, LINEAR KEYWDS 2 EPITOPE, ANTIBODY STRUCTURE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.REN,H.M.E.DUYVESTEYN,D.I.STUART REVDAT 1 14-JAN-26 9HV2 0 JRNL AUTH M.BONNET-DI PLACIDO,D.I.STUART JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF BROADLY JRNL TITL 2 NEUTRALIZING ANTI FOOT-AND-MOUTH DISEASE VIRUS BOVINE JRNL TITL 3 ANTIBODIES FROM A SERIAL VACCINATION STUDY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.77 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) : 1.77 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.73 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 71306 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 3614 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 40.7300 - 5.2500 1.00 2820 123 0.1625 0.1853 REMARK 3 2 5.2500 - 4.1700 1.00 2760 127 0.1392 0.1501 REMARK 3 3 4.1700 - 3.6400 1.00 2747 145 0.1773 0.1920 REMARK 3 4 3.6400 - 3.3100 1.00 2730 158 0.1853 0.2185 REMARK 3 5 3.3100 - 3.0700 1.00 2704 150 0.2096 0.2501 REMARK 3 6 3.0700 - 2.8900 1.00 2724 139 0.2237 0.2164 REMARK 3 7 2.8900 - 2.7400 1.00 2725 139 0.2161 0.2542 REMARK 3 8 2.7400 - 2.6200 1.00 2714 163 0.2392 0.2600 REMARK 3 9 2.6200 - 2.5200 1.00 2724 153 0.2431 0.2757 REMARK 3 10 2.5200 - 2.4400 1.00 2692 156 0.2438 0.2662 REMARK 3 11 2.4400 - 2.3600 1.00 2741 117 0.2367 0.2816 REMARK 3 12 2.3600 - 2.2900 1.00 2740 122 0.2374 0.3002 REMARK 3 13 2.2900 - 2.2300 1.00 2699 162 0.2301 0.2521 REMARK 3 14 2.2300 - 2.1800 1.00 2682 160 0.2298 0.2716 REMARK 3 15 2.1800 - 2.1300 1.00 2687 160 0.2398 0.2892 REMARK 3 16 2.1300 - 2.0800 1.00 2654 161 0.2453 0.2674 REMARK 3 17 2.0800 - 2.0400 1.00 2730 154 0.2491 0.2912 REMARK 3 18 2.0400 - 2.0000 1.00 2708 128 0.2738 0.3040 REMARK 3 19 2.0000 - 1.9700 1.00 2751 117 0.2864 0.3400 REMARK 3 20 1.9700 - 1.9300 1.00 2662 142 0.2925 0.2877 REMARK 3 21 1.9300 - 1.9000 1.00 2706 160 0.2983 0.3078 REMARK 3 22 1.9000 - 1.8700 0.96 2586 145 0.3373 0.3495 REMARK 3 23 1.8700 - 1.8500 0.90 2432 130 0.3544 0.3804 REMARK 3 24 1.8500 - 1.8200 0.81 2195 129 0.3916 0.4073 REMARK 3 25 1.8200 - 1.8000 0.71 1919 113 0.4139 0.4397 REMARK 3 26 1.8000 - 1.7700 0.54 1460 61 0.4359 0.3813 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) : 0.291 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.93 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 6443 REMARK 3 ANGLE : 0.732 8787 REMARK 3 CHIRALITY : 0.049 1041 REMARK 3 PLANARITY : 0.005 1110 REMARK 3 DIHEDRAL : 13.103 2265 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5193 -34.0790 11.7465 REMARK 3 T TENSOR REMARK 3 T11: 0.3784 T22: 0.1780 REMARK 3 T33: 0.3484 T12: -0.0045 REMARK 3 T13: -0.0400 T23: 0.0126 REMARK 3 L TENSOR REMARK 3 L11: 3.6292 L22: 5.6285 REMARK 3 L33: 8.5711 L12: -0.2240 REMARK 3 L13: 0.6538 L23: -1.9458 REMARK 3 S TENSOR REMARK 3 S11: 0.0596 S12: -0.7271 S13: -0.6893 REMARK 3 S21: -0.0843 S22: 0.2432 S23: 0.1931 REMARK 3 S31: 0.2571 S32: -1.0565 S33: -0.1954 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3379 -30.9182 0.8388 REMARK 3 T TENSOR REMARK 3 T11: 0.3138 T22: 0.2584 REMARK 3 T33: 0.2856 T12: 0.0034 REMARK 3 T13: -0.0370 T23: -0.0323 REMARK 3 L TENSOR REMARK 3 L11: 3.4245 L22: 3.6678 REMARK 3 L33: 4.5720 L12: -1.1857 REMARK 3 L13: 0.6146 L23: -2.2144 REMARK 3 S TENSOR REMARK 3 S11: 0.0707 S12: 0.2532 S13: -0.1918 REMARK 3 S21: -0.4092 S22: -0.0852 S23: -0.1448 REMARK 3 S31: 0.3201 S32: 0.2126 S33: 0.0206 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 231 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.6374 -23.2519 32.9806 REMARK 3 T TENSOR REMARK 3 T11: 0.3243 T22: 0.2022 REMARK 3 T33: 0.4086 T12: 0.0079 REMARK 3 T13: -0.0188 T23: -0.0067 REMARK 3 L TENSOR REMARK 3 L11: 2.6399 L22: 3.8903 REMARK 3 L33: 3.4872 L12: -1.2638 REMARK 3 L13: -1.0263 L23: 1.1217 REMARK 3 S TENSOR REMARK 3 S11: -0.1658 S12: -0.0731 S13: -0.0510 REMARK 3 S21: 0.3344 S22: 0.0511 S23: 0.6619 REMARK 3 S31: -0.0795 S32: -0.3795 S33: 0.0990 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.9101 -11.0795 -1.3111 REMARK 3 T TENSOR REMARK 3 T11: 0.2405 T22: 0.2104 REMARK 3 T33: 0.2893 T12: -0.0411 REMARK 3 T13: -0.0728 T23: 0.0280 REMARK 3 L TENSOR REMARK 3 L11: 4.4775 L22: 4.3122 REMARK 3 L33: 6.9209 L12: -0.8283 REMARK 3 L13: -0.0734 L23: 2.5627 REMARK 3 S TENSOR REMARK 3 S11: -0.1297 S12: 0.0364 S13: 0.4271 REMARK 3 S21: -0.1618 S22: -0.0262 S23: 0.0028 REMARK 3 S31: -0.4754 S32: 0.0661 S33: 0.0942 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 103 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.4949 -10.1995 30.9217 REMARK 3 T TENSOR REMARK 3 T11: 0.2546 T22: 0.2060 REMARK 3 T33: 0.3152 T12: 0.0139 REMARK 3 T13: -0.0434 T23: -0.0771 REMARK 3 L TENSOR REMARK 3 L11: 1.9289 L22: 2.3146 REMARK 3 L33: 6.5382 L12: -0.7948 REMARK 3 L13: -0.1833 L23: -0.3544 REMARK 3 S TENSOR REMARK 3 S11: -0.0929 S12: 0.0210 S13: -0.1427 REMARK 3 S21: 0.5135 S22: 0.0298 S23: 0.3722 REMARK 3 S31: -0.5546 S32: -0.2704 S33: -0.0908 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.8523 -8.5149 35.1175 REMARK 3 T TENSOR REMARK 3 T11: 0.3393 T22: 0.1699 REMARK 3 T33: 0.2835 T12: 0.0292 REMARK 3 T13: -0.0206 T23: -0.0278 REMARK 3 L TENSOR REMARK 3 L11: 4.7466 L22: 6.9235 REMARK 3 L33: 5.3732 L12: -2.0348 REMARK 3 L13: 1.9033 L23: -1.6753 REMARK 3 S TENSOR REMARK 3 S11: -0.2108 S12: -0.0022 S13: 0.2185 REMARK 3 S21: 0.0158 S22: 0.0910 S23: 0.0298 REMARK 3 S31: -0.2848 S32: 0.0528 S33: 0.0836 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3355 -10.6030 24.1022 REMARK 3 T TENSOR REMARK 3 T11: 0.3264 T22: 0.1540 REMARK 3 T33: 0.3517 T12: -0.0231 REMARK 3 T13: -0.0904 T23: 0.0218 REMARK 3 L TENSOR REMARK 3 L11: 3.6497 L22: 4.8072 REMARK 3 L33: 6.0338 L12: 0.5585 REMARK 3 L13: 0.5782 L23: 1.1053 REMARK 3 S TENSOR REMARK 3 S11: 0.1491 S12: -0.2050 S13: -0.3556 REMARK 3 S21: 0.3148 S22: 0.1276 S23: -0.5454 REMARK 3 S31: 0.4047 S32: -0.0177 S33: -0.2183 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 64 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.1252 -10.4756 26.1698 REMARK 3 T TENSOR REMARK 3 T11: 0.3823 T22: 0.2348 REMARK 3 T33: 0.3798 T12: -0.0215 REMARK 3 T13: -0.0932 T23: 0.0706 REMARK 3 L TENSOR REMARK 3 L11: 2.2699 L22: 4.5962 REMARK 3 L33: 3.6217 L12: 0.7616 REMARK 3 L13: 0.5645 L23: 0.9565 REMARK 3 S TENSOR REMARK 3 S11: 0.2868 S12: -0.2471 S13: -0.5548 REMARK 3 S21: 0.4378 S22: -0.0053 S23: -0.4787 REMARK 3 S31: 0.6030 S32: -0.0354 S33: -0.1945 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 122 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8978 -8.2985 4.4720 REMARK 3 T TENSOR REMARK 3 T11: 0.3356 T22: 0.3125 REMARK 3 T33: 0.3371 T12: -0.0211 REMARK 3 T13: -0.0086 T23: -0.1006 REMARK 3 L TENSOR REMARK 3 L11: 3.6376 L22: 2.5727 REMARK 3 L33: 3.0735 L12: 1.0191 REMARK 3 L13: -2.9893 L23: -0.6024 REMARK 3 S TENSOR REMARK 3 S11: -0.0727 S12: 0.4024 S13: -0.5373 REMARK 3 S21: -0.0830 S22: 0.0262 S23: -0.1358 REMARK 3 S31: 0.3798 S32: -0.2894 S33: 0.3305 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 135 THROUGH 227 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.3809 3.6949 1.5046 REMARK 3 T TENSOR REMARK 3 T11: 0.2935 T22: 0.1839 REMARK 3 T33: 0.2310 T12: 0.0411 REMARK 3 T13: -0.0253 T23: -0.0194 REMARK 3 L TENSOR REMARK 3 L11: 6.0384 L22: 7.1273 REMARK 3 L33: 4.5221 L12: -1.7305 REMARK 3 L13: -0.9972 L23: 1.4243 REMARK 3 S TENSOR REMARK 3 S11: 0.0422 S12: 0.1610 S13: 0.1853 REMARK 3 S21: -0.1410 S22: -0.0765 S23: -0.3975 REMARK 3 S31: -0.1652 S32: 0.2298 S33: 0.0592 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 3 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.9945 10.5999 32.0436 REMARK 3 T TENSOR REMARK 3 T11: 0.2985 T22: 0.2158 REMARK 3 T33: 0.1920 T12: 0.0431 REMARK 3 T13: -0.0059 T23: -0.0437 REMARK 3 L TENSOR REMARK 3 L11: 2.8813 L22: 6.4898 REMARK 3 L33: 4.2815 L12: 1.3921 REMARK 3 L13: 0.7066 L23: -1.0078 REMARK 3 S TENSOR REMARK 3 S11: 0.0092 S12: -0.1389 S13: 0.1794 REMARK 3 S21: 0.3783 S22: 0.0236 S23: 0.1713 REMARK 3 S31: -0.2817 S32: -0.4092 S33: -0.0423 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 92 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.0938 10.2992 10.3785 REMARK 3 T TENSOR REMARK 3 T11: 0.2026 T22: 0.1746 REMARK 3 T33: 0.2642 T12: 0.0383 REMARK 3 T13: -0.0606 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: 1.2505 L22: 1.4894 REMARK 3 L33: 4.3503 L12: 0.3148 REMARK 3 L13: -1.0981 L23: -1.3480 REMARK 3 S TENSOR REMARK 3 S11: -0.0143 S12: 0.0474 S13: -0.0631 REMARK 3 S21: -0.1967 S22: -0.0923 S23: 0.0293 REMARK 3 S31: 0.0923 S32: -0.0469 S33: 0.1881 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 131 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.9263 17.5642 -5.1655 REMARK 3 T TENSOR REMARK 3 T11: 0.3482 T22: 0.1892 REMARK 3 T33: 0.2774 T12: 0.0296 REMARK 3 T13: -0.0157 T23: -0.0183 REMARK 3 L TENSOR REMARK 3 L11: 2.5782 L22: 4.9201 REMARK 3 L33: 5.5758 L12: -0.1254 REMARK 3 L13: 0.4208 L23: -0.0563 REMARK 3 S TENSOR REMARK 3 S11: 0.0526 S12: 0.3984 S13: 0.0093 REMARK 3 S21: -0.8480 S22: -0.0868 S23: 0.1717 REMARK 3 S31: 0.0772 S32: -0.0273 S33: 0.0390 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 2 through 101 or REMARK 3 resid 107 through 227)) 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" and (resid 2 through 52 or REMARK 3 resid 55 through 227)) 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" and resid 3 through 212) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9HV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144284. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-FEB-23 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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72419 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770 REMARK 200 RESOLUTION RANGE LOW (A) : 64.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.09000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CHES PH 9.5 30 % W/V PEG 3K, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.73400 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, 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 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 ASN A 53 REMARK 465 ARG A 54 REMARK 465 GLY A 144 REMARK 465 ASP A 145 REMARK 465 LYS A 146 REMARK 465 SER A 147 REMARK 465 SER A 148 REMARK 465 SER A 149 REMARK 465 GLY A 201 REMARK 465 SER A 202 REMARK 465 THR A 203 REMARK 465 SER A 204 REMARK 465 LYS A 232 REMARK 465 HIS A 233 REMARK 465 HIS A 234 REMARK 465 HIS A 235 REMARK 465 HIS A 236 REMARK 465 HIS A 237 REMARK 465 HIS A 238 REMARK 465 SER B 2 REMARK 465 SER B 214 REMARK 465 GLN H 1 REMARK 465 GLU H 102 REMARK 465 GLY H 103 REMARK 465 ASP H 104 REMARK 465 VAL H 105 REMARK 465 GLY H 106 REMARK 465 GLY H 144 REMARK 465 ASP H 145 REMARK 465 LYS H 146 REMARK 465 SER H 147 REMARK 465 SER H 148 REMARK 465 SER H 149 REMARK 465 GLY H 201 REMARK 465 SER H 202 REMARK 465 THR H 203 REMARK 465 SER H 204 REMARK 465 PRO H 228 REMARK 465 ARG H 229 REMARK 465 CYS H 230 REMARK 465 GLY H 231 REMARK 465 LYS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 SER L 2 REMARK 465 CYS L 213 REMARK 465 SER L 214 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 O HOH A 319 O HOH B 302 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG SER A 19 OG SER B 67 2545 2.17 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 A 15 -7.22 74.25 REMARK 500 LYS A 43 1.29 98.95 REMARK 500 CYS A 99 28.48 -154.44 REMARK 500 ASP A 110 98.07 -69.90 REMARK 500 CYS A 142 -101.95 -51.65 REMARK 500 SER A 159 68.99 61.92 REMARK 500 ASP B 51 -50.16 68.31 REMARK 500 LYS B 69 38.68 -97.44 REMARK 500 SER B 172 -7.49 77.34 REMARK 500 SER H 15 -9.27 72.67 REMARK 500 LYS H 43 8.49 97.09 REMARK 500 CYS H 99 26.06 -155.48 REMARK 500 SER H 159 69.44 62.23 REMARK 500 ASP L 51 -49.48 68.67 REMARK 500 LYS L 69 38.96 -96.02 REMARK 500 SER L 172 -9.29 78.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9HV1 RELATED DB: PDB DBREF 9HV2 A 1 238 PDB 9HV2 9HV2 1 238 DBREF 9HV2 B 2 214 PDB 9HV2 9HV2 2 214 DBREF 9HV2 H 1 238 PDB 9HV2 9HV2 1 238 DBREF 9HV2 L 2 214 PDB 9HV2 9HV2 2 214 SEQRES 1 A 238 GLN VAL GLN LEU ARG GLU SER GLY PRO SER LEU VAL LYS SEQRES 2 A 238 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 238 PHE SER LEU THR ASP VAL HIS VAL GLY TRP VAL ARG GLN SEQRES 4 A 238 THR PRO GLY LYS ALA LEU GLU TRP VAL GLY VAL ILE CYS SEQRES 5 A 238 ASN ARG GLY ALA ILE GLY TYR ASN PRO ALA LEU GLU SER SEQRES 6 A 238 ARG LEU SER ILE THR GLU ASP ASN SER LYS SER GLN VAL SEQRES 7 A 238 SER LEU SER LEU SER SER VAL THR THR ALA ASP THR ALA SEQRES 8 A 238 THR TYR TYR CYS ALA SER SER CYS ARG THR GLU GLY ASP SEQRES 9 A 238 VAL GLY GLY ASP CYS ASP SER ASP HIS PHE PHE CYS ALA SEQRES 10 A 238 TRP GLY GLN GLY LEU LEU VAL THR VAL SER SER ALA SER SEQRES 11 A 238 THR THR ALA PRO LYS VAL TYR PRO LEU SER SER CYS CYS SEQRES 12 A 238 GLY ASP LYS SER SER SER THR VAL THR LEU GLY CYS LEU SEQRES 13 A 238 VAL SER SER TYR MET PRO GLU PRO VAL THR VAL THR TRP SEQRES 14 A 238 ASN SER GLY ALA LEU LYS SER GLY VAL HIS THR PHE PRO SEQRES 15 A 238 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 A 238 MET VAL THR VAL PRO GLY SER THR SER GLY THR GLN THR SEQRES 17 A 238 PHE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 18 A 238 VAL ASP LYS ALA VAL ASP PRO ARG CYS GLY LYS HIS HIS SEQRES 19 A 238 HIS HIS HIS HIS SEQRES 1 B 213 SER TYR GLU LEU THR GLN PRO THR SER VAL SER VAL ALA SEQRES 2 B 213 LEU GLY GLN THR ALA LYS ILE THR CYS SER GLY ASP LEU SEQRES 3 B 213 LEU ASP ARG GLN TYR ALA GLN TRP TYR GLN GLN LYS PRO SEQRES 4 B 213 GLY GLN GLY PRO VAL ARG VAL ILE TYR LYS ASP SER GLU SEQRES 5 B 213 ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SER SER SEQRES 6 B 213 SER GLY LYS THR ALA THR LEU THR VAL SER GLY ALA GLN SEQRES 7 B 213 THR GLU ASP GLU ALA ASP TYR TYR CYS HIS SER ALA ASP SEQRES 8 B 213 SER SER HIS TYR PRO VAL PHE GLY SER GLY SER THR LEU SEQRES 9 B 213 THR VAL LEU GLY GLN PRO LYS SER PRO PRO SER VAL THR SEQRES 10 B 213 LEU PHE PRO PRO SER THR GLU GLU LEU ASN GLY ASN LYS SEQRES 11 B 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 B 213 SER VAL THR VAL VAL TRP LYS ALA ASP GLY SER THR ILE SEQRES 13 B 213 THR ARG ASN VAL GLU THR THR ARG ALA SER LYS GLN SER SEQRES 14 B 213 ASN SER LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 B 213 SER SER ASP TRP LYS SER LYS GLY SER TYR SER CYS GLU SEQRES 16 B 213 VAL THR HIS GLU GLY SER THR VAL THR LYS THR VAL LYS SEQRES 17 B 213 PRO SER GLU CYS SER SEQRES 1 H 238 GLN VAL GLN LEU ARG GLU SER GLY PRO SER LEU VAL LYS SEQRES 2 H 238 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 238 PHE SER LEU THR ASP VAL HIS VAL GLY TRP VAL ARG GLN SEQRES 4 H 238 THR PRO GLY LYS ALA LEU GLU TRP VAL GLY VAL ILE CYS SEQRES 5 H 238 ASN ARG GLY ALA ILE GLY TYR ASN PRO ALA LEU GLU SER SEQRES 6 H 238 ARG LEU SER ILE THR GLU ASP ASN SER LYS SER GLN VAL SEQRES 7 H 238 SER LEU SER LEU SER SER VAL THR THR ALA ASP THR ALA SEQRES 8 H 238 THR TYR TYR CYS ALA SER SER CYS ARG THR GLU GLY ASP SEQRES 9 H 238 VAL GLY GLY ASP CYS ASP SER ASP HIS PHE PHE CYS ALA SEQRES 10 H 238 TRP GLY GLN GLY LEU LEU VAL THR VAL SER SER ALA SER SEQRES 11 H 238 THR THR ALA PRO LYS VAL TYR PRO LEU SER SER CYS CYS SEQRES 12 H 238 GLY ASP LYS SER SER SER THR VAL THR LEU GLY CYS LEU SEQRES 13 H 238 VAL SER SER TYR MET PRO GLU PRO VAL THR VAL THR TRP SEQRES 14 H 238 ASN SER GLY ALA LEU LYS SER GLY VAL HIS THR PHE PRO SEQRES 15 H 238 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 238 MET VAL THR VAL PRO GLY SER THR SER GLY THR GLN THR SEQRES 17 H 238 PHE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 18 H 238 VAL ASP LYS ALA VAL ASP PRO ARG CYS GLY LYS HIS HIS SEQRES 19 H 238 HIS HIS HIS HIS SEQRES 1 L 213 SER TYR GLU LEU THR GLN PRO THR SER VAL SER VAL ALA SEQRES 2 L 213 LEU GLY GLN THR ALA LYS ILE THR CYS SER GLY ASP LEU SEQRES 3 L 213 LEU ASP ARG GLN TYR ALA GLN TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 GLY GLN GLY PRO VAL ARG VAL ILE TYR LYS ASP SER GLU SEQRES 5 L 213 ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SER SER SEQRES 6 L 213 SER GLY LYS THR ALA THR LEU THR VAL SER GLY ALA GLN SEQRES 7 L 213 THR GLU ASP GLU ALA ASP TYR TYR CYS HIS SER ALA ASP SEQRES 8 L 213 SER SER HIS TYR PRO VAL PHE GLY SER GLY SER THR LEU SEQRES 9 L 213 THR VAL LEU GLY GLN PRO LYS SER PRO PRO SER VAL THR SEQRES 10 L 213 LEU PHE PRO PRO SER THR GLU GLU LEU ASN GLY ASN LYS SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 213 SER VAL THR VAL VAL TRP LYS ALA ASP GLY SER THR ILE SEQRES 13 L 213 THR ARG ASN VAL GLU THR THR ARG ALA SER LYS GLN SER SEQRES 14 L 213 ASN SER LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 213 SER SER ASP TRP LYS SER LYS GLY SER TYR SER CYS GLU SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL THR LYS THR VAL LYS SEQRES 17 L 213 PRO SER GLU CYS SER FORMUL 5 HOH *510(H2 O) HELIX 1 AA1 LEU A 63 SER A 65 5 3 HELIX 2 AA2 ASN A 73 LYS A 75 5 3 HELIX 3 AA3 THR A 86 THR A 90 5 5 HELIX 4 AA4 ASP A 110 PHE A 114 5 5 HELIX 5 AA5 SER A 171 ALA A 173 5 3 HELIX 6 AA6 PRO A 216 SER A 219 5 4 HELIX 7 AA7 GLN B 79 GLU B 83 5 5 HELIX 8 AA8 SER B 123 ASN B 128 1 6 HELIX 9 AA9 SER B 184 LYS B 190 1 7 HELIX 10 AB1 LYS B 209 CYS B 213 5 5 HELIX 11 AB2 LEU H 63 SER H 65 5 3 HELIX 12 AB3 ASN H 73 LYS H 75 5 3 HELIX 13 AB4 THR H 86 THR H 90 5 5 HELIX 14 AB5 ASP H 110 PHE H 114 5 5 HELIX 15 AB6 SER H 171 ALA H 173 5 3 HELIX 16 AB7 PRO H 216 SER H 219 5 4 HELIX 17 AB8 GLN L 79 GLU L 83 5 5 HELIX 18 AB9 SER L 123 ASN L 128 1 6 HELIX 19 AC1 SER L 184 LYS L 190 1 7 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O THR A 21 N SER A 7 SHEET 3 AA1 4 GLN A 77 LEU A 82 -1 O LEU A 80 N LEU A 20 SHEET 4 AA1 4 LEU A 67 ASP A 72 -1 N THR A 70 O SER A 79 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 LEU A 122 VAL A 126 1 O THR A 125 N VAL A 12 SHEET 3 AA2 6 ALA A 91 SER A 97 -1 N TYR A 93 O LEU A 122 SHEET 4 AA2 6 VAL A 34 GLN A 39 -1 N VAL A 37 O TYR A 94 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 ILE A 57 TYR A 59 -1 O GLY A 58 N VAL A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 LEU A 122 VAL A 126 1 O THR A 125 N VAL A 12 SHEET 3 AA3 4 ALA A 91 SER A 97 -1 N TYR A 93 O LEU A 122 SHEET 4 AA3 4 ALA A 117 TRP A 118 -1 O ALA A 117 N SER A 97 SHEET 1 AA4 4 LYS A 135 SER A 140 0 SHEET 2 AA4 4 VAL A 151 TYR A 160 -1 O GLY A 154 N LEU A 139 SHEET 3 AA4 4 TYR A 191 VAL A 199 -1 O VAL A 199 N VAL A 151 SHEET 4 AA4 4 VAL A 178 THR A 180 -1 N HIS A 179 O MET A 196 SHEET 1 AA5 4 LYS A 135 SER A 140 0 SHEET 2 AA5 4 VAL A 151 TYR A 160 -1 O GLY A 154 N LEU A 139 SHEET 3 AA5 4 TYR A 191 VAL A 199 -1 O VAL A 199 N VAL A 151 SHEET 4 AA5 4 VAL A 184 LEU A 185 -1 N VAL A 184 O SER A 192 SHEET 1 AA6 3 THR A 166 TRP A 169 0 SHEET 2 AA6 3 THR A 210 HIS A 215 -1 O ALA A 214 N THR A 166 SHEET 3 AA6 3 THR A 220 ALA A 225 -1 O VAL A 222 N VAL A 213 SHEET 1 AA7 5 SER B 10 ALA B 14 0 SHEET 2 AA7 5 SER B 103 LEU B 108 1 O LEU B 108 N VAL B 13 SHEET 3 AA7 5 ALA B 84 ALA B 91 -1 N ALA B 84 O LEU B 105 SHEET 4 AA7 5 GLN B 34 GLN B 38 -1 N GLN B 38 O ASP B 85 SHEET 5 AA7 5 VAL B 45 ILE B 48 -1 O VAL B 45 N GLN B 37 SHEET 1 AA8 4 SER B 10 ALA B 14 0 SHEET 2 AA8 4 SER B 103 LEU B 108 1 O LEU B 108 N VAL B 13 SHEET 3 AA8 4 ALA B 84 ALA B 91 -1 N ALA B 84 O LEU B 105 SHEET 4 AA8 4 PRO B 97 PHE B 99 -1 O VAL B 98 N SER B 90 SHEET 1 AA9 3 ALA B 19 SER B 24 0 SHEET 2 AA9 3 THR B 70 VAL B 75 -1 O LEU B 73 N ILE B 21 SHEET 3 AA9 3 PHE B 62 SER B 67 -1 N SER B 67 O THR B 70 SHEET 1 AB1 4 SER B 116 PHE B 120 0 SHEET 2 AB1 4 LYS B 131 PHE B 141 -1 O LEU B 137 N THR B 118 SHEET 3 AB1 4 TYR B 174 THR B 183 -1 O LEU B 182 N ALA B 132 SHEET 4 AB1 4 VAL B 161 THR B 163 -1 N GLU B 162 O TYR B 179 SHEET 1 AB2 4 SER B 116 PHE B 120 0 SHEET 2 AB2 4 LYS B 131 PHE B 141 -1 O LEU B 137 N THR B 118 SHEET 3 AB2 4 TYR B 174 THR B 183 -1 O LEU B 182 N ALA B 132 SHEET 4 AB2 4 SER B 167 LYS B 168 -1 N SER B 167 O ALA B 175 SHEET 1 AB3 4 SER B 155 ILE B 157 0 SHEET 2 AB3 4 THR B 147 ALA B 152 -1 N ALA B 152 O SER B 155 SHEET 3 AB3 4 TYR B 193 HIS B 199 -1 O GLU B 196 N VAL B 149 SHEET 4 AB3 4 SER B 202 VAL B 208 -1 O SER B 202 N HIS B 199 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AB4 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AB4 4 LEU H 67 ASP H 72 -1 N THR H 70 O SER H 79 SHEET 1 AB5 6 LEU H 11 VAL H 12 0 SHEET 2 AB5 6 LEU H 122 VAL H 126 1 O THR H 125 N VAL H 12 SHEET 3 AB5 6 ALA H 91 SER H 97 -1 N TYR H 93 O LEU H 122 SHEET 4 AB5 6 VAL H 34 GLN H 39 -1 N VAL H 37 O TYR H 94 SHEET 5 AB5 6 LEU H 45 ILE H 51 -1 O ILE H 51 N VAL H 34 SHEET 6 AB5 6 ILE H 57 TYR H 59 -1 O GLY H 58 N VAL H 50 SHEET 1 AB6 4 LEU H 11 VAL H 12 0 SHEET 2 AB6 4 LEU H 122 VAL H 126 1 O THR H 125 N VAL H 12 SHEET 3 AB6 4 ALA H 91 SER H 97 -1 N TYR H 93 O LEU H 122 SHEET 4 AB6 4 ALA H 117 TRP H 118 -1 O ALA H 117 N SER H 97 SHEET 1 AB7 4 LYS H 135 SER H 140 0 SHEET 2 AB7 4 VAL H 151 TYR H 160 -1 O SER H 158 N LYS H 135 SHEET 3 AB7 4 TYR H 191 VAL H 199 -1 O TYR H 191 N TYR H 160 SHEET 4 AB7 4 VAL H 178 THR H 180 -1 N HIS H 179 O MET H 196 SHEET 1 AB8 4 LYS H 135 SER H 140 0 SHEET 2 AB8 4 VAL H 151 TYR H 160 -1 O SER H 158 N LYS H 135 SHEET 3 AB8 4 TYR H 191 VAL H 199 -1 O TYR H 191 N TYR H 160 SHEET 4 AB8 4 VAL H 184 LEU H 185 -1 N VAL H 184 O SER H 192 SHEET 1 AB9 3 THR H 166 TRP H 169 0 SHEET 2 AB9 3 PHE H 209 HIS H 215 -1 O ASN H 212 N THR H 168 SHEET 3 AB9 3 THR H 220 VAL H 226 -1 O VAL H 226 N PHE H 209 SHEET 1 AC1 5 SER L 10 ALA L 14 0 SHEET 2 AC1 5 SER L 103 LEU L 108 1 O THR L 106 N VAL L 11 SHEET 3 AC1 5 ASP L 85 ALA L 91 -1 N TYR L 86 O SER L 103 SHEET 4 AC1 5 GLN L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AC1 5 VAL L 45 ILE L 48 -1 O VAL L 45 N GLN L 37 SHEET 1 AC2 4 SER L 10 ALA L 14 0 SHEET 2 AC2 4 SER L 103 LEU L 108 1 O THR L 106 N VAL L 11 SHEET 3 AC2 4 ASP L 85 ALA L 91 -1 N TYR L 86 O SER L 103 SHEET 4 AC2 4 PRO L 97 PHE L 99 -1 O VAL L 98 N SER L 90 SHEET 1 AC3 3 ALA L 19 SER L 24 0 SHEET 2 AC3 3 THR L 70 VAL L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AC3 3 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AC4 4 SER L 116 PHE L 120 0 SHEET 2 AC4 4 LYS L 131 PHE L 141 -1 O SER L 139 N SER L 116 SHEET 3 AC4 4 TYR L 174 THR L 183 -1 O LEU L 182 N ALA L 132 SHEET 4 AC4 4 VAL L 161 THR L 163 -1 N GLU L 162 O TYR L 179 SHEET 1 AC5 4 SER L 116 PHE L 120 0 SHEET 2 AC5 4 LYS L 131 PHE L 141 -1 O SER L 139 N SER L 116 SHEET 3 AC5 4 TYR L 174 THR L 183 -1 O LEU L 182 N ALA L 132 SHEET 4 AC5 4 SER L 167 LYS L 168 -1 N SER L 167 O ALA L 175 SHEET 1 AC6 4 SER L 155 ILE L 157 0 SHEET 2 AC6 4 THR L 147 ALA L 152 -1 N TRP L 150 O ILE L 157 SHEET 3 AC6 4 TYR L 193 HIS L 199 -1 O GLU L 196 N VAL L 149 SHEET 4 AC6 4 SER L 202 VAL L 208 -1 O SER L 202 N HIS L 199 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.02 SSBOND 2 CYS A 52 CYS A 109 1555 1555 2.02 SSBOND 3 CYS A 99 CYS A 116 1555 1555 2.04 SSBOND 4 CYS A 142 CYS A 230 1555 1555 2.03 SSBOND 5 CYS A 143 CYS B 213 1555 1555 2.04 SSBOND 6 CYS A 155 CYS A 211 1555 1555 2.03 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 8 CYS B 136 CYS B 195 1555 1555 2.03 SSBOND 9 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 10 CYS H 52 CYS H 109 1555 1555 2.03 SSBOND 11 CYS H 99 CYS H 116 1555 1555 2.03 SSBOND 12 CYS H 155 CYS H 211 1555 1555 2.03 SSBOND 13 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 14 CYS L 136 CYS L 195 1555 1555 2.03 CISPEP 1 MET A 161 PRO A 162 0 -4.54 CISPEP 2 GLU A 163 PRO A 164 0 -0.56 CISPEP 3 TYR B 142 PRO B 143 0 0.74 CISPEP 4 MET H 161 PRO H 162 0 -4.52 CISPEP 5 GLU H 163 PRO H 164 0 -1.73 CISPEP 6 TYR L 142 PRO L 143 0 1.55 CRYST1 71.411 81.468 74.472 90.00 116.03 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014003 0.000000 0.006839 0.00000 SCALE2 0.000000 0.012275 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014944 0.00000 MTRIX1 1 -0.984739 -0.111914 0.133281 12.73673 1 MTRIX2 1 -0.089663 0.982608 0.162610 19.28256 1 MTRIX3 1 -0.149161 0.148178 -0.977647 33.00175 1 MTRIX1 2 -0.965917 -0.193301 0.172158 13.42180 1 MTRIX2 2 -0.177218 0.978609 0.104486 19.80627 1 MTRIX3 2 -0.188672 0.070415 -0.979512 29.44359 1