HEADER IMMUNE SYSTEM 29-OCT-24 9E69 TITLE ANTIBODY 5E10 CAVEAT 9E69 RESIDUES VAL H 127 AND THR H 132 THAT ARE NEXT TO EACH OTHER CAVEAT 2 9E69 IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 3 9E69 BETWEEN C AND N IS 12.50. RESIDUES PRO A 126 AND THR A 132 CAVEAT 4 9E69 THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT CAVEAT 5 9E69 PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 12.21. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF ANTIBODY 5E10; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF ANTIBODY 5E10; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEAVY CHAIN OF ANTIBODY 5E10; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: LIGHT CHAIN OF ANTIBODY 5E10; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.ZHOU,C.SAO-FONG CHEUNG,P.D.KWONG REVDAT 1 16-JUL-25 9E69 0 JRNL AUTH T.ZHOU,C.SAO-FONG CHEUNG,P.D.KWONG JRNL TITL STRUCTURE OF ANTIBODY 5E10 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.63 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2-4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.06 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 30791 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 1563 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 38.0600 - 5.8500 0.97 2643 138 0.1658 0.1946 REMARK 3 2 5.8400 - 4.6500 0.98 2659 146 0.1821 0.2040 REMARK 3 3 4.6400 - 4.0600 0.96 2604 130 0.2014 0.2120 REMARK 3 4 4.0600 - 3.6900 0.99 2700 150 0.2436 0.2748 REMARK 3 5 3.6900 - 3.4200 0.99 2688 142 0.2592 0.2746 REMARK 3 6 3.4200 - 3.2200 0.99 2663 155 0.2869 0.3307 REMARK 3 7 3.2200 - 3.0600 0.99 2709 142 0.3281 0.3334 REMARK 3 8 3.0600 - 2.9300 0.97 2623 135 0.2962 0.3353 REMARK 3 9 2.9300 - 2.8100 0.99 2690 145 0.2978 0.3696 REMARK 3 10 2.8100 - 2.7200 0.99 2686 138 0.3199 0.3600 REMARK 3 11 2.7200 - 2.6300 0.94 2563 142 0.3400 0.3526 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.180 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 80.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 6607 REMARK 3 ANGLE : 0.816 9038 REMARK 3 CHIRALITY : 0.049 1063 REMARK 3 PLANARITY : 0.007 1131 REMARK 3 DIHEDRAL : 15.320 902 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.8887 41.4232 -11.5480 REMARK 3 T TENSOR REMARK 3 T11: 1.0429 T22: 0.5868 REMARK 3 T33: 0.8010 T12: -0.1904 REMARK 3 T13: 0.1770 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 0.2387 L22: 0.0606 REMARK 3 L33: 0.2926 L12: 0.0080 REMARK 3 L13: -0.2389 L23: -0.1083 REMARK 3 S TENSOR REMARK 3 S11: -0.5426 S12: 0.4632 S13: -0.1205 REMARK 3 S21: 0.4578 S22: -0.1134 S23: 0.0027 REMARK 3 S31: 0.4496 S32: -0.2159 S33: -0.0093 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3460 44.0363 -6.0586 REMARK 3 T TENSOR REMARK 3 T11: 0.9009 T22: 0.4338 REMARK 3 T33: 0.6656 T12: -0.1424 REMARK 3 T13: 0.0193 T23: 0.1797 REMARK 3 L TENSOR REMARK 3 L11: 0.7089 L22: 0.2618 REMARK 3 L33: 0.9931 L12: -0.2967 REMARK 3 L13: -0.7339 L23: 0.1458 REMARK 3 S TENSOR REMARK 3 S11: -0.3397 S12: 0.0823 S13: -0.0606 REMARK 3 S21: 0.5157 S22: -0.2422 S23: 0.0549 REMARK 3 S31: 0.1577 S32: -0.0035 S33: -0.5420 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.8619 51.7226 2.3294 REMARK 3 T TENSOR REMARK 3 T11: 1.1901 T22: 1.0724 REMARK 3 T33: 1.0434 T12: -0.1198 REMARK 3 T13: -0.2327 T23: 0.3802 REMARK 3 L TENSOR REMARK 3 L11: 0.1680 L22: 0.2421 REMARK 3 L33: 0.1466 L12: 0.0236 REMARK 3 L13: -0.0677 L23: 0.1575 REMARK 3 S TENSOR REMARK 3 S11: -0.1059 S12: -0.2004 S13: 0.3691 REMARK 3 S21: 0.1977 S22: -0.3453 S23: 0.4514 REMARK 3 S31: 0.4066 S32: 0.4923 S33: -0.0170 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 188 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.8365 52.2532 11.6426 REMARK 3 T TENSOR REMARK 3 T11: 1.7530 T22: 1.5390 REMARK 3 T33: 0.7887 T12: -0.2285 REMARK 3 T13: -0.2211 T23: 0.1710 REMARK 3 L TENSOR REMARK 3 L11: 0.0040 L22: 0.2786 REMARK 3 L33: 0.0108 L12: -0.0090 REMARK 3 L13: -0.0083 L23: 0.0784 REMARK 3 S TENSOR REMARK 3 S11: -0.2008 S12: -0.1530 S13: -0.1394 REMARK 3 S21: 0.3544 S22: 0.1858 S23: 0.4739 REMARK 3 S31: -0.2733 S32: 0.3193 S33: -0.0004 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2237 7.5216 32.9435 REMARK 3 T TENSOR REMARK 3 T11: 0.6851 T22: 0.7927 REMARK 3 T33: 0.6950 T12: 0.1273 REMARK 3 T13: -0.0192 T23: 0.0809 REMARK 3 L TENSOR REMARK 3 L11: 0.3027 L22: 0.3401 REMARK 3 L33: 0.3518 L12: 0.1248 REMARK 3 L13: -0.2254 L23: -0.3578 REMARK 3 S TENSOR REMARK 3 S11: 0.0513 S12: -0.1309 S13: -0.1340 REMARK 3 S21: 0.0211 S22: -0.4993 S23: -0.0428 REMARK 3 S31: -0.3312 S32: 0.2950 S33: -0.0004 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.0957 9.6206 11.0446 REMARK 3 T TENSOR REMARK 3 T11: 0.8009 T22: 1.4155 REMARK 3 T33: 1.0640 T12: -0.0926 REMARK 3 T13: 0.1503 T23: 0.6492 REMARK 3 L TENSOR REMARK 3 L11: 0.1274 L22: 0.1887 REMARK 3 L33: 0.1039 L12: -0.0717 REMARK 3 L13: -0.0678 L23: 0.1322 REMARK 3 S TENSOR REMARK 3 S11: -0.3130 S12: -0.0455 S13: 0.1140 REMARK 3 S21: -0.2531 S22: -0.1477 S23: -0.1208 REMARK 3 S31: -0.3248 S32: 0.7149 S33: -0.3288 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8353 9.4457 8.2363 REMARK 3 T TENSOR REMARK 3 T11: 1.2750 T22: 0.4854 REMARK 3 T33: 0.8086 T12: 0.1131 REMARK 3 T13: -0.0384 T23: 0.0679 REMARK 3 L TENSOR REMARK 3 L11: 0.0790 L22: 0.0008 REMARK 3 L33: 0.0204 L12: 0.0285 REMARK 3 L13: 0.0522 L23: 0.0084 REMARK 3 S TENSOR REMARK 3 S11: -0.1679 S12: -0.0309 S13: -0.3078 REMARK 3 S21: -0.3156 S22: -0.5141 S23: 0.2136 REMARK 3 S31: -0.2282 S32: -0.1715 S33: -0.0230 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.1602 13.8752 16.6755 REMARK 3 T TENSOR REMARK 3 T11: 0.9756 T22: 0.5816 REMARK 3 T33: 0.7525 T12: 0.1884 REMARK 3 T13: -0.2151 T23: -0.0851 REMARK 3 L TENSOR REMARK 3 L11: 0.0710 L22: 0.0302 REMARK 3 L33: 0.3841 L12: 0.0259 REMARK 3 L13: 0.0719 L23: -0.1274 REMARK 3 S TENSOR REMARK 3 S11: -0.3323 S12: -0.2846 S13: 0.1644 REMARK 3 S21: 0.0947 S22: 0.0342 S23: 0.0356 REMARK 3 S31: -0.5316 S32: -0.2865 S33: -0.0002 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.8000 15.6113 13.4819 REMARK 3 T TENSOR REMARK 3 T11: 0.8434 T22: 0.5486 REMARK 3 T33: 0.6980 T12: 0.0356 REMARK 3 T13: -0.1746 T23: 0.0287 REMARK 3 L TENSOR REMARK 3 L11: 0.0582 L22: -0.0018 REMARK 3 L33: 0.0232 L12: -0.0169 REMARK 3 L13: 0.0362 L23: -0.0154 REMARK 3 S TENSOR REMARK 3 S11: -0.1908 S12: -0.1738 S13: 0.1936 REMARK 3 S21: -0.1256 S22: 0.1123 S23: -0.1541 REMARK 3 S31: -0.3719 S32: 0.1742 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 92 THROUGH 139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.2172 6.2312 6.2300 REMARK 3 T TENSOR REMARK 3 T11: 0.9713 T22: 0.6948 REMARK 3 T33: 0.3555 T12: 0.0895 REMARK 3 T13: 0.2586 T23: 0.5317 REMARK 3 L TENSOR REMARK 3 L11: 1.5649 L22: 0.7321 REMARK 3 L33: 0.7604 L12: 0.0149 REMARK 3 L13: 0.5900 L23: 0.6223 REMARK 3 S TENSOR REMARK 3 S11: -0.5431 S12: 0.0950 S13: 0.2818 REMARK 3 S21: -0.9545 S22: -0.2219 S23: 0.2161 REMARK 3 S31: 0.0102 S32: 0.5487 S33: -1.5017 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 140 THROUGH 171 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5864 4.2796 1.2141 REMARK 3 T TENSOR REMARK 3 T11: 1.2479 T22: 1.0613 REMARK 3 T33: 1.1555 T12: 0.0967 REMARK 3 T13: 0.0447 T23: 0.2659 REMARK 3 L TENSOR REMARK 3 L11: 0.0954 L22: 0.0003 REMARK 3 L33: 0.0368 L12: -0.0154 REMARK 3 L13: 0.0426 L23: -0.0103 REMARK 3 S TENSOR REMARK 3 S11: -0.0459 S12: 0.3928 S13: -0.2151 REMARK 3 S21: 0.0007 S22: -0.0036 S23: -0.2429 REMARK 3 S31: -0.3054 S32: 0.0170 S33: -0.0006 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 172 THROUGH 207 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.4136 -0.0539 -3.2477 REMARK 3 T TENSOR REMARK 3 T11: 1.3479 T22: 1.2092 REMARK 3 T33: 0.8796 T12: 0.3743 REMARK 3 T13: 0.1509 T23: 0.2047 REMARK 3 L TENSOR REMARK 3 L11: 0.0905 L22: 0.0643 REMARK 3 L33: 0.0273 L12: 0.0779 REMARK 3 L13: 0.0680 L23: 0.0731 REMARK 3 S TENSOR REMARK 3 S11: -0.2041 S12: 0.2548 S13: 0.1271 REMARK 3 S21: -0.4608 S22: -0.1098 S23: 0.1366 REMARK 3 S31: 0.2191 S32: 0.4147 S33: -0.0034 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2059 46.7167 -29.0477 REMARK 3 T TENSOR REMARK 3 T11: 0.7571 T22: 0.8517 REMARK 3 T33: 0.7093 T12: -0.1014 REMARK 3 T13: -0.0097 T23: 0.0679 REMARK 3 L TENSOR REMARK 3 L11: 0.2415 L22: 0.3683 REMARK 3 L33: 0.5291 L12: -0.0106 REMARK 3 L13: 0.2333 L23: -0.4532 REMARK 3 S TENSOR REMARK 3 S11: 0.2252 S12: 0.2264 S13: 0.1401 REMARK 3 S21: 0.0520 S22: -0.5624 S23: -0.0127 REMARK 3 S31: 0.4712 S32: 0.3382 S33: -0.0001 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.9627 44.5096 -7.3786 REMARK 3 T TENSOR REMARK 3 T11: 0.8841 T22: 1.4604 REMARK 3 T33: 1.1962 T12: 0.0524 REMARK 3 T13: -0.0628 T23: 0.5925 REMARK 3 L TENSOR REMARK 3 L11: 0.0194 L22: 0.0453 REMARK 3 L33: 0.0754 L12: -0.0147 REMARK 3 L13: 0.0057 L23: 0.0727 REMARK 3 S TENSOR REMARK 3 S11: -0.2054 S12: -0.0730 S13: -0.3305 REMARK 3 S21: 0.1681 S22: 0.0555 S23: -0.0647 REMARK 3 S31: 0.2126 S32: 0.6768 S33: -0.0087 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9E69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1000289345. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-DEC-19 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 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 : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30869 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.06800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 31.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.150 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 (%): 55.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG1 A8 (#8) 0.2 M SODIUM ACETATE 20% REMARK 280 PEG3350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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 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 71.77800 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 35.88900 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL 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 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 H -18 REMARK 465 GLY H -17 REMARK 465 ARG H -16 REMARK 465 LEU H -15 REMARK 465 THR H -14 REMARK 465 SER H -13 REMARK 465 SER H -12 REMARK 465 PHE H -11 REMARK 465 LEU H -10 REMARK 465 LEU H -9 REMARK 465 LEU H -8 REMARK 465 ILE H -7 REMARK 465 VAL H -6 REMARK 465 PRO H -5 REMARK 465 ALA H -4 REMARK 465 TYR H -3 REMARK 465 VAL H -2 REMARK 465 LEU H -1 REMARK 465 SER H 0 REMARK 465 MET L -18 REMARK 465 ALA L -17 REMARK 465 TRP L -16 REMARK 465 THR L -15 REMARK 465 SER L -14 REMARK 465 LEU L -13 REMARK 465 ILE L -12 REMARK 465 LEU L -11 REMARK 465 SER L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 ALA L -7 REMARK 465 LEU L -6 REMARK 465 CYS L -5 REMARK 465 SER L -4 REMARK 465 GLY L -3 REMARK 465 ALA L -2 REMARK 465 SER L -1 REMARK 465 SER L 0 REMARK 465 MET A -18 REMARK 465 GLY A -17 REMARK 465 ARG A -16 REMARK 465 LEU A -15 REMARK 465 THR A -14 REMARK 465 SER A -13 REMARK 465 SER A -12 REMARK 465 PHE A -11 REMARK 465 LEU A -10 REMARK 465 LEU A -9 REMARK 465 LEU A -8 REMARK 465 ILE A -7 REMARK 465 VAL A -6 REMARK 465 PRO A -5 REMARK 465 ALA A -4 REMARK 465 TYR A -3 REMARK 465 VAL A -2 REMARK 465 LEU A -1 REMARK 465 SER A 0 REMARK 465 MET B -18 REMARK 465 ALA B -17 REMARK 465 TRP B -16 REMARK 465 THR B -15 REMARK 465 SER B -14 REMARK 465 LEU B -13 REMARK 465 ILE B -12 REMARK 465 LEU B -11 REMARK 465 SER B -10 REMARK 465 LEU B -9 REMARK 465 LEU B -8 REMARK 465 ALA B -7 REMARK 465 LEU B -6 REMARK 465 CYS B -5 REMARK 465 SER B -4 REMARK 465 GLY B -3 REMARK 465 ALA B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER H 185 OG REMARK 470 LYS H 205 CE NZ REMARK 470 GLU L 186 OE1 OE2 REMARK 470 SER A 185 OG REMARK 470 LYS A 205 CE NZ REMARK 470 GLU B 186 OE1 OE2 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 OE2 GLU B 203 OG SER B 205 2.16 REMARK 500 OE1 GLU B 7 OG1 THR B 22 2.17 REMARK 500 O VAL B 150 OG1 THR B 153 2.18 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 O ASN A 55 NH1 ARG B 24 2664 1.99 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 H 41 127.22 66.78 REMARK 500 LEU H 48 -62.29 -91.62 REMARK 500 ASP H 54 33.57 -89.66 REMARK 500 ASN H 82B 70.77 56.22 REMARK 500 SER H 113 44.68 -98.26 REMARK 500 PRO H 147 -165.12 -102.32 REMARK 500 ALA L 2 115.78 65.42 REMARK 500 THR L 51 -59.12 70.05 REMARK 500 SER L 93 -53.33 67.18 REMARK 500 GLU L 160 102.23 -161.45 REMARK 500 GLN L 167 -160.50 -100.56 REMARK 500 LYS L 171 -145.49 -82.28 REMARK 500 LEU L 180 -168.25 -117.75 REMARK 500 ARG L 187 -72.15 -54.09 REMARK 500 SER L 189 -26.12 -145.84 REMARK 500 SER A 41 117.35 64.36 REMARK 500 ASP A 54 37.51 -84.58 REMARK 500 ASN A 55 28.32 43.84 REMARK 500 ASN A 76 64.05 64.69 REMARK 500 SER A 113 44.06 -99.28 REMARK 500 PRO A 147 -164.97 -103.87 REMARK 500 SER A 185 -7.22 -57.17 REMARK 500 ALA B 2 111.86 64.01 REMARK 500 THR B 51 -58.02 66.88 REMARK 500 ASP B 83 103.71 -55.41 REMARK 500 SER B 93 -53.11 67.17 REMARK 500 LYS B 171 -153.17 -83.63 REMARK 500 HIS B 188 -138.24 64.03 REMARK 500 SER B 189 49.95 72.74 REMARK 500 SER B 190 116.85 69.70 REMARK 500 REMARK 500 REMARK: NULL DBREF 9E69 H -18 214 PDB 9E69 9E69 -18 214 DBREF 9E69 L -18 207 PDB 9E69 9E69 -18 207 DBREF 9E69 A -18 213 PDB 9E69 9E69 -18 213 DBREF 9E69 B -18 208 PDB 9E69 9E69 -18 208 SEQRES 1 H 238 MET GLY ARG LEU THR SER SER PHE LEU LEU LEU ILE VAL SEQRES 2 H 238 PRO ALA TYR VAL LEU SER GLN VAL THR LEU LYS GLU SER SEQRES 3 H 238 GLY PRO GLY ILE LEU GLN PRO SER GLN THR LEU SER LEU SEQRES 4 H 238 THR CYS SER PHE SER GLY PHE SER LEU SER THR PHE GLY SEQRES 5 H 238 MET GLY VAL GLY TRP ILE ARG GLN PRO SER GLY LYS GLY SEQRES 6 H 238 LEU GLU TRP LEU ALA HIS ILE TRP TRP ASP ASN ASP GLU SEQRES 7 H 238 TYR CYS ASN PRO ALA LEU LYS SER ARG LEU THR ILE SER SEQRES 8 H 238 LYS ASP THR SER LYS ASN HIS ILE PHE LEU LYS ILE ALA SEQRES 9 H 238 ASN VAL ASP THR ALA ASP THR ALA THR TYR TYR CYS ALA SEQRES 10 H 238 ARG ILE PHE ALA ASN TYR GLY GLY ASP ALA MET ASP TYR SEQRES 11 H 238 TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SER SEQRES 12 H 238 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO VAL THR SEQRES 13 H 238 GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 14 H 238 PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER SEQRES 15 H 238 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 16 H 238 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR SEQRES 17 H 238 SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL SEQRES 18 H 238 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 19 H 238 ASP PRO ALA GLY SEQRES 1 L 229 MET ALA TRP THR SER LEU ILE LEU SER LEU LEU ALA LEU SEQRES 2 L 229 CYS SER GLY ALA SER SER GLN ALA VAL VAL THR GLN GLU SEQRES 3 L 229 SER ALA LEU THR THR SER PRO GLY GLY THR VAL ILE LEU SEQRES 4 L 229 THR CYS ARG SER SER THR GLY ALA VAL THR THR SER ASN SEQRES 5 L 229 TYR ALA ASN TRP VAL GLN LYS LYS PRO ASP HIS LEU PHE SEQRES 6 L 229 THR GLY LEU ILE GLY GLY THR SER ASN ARG VAL SER GLY SEQRES 7 L 229 VAL PRO VAL ARG PHE SER GLY SER LEU ILE GLY ASP LYS SEQRES 8 L 229 ALA ALA LEU THR ILE THR GLY ALA GLN THR GLU ASP ASP SEQRES 9 L 229 ALA MET TYR PHE CYS ALA LEU TRP PHE SER THR HIS TYR SEQRES 10 L 229 VAL PHE GLY GLY GLY THR LYS VAL THR VAL LEU SER GLN SEQRES 11 L 229 PRO LYS SER SER PRO SER VAL THR LEU PHE PRO PRO SER SEQRES 12 L 229 SER GLU GLU LEU GLU THR ASN LYS ALA THR LEU VAL CYS SEQRES 13 L 229 THR ILE THR ASP PHE TYR PRO GLY VAL VAL THR VAL ASP SEQRES 14 L 229 TRP LYS VAL ASP GLY THR PRO VAL THR GLN GLY MET GLU SEQRES 15 L 229 THR THR GLN PRO SER LYS GLN SER ASN ASN LYS TYR MET SEQRES 16 L 229 ALA SER SER TYR LEU THR LEU THR ALA ARG ALA TRP GLU SEQRES 17 L 229 ARG HIS SER SER TYR SER CYS GLN VAL THR HIS GLU GLY SEQRES 18 L 229 HIS THR VAL GLU LYS SER LEU SER SEQRES 1 A 236 MET GLY ARG LEU THR SER SER PHE LEU LEU LEU ILE VAL SEQRES 2 A 236 PRO ALA TYR VAL LEU SER GLN VAL THR LEU LYS GLU SER SEQRES 3 A 236 GLY PRO GLY ILE LEU GLN PRO SER GLN THR LEU SER LEU SEQRES 4 A 236 THR CYS SER PHE SER GLY PHE SER LEU SER THR PHE GLY SEQRES 5 A 236 MET GLY VAL GLY TRP ILE ARG GLN PRO SER GLY LYS GLY SEQRES 6 A 236 LEU GLU TRP LEU ALA HIS ILE TRP TRP ASP ASN ASP GLU SEQRES 7 A 236 TYR CYS ASN PRO ALA LEU LYS SER ARG LEU THR ILE SER SEQRES 8 A 236 LYS ASP THR SER LYS ASN HIS ILE PHE LEU LYS ILE ALA SEQRES 9 A 236 ASN VAL ASP THR ALA ASP THR ALA THR TYR TYR CYS ALA SEQRES 10 A 236 ARG ILE PHE ALA ASN TYR GLY GLY ASP ALA MET ASP TYR SEQRES 11 A 236 TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SER SEQRES 12 A 236 THR THR ALA PRO SER VAL TYR PRO LEU ALA PRO THR GLY SEQRES 13 A 236 SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE SEQRES 14 A 236 PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER LEU SEQRES 15 A 236 SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 16 A 236 ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR SER SEQRES 17 A 236 SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL ALA SEQRES 18 A 236 HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE ASP SEQRES 19 A 236 PRO ALA SEQRES 1 B 230 MET ALA TRP THR SER LEU ILE LEU SER LEU LEU ALA LEU SEQRES 2 B 230 CYS SER GLY ALA SER SER GLN ALA VAL VAL THR GLN GLU SEQRES 3 B 230 SER ALA LEU THR THR SER PRO GLY GLY THR VAL ILE LEU SEQRES 4 B 230 THR CYS ARG SER SER THR GLY ALA VAL THR THR SER ASN SEQRES 5 B 230 TYR ALA ASN TRP VAL GLN LYS LYS PRO ASP HIS LEU PHE SEQRES 6 B 230 THR GLY LEU ILE GLY GLY THR SER ASN ARG VAL SER GLY SEQRES 7 B 230 VAL PRO VAL ARG PHE SER GLY SER LEU ILE GLY ASP LYS SEQRES 8 B 230 ALA ALA LEU THR ILE THR GLY ALA GLN THR GLU ASP ASP SEQRES 9 B 230 ALA MET TYR PHE CYS ALA LEU TRP PHE SER THR HIS TYR SEQRES 10 B 230 VAL PHE GLY GLY GLY THR LYS VAL THR VAL LEU SER GLN SEQRES 11 B 230 PRO LYS SER SER PRO SER VAL THR LEU PHE PRO PRO SER SEQRES 12 B 230 SER GLU GLU LEU GLU THR ASN LYS ALA THR LEU VAL CYS SEQRES 13 B 230 THR ILE THR ASP PHE TYR PRO GLY VAL VAL THR VAL ASP SEQRES 14 B 230 TRP LYS VAL ASP GLY THR PRO VAL THR GLN GLY MET GLU SEQRES 15 B 230 THR THR GLN PRO SER LYS GLN SER ASN ASN LYS TYR MET SEQRES 16 B 230 ALA SER SER TYR LEU THR LEU THR ALA ARG ALA TRP GLU SEQRES 17 B 230 ARG HIS SER SER TYR SER CYS GLN VAL THR HIS GLU GLY SEQRES 18 B 230 HIS THR VAL GLU LYS SER LEU SER ARG HELIX 1 AA1 PRO H 61 SER H 65 5 5 HELIX 2 AA2 ASP H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 SER H 158 5 3 HELIX 4 AA4 THR L 28 TYR L 32 5 5 HELIX 5 AA5 GLN L 79 ASP L 83 5 5 HELIX 6 AA6 GLU L 123 THR L 127 5 5 HELIX 7 AA7 ALA L 182 HIS L 188 1 7 HELIX 8 AA8 PRO A 61 LYS A 64 5 4 HELIX 9 AA9 ASP A 83 THR A 87 5 5 HELIX 10 AB1 THR B 28 TYR B 32 5 5 HELIX 11 AB2 GLN B 79 ASP B 83 5 5 HELIX 12 AB3 SER B 121 THR B 127 1 7 HELIX 13 AB4 ALA B 182 HIS B 188 1 7 SHEET 1 AA1 4 THR H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 HIS H 77 ILE H 82 -1 O ILE H 82 N LEU H 18 SHEET 4 AA1 4 LEU H 67 ASP H 72 -1 N SER H 70 O PHE H 79 SHEET 1 AA2 6 ILE H 11 LEU H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AA2 6 ALA H 88 ASN H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 TRP H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 GLU H 57 CYS H 59 -1 O TYR H 58 N HIS H 50 SHEET 1 AA3 4 ILE H 11 LEU H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AA3 4 ALA H 88 ASN H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 GLY H 100A ALA H 100C-1 O GLY H 100A N ASN H 98 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 SER H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 175 THR H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 SER H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA5 4 TYR H 175 THR H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O THR H 176 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AA6 3 THR H 204 LYS H 209 -1 O LYS H 208 N CYS H 195 SHEET 1 AA7 4 VAL L 4 THR L 5 0 SHEET 2 AA7 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 LYS L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA7 4 PHE L 62 ILE L 67 -1 N SER L 65 O ALA L 72 SHEET 1 AA8 6 ALA L 9 THR L 13 0 SHEET 2 AA8 6 THR L 102 VAL L 106 1 O THR L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 TRP L 91 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 ASN L 34 LYS L 38 -1 N LYS L 38 O MET L 85 SHEET 5 AA8 6 PHE L 44 GLY L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N GLY L 49 SHEET 1 AA9 4 ALA L 9 THR L 13 0 SHEET 2 AA9 4 THR L 102 VAL L 106 1 O THR L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 TRP L 91 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 TYR L 96 PHE L 98 -1 O VAL L 97 N LEU L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 LYS L 129 PHE L 139 -1 O THR L 137 N SER L 114 SHEET 3 AB1 4 TYR L 172 THR L 181 -1 O ALA L 174 N ILE L 136 SHEET 4 AB1 4 MET L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AB2 4 THR L 153 PRO L 154 0 SHEET 2 AB2 4 THR L 145 VAL L 150 -1 N VAL L 150 O THR L 153 SHEET 3 AB2 4 TYR L 191 HIS L 197 -1 O SER L 192 N LYS L 149 SHEET 4 AB2 4 HIS L 200 LEU L 206 -1 O HIS L 200 N HIS L 197 SHEET 1 AB3 4 THR A 3 SER A 7 0 SHEET 2 AB3 4 THR A 17 SER A 25 -1 O SER A 23 N LYS A 5 SHEET 3 AB3 4 HIS A 77 ALA A 82A-1 O ILE A 82 N LEU A 18 SHEET 4 AB3 4 LEU A 67 ASP A 72 -1 N SER A 70 O PHE A 79 SHEET 1 AB4 6 ILE A 11 LEU A 12 0 SHEET 2 AB4 6 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AB4 6 ALA A 88 ASN A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AB4 6 MET A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AB4 6 GLU A 46 TRP A 52 -1 O ILE A 51 N VAL A 35A SHEET 6 AB4 6 GLU A 57 CYS A 59 -1 O TYR A 58 N HIS A 50 SHEET 1 AB5 4 ILE A 11 LEU A 12 0 SHEET 2 AB5 4 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AB5 4 ALA A 88 ASN A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AB5 4 GLY A 100A ALA A 100C-1 O GLY A 100A N ASN A 98 SHEET 1 AB6 4 SER A 120 LEU A 124 0 SHEET 2 AB6 4 SER A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB6 4 LEU A 174 THR A 184 -1 O TYR A 175 N TYR A 145 SHEET 4 AB6 4 VAL A 163 THR A 165 -1 N HIS A 164 O SER A 180 SHEET 1 AB7 4 SER A 120 LEU A 124 0 SHEET 2 AB7 4 SER A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB7 4 LEU A 174 THR A 184 -1 O TYR A 175 N TYR A 145 SHEET 4 AB7 4 VAL A 169 GLN A 171 -1 N GLN A 171 O LEU A 174 SHEET 1 AB8 3 THR A 151 TRP A 154 0 SHEET 2 AB8 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AB8 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AB9 4 VAL B 4 GLN B 6 0 SHEET 2 AB9 4 VAL B 19 SER B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB9 4 LYS B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 4 AB9 4 PHE B 62 ILE B 67 -1 N SER B 63 O THR B 74 SHEET 1 AC1 6 ALA B 9 THR B 13 0 SHEET 2 AC1 6 THR B 102 VAL B 106 1 O THR B 105 N LEU B 11 SHEET 3 AC1 6 ALA B 84 TRP B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AC1 6 ASN B 34 LYS B 38 -1 N LYS B 38 O MET B 85 SHEET 5 AC1 6 PHE B 44 GLY B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AC1 6 ASN B 53 ARG B 54 -1 O ASN B 53 N GLY B 49 SHEET 1 AC2 4 ALA B 9 THR B 13 0 SHEET 2 AC2 4 THR B 102 VAL B 106 1 O THR B 105 N LEU B 11 SHEET 3 AC2 4 ALA B 84 TRP B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AC2 4 TYR B 96 PHE B 98 -1 O VAL B 97 N LEU B 90 SHEET 1 AC3 4 SER B 114 PHE B 118 0 SHEET 2 AC3 4 LYS B 129 PHE B 139 -1 O THR B 137 N SER B 114 SHEET 3 AC3 4 TYR B 172 THR B 181 -1 O ALA B 174 N ILE B 136 SHEET 4 AC3 4 MET B 159 THR B 161 -1 N GLU B 160 O TYR B 177 SHEET 1 AC4 4 SER B 114 PHE B 118 0 SHEET 2 AC4 4 LYS B 129 PHE B 139 -1 O THR B 137 N SER B 114 SHEET 3 AC4 4 TYR B 172 THR B 181 -1 O ALA B 174 N ILE B 136 SHEET 4 AC4 4 SER B 165 LYS B 166 -1 N SER B 165 O MET B 173 SHEET 1 AC5 4 THR B 153 PRO B 154 0 SHEET 2 AC5 4 THR B 145 VAL B 150 -1 N VAL B 150 O THR B 153 SHEET 3 AC5 4 TYR B 191 HIS B 197 -1 O SER B 192 N LYS B 149 SHEET 4 AC5 4 HIS B 200 LEU B 206 -1 O VAL B 202 N VAL B 195 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 195 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 193 1555 1555 2.03 SSBOND 5 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 6 CYS A 140 CYS A 195 1555 1555 2.03 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 8 CYS B 134 CYS B 193 1555 1555 2.04 CISPEP 1 PHE H 146 PRO H 147 0 -4.94 CISPEP 2 GLU H 148 PRO H 149 0 -3.96 CISPEP 3 TRP H 188 PRO H 189 0 6.06 CISPEP 4 TYR L 140 PRO L 141 0 1.34 CISPEP 5 PHE A 146 PRO A 147 0 -3.59 CISPEP 6 GLU A 148 PRO A 149 0 -4.13 CISPEP 7 TRP A 188 PRO A 189 0 4.41 CISPEP 8 TYR B 140 PRO B 141 0 0.50 CRYST1 93.969 93.969 107.667 90.00 90.00 120.00 P 32 3 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 0.010642 0.006144 0.000000 0.00000 SCALE2 0.000000 0.012288 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009288 0.00000