HEADER IMMUNE SYSTEM 27-APR-25 9UP7 TITLE ANTI-HPV18 E7 MONOCLONAL ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF THE ANTI-HPV18 E7 MONOCLONAL ANTIBODY 17F2; COMPND 3 CHAIN: A, H; COMPND 4 OTHER_DETAILS: HEAVY CHAIN OF THE FAB FRAGMENT OF THE ANTI-HPV18 E7 COMPND 5 MONOCLONAL ANTIBODY 17F2; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN OF THE ANTI-HPV18 E7 MONOCLONAL ANTIBODY 17F2; COMPND 8 CHAIN: B, L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090 KEYWDS MONOCLONAL ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR H.FENG,L.TINGTING,G.YING,L.SHAOWEI REVDAT 1 21-JAN-26 9UP7 0 JRNL AUTH H.FENG,G.XINYING,C.LINYAN,L.TINGTING,G.YING,X.NINGSHAO, JRNL AUTH 2 L.SHAOWEI JRNL TITL MRNA SCFV TARGETING THE HELIX-ALPHA3 OF E7 AS AN EFFECTIVE JRNL TITL 2 TREATMENT FOR HPV18-POSITIVE TUMORS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.130 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 3 NUMBER OF REFLECTIONS : 48834 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1927 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 50.2600 - 5.0600 0.95 3538 142 0.2213 0.2515 REMARK 3 2 5.0600 - 4.0200 0.96 3442 148 0.1614 0.1968 REMARK 3 3 4.0200 - 3.5100 0.96 3460 138 0.1810 0.2432 REMARK 3 4 3.5100 - 3.1900 0.96 3445 140 0.1950 0.2284 REMARK 3 5 3.1900 - 2.9600 0.96 3453 139 0.1999 0.2207 REMARK 3 6 2.9600 - 2.7900 0.97 3445 147 0.2048 0.2760 REMARK 3 7 2.7900 - 2.6500 0.96 3425 130 0.2221 0.2770 REMARK 3 8 2.6500 - 2.5300 0.95 3380 147 0.2298 0.3092 REMARK 3 9 2.5300 - 2.4300 0.94 3336 128 0.2454 0.3055 REMARK 3 10 2.4300 - 2.3500 0.93 3321 147 0.2535 0.3577 REMARK 3 11 2.3500 - 2.2800 0.93 3307 131 0.2579 0.3128 REMARK 3 12 2.2800 - 2.2100 0.90 3191 135 0.2697 0.3101 REMARK 3 13 2.2100 - 2.1500 0.87 3142 115 0.2804 0.3177 REMARK 3 14 2.1500 - 2.1000 0.86 3022 140 0.3090 0.3384 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) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.120 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.18 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 : 0.010 6672 REMARK 3 ANGLE : 0.841 9078 REMARK 3 CHIRALITY : 0.055 1033 REMARK 3 PLANARITY : 0.007 1153 REMARK 3 DIHEDRAL : 13.011 2410 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.0438 -27.0998 -13.8448 REMARK 3 T TENSOR REMARK 3 T11: 0.4222 T22: 0.3164 REMARK 3 T33: 0.2673 T12: -0.0191 REMARK 3 T13: -0.0351 T23: -0.0027 REMARK 3 L TENSOR REMARK 3 L11: 0.1175 L22: 0.0723 REMARK 3 L33: 0.0312 L12: -0.1065 REMARK 3 L13: -0.0192 L23: 0.0100 REMARK 3 S TENSOR REMARK 3 S11: -0.1625 S12: -0.0563 S13: -0.0992 REMARK 3 S21: -0.0670 S22: -0.0171 S23: -0.2033 REMARK 3 S31: 0.2774 S32: 0.1617 S33: -0.0002 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.8836 -26.8560 -14.4443 REMARK 3 T TENSOR REMARK 3 T11: 0.2928 T22: 0.2691 REMARK 3 T33: 0.2655 T12: -0.0201 REMARK 3 T13: -0.0269 T23: -0.0018 REMARK 3 L TENSOR REMARK 3 L11: 0.2051 L22: 0.1805 REMARK 3 L33: 0.1984 L12: -0.1621 REMARK 3 L13: 0.0332 L23: -0.0211 REMARK 3 S TENSOR REMARK 3 S11: -0.0223 S12: -0.0631 S13: -0.1279 REMARK 3 S21: -0.0420 S22: 0.0039 S23: 0.0809 REMARK 3 S31: 0.0165 S32: -0.1362 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.9620 -10.0009 -39.5256 REMARK 3 T TENSOR REMARK 3 T11: 0.2734 T22: 0.3274 REMARK 3 T33: 0.3006 T12: -0.0185 REMARK 3 T13: -0.0475 T23: 0.0365 REMARK 3 L TENSOR REMARK 3 L11: 0.1153 L22: 0.1652 REMARK 3 L33: 0.2133 L12: -0.1020 REMARK 3 L13: -0.1493 L23: 0.0118 REMARK 3 S TENSOR REMARK 3 S11: 0.1527 S12: 0.0234 S13: 0.1144 REMARK 3 S21: 0.1322 S22: -0.1532 S23: 0.0196 REMARK 3 S31: 0.1692 S32: 0.2807 S33: 0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 96 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.9188 -5.1426 -6.6015 REMARK 3 T TENSOR REMARK 3 T11: 0.3456 T22: 0.2777 REMARK 3 T33: 0.2201 T12: 0.0224 REMARK 3 T13: 0.0217 T23: 0.0135 REMARK 3 L TENSOR REMARK 3 L11: 0.1390 L22: 0.3121 REMARK 3 L33: 0.0863 L12: -0.1402 REMARK 3 L13: 0.0546 L23: -0.0257 REMARK 3 S TENSOR REMARK 3 S11: 0.0683 S12: 0.1089 S13: -0.0091 REMARK 3 S21: 0.1746 S22: 0.0518 S23: 0.0358 REMARK 3 S31: -0.2164 S32: -0.0985 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 97 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.2666 -4.5238 -38.2660 REMARK 3 T TENSOR REMARK 3 T11: 0.1932 T22: 0.2415 REMARK 3 T33: 0.2300 T12: -0.0103 REMARK 3 T13: -0.0172 T23: -0.0346 REMARK 3 L TENSOR REMARK 3 L11: 0.0129 L22: 0.0740 REMARK 3 L33: 0.2573 L12: 0.0332 REMARK 3 L13: -0.2811 L23: -0.2110 REMARK 3 S TENSOR REMARK 3 S11: 0.0138 S12: -0.0557 S13: -0.0184 REMARK 3 S21: 0.0160 S22: 0.0485 S23: 0.0075 REMARK 3 S31: -0.0537 S32: -0.0401 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 195 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.2627 3.7526 -51.0741 REMARK 3 T TENSOR REMARK 3 T11: 0.1788 T22: 0.2092 REMARK 3 T33: 0.2413 T12: -0.0022 REMARK 3 T13: -0.0198 T23: 0.0410 REMARK 3 L TENSOR REMARK 3 L11: 0.0866 L22: 0.1459 REMARK 3 L33: 0.2817 L12: 0.0527 REMARK 3 L13: 0.0077 L23: -0.1673 REMARK 3 S TENSOR REMARK 3 S11: 0.2378 S12: 0.0944 S13: 0.1850 REMARK 3 S21: 0.2228 S22: 0.1531 S23: -0.1903 REMARK 3 S31: -0.0680 S32: -0.0345 S33: 0.0304 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.6869 15.3867 -33.7915 REMARK 3 T TENSOR REMARK 3 T11: 0.4615 T22: 0.4378 REMARK 3 T33: 0.3759 T12: 0.0536 REMARK 3 T13: 0.0579 T23: -0.0616 REMARK 3 L TENSOR REMARK 3 L11: 0.0365 L22: 0.0301 REMARK 3 L33: 0.0726 L12: -0.0178 REMARK 3 L13: 0.0516 L23: -0.0537 REMARK 3 S TENSOR REMARK 3 S11: -0.1129 S12: -0.0208 S13: -0.0094 REMARK 3 S21: -0.1820 S22: -0.0023 S23: 0.1072 REMARK 3 S31: -0.3253 S32: -0.2255 S33: -0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.7803 13.1124 -24.3865 REMARK 3 T TENSOR REMARK 3 T11: 0.4910 T22: 0.3580 REMARK 3 T33: 0.2792 T12: -0.0064 REMARK 3 T13: -0.0027 T23: -0.0894 REMARK 3 L TENSOR REMARK 3 L11: 0.0973 L22: 0.0991 REMARK 3 L33: 0.0415 L12: 0.0756 REMARK 3 L13: -0.0077 L23: -0.0502 REMARK 3 S TENSOR REMARK 3 S11: -0.2193 S12: -0.2918 S13: -0.2099 REMARK 3 S21: -0.1132 S22: -0.0410 S23: 0.0284 REMARK 3 S31: -0.2705 S32: 0.2313 S33: -0.0191 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 68 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.9039 19.6960 -31.1517 REMARK 3 T TENSOR REMARK 3 T11: 0.5573 T22: 0.3475 REMARK 3 T33: 0.3766 T12: -0.0132 REMARK 3 T13: -0.0240 T23: -0.0812 REMARK 3 L TENSOR REMARK 3 L11: 0.0079 L22: 0.0238 REMARK 3 L33: 0.0709 L12: 0.0212 REMARK 3 L13: 0.0165 L23: 0.0481 REMARK 3 S TENSOR REMARK 3 S11: -0.1454 S12: 0.1857 S13: 0.0176 REMARK 3 S21: 0.1530 S22: 0.0480 S23: 0.1132 REMARK 3 S31: -0.6198 S32: 0.2266 S33: 0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.3744 9.9111 -37.3509 REMARK 3 T TENSOR REMARK 3 T11: 0.3229 T22: 0.2965 REMARK 3 T33: 0.2393 T12: -0.0315 REMARK 3 T13: 0.0395 T23: -0.0471 REMARK 3 L TENSOR REMARK 3 L11: 0.0990 L22: 0.0262 REMARK 3 L33: 0.1216 L12: -0.0847 REMARK 3 L13: 0.1368 L23: -0.0123 REMARK 3 S TENSOR REMARK 3 S11: 0.0136 S12: -0.0642 S13: -0.1174 REMARK 3 S21: 0.0490 S22: -0.1463 S23: 0.0417 REMARK 3 S31: -0.4172 S32: -0.0018 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 168 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.5684 -1.9684 -56.0374 REMARK 3 T TENSOR REMARK 3 T11: 0.0943 T22: 0.2032 REMARK 3 T33: 0.4503 T12: -0.0269 REMARK 3 T13: 0.0136 T23: -0.0482 REMARK 3 L TENSOR REMARK 3 L11: 0.0953 L22: 0.4010 REMARK 3 L33: 0.4244 L12: 0.1223 REMARK 3 L13: 0.0181 L23: -0.2264 REMARK 3 S TENSOR REMARK 3 S11: -0.0588 S12: 0.0438 S13: -0.2594 REMARK 3 S21: 0.2775 S22: -0.0670 S23: 0.3377 REMARK 3 S31: -0.1967 S32: -0.1040 S33: -0.0601 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 169 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6605 -0.4430 -59.5236 REMARK 3 T TENSOR REMARK 3 T11: 0.0877 T22: 0.2481 REMARK 3 T33: 0.4863 T12: 0.0303 REMARK 3 T13: 0.0042 T23: -0.0707 REMARK 3 L TENSOR REMARK 3 L11: 0.1989 L22: 0.4264 REMARK 3 L33: 0.3962 L12: 0.1507 REMARK 3 L13: -0.1529 L23: -0.3836 REMARK 3 S TENSOR REMARK 3 S11: 0.0915 S12: 0.1979 S13: 0.0585 REMARK 3 S21: 0.2980 S22: -0.1542 S23: 0.3837 REMARK 3 S31: -0.2148 S32: -0.0685 S33: -0.0338 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 96 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.5057 -7.6836 -21.3914 REMARK 3 T TENSOR REMARK 3 T11: 0.7081 T22: 0.2995 REMARK 3 T33: -0.0567 T12: -0.0668 REMARK 3 T13: 0.3804 T23: -0.0587 REMARK 3 L TENSOR REMARK 3 L11: 1.0639 L22: 0.1560 REMARK 3 L33: 0.7190 L12: -0.0782 REMARK 3 L13: 0.5499 L23: -0.2168 REMARK 3 S TENSOR REMARK 3 S11: -0.5541 S12: -0.1522 S13: 0.5013 REMARK 3 S21: 0.1073 S22: -0.1693 S23: -0.2509 REMARK 3 S31: 0.6081 S32: -0.0995 S33: -0.8794 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 97 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.0682 -10.3712 -49.0647 REMARK 3 T TENSOR REMARK 3 T11: 0.2895 T22: 0.1488 REMARK 3 T33: 0.2295 T12: -0.0108 REMARK 3 T13: 0.0144 T23: -0.0134 REMARK 3 L TENSOR REMARK 3 L11: 0.3880 L22: 0.3512 REMARK 3 L33: 0.3574 L12: -0.0362 REMARK 3 L13: -0.0313 L23: 0.6296 REMARK 3 S TENSOR REMARK 3 S11: -0.0697 S12: 0.0642 S13: -0.0484 REMARK 3 S21: 0.2184 S22: -0.0491 S23: 0.0473 REMARK 3 S31: 0.0758 S32: 0.1131 S33: -0.0388 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 181 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6971 -13.1557 -64.3644 REMARK 3 T TENSOR REMARK 3 T11: 0.1888 T22: 0.2017 REMARK 3 T33: 0.2371 T12: 0.0140 REMARK 3 T13: -0.0345 T23: -0.0064 REMARK 3 L TENSOR REMARK 3 L11: 0.0834 L22: 0.1596 REMARK 3 L33: 0.1469 L12: -0.0342 REMARK 3 L13: -0.0019 L23: 0.1652 REMARK 3 S TENSOR REMARK 3 S11: 0.0489 S12: -0.0053 S13: 0.0043 REMARK 3 S21: 0.1234 S22: 0.1190 S23: -0.1608 REMARK 3 S31: -0.0205 S32: 0.1037 S33: 0.0065 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 9UP7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 29-APR-25. REMARK 100 THE DEPOSITION ID IS D_1300058928. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-APR-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 : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50750 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 66.140 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.58400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE +26% PEG 4000, REMARK 280 EVAPORATION, TEMPERATURE 293.15K 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 27.34900 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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: 3000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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 SER A 128 REMARK 465 ALA A 129 REMARK 465 ALA A 130 REMARK 465 GLN A 131 REMARK 465 THR A 132 REMARK 465 ASN A 133 REMARK 465 SER A 134 REMARK 465 GLY H 127 REMARK 465 SER H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 GLN H 131 REMARK 465 THR H 132 REMARK 465 ASN H 133 REMARK 465 SER H 134 REMARK 465 GLY H 214 REMARK 465 CYS L 220 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 H 346 O HOH H 358 1.81 REMARK 500 OE2 GLU H 73 O HOH H 301 1.85 REMARK 500 O HOH A 358 O HOH A 360 1.86 REMARK 500 O ARG H 213 O HOH H 302 1.86 REMARK 500 O GLN H 62 O HOH H 303 1.90 REMARK 500 OG SER B 214 O HOH B 301 1.91 REMARK 500 O HOH B 402 O HOH B 408 1.92 REMARK 500 O LYS B 113 O HOH B 302 1.97 REMARK 500 O HOH A 357 O HOH A 366 1.98 REMARK 500 O HOH L 341 O HOH L 366 1.98 REMARK 500 O HOH A 348 O HOH A 360 1.99 REMARK 500 O HOH A 357 O HOH A 365 2.00 REMARK 500 OG1 THR B 186 O HOH B 303 2.01 REMARK 500 OH TYR L 98 O HOH L 301 2.01 REMARK 500 O HOH H 330 O HOH H 362 2.02 REMARK 500 N SER H 185 O HOH H 304 2.02 REMARK 500 O THR B 208 O HOH B 304 2.02 REMARK 500 O HOH L 349 O HOH L 388 2.03 REMARK 500 O HOH H 326 O HOH H 342 2.04 REMARK 500 OE2 GLU B 160 O HOH B 305 2.05 REMARK 500 O HOH A 350 O HOH A 367 2.05 REMARK 500 N ALA L 86 O HOH L 302 2.07 REMARK 500 N LEU L 52 O HOH L 303 2.08 REMARK 500 O HOH A 364 O HOH B 413 2.09 REMARK 500 O HOH H 328 O HOH H 348 2.09 REMARK 500 O HOH H 362 O HOH H 363 2.10 REMARK 500 NZ LYS H 115 O HOH H 305 2.10 REMARK 500 O HOH B 384 O HOH B 412 2.12 REMARK 500 O HOH H 317 O HOH H 370 2.13 REMARK 500 O HOH H 356 O HOH H 368 2.15 REMARK 500 OG1 THR B 186 O HOH B 306 2.15 REMARK 500 O GLY L 72 O HOH L 304 2.16 REMARK 500 O ASP B 149 O HOH B 307 2.18 REMARK 500 O HOH H 371 O HOH H 373 2.18 REMARK 500 OE2 GLU L 129 O HOH L 305 2.18 REMARK 500 N MET A 135 O HOH A 301 2.18 REMARK 500 OG SER H 25 O HOH H 306 2.19 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 HOH B 404 O HOH L 380 2554 1.80 REMARK 500 O HOH B 346 O HOH H 342 2544 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS H 195 CB CYS H 195 SG -0.097 REMARK 500 CYS L 140 CB CYS L 140 SG -0.105 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 ASN A 55 -9.59 71.83 REMARK 500 SER A 113 -157.82 -175.53 REMARK 500 LYS A 115 90.65 107.22 REMARK 500 GLU A 148 -73.05 -56.66 REMARK 500 PRO A 149 107.74 -31.63 REMARK 500 ALA B 57 -36.82 77.61 REMARK 500 GLU B 219 87.93 52.19 REMARK 500 ASN H 55 -8.66 74.72 REMARK 500 ALA H 92 -178.95 -175.17 REMARK 500 SER H 113 -151.10 -175.09 REMARK 500 LYS H 115 149.10 99.27 REMARK 500 ALA L 57 -37.22 77.96 REMARK 500 SER L 207 20.65 99.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 371 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH H 372 DISTANCE = 6.50 ANGSTROMS REMARK 525 HOH H 373 DISTANCE = 6.59 ANGSTROMS REMARK 525 HOH L 389 DISTANCE = 5.85 ANGSTROMS DBREF 9UP7 A 1 214 PDB 9UP7 9UP7 1 214 DBREF 9UP7 B 1 220 PDB 9UP7 9UP7 1 220 DBREF 9UP7 H 1 214 PDB 9UP7 9UP7 1 214 DBREF 9UP7 L 1 220 PDB 9UP7 9UP7 1 220 SEQRES 1 A 214 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 A 214 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 214 TYR THR PHE THR ASP SER ASN ILE HIS TRP VAL LYS GLN SEQRES 4 A 214 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 A 214 PRO TYR ASN GLY ASN THR GLY TYR SER GLN LYS PHE LYS SEQRES 6 A 214 SER LYS ALA THR LEU THR VAL GLU ASN SER SER ASN THR SEQRES 7 A 214 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 A 214 ALA VAL TYR TYR CYS ALA ARG ALA SER GLY LEU ASP TRP SEQRES 9 A 214 GLY GLN GLY THR THR LEU THR VAL SER GLN LYS THR THR SEQRES 10 A 214 PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA SEQRES 11 A 214 GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 A 214 GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER SEQRES 13 A 214 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 A 214 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 A 214 VAL PRO SER SER PRO ARG PRO SER GLU THR VAL THR CYS SEQRES 16 A 214 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 A 214 LYS ILE VAL PRO ARG GLY SEQRES 1 B 220 ASP ILE VAL MET THR GLN SER PRO SER SER LEU THR MET SEQRES 2 B 220 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 B 220 GLN SER LEU LEU ASN SER ILE ASN GLN LYS SER TYR LEU SEQRES 4 B 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 B 220 LEU ILE TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 B 220 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 B 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP SEQRES 8 B 220 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE SEQRES 9 B 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 B 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 B 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 B 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 B 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 B 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 B 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 B 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 B 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 214 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 214 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 214 TYR THR PHE THR ASP SER ASN ILE HIS TRP VAL LYS GLN SEQRES 4 H 214 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 214 PRO TYR ASN GLY ASN THR GLY TYR SER GLN LYS PHE LYS SEQRES 6 H 214 SER LYS ALA THR LEU THR VAL GLU ASN SER SER ASN THR SEQRES 7 H 214 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 H 214 ALA VAL TYR TYR CYS ALA ARG ALA SER GLY LEU ASP TRP SEQRES 9 H 214 GLY GLN GLY THR THR LEU THR VAL SER GLN LYS THR THR SEQRES 10 H 214 PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA SEQRES 11 H 214 GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 H 214 GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER SEQRES 13 H 214 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 H 214 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 H 214 VAL PRO SER SER PRO ARG PRO SER GLU THR VAL THR CYS SEQRES 16 H 214 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 H 214 LYS ILE VAL PRO ARG GLY SEQRES 1 L 220 ASP ILE VAL MET THR GLN SER PRO SER SER LEU THR MET SEQRES 2 L 220 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU ASN SER ILE ASN GLN LYS SER TYR LEU SEQRES 4 L 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 L 220 LEU ILE TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP SEQRES 8 L 220 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE SEQRES 9 L 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 L 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 L 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 L 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 L 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 L 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 L 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 L 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS FORMUL 5 HOH *354(H2 O) HELIX 1 AA1 THR A 28 SER A 32 5 5 HELIX 2 AA2 GLN A 62 LYS A 65 5 4 HELIX 3 AA3 ASN A 74 SER A 76 5 3 HELIX 4 AA4 THR A 87 SER A 91 5 5 HELIX 5 AA5 SER A 156 SER A 158 5 3 HELIX 6 AA6 PRO A 200 SER A 203 5 4 HELIX 7 AA7 GLN B 85 LEU B 89 5 5 HELIX 8 AA8 SER B 127 SER B 133 1 7 HELIX 9 AA9 LYS B 189 GLU B 193 1 5 HELIX 10 AB1 THR H 28 SER H 32 5 5 HELIX 11 AB2 GLN H 62 LYS H 65 5 4 HELIX 12 AB3 ASN H 74 SER H 76 5 3 HELIX 13 AB4 THR H 87 SER H 91 5 5 HELIX 14 AB5 SER H 156 SER H 158 5 3 HELIX 15 AB6 PRO H 200 SER H 203 5 4 HELIX 16 AB7 GLN L 85 LEU L 89 5 5 HELIX 17 AB8 SER L 127 SER L 133 1 7 HELIX 18 AB9 LYS L 189 ARG L 194 1 6 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O MET A 81 N ILE A 20 SHEET 4 AA1 4 ALA A 68 GLU A 73 -1 N GLU A 73 O THR A 78 SHEET 1 AA2 6 GLU A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 108 VAL A 112 1 O THR A 111 N VAL A 12 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N ALA A 92 O LEU A 110 SHEET 4 AA2 6 ILE A 34 GLN A 39 -1 N HIS A 35 O ALA A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O GLY A 59 N TYR A 50 SHEET 1 AA3 4 GLU A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 108 VAL A 112 1 O THR A 111 N VAL A 12 SHEET 3 AA3 4 ALA A 92 ARG A 98 -1 N ALA A 92 O LEU A 110 SHEET 4 AA3 4 ASP A 103 TRP A 104 -1 O ASP A 103 N ARG A 98 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 VAL A 136 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA4 4 LEU A 174 VAL A 183 -1 O VAL A 183 N VAL A 136 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O SER A 180 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 VAL A 136 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA5 4 LEU A 174 VAL A 183 -1 O VAL A 183 N VAL A 136 SHEET 4 AA5 4 VAL A 169 GLN A 171 -1 N GLN A 171 O LEU A 174 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AA6 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA7 4 ASP B 76 ILE B 81 -1 O LEU B 79 N MET B 21 SHEET 4 AA7 4 PHE B 68 SER B 73 -1 N ILE B 69 O THR B 80 SHEET 1 AA8 6 SER B 10 SER B 14 0 SHEET 2 AA8 6 THR B 108 LYS B 113 1 O GLU B 111 N LEU B 11 SHEET 3 AA8 6 ALA B 90 GLN B 96 -1 N ALA B 90 O LEU B 110 SHEET 4 AA8 6 LEU B 39 GLN B 44 -1 N TYR B 42 O PHE B 93 SHEET 5 AA8 6 LYS B 51 TYR B 55 -1 O LEU B 53 N TRP B 41 SHEET 6 AA8 6 THR B 59 ARG B 60 -1 O THR B 59 N TYR B 55 SHEET 1 AA9 4 THR B 120 PHE B 124 0 SHEET 2 AA9 4 GLY B 135 PHE B 145 -1 O PHE B 141 N SER B 122 SHEET 3 AA9 4 TYR B 179 THR B 188 -1 O LEU B 185 N VAL B 138 SHEET 4 AA9 4 VAL B 165 TRP B 169 -1 N SER B 168 O SER B 182 SHEET 1 AB1 4 SER B 159 ARG B 161 0 SHEET 2 AB1 4 ASN B 151 ILE B 156 -1 N TRP B 154 O ARG B 161 SHEET 3 AB1 4 SER B 197 THR B 203 -1 O THR B 199 N LYS B 155 SHEET 4 AB1 4 ILE B 211 ASN B 216 -1 O ILE B 211 N ALA B 202 SHEET 1 AB2 4 GLN H 3 GLN H 6 0 SHEET 2 AB2 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB2 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AB2 4 ALA H 68 GLU H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AB3 6 GLU H 10 VAL H 12 0 SHEET 2 AB3 6 THR H 108 VAL H 112 1 O THR H 111 N VAL H 12 SHEET 3 AB3 6 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 110 SHEET 4 AB3 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB3 6 LEU H 45 TYR H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 AB3 6 ASN H 57 TYR H 60 -1 O ASN H 57 N TYR H 52 SHEET 1 AB4 4 GLU H 10 VAL H 12 0 SHEET 2 AB4 4 THR H 108 VAL H 112 1 O THR H 111 N VAL H 12 SHEET 3 AB4 4 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 110 SHEET 4 AB4 4 ASP H 103 TRP H 104 -1 O ASP H 103 N ARG H 98 SHEET 1 AB5 4 SER H 120 LEU H 124 0 SHEET 2 AB5 4 VAL H 136 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB5 4 LEU H 174 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AB5 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AB6 4 SER H 120 LEU H 124 0 SHEET 2 AB6 4 VAL H 136 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB6 4 LEU H 174 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AB6 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AB7 3 THR H 151 TRP H 154 0 SHEET 2 AB7 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AB7 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 AB8 4 MET L 4 SER L 7 0 SHEET 2 AB8 4 VAL L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB8 4 ASP L 76 ILE L 81 -1 O PHE L 77 N CYS L 23 SHEET 4 AB8 4 PHE L 68 SER L 73 -1 N ILE L 69 O THR L 80 SHEET 1 AB9 6 SER L 10 SER L 14 0 SHEET 2 AB9 6 THR L 108 LYS L 113 1 O GLU L 111 N LEU L 11 SHEET 3 AB9 6 ALA L 90 GLN L 96 -1 N ALA L 90 O LEU L 110 SHEET 4 AB9 6 LEU L 39 GLN L 44 -1 N GLN L 44 O ASP L 91 SHEET 5 AB9 6 LYS L 51 TYR L 55 -1 O LYS L 51 N GLN L 43 SHEET 6 AB9 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AC1 4 THR L 120 PHE L 124 0 SHEET 2 AC1 4 GLY L 135 PHE L 145 -1 O ASN L 143 N THR L 120 SHEET 3 AC1 4 TYR L 179 THR L 188 -1 O LEU L 185 N VAL L 138 SHEET 4 AC1 4 VAL L 165 TRP L 169 -1 N SER L 168 O SER L 182 SHEET 1 AC2 4 SER L 159 ARG L 161 0 SHEET 2 AC2 4 ASN L 151 ILE L 156 -1 N ILE L 156 O SER L 159 SHEET 3 AC2 4 SER L 197 THR L 203 -1 O GLU L 201 N LYS L 153 SHEET 4 AC2 4 ILE L 211 ASN L 216 -1 O ILE L 211 N ALA L 202 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.08 SSBOND 2 CYS A 140 CYS A 195 1555 1555 2.06 SSBOND 3 CYS B 23 CYS B 94 1555 1555 2.11 SSBOND 4 CYS B 140 CYS B 200 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 6 CYS H 140 CYS H 195 1555 1555 2.10 SSBOND 7 CYS L 23 CYS L 94 1555 1555 2.06 SSBOND 8 CYS L 140 CYS L 200 1555 1555 2.00 CISPEP 1 PHE A 146 PRO A 147 0 -4.16 CISPEP 2 ARG A 188 PRO A 189 0 3.87 CISPEP 3 SER B 7 PRO B 8 0 -5.23 CISPEP 4 THR B 100 PRO B 101 0 -3.54 CISPEP 5 TYR B 146 PRO B 147 0 2.06 CISPEP 6 PHE H 146 PRO H 147 0 -8.36 CISPEP 7 GLU H 148 PRO H 149 0 -8.66 CISPEP 8 ARG H 188 PRO H 189 0 3.47 CISPEP 9 SER L 7 PRO L 8 0 -5.17 CISPEP 10 THR L 100 PRO L 101 0 -2.96 CISPEP 11 TYR L 146 PRO L 147 0 2.98 CRYST1 67.644 54.698 124.060 90.00 102.11 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 0.014783 0.000000 0.003172 0.00000 SCALE2 0.000000 0.018282 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008244 0.00000