HEADER IMMUNE SYSTEM 14-NOV-24 9ECI TITLE CRYSTAL STRUCTURE OF A HUMANIZED 5E5 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5E5 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 5E5 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 8 ORGANISM_TAXID: 32630; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HUMANIZED 5E5 ANTIBODY, TN-MUC1, CANCER, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR W.LI,S.V.EVANS REVDAT 1 30-APR-25 9ECI 0 JRNL AUTH W.LI,U.MANDEL,H.VAN FAASSEN,M.J.PARKER,M.S.G.LEGG,G.HUSSACK, JRNL AUTH 2 H.CLAUSEN,S.V.EVANS JRNL TITL STRUCTURE OF THE FAB FRAGMENT OF A HUMANIZED 5E5 ANTIBODY TO JRNL TITL 2 A CANCER-SPECIFIC TN-MUC1 EPITOPE. JRNL REF ACTA CRYSTALLOGR D STRUCT 2025 JRNL REF 2 BIOL JRNL REFN ISSN 2059-7983 JRNL PMID 40221891 JRNL DOI 10.1107/S2059798325002554 REMARK 2 REMARK 2 RESOLUTION. 1.57 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN 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) : 1.57 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.43 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 69451 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.157 REMARK 3 R VALUE (WORKING SET) : 0.156 REMARK 3 FREE R VALUE : 0.183 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3403 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.57 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2193 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.83 REMARK 3 BIN R VALUE (WORKING SET) : 0.2044 REMARK 3 BIN FREE R VALUE SET COUNT : 115 REMARK 3 BIN FREE R VALUE : 0.2711 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3293 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 738 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.87 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.07 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 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 120 L 134 REMARK 3 ORIGIN FOR THE GROUP (A): 30.0571 26.0304 52.7550 REMARK 3 T TENSOR REMARK 3 T11: 0.1024 T22: 0.1608 REMARK 3 T33: 0.1490 T12: -0.0430 REMARK 3 T13: -0.0208 T23: -0.0106 REMARK 3 L TENSOR REMARK 3 L11: 0.0884 L22: 0.1702 REMARK 3 L33: 0.1760 L12: -0.1767 REMARK 3 L13: -0.1406 L23: 0.1501 REMARK 3 S TENSOR REMARK 3 S11: 0.1549 S12: -0.3794 S13: -0.0093 REMARK 3 S21: 0.1826 S22: -0.1396 S23: -0.1304 REMARK 3 S31: 0.0167 S32: 0.0880 S33: 0.0028 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 135 L 156 REMARK 3 ORIGIN FOR THE GROUP (A): 14.7732 25.1520 49.3843 REMARK 3 T TENSOR REMARK 3 T11: 0.0954 T22: 0.1270 REMARK 3 T33: 0.1151 T12: -0.0064 REMARK 3 T13: 0.0063 T23: -0.0329 REMARK 3 L TENSOR REMARK 3 L11: 0.2003 L22: 0.0413 REMARK 3 L33: 0.2209 L12: 0.1517 REMARK 3 L13: -0.1908 L23: -0.0644 REMARK 3 S TENSOR REMARK 3 S11: 0.0732 S12: -0.1741 S13: 0.0925 REMARK 3 S21: 0.0135 S22: -0.0814 S23: 0.0471 REMARK 3 S31: -0.0780 S32: -0.0593 S33: 0.0060 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 157 L 180 REMARK 3 ORIGIN FOR THE GROUP (A): 14.4104 24.6631 45.3044 REMARK 3 T TENSOR REMARK 3 T11: 0.0940 T22: 0.1112 REMARK 3 T33: 0.1165 T12: 0.0033 REMARK 3 T13: 0.0072 T23: -0.0020 REMARK 3 L TENSOR REMARK 3 L11: 0.5166 L22: 0.1648 REMARK 3 L33: 0.1495 L12: 0.0900 REMARK 3 L13: 0.1279 L23: -0.1662 REMARK 3 S TENSOR REMARK 3 S11: -0.0030 S12: -0.0619 S13: 0.1168 REMARK 3 S21: -0.0218 S22: -0.0557 S23: 0.1572 REMARK 3 S31: -0.0204 S32: -0.0407 S33: 0.0003 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 181 L 203 REMARK 3 ORIGIN FOR THE GROUP (A): 22.5239 32.3055 55.5134 REMARK 3 T TENSOR REMARK 3 T11: 0.1358 T22: 0.1280 REMARK 3 T33: 0.1259 T12: -0.0389 REMARK 3 T13: 0.0191 T23: -0.0410 REMARK 3 L TENSOR REMARK 3 L11: 0.2018 L22: 0.3976 REMARK 3 L33: 0.2375 L12: 0.0760 REMARK 3 L13: 0.1670 L23: 0.1574 REMARK 3 S TENSOR REMARK 3 S11: 0.0367 S12: -0.1658 S13: 0.0974 REMARK 3 S21: 0.0247 S22: -0.1790 S23: 0.1395 REMARK 3 S31: -0.1478 S32: -0.2012 S33: -0.0526 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 204 L 219 REMARK 3 ORIGIN FOR THE GROUP (A): 15.1170 23.7164 58.9389 REMARK 3 T TENSOR REMARK 3 T11: 0.0392 T22: 0.2215 REMARK 3 T33: -0.0213 T12: -0.1623 REMARK 3 T13: 0.1712 T23: -0.0119 REMARK 3 L TENSOR REMARK 3 L11: 0.9000 L22: 0.8845 REMARK 3 L33: 0.7388 L12: 0.2887 REMARK 3 L13: 0.5190 L23: -0.1597 REMARK 3 S TENSOR REMARK 3 S11: 0.1530 S12: -0.3907 S13: 0.2634 REMARK 3 S21: 0.5856 S22: -0.5129 S23: 0.0133 REMARK 3 S31: -0.1939 S32: -0.5367 S33: -0.3794 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 17 REMARK 3 ORIGIN FOR THE GROUP (A): 26.9696 29.0094 16.3515 REMARK 3 T TENSOR REMARK 3 T11: 0.1200 T22: 0.1391 REMARK 3 T33: 0.1342 T12: -0.0041 REMARK 3 T13: -0.0046 T23: -0.0379 REMARK 3 L TENSOR REMARK 3 L11: 0.0418 L22: 0.0670 REMARK 3 L33: 0.2932 L12: 0.0567 REMARK 3 L13: 0.0693 L23: -0.1595 REMARK 3 S TENSOR REMARK 3 S11: 0.0110 S12: 0.0598 S13: -0.0708 REMARK 3 S21: -0.1001 S22: 0.0231 S23: -0.1654 REMARK 3 S31: -0.1092 S32: 0.1367 S33: -0.0005 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 18 H 52 REMARK 3 ORIGIN FOR THE GROUP (A): 17.6642 25.9958 10.0514 REMARK 3 T TENSOR REMARK 3 T11: 0.1007 T22: 0.1027 REMARK 3 T33: 0.0777 T12: -0.0202 REMARK 3 T13: 0.0094 T23: -0.0255 REMARK 3 L TENSOR REMARK 3 L11: 0.5768 L22: 0.5891 REMARK 3 L33: 0.0842 L12: 0.6041 REMARK 3 L13: 0.3033 L23: 0.1075 REMARK 3 S TENSOR REMARK 3 S11: -0.0792 S12: 0.0154 S13: -0.0814 REMARK 3 S21: -0.1700 S22: 0.0875 S23: -0.0522 REMARK 3 S31: -0.1018 S32: 0.1209 S33: -0.0415 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 53 H 67 REMARK 3 ORIGIN FOR THE GROUP (A): 14.4845 35.6314 5.7155 REMARK 3 T TENSOR REMARK 3 T11: 0.2324 T22: 0.1235 REMARK 3 T33: 0.1209 T12: -0.0434 REMARK 3 T13: -0.0558 T23: 0.0208 REMARK 3 L TENSOR REMARK 3 L11: 0.4172 L22: 0.1509 REMARK 3 L33: 0.0528 L12: 0.1501 REMARK 3 L13: 0.0998 L23: -0.0667 REMARK 3 S TENSOR REMARK 3 S11: -0.2113 S12: 0.1608 S13: 0.2328 REMARK 3 S21: -0.2469 S22: 0.1523 S23: 0.2347 REMARK 3 S31: 0.0901 S32: -0.0364 S33: 0.0266 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 68 H 91 REMARK 3 ORIGIN FOR THE GROUP (A): 23.5010 32.5036 8.9887 REMARK 3 T TENSOR REMARK 3 T11: 0.1624 T22: 0.1372 REMARK 3 T33: 0.1078 T12: -0.0563 REMARK 3 T13: 0.0585 T23: -0.0335 REMARK 3 L TENSOR REMARK 3 L11: 0.3404 L22: 0.2260 REMARK 3 L33: 0.6458 L12: 0.2778 REMARK 3 L13: 0.2489 L23: -0.3349 REMARK 3 S TENSOR REMARK 3 S11: -0.2535 S12: 0.1262 S13: -0.0565 REMARK 3 S21: -0.2215 S22: 0.0419 S23: -0.1213 REMARK 3 S31: -0.2007 S32: 0.1978 S33: -0.2839 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 92 H 122 REMARK 3 ORIGIN FOR THE GROUP (A): 20.5722 25.3004 18.0129 REMARK 3 T TENSOR REMARK 3 T11: 0.0783 T22: 0.0868 REMARK 3 T33: 0.0801 T12: -0.0057 REMARK 3 T13: 0.0060 T23: -0.0045 REMARK 3 L TENSOR REMARK 3 L11: 0.2718 L22: -0.0343 REMARK 3 L33: 0.2143 L12: -0.1874 REMARK 3 L13: 0.1853 L23: -0.1507 REMARK 3 S TENSOR REMARK 3 S11: -0.0397 S12: 0.0333 S13: -0.0273 REMARK 3 S21: -0.0514 S22: 0.0162 S23: -0.0554 REMARK 3 S31: -0.0645 S32: 0.0380 S33: -0.0803 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 123 H 148 REMARK 3 ORIGIN FOR THE GROUP (A): 29.0104 20.8772 47.4078 REMARK 3 T TENSOR REMARK 3 T11: 0.1251 T22: 0.0980 REMARK 3 T33: 0.1350 T12: 0.0058 REMARK 3 T13: 0.0110 T23: 0.0205 REMARK 3 L TENSOR REMARK 3 L11: 0.0729 L22: 0.0478 REMARK 3 L33: 0.0817 L12: 0.0317 REMARK 3 L13: 0.0390 L23: 0.0738 REMARK 3 S TENSOR REMARK 3 S11: -0.0098 S12: -0.0674 S13: -0.1146 REMARK 3 S21: 0.2165 S22: 0.0012 S23: -0.0412 REMARK 3 S31: -0.1007 S32: 0.0586 S33: 0.0005 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 149 H 191 REMARK 3 ORIGIN FOR THE GROUP (A): 26.2445 19.5047 40.2954 REMARK 3 T TENSOR REMARK 3 T11: 0.0913 T22: 0.0766 REMARK 3 T33: 0.1270 T12: -0.0021 REMARK 3 T13: 0.0037 T23: 0.0004 REMARK 3 L TENSOR REMARK 3 L11: 0.1961 L22: 0.2444 REMARK 3 L33: 0.4252 L12: 0.2812 REMARK 3 L13: -0.2697 L23: -0.1351 REMARK 3 S TENSOR REMARK 3 S11: -0.0218 S12: 0.0317 S13: -0.0446 REMARK 3 S21: -0.0049 S22: 0.0327 S23: 0.0091 REMARK 3 S31: 0.0230 S32: -0.0324 S33: 0.0132 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 192 H 206 REMARK 3 ORIGIN FOR THE GROUP (A): 34.2774 14.5115 41.7255 REMARK 3 T TENSOR REMARK 3 T11: 0.1036 T22: 0.1144 REMARK 3 T33: 0.1776 T12: 0.0155 REMARK 3 T13: 0.0197 T23: 0.0227 REMARK 3 L TENSOR REMARK 3 L11: 0.1103 L22: 0.0749 REMARK 3 L33: 0.0117 L12: 0.2311 REMARK 3 L13: 0.0695 L23: 0.0231 REMARK 3 S TENSOR REMARK 3 S11: 0.0295 S12: -0.0189 S13: -0.1638 REMARK 3 S21: -0.1676 S22: -0.1375 S23: -0.1427 REMARK 3 S31: 0.2042 S32: 0.2280 S33: 0.0008 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 207 H 216 REMARK 3 ORIGIN FOR THE GROUP (A): 37.3701 17.5085 43.4002 REMARK 3 T TENSOR REMARK 3 T11: 0.1089 T22: 0.1837 REMARK 3 T33: 0.1852 T12: 0.0025 REMARK 3 T13: 0.0088 T23: 0.0548 REMARK 3 L TENSOR REMARK 3 L11: 0.0487 L22: 0.0779 REMARK 3 L33: 0.0649 L12: -0.0262 REMARK 3 L13: -0.0528 L23: -0.0264 REMARK 3 S TENSOR REMARK 3 S11: -0.0191 S12: -0.1460 S13: -0.3020 REMARK 3 S21: 0.0874 S22: -0.1210 S23: -0.2547 REMARK 3 S31: -0.1048 S32: 0.2226 S33: 0.0149 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 25 REMARK 3 ORIGIN FOR THE GROUP (A): -2.9821 21.9195 25.9221 REMARK 3 T TENSOR REMARK 3 T11: 0.1083 T22: 0.1153 REMARK 3 T33: 0.1043 T12: 0.0165 REMARK 3 T13: 0.0130 T23: 0.0180 REMARK 3 L TENSOR REMARK 3 L11: 0.0067 L22: -0.0293 REMARK 3 L33: 0.2460 L12: -0.0147 REMARK 3 L13: 0.1907 L23: -0.0648 REMARK 3 S TENSOR REMARK 3 S11: 0.0240 S12: -0.0836 S13: -0.0064 REMARK 3 S21: 0.1453 S22: 0.0509 S23: 0.0409 REMARK 3 S31: -0.1556 S32: -0.0991 S33: 0.0133 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 26 L 38 REMARK 3 ORIGIN FOR THE GROUP (A): -6.1373 25.3886 5.7619 REMARK 3 T TENSOR REMARK 3 T11: 0.1449 T22: 0.1152 REMARK 3 T33: 0.0788 T12: 0.0185 REMARK 3 T13: -0.0298 T23: 0.0031 REMARK 3 L TENSOR REMARK 3 L11: 0.0669 L22: 0.0447 REMARK 3 L33: 0.1032 L12: -0.0051 REMARK 3 L13: 0.0736 L23: -0.0343 REMARK 3 S TENSOR REMARK 3 S11: 0.0074 S12: 0.1866 S13: 0.0386 REMARK 3 S21: -0.2712 S22: -0.0165 S23: 0.0709 REMARK 3 S31: -0.1633 S32: -0.0475 S33: 0.0130 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 39 L 54 REMARK 3 ORIGIN FOR THE GROUP (A): 7.9649 18.0142 19.1442 REMARK 3 T TENSOR REMARK 3 T11: 0.0785 T22: 0.1100 REMARK 3 T33: 0.0813 T12: 0.0086 REMARK 3 T13: -0.0094 T23: 0.0109 REMARK 3 L TENSOR REMARK 3 L11: 0.1199 L22: 0.0971 REMARK 3 L33: 0.1506 L12: -0.0452 REMARK 3 L13: -0.1837 L23: 0.1014 REMARK 3 S TENSOR REMARK 3 S11: -0.0028 S12: -0.1314 S13: 0.0254 REMARK 3 S21: 0.0102 S22: 0.0308 S23: -0.0343 REMARK 3 S31: -0.0828 S32: 0.1086 S33: 0.0302 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 55 L 81 REMARK 3 ORIGIN FOR THE GROUP (A): -2.9917 15.3454 15.9600 REMARK 3 T TENSOR REMARK 3 T11: 0.1056 T22: 0.1035 REMARK 3 T33: 0.0973 T12: 0.0149 REMARK 3 T13: -0.0055 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 0.2766 L22: 0.1399 REMARK 3 L33: 0.3189 L12: 0.2513 REMARK 3 L13: -0.0882 L23: -0.0356 REMARK 3 S TENSOR REMARK 3 S11: -0.0060 S12: -0.0467 S13: -0.1075 REMARK 3 S21: -0.0182 S22: 0.0073 S23: 0.0555 REMARK 3 S31: 0.0886 S32: -0.0472 S33: -0.0171 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 82 L 119 REMARK 3 ORIGIN FOR THE GROUP (A): 3.7295 19.6858 25.4952 REMARK 3 T TENSOR REMARK 3 T11: 0.0729 T22: 0.1092 REMARK 3 T33: 0.0852 T12: 0.0109 REMARK 3 T13: 0.0024 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: -0.0369 L22: 0.1753 REMARK 3 L33: 0.3834 L12: 0.2080 REMARK 3 L13: -0.1016 L23: 0.0446 REMARK 3 S TENSOR REMARK 3 S11: 0.0117 S12: -0.0394 S13: 0.0091 REMARK 3 S21: -0.0127 S22: -0.0352 S23: 0.0532 REMARK 3 S31: -0.0003 S32: 0.0317 S33: -0.1009 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9ECI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289670. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JAN-20 REMARK 200 TEMPERATURE (KELVIN) : 292.15 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R 200K-A REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70587 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60 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 (%): 54.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, TRIS, PH REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.11850 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.67150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.11850 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.67150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: 19580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 690 LIES ON A SPECIAL POSITION. 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 H 131 REMARK 465 LYS H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 LYS H 217 REMARK 465 SER H 218 REMARK 465 CYS H 219 REMARK 465 CYS L 220 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 99 -176.46 61.82 REMARK 500 THR H 100 -71.54 -89.01 REMARK 500 PHE H 101 24.61 -141.33 REMARK 500 PHE H 103 75.35 -160.60 REMARK 500 ALA L 57 -33.33 67.71 REMARK 500 ASN L 144 66.79 62.01 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 639 DISTANCE = 5.83 ANGSTROMS REMARK 525 HOH H 640 DISTANCE = 6.35 ANGSTROMS REMARK 525 HOH H 641 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH H 642 DISTANCE = 6.54 ANGSTROMS DBREF 9ECI H 1 219 PDB 9ECI 9ECI 1 219 DBREF 9ECI L 1 220 PDB 9ECI 9ECI 1 220 SEQRES 1 H 219 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 219 THR GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 219 TYR THR PHE THR ASP HIS ALA ILE HIS TRP VAL ARG GLN SEQRES 4 H 219 ALA PRO GLY GLN ALA LEU GLU TRP MET GLY HIS PHE SER SEQRES 5 H 219 PRO GLY ASN THR ASP ILE LYS TYR ASN ASP LYS PHE LYS SEQRES 6 H 219 GLY ARG VAL THR LEU THR VAL ASP ARG SER MET SER THR SEQRES 7 H 219 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 219 ALA MET TYR TYR CYS LYS THR SER THR PHE PHE PHE ASP SEQRES 9 H 219 TYR TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA SEQRES 10 H 219 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 219 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 219 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 219 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 219 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 219 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 219 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 219 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 220 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU ASN SER GLY ASP GLN LYS ASN TYR LEU SEQRES 4 L 220 THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 L 220 TYR TYR CYS GLN ASN ASP TYR SER TYR PRO LEU THR PHE SEQRES 9 L 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET MPD L 301 8 HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL FORMUL 3 MPD C6 H14 O2 FORMUL 4 HOH *738(H2 O) HELIX 1 AA1 THR H 28 HIS H 32 5 5 HELIX 2 AA2 ARG H 74 MET H 76 5 3 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 SER H 159 ALA H 161 5 3 HELIX 5 AA5 SER H 190 LEU H 192 5 3 HELIX 6 AA6 LYS H 204 ASN H 207 5 4 HELIX 7 AA7 GLN L 85 VAL L 89 5 5 HELIX 8 AA8 SER L 127 LYS L 132 1 6 HELIX 9 AA9 LYS L 189 HIS L 195 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 110 VAL H 114 1 O THR H 113 N GLU H 10 SHEET 3 AA2 6 ALA H 92 THR H 98 -1 N TYR H 94 O THR H 110 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 GLU H 46 PHE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 ILE H 58 TYR H 60 -1 O LYS H 59 N HIS H 50 SHEET 1 AA3 4 SER H 123 LEU H 127 0 SHEET 2 AA3 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA3 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145 SHEET 4 AA3 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AA4 4 SER H 123 LEU H 127 0 SHEET 2 AA4 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA4 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145 SHEET 4 AA4 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AA5 3 THR H 154 TRP H 157 0 SHEET 2 AA5 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AA5 3 THR H 208 LYS H 213 -1 O VAL H 210 N VAL H 201 SHEET 1 AA6 4 MET L 4 SER L 7 0 SHEET 2 AA6 4 ALA L 19 SER L 25 -1 O ASN L 22 N SER L 7 SHEET 3 AA6 4 ASP L 76 ILE L 81 -1 O PHE L 77 N CYS L 23 SHEET 4 AA6 4 PHE L 68 SER L 73 -1 N SER L 69 O THR L 80 SHEET 1 AA7 6 SER L 10 SER L 14 0 SHEET 2 AA7 6 THR L 108 LYS L 113 1 O LYS L 109 N LEU L 11 SHEET 3 AA7 6 ALA L 90 ASN L 96 -1 N ALA L 90 O VAL L 110 SHEET 4 AA7 6 LEU L 39 GLN L 44 -1 N TYR L 42 O TYR L 93 SHEET 5 AA7 6 LYS L 51 TYR L 55 -1 O LEU L 53 N TRP L 41 SHEET 6 AA7 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AA8 4 SER L 10 SER L 14 0 SHEET 2 AA8 4 THR L 108 LYS L 113 1 O LYS L 109 N LEU L 11 SHEET 3 AA8 4 ALA L 90 ASN L 96 -1 N ALA L 90 O VAL L 110 SHEET 4 AA8 4 THR L 103 PHE L 104 -1 O THR L 103 N ASN L 96 SHEET 1 AA9 4 SER L 120 PHE L 124 0 SHEET 2 AA9 4 THR L 135 PHE L 145 -1 O ASN L 143 N SER L 120 SHEET 3 AA9 4 TYR L 179 SER L 188 -1 O LEU L 187 N ALA L 136 SHEET 4 AA9 4 SER L 165 VAL L 169 -1 N SER L 168 O SER L 182 SHEET 1 AB1 4 ALA L 159 LEU L 160 0 SHEET 2 AB1 4 LYS L 151 VAL L 156 -1 N VAL L 156 O ALA L 159 SHEET 3 AB1 4 VAL L 197 THR L 203 -1 O GLU L 201 N GLN L 153 SHEET 4 AB1 4 VAL L 211 ASN L 216 -1 O VAL L 211 N VAL L 202 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 2 CYS H 143 CYS H 199 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 94 1555 1555 2.08 SSBOND 4 CYS L 140 CYS L 200 1555 1555 2.04 CISPEP 1 PHE H 149 PRO H 150 0 -9.77 CISPEP 2 GLU H 151 PRO H 152 0 -2.00 CISPEP 3 SER L 7 PRO L 8 0 -6.89 CISPEP 4 SER L 7 PRO L 8 0 -2.77 CISPEP 5 TYR L 100 PRO L 101 0 -3.06 CISPEP 6 TYR L 146 PRO L 147 0 0.76 CRYST1 102.237 75.343 69.651 90.00 106.28 90.00 C 1 2 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 0.009781 0.000000 0.002857 0.00000 SCALE2 0.000000 0.013273 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014957 0.00000