HEADER VIRAL PROTEIN 29-JUN-23 8PN0 TITLE HEV GT3 P DOMAIN IN COMPLEX WITH GLYCAN-SENSITIVE NAB P60.12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB_P60.12-HC; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB_P60.12-LC; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CAPSID PROTEIN; COMPND 11 CHAIN: C, D, E, F; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2 CELLS; SOURCE 7 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMT; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER'S S2 CELLS; SOURCE 16 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PMT; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: PASLAHEPEVIRUS BALAYANI; SOURCE 21 ORGANISM_TAXID: 1678143; SOURCE 22 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER'S S2 CELLS; SOURCE 25 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PMT KEYWDS HEV, P DOMAIN, NON-GLYCOSYLATED, GLYCAN-SENSITIVE, NEUTRALIZING KEYWDS 2 ANTIBODY (NAB), VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.SSEBYATIKA,T.KREY JRNL AUTH G.SSEBYATIKA,K.DINKELBORG,L.J.STROEH,F.HINTE,L.CORNEILLIE, JRNL AUTH 2 L.HUEFFNER,E.M.GUZMAN,P.L.NANKYA,N.PLUECKEBAUM,S.PRALLET, JRNL AUTH 3 A.K.MEHNERT,L.VERHOYE,C.JUERGENS,E.STEINMANN,H.WEDEMEYER, JRNL AUTH 4 A.VIEJO-BORBOLLA,L.V.DAO THI,T.PIETSCHMANN,M.LUETGEHETMANN, JRNL AUTH 5 P.MEULEMAN,M.DANDRI,T.KREY,P.BEHRENDT JRNL TITL A NOVEL CLASS OF BROADLY NEUTRALIZING HEPATITIS E JRNL TITL 2 VIRUS-SPECIFIC HUMAN ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.07 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.4 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.24 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 84.8 REMARK 3 NUMBER OF REFLECTIONS : 77331 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 3868 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.11 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 31.62 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3892 REMARK 3 BIN FREE R VALUE : 0.3754 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10963 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 184 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.06430 REMARK 3 B22 (A**2) : -4.55450 REMARK 3 B33 (A**2) : 3.49020 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.00530 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.272 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.209 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.288 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.217 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 11236 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 15379 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 3584 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1859 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 11236 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1560 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 8274 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.01 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.79 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.09 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|2 - 31} REMARK 3 ORIGIN FOR THE GROUP (A): 27.1466 21.6587 21.5126 REMARK 3 T TENSOR REMARK 3 T11: -0.039 T22: 0.0368 REMARK 3 T33: -0.0365 T12: -0.0526 REMARK 3 T13: 0.0252 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 0.0081 L22: 1.2932 REMARK 3 L33: 0.0025 L12: 0.5781 REMARK 3 L13: -0.791 L23: 0.8409 REMARK 3 S TENSOR REMARK 3 S11: 0.0419 S12: 0.0873 S13: -0.3875 REMARK 3 S21: 0.0873 S22: -0.1057 S23: 0.284 REMARK 3 S31: -0.3875 S32: 0.284 S33: 0.0638 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {A|32 - 121} REMARK 3 ORIGIN FOR THE GROUP (A): 21.8682 15.5841 19.0406 REMARK 3 T TENSOR REMARK 3 T11: -0.0115 T22: 0.0533 REMARK 3 T33: -0.0696 T12: -0.0165 REMARK 3 T13: 0.0101 T23: 0.0068 REMARK 3 L TENSOR REMARK 3 L11: 1.1145 L22: 0 REMARK 3 L33: 0.4402 L12: -0.3396 REMARK 3 L13: 0.3254 L23: -0.7159 REMARK 3 S TENSOR REMARK 3 S11: 0.0868 S12: -0.0199 S13: -0.0768 REMARK 3 S21: -0.0199 S22: -0.1092 S23: 0.1326 REMARK 3 S31: -0.0768 S32: 0.1326 S33: 0.0224 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: {A|122 - 176} REMARK 3 ORIGIN FOR THE GROUP (A): 53.6471 10.1159 3.7651 REMARK 3 T TENSOR REMARK 3 T11: -0.0787 T22: 0.2846 REMARK 3 T33: -0.2221 T12: -0.0803 REMARK 3 T13: 0.0387 T23: 0.1517 REMARK 3 L TENSOR REMARK 3 L11: 0.7598 L22: 0 REMARK 3 L33: 2.1646 L12: -1.5289 REMARK 3 L13: 2.1428 L23: -0.9602 REMARK 3 S TENSOR REMARK 3 S11: -0.0386 S12: 0.1301 S13: 0.3723 REMARK 3 S21: 0.1301 S22: 0.4188 S23: -0.1096 REMARK 3 S31: 0.3723 S32: -0.1096 S33: -0.3802 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: {A|177 - 224} REMARK 3 ORIGIN FOR THE GROUP (A): 57.1486 9.9032 2.5627 REMARK 3 T TENSOR REMARK 3 T11: -0.1538 T22: 0.1805 REMARK 3 T33: -0.1346 T12: -0.0411 REMARK 3 T13: -0.0324 T23: 0.0637 REMARK 3 L TENSOR REMARK 3 L11: 3.6822 L22: 0 REMARK 3 L33: 3.1556 L12: -0.653 REMARK 3 L13: -0.7613 L23: -1.0549 REMARK 3 S TENSOR REMARK 3 S11: 0.0497 S12: 0.3594 S13: 0.2388 REMARK 3 S21: 0.3594 S22: 0.2375 S23: 0.1578 REMARK 3 S31: 0.2388 S32: 0.1578 S33: -0.2872 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: {B|3 - 76} REMARK 3 ORIGIN FOR THE GROUP (A): 14.4805 12.1951 -0.6886 REMARK 3 T TENSOR REMARK 3 T11: -0.0012 T22: 0.0556 REMARK 3 T33: -0.0861 T12: 0.0703 REMARK 3 T13: 0.0043 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: -0.0038 L22: 0 REMARK 3 L33: 1.6548 L12: -0.3406 REMARK 3 L13: 0.5162 L23: -0.5912 REMARK 3 S TENSOR REMARK 3 S11: 0.2093 S12: 0.1009 S13: 0.2224 REMARK 3 S21: 0.1009 S22: -0.1428 S23: 0.186 REMARK 3 S31: 0.2224 S32: 0.186 S33: -0.0666 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: {B|77 - 123} REMARK 3 ORIGIN FOR THE GROUP (A): 25.468 9.0938 -2.5933 REMARK 3 T TENSOR REMARK 3 T11: -0.0137 T22: 0.1509 REMARK 3 T33: -0.1262 T12: 0.1511 REMARK 3 T13: -0.0312 T23: -0.0111 REMARK 3 L TENSOR REMARK 3 L11: 0.0037 L22: 0 REMARK 3 L33: 1.0323 L12: -1.2468 REMARK 3 L13: -0.5016 L23: 0.2183 REMARK 3 S TENSOR REMARK 3 S11: 0.3616 S12: 0.042 S13: 0.2267 REMARK 3 S21: 0.042 S22: -0.1814 S23: 0.2707 REMARK 3 S31: 0.2267 S32: 0.2707 S33: -0.1802 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: {B|124 - 186} REMARK 3 ORIGIN FOR THE GROUP (A): 45.5836 -0.7304 -1.2558 REMARK 3 T TENSOR REMARK 3 T11: -0.1592 T22: 0.1152 REMARK 3 T33: -0.0924 T12: 0.0685 REMARK 3 T13: -0.1522 T23: 0.1522 REMARK 3 L TENSOR REMARK 3 L11: 2.3939 L22: 0.2143 REMARK 3 L33: 2.8755 L12: -0.8007 REMARK 3 L13: 1.8218 L23: -1.4197 REMARK 3 S TENSOR REMARK 3 S11: 0.1156 S12: 0.2932 S13: -0.2279 REMARK 3 S21: 0.2932 S22: 0.3174 S23: -0.145 REMARK 3 S31: -0.2279 S32: -0.145 S33: -0.4331 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: {B|187 - 216} REMARK 3 ORIGIN FOR THE GROUP (A): 48.5678 -10.0617 -3.8901 REMARK 3 T TENSOR REMARK 3 T11: -0.0725 T22: 0.0305 REMARK 3 T33: 0.0403 T12: 0.1518 REMARK 3 T13: -0.1524 T23: 0.0627 REMARK 3 L TENSOR REMARK 3 L11: 0.9107 L22: 0 REMARK 3 L33: 0.0213 L12: 1.9555 REMARK 3 L13: 2.9137 L23: 1.7251 REMARK 3 S TENSOR REMARK 3 S11: -0.0656 S12: 0.1432 S13: 0.5441 REMARK 3 S21: 0.1432 S22: 0.0859 S23: 0.0509 REMARK 3 S31: 0.5441 S32: 0.0509 S33: -0.0204 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: {E|459 - 604} REMARK 3 ORIGIN FOR THE GROUP (A): -14.0351 29.2917 3.0167 REMARK 3 T TENSOR REMARK 3 T11: -0.0026 T22: 0.0276 REMARK 3 T33: -0.0515 T12: 0.0133 REMARK 3 T13: 0.0163 T23: 0.1064 REMARK 3 L TENSOR REMARK 3 L11: 0.4095 L22: 0.4604 REMARK 3 L33: 0.4822 L12: -0.3686 REMARK 3 L13: -0.0192 L23: -0.2378 REMARK 3 S TENSOR REMARK 3 S11: -0.0694 S12: 0.0369 S13: 0.0044 REMARK 3 S21: 0.0369 S22: 0.1085 S23: -0.0741 REMARK 3 S31: 0.0044 S32: -0.0741 S33: -0.0391 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: {F|459 - 604} REMARK 3 ORIGIN FOR THE GROUP (A): -10.463 15.6435 23.02 REMARK 3 T TENSOR REMARK 3 T11: 0.0241 T22: -0.0291 REMARK 3 T33: -0.03 T12: -0.0031 REMARK 3 T13: 0.0036 T23: 0.0495 REMARK 3 L TENSOR REMARK 3 L11: 1.0353 L22: 0.0963 REMARK 3 L33: 0.2482 L12: 0.1768 REMARK 3 L13: -0.3374 L23: -0.0787 REMARK 3 S TENSOR REMARK 3 S11: 0.0368 S12: -0.0139 S13: -0.015 REMARK 3 S21: -0.0139 S22: 0.0165 S23: -0.0237 REMARK 3 S31: -0.015 S32: -0.0237 S33: -0.0533 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: {C|459 - 604} REMARK 3 ORIGIN FOR THE GROUP (A): -17.1864 -28.7555 42.6005 REMARK 3 T TENSOR REMARK 3 T11: 0.0316 T22: -0.0296 REMARK 3 T33: -0.0279 T12: -0.0406 REMARK 3 T13: 0.0207 T23: 0.008 REMARK 3 L TENSOR REMARK 3 L11: 0.1264 L22: 0 REMARK 3 L33: 0.9933 L12: 0.3548 REMARK 3 L13: -0.0632 L23: -0.1714 REMARK 3 S TENSOR REMARK 3 S11: -0.1146 S12: -0.012 S13: 0.1605 REMARK 3 S21: -0.012 S22: 0.0804 S23: -0.1651 REMARK 3 S31: 0.1605 S32: -0.1651 S33: 0.0342 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: {D|459 - 604} REMARK 3 ORIGIN FOR THE GROUP (A): -13.7332 -14.8586 22.7127 REMARK 3 T TENSOR REMARK 3 T11: -0.0077 T22: 0.0224 REMARK 3 T33: -0.0414 T12: -0.0437 REMARK 3 T13: 0.0175 T23: 0.0052 REMARK 3 L TENSOR REMARK 3 L11: 0.6358 L22: 0.2176 REMARK 3 L33: 0.2334 L12: -0.0284 REMARK 3 L13: 0.1049 L23: -0.2246 REMARK 3 S TENSOR REMARK 3 S11: -0.1187 S12: 0.0313 S13: 0.0753 REMARK 3 S21: 0.0313 S22: 0.0723 S23: -0.071 REMARK 3 S31: 0.0753 S32: -0.071 S33: 0.0464 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: {H|2 - 45} REMARK 3 ORIGIN FOR THE GROUP (A): 22.7362 -18.5327 26.6127 REMARK 3 T TENSOR REMARK 3 T11: -0.0225 T22: -0.0321 REMARK 3 T33: 0.0194 T12: 0.0131 REMARK 3 T13: 0.044 T23: 0.0009 REMARK 3 L TENSOR REMARK 3 L11: 1.115 L22: 0.2242 REMARK 3 L33: 0.5453 L12: 0.5586 REMARK 3 L13: 0.6504 L23: 0.1872 REMARK 3 S TENSOR REMARK 3 S11: -0.0481 S12: 0.098 S13: 0.0834 REMARK 3 S21: 0.098 S22: -0.0933 S23: 0.0791 REMARK 3 S31: 0.0834 S32: 0.0791 S33: 0.1414 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: {H|46 - 83} REMARK 3 ORIGIN FOR THE GROUP (A): 16.6289 -14.9716 20.6901 REMARK 3 T TENSOR REMARK 3 T11: -0.0135 T22: 0.0215 REMARK 3 T33: -0.0473 T12: 0.0029 REMARK 3 T13: 0.0521 T23: -0.0005 REMARK 3 L TENSOR REMARK 3 L11: 1.0542 L22: 1.8324 REMARK 3 L33: 0.066 L12: 0.1072 REMARK 3 L13: -0.0686 L23: -0.6248 REMARK 3 S TENSOR REMARK 3 S11: 0.0773 S12: -0.0089 S13: 0.085 REMARK 3 S21: -0.0089 S22: -0.0153 S23: -0.2392 REMARK 3 S31: 0.085 S32: -0.2392 S33: -0.062 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: {H|84 - 156} REMARK 3 ORIGIN FOR THE GROUP (A): 32.9436 -11.8412 34.4852 REMARK 3 T TENSOR REMARK 3 T11: -0.0015 T22: 0.0221 REMARK 3 T33: -0.0462 T12: 0.0137 REMARK 3 T13: 0.0302 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 0.7755 L22: 0 REMARK 3 L33: 0.0074 L12: -0.0694 REMARK 3 L13: 0.0591 L23: 0.0472 REMARK 3 S TENSOR REMARK 3 S11: -0.0966 S12: -0.0033 S13: 0.046 REMARK 3 S21: -0.0033 S22: 0.0537 S23: 0.0854 REMARK 3 S31: 0.046 S32: 0.0854 S33: 0.0429 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: {H|157 - 224} REMARK 3 ORIGIN FOR THE GROUP (A): 53.187 -10.767 44.6614 REMARK 3 T TENSOR REMARK 3 T11: -0.0619 T22: 0.0517 REMARK 3 T33: -0.0444 T12: 0.0548 REMARK 3 T13: 0.0228 T23: 0.0125 REMARK 3 L TENSOR REMARK 3 L11: 0.544 L22: 0.0392 REMARK 3 L33: 2.4127 L12: 0.4184 REMARK 3 L13: 0.4784 L23: -0.9869 REMARK 3 S TENSOR REMARK 3 S11: -0.1421 S12: 0.0377 S13: 0.044 REMARK 3 S21: 0.0377 S22: 0.1816 S23: -0.0478 REMARK 3 S31: 0.044 S32: -0.0478 S33: -0.0395 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: {L|3 - 68} REMARK 3 ORIGIN FOR THE GROUP (A): 11.8755 -12.0996 46.0858 REMARK 3 T TENSOR REMARK 3 T11: 0.0008 T22: -0.028 REMARK 3 T33: -0.0164 T12: 0.0252 REMARK 3 T13: 0.013 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 0.6159 L22: 0.2421 REMARK 3 L33: 1.1111 L12: 0.2212 REMARK 3 L13: 0.7711 L23: -0.0012 REMARK 3 S TENSOR REMARK 3 S11: -0.0054 S12: -0.0374 S13: -0.0459 REMARK 3 S21: -0.0374 S22: -0.0779 S23: -0.0503 REMARK 3 S31: -0.0459 S32: -0.0503 S33: 0.0833 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: {L|69 - 110} REMARK 3 ORIGIN FOR THE GROUP (A): 14.5542 -9.5018 44.9231 REMARK 3 T TENSOR REMARK 3 T11: -0.0097 T22: -0.005 REMARK 3 T33: -0.0098 T12: 0.02 REMARK 3 T13: 0.019 T23: 0.0004 REMARK 3 L TENSOR REMARK 3 L11: 0.5793 L22: 0 REMARK 3 L33: 0.0026 L12: 0.9678 REMARK 3 L13: 0.3543 L23: 0.7778 REMARK 3 S TENSOR REMARK 3 S11: -0.0704 S12: 0.0595 S13: -0.216 REMARK 3 S21: 0.0595 S22: 0.0179 S23: 0.147 REMARK 3 S31: -0.216 S32: 0.147 S33: 0.0525 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: {L|111 - 161} REMARK 3 ORIGIN FOR THE GROUP (A): 44.0581 2.0257 49.8942 REMARK 3 T TENSOR REMARK 3 T11: -0.0477 T22: 0.0199 REMARK 3 T33: 0.0062 T12: 0.0173 REMARK 3 T13: 0.062 T23: 0.0368 REMARK 3 L TENSOR REMARK 3 L11: 2.004 L22: 0.0575 REMARK 3 L33: 0.7289 L12: 0.85 REMARK 3 L13: -0.8755 L23: -0.584 REMARK 3 S TENSOR REMARK 3 S11: 0.0602 S12: 0.1185 S13: 0.0561 REMARK 3 S21: 0.1185 S22: -0.0114 S23: -0.0544 REMARK 3 S31: 0.0561 S32: -0.0544 S33: -0.0488 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: {L|162 - 216} REMARK 3 ORIGIN FOR THE GROUP (A): 44.057 4.16 49.2203 REMARK 3 T TENSOR REMARK 3 T11: -0.0806 T22: -0.0394 REMARK 3 T33: 0.0203 T12: 0.0374 REMARK 3 T13: 0.0624 T23: 0.0644 REMARK 3 L TENSOR REMARK 3 L11: 2.5995 L22: 0.0069 REMARK 3 L33: 1.9581 L12: 0.9669 REMARK 3 L13: -2.1237 L23: -0.7808 REMARK 3 S TENSOR REMARK 3 S11: 0.2258 S12: 0.0976 S13: -0.0593 REMARK 3 S21: 0.0976 S22: 0.0906 S23: -0.2403 REMARK 3 S31: -0.0593 S32: -0.2403 S33: -0.3164 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8PN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292131532. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-NOV-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.999987 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 : POINTLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77331 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.072 REMARK 200 RESOLUTION RANGE LOW (A) : 47.240 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.8 REMARK 200 DATA REDUNDANCY : 3.270 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG 4000, 0.2M CALCIUM REMARK 280 CHLORIDE AND 0.1M TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 47.24000 REMARK 290 SMTRY3 2 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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 GLN A 1 REMARK 465 SER A 136 REMARK 465 SER A 137 REMARK 465 LYS A 138 REMARK 465 SER A 139 REMARK 465 THR A 140 REMARK 465 SER A 141 REMARK 465 GLY A 142 REMARK 465 GLY A 143 REMARK 465 LYS A 223 REMARK 465 SER A 224 REMARK 465 CYS A 225 REMARK 465 ASP A 226 REMARK 465 LYS A 227 REMARK 465 THR A 228 REMARK 465 ASP A 229 REMARK 465 ASP A 230 REMARK 465 ASP A 231 REMARK 465 ASP A 232 REMARK 465 LYS A 233 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 CYS B 216 REMARK 465 SER B 217 REMARK 465 GLY C 450 REMARK 465 ASP C 451 REMARK 465 ASP C 452 REMARK 465 ASP C 453 REMARK 465 ASP C 454 REMARK 465 LYS C 455 REMARK 465 PRO C 456 REMARK 465 LEU C 607 REMARK 465 ALA C 608 REMARK 465 VAL C 609 REMARK 465 LEU C 610 REMARK 465 GLU C 611 REMARK 465 ASP C 612 REMARK 465 THR C 613 REMARK 465 THR C 614 REMARK 465 ASP C 615 REMARK 465 TYR C 616 REMARK 465 PRO C 617 REMARK 465 ALA C 618 REMARK 465 ARG C 619 REMARK 465 ALA C 620 REMARK 465 HIS C 621 REMARK 465 THR C 622 REMARK 465 PHE C 623 REMARK 465 ASP C 624 REMARK 465 ASP C 625 REMARK 465 PHE C 626 REMARK 465 CYS C 627 REMARK 465 PRO C 628 REMARK 465 GLU C 629 REMARK 465 CYS C 630 REMARK 465 ARG C 631 REMARK 465 THR C 632 REMARK 465 LEU C 633 REMARK 465 GLY C 634 REMARK 465 LEU C 635 REMARK 465 GLN C 636 REMARK 465 GLY C 637 REMARK 465 CYS C 638 REMARK 465 ALA C 639 REMARK 465 PHE C 640 REMARK 465 GLN C 641 REMARK 465 SER C 642 REMARK 465 THR C 643 REMARK 465 ILE C 644 REMARK 465 ALA C 645 REMARK 465 GLU C 646 REMARK 465 LEU C 647 REMARK 465 GLN C 648 REMARK 465 ARG C 649 REMARK 465 LEU C 650 REMARK 465 LYS C 651 REMARK 465 MET C 652 REMARK 465 LYS C 653 REMARK 465 VAL C 654 REMARK 465 GLY C 655 REMARK 465 LYS C 656 REMARK 465 THR C 657 REMARK 465 ARG C 658 REMARK 465 GLU C 659 REMARK 465 SER C 660 REMARK 465 GLY D 450 REMARK 465 ASP D 451 REMARK 465 ASP D 452 REMARK 465 ASP D 453 REMARK 465 ASP D 454 REMARK 465 LYS D 455 REMARK 465 PRO D 456 REMARK 465 LEU D 610 REMARK 465 GLU D 611 REMARK 465 ASP D 612 REMARK 465 THR D 613 REMARK 465 THR D 614 REMARK 465 ASP D 615 REMARK 465 TYR D 616 REMARK 465 PRO D 617 REMARK 465 ALA D 618 REMARK 465 ARG D 619 REMARK 465 ALA D 620 REMARK 465 HIS D 621 REMARK 465 THR D 622 REMARK 465 PHE D 623 REMARK 465 ASP D 624 REMARK 465 ASP D 625 REMARK 465 PHE D 626 REMARK 465 CYS D 627 REMARK 465 PRO D 628 REMARK 465 GLU D 629 REMARK 465 CYS D 630 REMARK 465 ARG D 631 REMARK 465 THR D 632 REMARK 465 LEU D 633 REMARK 465 GLY D 634 REMARK 465 LEU D 635 REMARK 465 GLN D 636 REMARK 465 GLY D 637 REMARK 465 CYS D 638 REMARK 465 ALA D 639 REMARK 465 PHE D 640 REMARK 465 GLN D 641 REMARK 465 SER D 642 REMARK 465 THR D 643 REMARK 465 ILE D 644 REMARK 465 ALA D 645 REMARK 465 GLU D 646 REMARK 465 LEU D 647 REMARK 465 GLN D 648 REMARK 465 ARG D 649 REMARK 465 LEU D 650 REMARK 465 LYS D 651 REMARK 465 MET D 652 REMARK 465 LYS D 653 REMARK 465 VAL D 654 REMARK 465 GLY D 655 REMARK 465 LYS D 656 REMARK 465 THR D 657 REMARK 465 ARG D 658 REMARK 465 GLU D 659 REMARK 465 SER D 660 REMARK 465 GLY E 450 REMARK 465 ASP E 451 REMARK 465 ASP E 452 REMARK 465 ASP E 453 REMARK 465 ASP E 454 REMARK 465 LYS E 455 REMARK 465 PRO E 456 REMARK 465 ALA E 457 REMARK 465 PRO E 458 REMARK 465 LEU E 607 REMARK 465 ALA E 608 REMARK 465 VAL E 609 REMARK 465 LEU E 610 REMARK 465 GLU E 611 REMARK 465 ASP E 612 REMARK 465 THR E 613 REMARK 465 THR E 614 REMARK 465 ASP E 615 REMARK 465 TYR E 616 REMARK 465 PRO E 617 REMARK 465 ALA E 618 REMARK 465 ARG E 619 REMARK 465 ALA E 620 REMARK 465 HIS E 621 REMARK 465 THR E 622 REMARK 465 PHE E 623 REMARK 465 ASP E 624 REMARK 465 ASP E 625 REMARK 465 PHE E 626 REMARK 465 CYS E 627 REMARK 465 PRO E 628 REMARK 465 GLU E 629 REMARK 465 CYS E 630 REMARK 465 ARG E 631 REMARK 465 THR E 632 REMARK 465 LEU E 633 REMARK 465 GLY E 634 REMARK 465 LEU E 635 REMARK 465 GLN E 636 REMARK 465 GLY E 637 REMARK 465 CYS E 638 REMARK 465 ALA E 639 REMARK 465 PHE E 640 REMARK 465 GLN E 641 REMARK 465 SER E 642 REMARK 465 THR E 643 REMARK 465 ILE E 644 REMARK 465 ALA E 645 REMARK 465 GLU E 646 REMARK 465 LEU E 647 REMARK 465 GLN E 648 REMARK 465 ARG E 649 REMARK 465 LEU E 650 REMARK 465 LYS E 651 REMARK 465 MET E 652 REMARK 465 LYS E 653 REMARK 465 VAL E 654 REMARK 465 GLY E 655 REMARK 465 LYS E 656 REMARK 465 THR E 657 REMARK 465 ARG E 658 REMARK 465 GLU E 659 REMARK 465 SER E 660 REMARK 465 GLY F 450 REMARK 465 ASP F 451 REMARK 465 ASP F 452 REMARK 465 ASP F 453 REMARK 465 ASP F 454 REMARK 465 LYS F 455 REMARK 465 PRO F 456 REMARK 465 LEU F 610 REMARK 465 GLU F 611 REMARK 465 ASP F 612 REMARK 465 THR F 613 REMARK 465 THR F 614 REMARK 465 ASP F 615 REMARK 465 TYR F 616 REMARK 465 PRO F 617 REMARK 465 ALA F 618 REMARK 465 ARG F 619 REMARK 465 ALA F 620 REMARK 465 HIS F 621 REMARK 465 THR F 622 REMARK 465 PHE F 623 REMARK 465 ASP F 624 REMARK 465 ASP F 625 REMARK 465 PHE F 626 REMARK 465 CYS F 627 REMARK 465 PRO F 628 REMARK 465 GLU F 629 REMARK 465 CYS F 630 REMARK 465 ARG F 631 REMARK 465 THR F 632 REMARK 465 LEU F 633 REMARK 465 GLY F 634 REMARK 465 LEU F 635 REMARK 465 GLN F 636 REMARK 465 GLY F 637 REMARK 465 CYS F 638 REMARK 465 ALA F 639 REMARK 465 PHE F 640 REMARK 465 GLN F 641 REMARK 465 SER F 642 REMARK 465 THR F 643 REMARK 465 ILE F 644 REMARK 465 ALA F 645 REMARK 465 GLU F 646 REMARK 465 LEU F 647 REMARK 465 GLN F 648 REMARK 465 ARG F 649 REMARK 465 LEU F 650 REMARK 465 LYS F 651 REMARK 465 MET F 652 REMARK 465 LYS F 653 REMARK 465 VAL F 654 REMARK 465 GLY F 655 REMARK 465 LYS F 656 REMARK 465 THR F 657 REMARK 465 ARG F 658 REMARK 465 GLU F 659 REMARK 465 SER F 660 REMARK 465 GLN H 1 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 CYS H 225 REMARK 465 ASP H 226 REMARK 465 LYS H 227 REMARK 465 THR H 228 REMARK 465 ASP H 229 REMARK 465 ASP H 230 REMARK 465 ASP H 231 REMARK 465 ASP H 232 REMARK 465 LYS H 233 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 CYS L 216 REMARK 465 SER L 217 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 PHE A 29 -13.67 62.16 REMARK 500 THR A 57 108.97 -56.79 REMARK 500 SER A 98 -164.32 -100.06 REMARK 500 LEU A 102 -114.38 61.95 REMARK 500 ASP A 110 141.28 -177.03 REMARK 500 LEU A 133 79.51 -111.90 REMARK 500 ASP A 153 62.32 33.63 REMARK 500 THR A 200 -48.33 -130.79 REMARK 500 ASP B 28 -80.52 -136.84 REMARK 500 ASN B 33 50.51 -113.03 REMARK 500 VAL B 53 -56.97 70.05 REMARK 500 LEU B 111 94.96 -61.69 REMARK 500 SER B 192 -25.10 -159.14 REMARK 500 ASN C 490 59.34 -166.89 REMARK 500 THR D 483 -36.71 -130.58 REMARK 500 ASN D 490 59.82 -168.34 REMARK 500 THR D 585 108.83 -44.40 REMARK 500 THR E 483 -38.97 -130.97 REMARK 500 THR E 484 -61.93 -109.68 REMARK 500 ASN E 490 59.20 -169.24 REMARK 500 THR F 483 -35.72 -130.43 REMARK 500 ASN F 490 60.69 -168.74 REMARK 500 THR F 585 104.52 -35.12 REMARK 500 ASP H 27 109.42 -167.75 REMARK 500 PHE H 29 96.85 2.49 REMARK 500 SER H 98 -159.31 -101.32 REMARK 500 LEU H 102 -114.45 61.90 REMARK 500 ASP H 110 141.82 -176.44 REMARK 500 LEU H 133 79.55 -112.22 REMARK 500 THR H 200 -48.53 -131.72 REMARK 500 ASP L 28 -86.51 -137.93 REMARK 500 ASN L 33 50.51 -113.26 REMARK 500 VAL L 53 -57.28 70.40 REMARK 500 LEU L 111 95.13 -67.16 REMARK 500 REMARK 500 REMARK: NULL DBREF 8PN0 A 1 233 PDB 8PN0 8PN0 1 233 DBREF 8PN0 B 1 217 PDB 8PN0 8PN0 1 217 DBREF1 8PN0 C 456 660 UNP A0A6C0PR31_HEV DBREF2 8PN0 C A0A6C0PR31 44 248 DBREF1 8PN0 D 456 660 UNP A0A6C0PR31_HEV DBREF2 8PN0 D A0A6C0PR31 44 248 DBREF1 8PN0 E 456 660 UNP A0A6C0PR31_HEV DBREF2 8PN0 E A0A6C0PR31 44 248 DBREF1 8PN0 F 456 660 UNP A0A6C0PR31_HEV DBREF2 8PN0 F A0A6C0PR31 44 248 DBREF 8PN0 H 1 233 PDB 8PN0 8PN0 1 233 DBREF 8PN0 L 1 217 PDB 8PN0 8PN0 1 217 SEQADV 8PN0 GLY C 450 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP C 451 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP C 452 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP C 453 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP C 454 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 LYS C 455 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 PHE C 500 UNP A0A6C0PR3 LEU 88 CONFLICT SEQADV 8PN0 GLY D 450 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP D 451 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP D 452 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP D 453 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP D 454 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 LYS D 455 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 PHE D 500 UNP A0A6C0PR3 LEU 88 CONFLICT SEQADV 8PN0 GLY E 450 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP E 451 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP E 452 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP E 453 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP E 454 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 LYS E 455 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 PHE E 500 UNP A0A6C0PR3 LEU 88 CONFLICT SEQADV 8PN0 GLY F 450 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP F 451 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP F 452 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP F 453 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 ASP F 454 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 LYS F 455 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PN0 PHE F 500 UNP A0A6C0PR3 LEU 88 CONFLICT SEQRES 1 A 233 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 233 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 233 ASP THR PHE SER SER TYR VAL ILE SER TRP VAL ARG GLN SEQRES 4 A 233 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 A 233 PRO ILE ILE GLY THR ALA ASN TYR ALA PRO LYS PHE GLN SEQRES 6 A 233 ASP THR VAL THR ILE THR ALA ASP LYS SER THR ASN THR SEQRES 7 A 233 VAL TYR MET GLU MET ARG SER LEU ARG SER GLU ASP THR SEQRES 8 A 233 ALA VAL TYR TYR CYS ALA SER ASN VAL GLN LEU GLN ARG SEQRES 9 A 233 ARG GLY ASN TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 A 233 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 233 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 233 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 233 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 233 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 233 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 233 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 233 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 A 233 PRO LYS SER CYS ASP LYS THR ASP ASP ASP ASP LYS SEQRES 1 B 217 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 B 217 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 B 217 SER ASP ILE GLY ASP TYR ASN PHE VAL SER TRP TYR GLN SEQRES 4 B 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE PHE ASP SEQRES 5 B 217 VAL THR ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 B 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 B 217 GLY LEU GLN VAL GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 B 217 SER TYR THR SER THR ASN THR PRO VAL VAL PHE GLY GLY SEQRES 9 B 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 B 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 B 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 B 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 B 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 B 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 B 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 B 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 B 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 211 GLY ASP ASP ASP ASP LYS PRO ALA PRO SER ARG PRO PHE SEQRES 2 C 211 SER VAL LEU ARG ALA ASN ASP VAL LEU TRP LEU SER LEU SEQRES 3 C 211 THR ALA ALA GLU TYR ASP GLN THR THR TYR GLY SER SER SEQRES 4 C 211 THR ASN PRO MET TYR VAL SER ASP THR VAL THR PHE VAL SEQRES 5 C 211 ASN VAL ALA THR GLY ALA GLN ALA VAL ALA ARG SER LEU SEQRES 6 C 211 ASP TRP SER LYS VAL THR LEU ASP GLY ARG PRO LEU THR SEQRES 7 C 211 THR ILE GLN GLN TYR SER LYS THR PHE TYR VAL LEU PRO SEQRES 8 C 211 LEU ARG GLY LYS LEU SER PHE TRP GLU ALA GLY THR THR SEQRES 9 C 211 LYS ALA GLY TYR PRO TYR ASN TYR ASN THR THR ALA SER SEQRES 10 C 211 ASP GLN ILE LEU ILE GLU ASN ALA ALA GLY HIS ARG VAL SEQRES 11 C 211 ALA ILE SER THR TYR THR THR SER LEU GLY ALA GLY PRO SEQRES 12 C 211 THR SER ILE SER ALA VAL GLY VAL LEU ALA PRO HIS SER SEQRES 13 C 211 ALA LEU ALA VAL LEU GLU ASP THR THR ASP TYR PRO ALA SEQRES 14 C 211 ARG ALA HIS THR PHE ASP ASP PHE CYS PRO GLU CYS ARG SEQRES 15 C 211 THR LEU GLY LEU GLN GLY CYS ALA PHE GLN SER THR ILE SEQRES 16 C 211 ALA GLU LEU GLN ARG LEU LYS MET LYS VAL GLY LYS THR SEQRES 17 C 211 ARG GLU SER SEQRES 1 D 211 GLY ASP ASP ASP ASP LYS PRO ALA PRO SER ARG PRO PHE SEQRES 2 D 211 SER VAL LEU ARG ALA ASN ASP VAL LEU TRP LEU SER LEU SEQRES 3 D 211 THR ALA ALA GLU TYR ASP GLN THR THR TYR GLY SER SER SEQRES 4 D 211 THR ASN PRO MET TYR VAL SER ASP THR VAL THR PHE VAL SEQRES 5 D 211 ASN VAL ALA THR GLY ALA GLN ALA VAL ALA ARG SER LEU SEQRES 6 D 211 ASP TRP SER LYS VAL THR LEU ASP GLY ARG PRO LEU THR SEQRES 7 D 211 THR ILE GLN GLN TYR SER LYS THR PHE TYR VAL LEU PRO SEQRES 8 D 211 LEU ARG GLY LYS LEU SER PHE TRP GLU ALA GLY THR THR SEQRES 9 D 211 LYS ALA GLY TYR PRO TYR ASN TYR ASN THR THR ALA SER SEQRES 10 D 211 ASP GLN ILE LEU ILE GLU ASN ALA ALA GLY HIS ARG VAL SEQRES 11 D 211 ALA ILE SER THR TYR THR THR SER LEU GLY ALA GLY PRO SEQRES 12 D 211 THR SER ILE SER ALA VAL GLY VAL LEU ALA PRO HIS SER SEQRES 13 D 211 ALA LEU ALA VAL LEU GLU ASP THR THR ASP TYR PRO ALA SEQRES 14 D 211 ARG ALA HIS THR PHE ASP ASP PHE CYS PRO GLU CYS ARG SEQRES 15 D 211 THR LEU GLY LEU GLN GLY CYS ALA PHE GLN SER THR ILE SEQRES 16 D 211 ALA GLU LEU GLN ARG LEU LYS MET LYS VAL GLY LYS THR SEQRES 17 D 211 ARG GLU SER SEQRES 1 E 211 GLY ASP ASP ASP ASP LYS PRO ALA PRO SER ARG PRO PHE SEQRES 2 E 211 SER VAL LEU ARG ALA ASN ASP VAL LEU TRP LEU SER LEU SEQRES 3 E 211 THR ALA ALA GLU TYR ASP GLN THR THR TYR GLY SER SER SEQRES 4 E 211 THR ASN PRO MET TYR VAL SER ASP THR VAL THR PHE VAL SEQRES 5 E 211 ASN VAL ALA THR GLY ALA GLN ALA VAL ALA ARG SER LEU SEQRES 6 E 211 ASP TRP SER LYS VAL THR LEU ASP GLY ARG PRO LEU THR SEQRES 7 E 211 THR ILE GLN GLN TYR SER LYS THR PHE TYR VAL LEU PRO SEQRES 8 E 211 LEU ARG GLY LYS LEU SER PHE TRP GLU ALA GLY THR THR SEQRES 9 E 211 LYS ALA GLY TYR PRO TYR ASN TYR ASN THR THR ALA SER SEQRES 10 E 211 ASP GLN ILE LEU ILE GLU ASN ALA ALA GLY HIS ARG VAL SEQRES 11 E 211 ALA ILE SER THR TYR THR THR SER LEU GLY ALA GLY PRO SEQRES 12 E 211 THR SER ILE SER ALA VAL GLY VAL LEU ALA PRO HIS SER SEQRES 13 E 211 ALA LEU ALA VAL LEU GLU ASP THR THR ASP TYR PRO ALA SEQRES 14 E 211 ARG ALA HIS THR PHE ASP ASP PHE CYS PRO GLU CYS ARG SEQRES 15 E 211 THR LEU GLY LEU GLN GLY CYS ALA PHE GLN SER THR ILE SEQRES 16 E 211 ALA GLU LEU GLN ARG LEU LYS MET LYS VAL GLY LYS THR SEQRES 17 E 211 ARG GLU SER SEQRES 1 F 211 GLY ASP ASP ASP ASP LYS PRO ALA PRO SER ARG PRO PHE SEQRES 2 F 211 SER VAL LEU ARG ALA ASN ASP VAL LEU TRP LEU SER LEU SEQRES 3 F 211 THR ALA ALA GLU TYR ASP GLN THR THR TYR GLY SER SER SEQRES 4 F 211 THR ASN PRO MET TYR VAL SER ASP THR VAL THR PHE VAL SEQRES 5 F 211 ASN VAL ALA THR GLY ALA GLN ALA VAL ALA ARG SER LEU SEQRES 6 F 211 ASP TRP SER LYS VAL THR LEU ASP GLY ARG PRO LEU THR SEQRES 7 F 211 THR ILE GLN GLN TYR SER LYS THR PHE TYR VAL LEU PRO SEQRES 8 F 211 LEU ARG GLY LYS LEU SER PHE TRP GLU ALA GLY THR THR SEQRES 9 F 211 LYS ALA GLY TYR PRO TYR ASN TYR ASN THR THR ALA SER SEQRES 10 F 211 ASP GLN ILE LEU ILE GLU ASN ALA ALA GLY HIS ARG VAL SEQRES 11 F 211 ALA ILE SER THR TYR THR THR SER LEU GLY ALA GLY PRO SEQRES 12 F 211 THR SER ILE SER ALA VAL GLY VAL LEU ALA PRO HIS SER SEQRES 13 F 211 ALA LEU ALA VAL LEU GLU ASP THR THR ASP TYR PRO ALA SEQRES 14 F 211 ARG ALA HIS THR PHE ASP ASP PHE CYS PRO GLU CYS ARG SEQRES 15 F 211 THR LEU GLY LEU GLN GLY CYS ALA PHE GLN SER THR ILE SEQRES 16 F 211 ALA GLU LEU GLN ARG LEU LYS MET LYS VAL GLY LYS THR SEQRES 17 F 211 ARG GLU SER SEQRES 1 H 233 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 233 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 233 ASP THR PHE SER SER TYR VAL ILE SER TRP VAL ARG GLN SEQRES 4 H 233 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 H 233 PRO ILE ILE GLY THR ALA ASN TYR ALA PRO LYS PHE GLN SEQRES 6 H 233 ASP THR VAL THR ILE THR ALA ASP LYS SER THR ASN THR SEQRES 7 H 233 VAL TYR MET GLU MET ARG SER LEU ARG SER GLU ASP THR SEQRES 8 H 233 ALA VAL TYR TYR CYS ALA SER ASN VAL GLN LEU GLN ARG SEQRES 9 H 233 ARG GLY ASN TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 H 233 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 233 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 233 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 233 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 233 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 233 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 233 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 233 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 233 PRO LYS SER CYS ASP LYS THR ASP ASP ASP ASP LYS SEQRES 1 L 217 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 217 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 L 217 SER ASP ILE GLY ASP TYR ASN PHE VAL SER TRP TYR GLN SEQRES 4 L 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE PHE ASP SEQRES 5 L 217 VAL THR ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 217 GLY LEU GLN VAL GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 217 SER TYR THR SER THR ASN THR PRO VAL VAL PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER FORMUL 9 HOH *184(H2 O) HELIX 1 AA1 PRO A 62 GLN A 65 5 4 HELIX 2 AA2 ARG A 87 THR A 91 5 5 HELIX 3 AA3 SER A 165 ALA A 167 5 3 HELIX 4 AA4 PRO A 194 LEU A 198 5 5 HELIX 5 AA5 LYS A 210 ASN A 213 5 4 HELIX 6 AA6 GLN B 81 GLU B 85 5 5 HELIX 7 AA7 SER B 126 ALA B 132 1 7 HELIX 8 AA8 THR B 186 LYS B 191 1 6 HELIX 9 AA9 ARG C 512 LEU C 514 5 3 HELIX 10 AB1 ASP C 515 LYS C 518 5 4 HELIX 11 AB2 ARG D 512 LEU D 514 5 3 HELIX 12 AB3 ASP D 515 LYS D 518 5 4 HELIX 13 AB4 HIS D 604 ALA D 608 5 5 HELIX 14 AB5 ASP E 515 LYS E 518 5 4 HELIX 15 AB6 ARG F 512 LEU F 514 5 3 HELIX 16 AB7 ASP F 515 LYS F 518 5 4 HELIX 17 AB8 PRO H 62 GLN H 65 5 4 HELIX 18 AB9 ARG H 87 THR H 91 5 5 HELIX 19 AC1 SER H 165 ALA H 167 5 3 HELIX 20 AC2 SER H 196 LEU H 198 5 3 HELIX 21 AC3 LYS H 210 ASN H 213 5 4 HELIX 22 AC4 GLN L 81 GLU L 85 5 5 HELIX 23 AC5 SER L 126 ALA L 132 1 7 HELIX 24 AC6 THR L 186 SER L 192 1 7 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 VAL A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O VAL A 79 N CYS A 22 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 THR A 116 VAL A 120 1 O THR A 119 N GLU A 10 SHEET 3 AA2 6 ALA A 92 ALA A 97 -1 N TYR A 94 O THR A 116 SHEET 4 AA2 6 ILE A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLY A 49 N TRP A 36 SHEET 6 AA2 6 ALA A 58 TYR A 60 -1 O ASN A 59 N GLY A 50 SHEET 1 AA3 2 VAL A 100 GLN A 101 0 SHEET 2 AA3 2 ARG A 104 ARG A 105 -1 O ARG A 104 N GLN A 101 SHEET 1 AA4 5 SER A 129 LEU A 133 0 SHEET 2 AA4 5 ALA A 145 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA4 5 VAL A 172 THR A 174 0 SHEET 4 AA4 5 VAL A 178 LEU A 179 0 SHEET 5 AA4 5 TYR A 185 VAL A 193 -1 O SER A 186 N VAL A 178 SHEET 1 AA5 3 THR A 160 TRP A 163 0 SHEET 2 AA5 3 ILE A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA5 3 THR A 214 ARG A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA6 6 SER B 9 GLY B 12 0 SHEET 2 AA6 6 VAL B 35 GLN B 40 0 SHEET 3 AA6 6 LYS B 47 ILE B 50 -1 O MET B 49 N TRP B 37 SHEET 4 AA6 6 ALA B 86 TYR B 93 -1 O ASP B 87 N GLN B 40 SHEET 5 AA6 6 VAL B 100 PHE B 102 -1 O VAL B 101 N SER B 92 SHEET 6 AA6 6 THR B 106 VAL B 110 -1 O LEU B 108 N ALA B 86 SHEET 1 AA7 3 ILE B 18 THR B 23 0 SHEET 2 AA7 3 THR B 72 ILE B 77 -1 O ALA B 73 N CYS B 22 SHEET 3 AA7 3 PHE B 64 SER B 69 -1 N SER B 65 O THR B 76 SHEET 1 AA8 5 SER B 119 PHE B 123 0 SHEET 2 AA8 5 ALA B 135 PHE B 144 -1 O VAL B 138 N PHE B 123 SHEET 3 AA8 5 VAL B 164 THR B 166 0 SHEET 4 AA8 5 SER B 170 LYS B 171 0 SHEET 5 AA8 5 TYR B 177 LEU B 185 -1 O ALA B 178 N SER B 170 SHEET 1 AA9 4 SER B 158 PRO B 159 0 SHEET 2 AA9 4 THR B 150 ALA B 155 -1 N ALA B 155 O SER B 158 SHEET 3 AA9 4 TYR B 196 HIS B 202 -1 O GLN B 199 N ALA B 152 SHEET 4 AA9 4 SER B 205 VAL B 211 -1 O SER B 205 N HIS B 202 SHEET 1 AB1 3 VAL C 464 LEU C 465 0 SHEET 2 AB1 3 THR C 520 LEU C 521 1 O THR C 520 N LEU C 465 SHEET 3 AB1 3 ARG C 524 PRO C 525 -1 O ARG C 524 N LEU C 521 SHEET 1 AB210 VAL C 470 ASP C 481 0 SHEET 2 AB210 MET C 492 SER C 495 -1 O MET C 492 N ASP C 481 SHEET 3 AB210 VAL C 498 ASN C 502 -1 O VAL C 501 N TRP C 472 SHEET 4 AB210 GLN C 508 VAL C 510 -1 O ALA C 509 N PHE C 500 SHEET 5 AB210 THR C 527 GLN C 531 0 SHEET 6 AB210 LYS C 534 GLU C 549 -1 O VAL C 538 N THR C 527 SHEET 7 AB210 ALA C 555 GLY C 556 -1 O GLY C 556 N PHE C 547 SHEET 8 AB210 GLN C 568 GLU C 572 -1 O ILE C 571 N TYR C 537 SHEET 9 AB210 VAL C 579 SER C 582 -1 O ALA C 580 N LEU C 570 SHEET 10 AB210 THR C 593 LEU C 601 -1 O SER C 596 N TRP C 548 SHEET 1 AB3 3 VAL D 464 LEU D 465 0 SHEET 2 AB3 3 THR D 520 LEU D 521 1 O THR D 520 N LEU D 465 SHEET 3 AB3 3 ARG D 524 PRO D 525 -1 O ARG D 524 N LEU D 521 SHEET 1 AB418 VAL D 470 ASP D 481 0 SHEET 2 AB418 MET D 492 SER D 495 -1 O MET D 492 N ASP D 481 SHEET 3 AB418 VAL D 498 ASN D 502 -1 O VAL D 501 N TRP D 472 SHEET 4 AB418 GLN D 508 VAL D 510 -1 O ALA D 509 N PHE D 500 SHEET 5 AB418 THR D 527 GLN D 531 0 SHEET 6 AB418 LYS D 534 GLU D 549 -1 O PHE D 536 N ILE D 529 SHEET 7 AB418 GLN D 568 GLU D 572 -1 O ILE D 571 N TYR D 537 SHEET 8 AB418 VAL D 579 SER D 582 -1 O ALA D 580 N LEU D 570 SHEET 9 AB418 THR D 593 LEU D 601 -1 O SER D 596 N TRP D 548 SHEET 10 AB418 VAL F 470 ASP F 481 0 SHEET 11 AB418 MET F 492 SER F 495 -1 O MET F 492 N ASP F 481 SHEET 12 AB418 VAL F 498 ASN F 502 -1 O VAL F 501 N TRP F 472 SHEET 13 AB418 GLN F 508 VAL F 510 -1 O ALA F 509 N PHE F 500 SHEET 14 AB418 THR F 527 GLN F 531 1 O THR F 528 N THR D 528 SHEET 15 AB418 LYS F 534 GLU F 549 -1 O VAL F 538 N THR F 527 SHEET 16 AB418 GLN F 568 GLU F 572 -1 O ILE F 571 N TYR F 537 SHEET 17 AB418 VAL F 579 SER F 582 -1 O ALA F 580 N LEU F 570 SHEET 18 AB418 THR F 593 LEU F 601 -1 O SER F 596 N TRP F 548 SHEET 1 AB5 3 VAL E 464 LEU E 465 0 SHEET 2 AB5 3 THR E 520 LEU E 521 1 O THR E 520 N LEU E 465 SHEET 3 AB5 3 ARG E 524 PRO E 525 -1 O ARG E 524 N LEU E 521 SHEET 1 AB6 9 VAL E 470 ASP E 481 0 SHEET 2 AB6 9 MET E 492 SER E 495 -1 O MET E 492 N ASP E 481 SHEET 3 AB6 9 VAL E 498 ASN E 502 -1 O VAL E 501 N TRP E 472 SHEET 4 AB6 9 GLN E 508 VAL E 510 -1 O ALA E 509 N PHE E 500 SHEET 5 AB6 9 THR E 527 GLN E 531 0 SHEET 6 AB6 9 LYS E 534 GLU E 549 -1 O PHE E 536 N ILE E 529 SHEET 7 AB6 9 GLN E 568 GLU E 572 -1 O ILE E 571 N TYR E 537 SHEET 8 AB6 9 VAL E 579 SER E 582 -1 O ALA E 580 N LEU E 570 SHEET 9 AB6 9 THR E 593 LEU E 601 -1 O SER E 596 N TRP E 548 SHEET 1 AB7 3 VAL F 464 LEU F 465 0 SHEET 2 AB7 3 THR F 520 LEU F 521 1 O THR F 520 N LEU F 465 SHEET 3 AB7 3 ARG F 524 PRO F 525 -1 O ARG F 524 N LEU F 521 SHEET 1 AB8 4 GLN H 3 GLN H 6 0 SHEET 2 AB8 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB8 4 THR H 78 MET H 83 -1 O VAL H 79 N CYS H 22 SHEET 4 AB8 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AB9 6 GLU H 10 LYS H 12 0 SHEET 2 AB9 6 THR H 116 VAL H 120 1 O THR H 119 N GLU H 10 SHEET 3 AB9 6 ALA H 92 ALA H 97 -1 N ALA H 92 O VAL H 118 SHEET 4 AB9 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB9 6 GLU H 46 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AB9 6 ALA H 58 TYR H 60 -1 O ASN H 59 N GLY H 50 SHEET 1 AC1 2 VAL H 100 GLN H 101 0 SHEET 2 AC1 2 ARG H 104 ARG H 105 -1 O ARG H 104 N GLN H 101 SHEET 1 AC2 5 SER H 129 LEU H 133 0 SHEET 2 AC2 5 THR H 144 TYR H 154 -1 O LEU H 150 N PHE H 131 SHEET 3 AC2 5 VAL H 172 THR H 174 0 SHEET 4 AC2 5 VAL H 178 LEU H 179 0 SHEET 5 AC2 5 TYR H 185 PRO H 194 -1 O SER H 186 N VAL H 178 SHEET 1 AC3 3 THR H 160 TRP H 163 0 SHEET 2 AC3 3 ILE H 204 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AC3 3 THR H 214 ARG H 219 -1 O VAL H 216 N VAL H 207 SHEET 1 AC4 6 SER L 9 GLY L 12 0 SHEET 2 AC4 6 VAL L 35 GLN L 40 0 SHEET 3 AC4 6 LYS L 47 ILE L 50 -1 O MET L 49 N TRP L 37 SHEET 4 AC4 6 ALA L 86 TYR L 93 -1 O ASP L 87 N GLN L 40 SHEET 5 AC4 6 VAL L 100 PHE L 102 -1 O VAL L 101 N SER L 92 SHEET 6 AC4 6 THR L 106 VAL L 110 -1 O LEU L 108 N ALA L 86 SHEET 1 AC5 3 ILE L 18 THR L 23 0 SHEET 2 AC5 3 THR L 72 ILE L 77 -1 O ALA L 73 N CYS L 22 SHEET 3 AC5 3 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76 SHEET 1 AC6 5 SER L 119 PHE L 123 0 SHEET 2 AC6 5 ALA L 135 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AC6 5 VAL L 164 THR L 166 0 SHEET 4 AC6 5 SER L 170 LYS L 171 0 SHEET 5 AC6 5 TYR L 177 LEU L 185 -1 O ALA L 178 N SER L 170 SHEET 1 AC7 4 PRO L 159 VAL L 160 0 SHEET 2 AC7 4 THR L 150 ALA L 155 -1 N TRP L 153 O VAL L 160 SHEET 3 AC7 4 TYR L 196 HIS L 202 -1 O GLN L 199 N ALA L 152 SHEET 4 AC7 4 SER L 205 VAL L 211 -1 O VAL L 207 N VAL L 200 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 90 1555 1555 2.03 SSBOND 4 CYS B 139 CYS B 198 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 6 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 7 CYS L 22 CYS L 90 1555 1555 2.04 SSBOND 8 CYS L 139 CYS L 198 1555 1555 2.03 CISPEP 1 ASP A 110 PRO A 111 0 -11.14 CISPEP 2 PHE A 155 PRO A 156 0 -7.08 CISPEP 3 GLU A 157 PRO A 158 0 8.21 CISPEP 4 TYR B 145 PRO B 146 0 -0.55 CISPEP 5 GLY C 591 PRO C 592 0 0.45 CISPEP 6 GLY D 591 PRO D 592 0 -4.55 CISPEP 7 GLY E 591 PRO E 592 0 -1.20 CISPEP 8 GLY F 591 PRO F 592 0 -4.96 CISPEP 9 ASP H 110 PRO H 111 0 -11.09 CISPEP 10 PHE H 155 PRO H 156 0 -7.90 CISPEP 11 GLU H 157 PRO H 158 0 7.42 CISPEP 12 TYR L 145 PRO L 146 0 -1.86 CRYST1 88.430 94.480 91.250 90.00 90.21 90.00 P 1 21 1 8 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 0.011308 0.000000 0.000041 0.00000 SCALE2 0.000000 0.010584 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010959 0.00000