HEADER IMMUNE SYSTEM 25-SEP-24 9GVO TITLE TYPE-I INTERFERONS AUTOANTIBODIES PMAB15 AND PMAB14 IN COMPLEX WITH TITLE 2 INTERFERON ALPHA-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV TYPE-I INTERFERONS AUTOANTIBODY PMAB14; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: INTERFERON ALPHA-2; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: IFN-ALPHA-2,INTERFERON ALPHA-A,LEIF A; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: SCFV TYPE-I INTERFERONS AUTOANTIBODY PMAB15; COMPND 12 CHAIN: H; COMPND 13 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 CELL; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: IFNA2, IFNA2A, IFNA2B, IFNA2C; SOURCE 12 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2 CELL; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2 CELL KEYWDS TYPE-I INTERFERON, INTERFERON ALPHA-2, AUTOANTIBODY, ANTIGEN ANTIBODY KEYWDS 2 COMPLEX, COVID-19 PNEUMONIA, SIGNALING PROTEIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.DUQUERROY,F.REY,O.AHOUZI,M.MAHEVAS,P.CHAPPERT REVDAT 1 08-OCT-25 9GVO 0 JRNL AUTH M.VANDERKERKEN,M.FOURNIER,K.DORGHAM,P.BASTARD,O.AHOUZI, JRNL AUTH 2 S.DUQUERROY,N.K.NGUYEN,M.BROUTIN,M.CHARLET,A.VANDENBERGHE, JRNL AUTH 3 L.BIZIEN,O.DA MATA-JARDIN,A.HAOUZ,T.BELMONDO,S.HUE, JRNL AUTH 4 A.BORGHESI,C.RODRIGUEZ-GALLEGO,D.VINH,V.ANDREAKOS, JRNL AUTH 5 F.HAERYNCK,R.HALWANI,T.Q.P.HAMMERSTROM,N.BJORKSTROM, JRNL AUTH 6 B.STRUNZ,T.MOGENSEN,S.TROUILLET,B.NEVEN,C.RODRIGUEZ-GALLEGO, JRNL AUTH 7 R.LEVY,T.LE VOYER,O.DELMONTE,C.O'FARRELLY,J.RIVIERE, JRNL AUTH 8 B.AMADOR BORRERO,A.SERVETTAZ,E.CRICKX,M.MICHEL,A.PUEL, JRNL AUTH 9 L.ABEL,C.E.LUYT,A.MATHIAN,Z.AMOURA,J.C.WEILL,J.L.CASANOVA, JRNL AUTH10 F.A.REY,G.GOROCHOV,P.CHAPPERT,M.MAHEVAS JRNL TITL TEMPORAL AND STRUCTURAL INSIGHTS INTO TYPE-I INTERFERONS JRNL TITL 2 AUTOANTIBODIES IN SEVERE COVID-19 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.81 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) : 1.81 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 104583 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) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 5205 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) : 1.81 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.82 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.31 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) : 0.3497 REMARK 3 BIN FREE R VALUE : 0.3788 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 108 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 : 4677 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 47 REMARK 3 SOLVENT ATOMS : 384 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.17 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.07400 REMARK 3 B22 (A**2) : -3.07400 REMARK 3 B33 (A**2) : 6.14800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.240 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.088 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.087 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.086 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.086 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 : 0.963 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 4902 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 6652 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1671 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 839 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 4902 ; 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 : 631 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : 12 ; 1.000 ; HARMONIC 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 : 4324 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.94 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.98 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.31 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|3 - A|35 } REMARK 3 ORIGIN FOR THE GROUP (A): 85.0829 -30.415 2.6154 REMARK 3 T TENSOR REMARK 3 T11: -0.0132 T22: 0.0719 REMARK 3 T33: -0.1404 T12: 0.0889 REMARK 3 T13: -0.0599 T23: -0.0577 REMARK 3 L TENSOR REMARK 3 L11: 1.045 L22: 7.6125 REMARK 3 L33: 2.9493 L12: -0.0385 REMARK 3 L13: -0.575 L23: -0.8359 REMARK 3 S TENSOR REMARK 3 S11: -0.2043 S12: 0.0237 S13: 0.2129 REMARK 3 S21: 0.0237 S22: 0.0244 S23: 0.4748 REMARK 3 S31: 0.2129 S32: 0.4748 S33: 0.1799 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|36 - A|100 } REMARK 3 ORIGIN FOR THE GROUP (A): 77.0098 -31.8485 -0.7882 REMARK 3 T TENSOR REMARK 3 T11: 0.0357 T22: 0.0453 REMARK 3 T33: -0.1129 T12: 0.0454 REMARK 3 T13: -0.0059 T23: -0.0322 REMARK 3 L TENSOR REMARK 3 L11: 0.2614 L22: 0.6866 REMARK 3 L33: 1.9966 L12: -0.4246 REMARK 3 L13: 0.0113 L23: -0.9413 REMARK 3 S TENSOR REMARK 3 S11: -0.2172 S12: -0.0674 S13: 0.2695 REMARK 3 S21: -0.0674 S22: 0.1759 S23: -0.1801 REMARK 3 S31: 0.2695 S32: -0.1801 S33: 0.0413 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|101 - A|147 } REMARK 3 ORIGIN FOR THE GROUP (A): 78.7717 -28.7117 -7.7861 REMARK 3 T TENSOR REMARK 3 T11: 0.0122 T22: -0.0393 REMARK 3 T33: -0.0572 T12: 0.047 REMARK 3 T13: 0.0164 T23: -0.0367 REMARK 3 L TENSOR REMARK 3 L11: 0.5193 L22: 1.0197 REMARK 3 L33: 1.1352 L12: -0.7441 REMARK 3 L13: 0.104 L23: 0.2334 REMARK 3 S TENSOR REMARK 3 S11: -0.1067 S12: -0.0124 S13: 0.1081 REMARK 3 S21: -0.0124 S22: 0.0166 S23: 0.0974 REMARK 3 S31: 0.1081 S32: 0.0974 S33: 0.0901 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { A|148 - A|169 } REMARK 3 ORIGIN FOR THE GROUP (A): 81.7074 -34.8811 -29.0507 REMARK 3 T TENSOR REMARK 3 T11: 0.136 T22: -0.0193 REMARK 3 T33: -0.1334 T12: 0.1423 REMARK 3 T13: 0.0075 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 3.0443 L22: 2.0823 REMARK 3 L33: 0 L12: -1.5704 REMARK 3 L13: -1.5934 L23: 1.6718 REMARK 3 S TENSOR REMARK 3 S11: 0.2568 S12: -0.3039 S13: 0.0655 REMARK 3 S21: -0.3039 S22: -0.3339 S23: -0.0515 REMARK 3 S31: 0.0655 S32: -0.0515 S33: 0.0771 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { A|170 - A|219 } REMARK 3 ORIGIN FOR THE GROUP (A): 82.8789 -25.6754 -21.8075 REMARK 3 T TENSOR REMARK 3 T11: 0.0524 T22: -0.0531 REMARK 3 T33: -0.0212 T12: 0.0602 REMARK 3 T13: 0.0535 T23: -0.0071 REMARK 3 L TENSOR REMARK 3 L11: 1.091 L22: 1.3023 REMARK 3 L33: 0.4318 L12: -1.0556 REMARK 3 L13: -0.5253 L23: 0.7909 REMARK 3 S TENSOR REMARK 3 S11: 0.1201 S12: -0.2351 S13: 0.0012 REMARK 3 S21: -0.2351 S22: -0.0209 S23: 0.1131 REMARK 3 S31: 0.0012 S32: 0.1131 S33: -0.0991 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { A|220 - A|254 } REMARK 3 ORIGIN FOR THE GROUP (A): 83.8791 -33.938 -22.2958 REMARK 3 T TENSOR REMARK 3 T11: 0.0915 T22: -0.0289 REMARK 3 T33: -0.0522 T12: 0.0878 REMARK 3 T13: 0.029 T23: -0.0189 REMARK 3 L TENSOR REMARK 3 L11: 1.2843 L22: 1.4571 REMARK 3 L33: 0.3942 L12: -1.5092 REMARK 3 L13: -0.5802 L23: 0.9092 REMARK 3 S TENSOR REMARK 3 S11: 0.1022 S12: -0.167 S13: 0.0913 REMARK 3 S21: -0.167 S22: -0.0742 S23: 0.066 REMARK 3 S31: 0.0913 S32: 0.066 S33: -0.028 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { B|8 - B|39 } REMARK 3 ORIGIN FOR THE GROUP (A): 50.2488 -15.4181 -15.2336 REMARK 3 T TENSOR REMARK 3 T11: 0.0295 T22: -0.1059 REMARK 3 T33: -0.0143 T12: 0.0213 REMARK 3 T13: 0.0128 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 0.9435 L22: 1.9967 REMARK 3 L33: 0.5617 L12: 1.3427 REMARK 3 L13: 0.0597 L23: 0.3743 REMARK 3 S TENSOR REMARK 3 S11: 0.0958 S12: 0.0186 S13: 0.0867 REMARK 3 S21: 0.0186 S22: -0.0464 S23: 0.002 REMARK 3 S31: 0.0867 S32: 0.002 S33: -0.0494 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { B|40 - B|77 } REMARK 3 ORIGIN FOR THE GROUP (A): 59.3063 -7.646 -9.0213 REMARK 3 T TENSOR REMARK 3 T11: 0.0436 T22: -0.0996 REMARK 3 T33: 0.0196 T12: -0.0159 REMARK 3 T13: 0.0207 T23: -0.0369 REMARK 3 L TENSOR REMARK 3 L11: 3.4689 L22: 1.5036 REMARK 3 L33: 5.5297 L12: -0.2133 REMARK 3 L13: 2.3822 L23: 1.6948 REMARK 3 S TENSOR REMARK 3 S11: 0.1543 S12: -0.0261 S13: 0.189 REMARK 3 S21: -0.0261 S22: 0.1103 S23: -0.2047 REMARK 3 S31: 0.189 S32: -0.2047 S33: -0.2646 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: { B|78 - B|108 } REMARK 3 ORIGIN FOR THE GROUP (A): 52.5067 -0.9541 -5.7175 REMARK 3 T TENSOR REMARK 3 T11: 0.0927 T22: -0.1392 REMARK 3 T33: 0.073 T12: 0.0336 REMARK 3 T13: 0.0443 T23: -0.1333 REMARK 3 L TENSOR REMARK 3 L11: 5.6479 L22: 3.8048 REMARK 3 L33: 0.8316 L12: 0.1787 REMARK 3 L13: 1.0653 L23: 3.9757 REMARK 3 S TENSOR REMARK 3 S11: 0.17 S12: 0.3737 S13: 0.4738 REMARK 3 S21: 0.3737 S22: 0.158 S23: -0.0797 REMARK 3 S31: 0.4738 S32: -0.0797 S33: -0.3279 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: { B|109 - B|157 } REMARK 3 ORIGIN FOR THE GROUP (A): 61.349 -13.3728 -12.7035 REMARK 3 T TENSOR REMARK 3 T11: 0.0498 T22: -0.1128 REMARK 3 T33: 0.0105 T12: 0.0009 REMARK 3 T13: 0.0123 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: 0.7043 L22: 1.1276 REMARK 3 L33: 0.5064 L12: -0.9354 REMARK 3 L13: 0.4094 L23: 0.29 REMARK 3 S TENSOR REMARK 3 S11: 0.0227 S12: -0.0287 S13: 0.0469 REMARK 3 S21: -0.0287 S22: 0.1035 S23: -0.1056 REMARK 3 S31: 0.0469 S32: -0.1056 S33: -0.1262 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: { H|3 - H|19 } REMARK 3 ORIGIN FOR THE GROUP (A): 31.9423 -43.8295 -27.4204 REMARK 3 T TENSOR REMARK 3 T11: -0.0743 T22: 0.0686 REMARK 3 T33: -0.066 T12: -0.1207 REMARK 3 T13: -0.0315 T23: -0.0255 REMARK 3 L TENSOR REMARK 3 L11: 0.3614 L22: 2.7912 REMARK 3 L33: 0 L12: 0.3433 REMARK 3 L13: 0.2952 L23: -0.2697 REMARK 3 S TENSOR REMARK 3 S11: 0.007 S12: -0.1444 S13: 0.2914 REMARK 3 S21: -0.1444 S22: 0.1829 S23: -0.3799 REMARK 3 S31: 0.2914 S32: -0.3799 S33: -0.1898 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: { H|20 - H|62 } REMARK 3 ORIGIN FOR THE GROUP (A): 39.0927 -34.7874 -24.4954 REMARK 3 T TENSOR REMARK 3 T11: 0.0017 T22: 0.0157 REMARK 3 T33: -0.0467 T12: -0.0331 REMARK 3 T13: -0.0154 T23: 0.0015 REMARK 3 L TENSOR REMARK 3 L11: 0.3259 L22: 0.8247 REMARK 3 L33: 0.9298 L12: 0.8083 REMARK 3 L13: 0.0375 L23: 0.0143 REMARK 3 S TENSOR REMARK 3 S11: 0.0111 S12: -0.0517 S13: 0.0182 REMARK 3 S21: -0.0517 S22: -0.005 S23: -0.1409 REMARK 3 S31: 0.0182 S32: -0.1409 S33: -0.0061 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: { H|63 - H|78 } REMARK 3 ORIGIN FOR THE GROUP (A): 39.7948 -34.3082 -32.0937 REMARK 3 T TENSOR REMARK 3 T11: -0.0103 T22: 0.0462 REMARK 3 T33: -0.0831 T12: -0.044 REMARK 3 T13: -0.0457 T23: 0.0381 REMARK 3 L TENSOR REMARK 3 L11: 3.4083 L22: 2.7635 REMARK 3 L33: 0.6585 L12: -1.1345 REMARK 3 L13: -0.9076 L23: 0.9904 REMARK 3 S TENSOR REMARK 3 S11: -0.193 S12: -0.4166 S13: -0.0803 REMARK 3 S21: -0.4166 S22: 0.1877 S23: -0.103 REMARK 3 S31: -0.0803 S32: -0.103 S33: 0.0053 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: { H|79 - H|159 } REMARK 3 ORIGIN FOR THE GROUP (A): 41.6959 -39.0277 -20.0734 REMARK 3 T TENSOR REMARK 3 T11: -0.0206 T22: -0.0101 REMARK 3 T33: -0.0729 T12: -0.0461 REMARK 3 T13: 0.0058 T23: -0.0148 REMARK 3 L TENSOR REMARK 3 L11: 0.5833 L22: 1.5489 REMARK 3 L33: 0.7183 L12: 0.4938 REMARK 3 L13: -0.2058 L23: -0.4188 REMARK 3 S TENSOR REMARK 3 S11: 0.0248 S12: 0.1154 S13: 0.0565 REMARK 3 S21: 0.1154 S22: -0.0617 S23: -0.2061 REMARK 3 S31: 0.0565 S32: -0.2061 S33: 0.0369 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: { H|160 - H|171 } REMARK 3 ORIGIN FOR THE GROUP (A): 47.4522 -43.8168 1.9215 REMARK 3 T TENSOR REMARK 3 T11: 0.1569 T22: 0.0206 REMARK 3 T33: -0.2296 T12: -0.186 REMARK 3 T13: -0.0866 T23: 0.0362 REMARK 3 L TENSOR REMARK 3 L11: 0.6196 L22: 1.5902 REMARK 3 L33: 2.2539 L12: -0.9879 REMARK 3 L13: -2.3851 L23: -1.0034 REMARK 3 S TENSOR REMARK 3 S11: 0.061 S12: 0.2489 S13: 0.2032 REMARK 3 S21: 0.2489 S22: -0.1829 S23: 0.2366 REMARK 3 S31: 0.2032 S32: 0.2366 S33: 0.1219 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: { H|172 - H|185 } REMARK 3 ORIGIN FOR THE GROUP (A): 50.128 -33.7407 -9.95 REMARK 3 T TENSOR REMARK 3 T11: 0.0896 T22: -0.0484 REMARK 3 T33: -0.1154 T12: -0.1208 REMARK 3 T13: -0.0316 T23: 0.008 REMARK 3 L TENSOR REMARK 3 L11: 3.337 L22: 1.9179 REMARK 3 L33: 1.5115 L12: 0.9009 REMARK 3 L13: -1.5921 L23: -1.4958 REMARK 3 S TENSOR REMARK 3 S11: 0.0541 S12: 0.5237 S13: -0.3096 REMARK 3 S21: 0.5237 S22: -0.2311 S23: 0.0452 REMARK 3 S31: -0.3096 S32: 0.0452 S33: 0.177 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: { H|186 - H|208 } REMARK 3 ORIGIN FOR THE GROUP (A): 38.0265 -34.5538 -4.712 REMARK 3 T TENSOR REMARK 3 T11: 0.1133 T22: -0.0294 REMARK 3 T33: -0.0824 T12: -0.0735 REMARK 3 T13: 0.117 T23: -0.0455 REMARK 3 L TENSOR REMARK 3 L11: 1.0411 L22: -0.022 REMARK 3 L33: 0.8477 L12: -0.8953 REMARK 3 L13: -0.7222 L23: -2.5012 REMARK 3 S TENSOR REMARK 3 S11: 0.0107 S12: 0.4293 S13: -0.4931 REMARK 3 S21: 0.4293 S22: 0.2262 S23: -0.184 REMARK 3 S31: -0.4931 S32: -0.184 S33: -0.2369 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: { H|209 - H|222 } REMARK 3 ORIGIN FOR THE GROUP (A): 49.8687 -35.3225 -0.8125 REMARK 3 T TENSOR REMARK 3 T11: 0.1109 T22: -0.0132 REMARK 3 T33: -0.251 T12: -0.1965 REMARK 3 T13: -0.1015 T23: 0.0162 REMARK 3 L TENSOR REMARK 3 L11: -0.7802 L22: 3.3717 REMARK 3 L33: 2.9529 L12: -0.2349 REMARK 3 L13: -3.6803 L23: 0.5537 REMARK 3 S TENSOR REMARK 3 S11: -0.0052 S12: 0.7277 S13: -0.0024 REMARK 3 S21: 0.7277 S22: -0.217 S23: 0.3075 REMARK 3 S31: -0.0024 S32: 0.3075 S33: 0.2222 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: { H|223 - H|237 } REMARK 3 ORIGIN FOR THE GROUP (A): 39.9084 -41.922 -2.2537 REMARK 3 T TENSOR REMARK 3 T11: 0.1082 T22: 0.0006 REMARK 3 T33: -0.0715 T12: -0.0945 REMARK 3 T13: 0.0494 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.5183 L22: 0.9272 REMARK 3 L33: 0 L12: -0.2042 REMARK 3 L13: -1.3766 L23: -0.1919 REMARK 3 S TENSOR REMARK 3 S11: -0.1432 S12: 0.3388 S13: -0.0811 REMARK 3 S21: 0.3388 S22: -0.0871 S23: 0.0938 REMARK 3 S31: -0.0811 S32: 0.0938 S33: 0.2303 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: { H|238 - H|258 } REMARK 3 ORIGIN FOR THE GROUP (A): 45.604 -43.9744 -8.6454 REMARK 3 T TENSOR REMARK 3 T11: 0.0214 T22: 0.0202 REMARK 3 T33: -0.0361 T12: -0.0857 REMARK 3 T13: 0.0078 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 0.9398 L22: 2.4786 REMARK 3 L33: 1.6477 L12: 0.8073 REMARK 3 L13: -1.4102 L23: -2.3367 REMARK 3 S TENSOR REMARK 3 S11: -0.1068 S12: -0.07 S13: -0.0102 REMARK 3 S21: -0.07 S22: -0.135 S23: 0.017 REMARK 3 S31: -0.0102 S32: 0.017 S33: 0.2418 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292142040. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-SEP-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857 REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 3.8.6 REMARK 200 DATA SCALING SOFTWARE : XIA2 3.8.6 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105167 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810 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 (%) : 100.0 REMARK 200 DATA REDUNDANCY : 55.70 REMARK 200 R MERGE (I) : 0.14600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 5.18400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.500 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: CUBIC REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5 0.8 M NA2H2PO4 0.8 REMARK 280 M KH2PO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.99133 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.98267 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.98267 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 51.99133 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H 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 A 502 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 ARG A 1 REMARK 465 SER A 2 REMARK 465 GLY A 125 REMARK 465 THR A 126 REMARK 465 GLY A 127 REMARK 465 GLY A 128 REMARK 465 SER A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 GLY A 138 REMARK 465 SER A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 GLY A 142 REMARK 465 GLU A 255 REMARK 465 ASP A 256 REMARK 465 ASP A 257 REMARK 465 ASP A 258 REMARK 465 ASP A 259 REMARK 465 LYS A 260 REMARK 465 ALA A 261 REMARK 465 GLY A 262 REMARK 465 TRP A 263 REMARK 465 SER A 264 REMARK 465 HIS A 265 REMARK 465 PRO A 266 REMARK 465 GLN A 267 REMARK 465 PHE A 268 REMARK 465 GLU A 269 REMARK 465 LYS A 270 REMARK 465 GLY A 271 REMARK 465 GLY A 272 REMARK 465 GLY A 273 REMARK 465 SER A 274 REMARK 465 GLY A 275 REMARK 465 GLY A 276 REMARK 465 GLY A 277 REMARK 465 SER A 278 REMARK 465 GLY A 279 REMARK 465 GLY A 280 REMARK 465 GLY A 281 REMARK 465 SER A 282 REMARK 465 TRP A 283 REMARK 465 SER A 284 REMARK 465 HIS A 285 REMARK 465 PRO A 286 REMARK 465 GLN A 287 REMARK 465 PHE A 288 REMARK 465 GLU A 289 REMARK 465 LYS A 290 REMARK 465 CYS B 1 REMARK 465 ASP B 2 REMARK 465 LEU B 3 REMARK 465 PRO B 4 REMARK 465 GLN B 5 REMARK 465 THR B 6 REMARK 465 HIS B 7 REMARK 465 GLY B 44 REMARK 465 ASN B 45 REMARK 465 GLN B 46 REMARK 465 PHE B 47 REMARK 465 GLN B 48 REMARK 465 LYS B 49 REMARK 465 VAL B 99 REMARK 465 ILE B 100 REMARK 465 GLN B 101 REMARK 465 GLY B 102 REMARK 465 VAL B 103 REMARK 465 GLY B 104 REMARK 465 VAL B 105 REMARK 465 THR B 106 REMARK 465 GLU B 107 REMARK 465 GLN B 158 REMARK 465 GLU B 159 REMARK 465 SER B 160 REMARK 465 LEU B 161 REMARK 465 ARG B 162 REMARK 465 SER B 163 REMARK 465 LYS B 164 REMARK 465 GLU B 165 REMARK 465 GLY B 166 REMARK 465 GLY B 167 REMARK 465 GLY B 168 REMARK 465 GLY B 169 REMARK 465 SER B 170 REMARK 465 LEU B 171 REMARK 465 VAL B 172 REMARK 465 PRO B 173 REMARK 465 ARG B 174 REMARK 465 GLY B 175 REMARK 465 SER B 176 REMARK 465 GLY B 177 REMARK 465 GLY B 178 REMARK 465 GLY B 179 REMARK 465 SER B 180 REMARK 465 HIS B 181 REMARK 465 HIS B 182 REMARK 465 HIS B 183 REMARK 465 HIS B 184 REMARK 465 HIS B 185 REMARK 465 HIS B 186 REMARK 465 HIS B 187 REMARK 465 HIS B 188 REMARK 465 ARG H 1 REMARK 465 SER H 2 REMARK 465 GLY H 127 REMARK 465 THR H 128 REMARK 465 GLY H 129 REMARK 465 GLY H 130 REMARK 465 SER H 131 REMARK 465 GLY H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 GLY H 135 REMARK 465 SER H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 GLY H 139 REMARK 465 GLY H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 ALA H 145 REMARK 465 GLU H 259 REMARK 465 ASP H 260 REMARK 465 ASP H 261 REMARK 465 ASP H 262 REMARK 465 ASP H 263 REMARK 465 LYS H 264 REMARK 465 ALA H 265 REMARK 465 GLY H 266 REMARK 465 TRP H 267 REMARK 465 SER H 268 REMARK 465 HIS H 269 REMARK 465 PRO H 270 REMARK 465 GLN H 271 REMARK 465 PHE H 272 REMARK 465 GLU H 273 REMARK 465 LYS H 274 REMARK 465 GLY H 275 REMARK 465 GLY H 276 REMARK 465 GLY H 277 REMARK 465 SER H 278 REMARK 465 GLY H 279 REMARK 465 GLY H 280 REMARK 465 GLY H 281 REMARK 465 SER H 282 REMARK 465 GLY H 283 REMARK 465 GLY H 284 REMARK 465 GLY H 285 REMARK 465 SER H 286 REMARK 465 TRP H 287 REMARK 465 SER H 288 REMARK 465 HIS H 289 REMARK 465 PRO H 290 REMARK 465 GLN H 291 REMARK 465 PHE H 292 REMARK 465 GLU H 293 REMARK 465 LYS H 294 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 3 CG CD OE1 OE2 REMARK 470 PHE A 254 CG CD1 CD2 CE1 CE2 CZ 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 487 O HOH H 519 2.07 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 THR A 107 155.47 78.51 REMARK 500 ASP A 112 127.55 -176.00 REMARK 500 SER A 174 -122.18 57.39 REMARK 500 ALA A 195 -39.47 69.19 REMARK 500 ALA H 94 163.94 178.32 REMARK 500 ASP H 109 46.92 -83.44 REMARK 500 ALA H 198 -33.20 66.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K B 206 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 428 O REMARK 620 2 HOH H 490 O 98.5 REMARK 620 3 HOH H 529 O 110.0 144.5 REMARK 620 4 HOH H 554 O 109.3 67.9 118.7 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9GVL RELATED DB: PDB REMARK 900 RELATED ID: 9GW5 RELATED DB: PDB DBREF 9GVO A 1 290 PDB 9GVO 9GVO 1 290 DBREF 9GVO B 1 165 UNP P01563 IFNA2_HUMAN 24 188 DBREF 9GVO H 1 294 PDB 9GVO 9GVO 1 294 SEQADV 9GVO GLY B 166 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 167 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 168 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 169 UNP P01563 EXPRESSION TAG SEQADV 9GVO SER B 170 UNP P01563 EXPRESSION TAG SEQADV 9GVO LEU B 171 UNP P01563 EXPRESSION TAG SEQADV 9GVO VAL B 172 UNP P01563 EXPRESSION TAG SEQADV 9GVO PRO B 173 UNP P01563 EXPRESSION TAG SEQADV 9GVO ARG B 174 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 175 UNP P01563 EXPRESSION TAG SEQADV 9GVO SER B 176 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 177 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 178 UNP P01563 EXPRESSION TAG SEQADV 9GVO GLY B 179 UNP P01563 EXPRESSION TAG SEQADV 9GVO SER B 180 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 181 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 182 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 183 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 184 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 185 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 186 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 187 UNP P01563 EXPRESSION TAG SEQADV 9GVO HIS B 188 UNP P01563 EXPRESSION TAG SEQRES 1 A 290 ARG SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 A 290 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 A 290 SER GLY PHE THR PHE SER SER HIS ALA MET SER TRP VAL SEQRES 4 A 290 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP VAL SER SER SEQRES 5 A 290 ILE SER ALA ALA GLY GLY SER THR TYR TYR ALA ALA SER SEQRES 6 A 290 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER ASN SEQRES 7 A 290 LYS THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 A 290 ASP THR ALA ILE TYR TYR CYS ALA LYS GLU SER ASP ARG SEQRES 9 A 290 VAL THR THR LEU ASP TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 A 290 THR LEU VAL THR VAL SER SER GLY THR GLY GLY SER GLY SEQRES 11 A 290 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA SEQRES 12 A 290 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 13 A 290 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 14 A 290 SER GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN SEQRES 15 A 290 LYS PRO GLY GLN ALA PRO LYS LEU LEU ILE TYR ALA ALA SEQRES 16 A 290 SER SER LEU GLN THR GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 A 290 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 18 A 290 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 19 A 290 SER TYR ILE THR PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 20 A 290 VAL GLU ILE LYS GLY PRO PHE GLU ASP ASP ASP ASP LYS SEQRES 21 A 290 ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SEQRES 22 A 290 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO SEQRES 23 A 290 GLN PHE GLU LYS SEQRES 1 B 188 CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG SEQRES 2 B 188 THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU SEQRES 3 B 188 PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO SEQRES 4 B 188 GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR SEQRES 5 B 188 ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN SEQRES 6 B 188 LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU SEQRES 7 B 188 THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN SEQRES 8 B 188 LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY SEQRES 9 B 188 VAL THR GLU THR PRO LEU MET LYS GLU ASP SER ILE LEU SEQRES 10 B 188 ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU SEQRES 11 B 188 LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL SEQRES 12 B 188 ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN SEQRES 13 B 188 LEU GLN GLU SER LEU ARG SER LYS GLU GLY GLY GLY GLY SEQRES 14 B 188 SER LEU VAL PRO ARG GLY SER GLY GLY GLY SER HIS HIS SEQRES 15 B 188 HIS HIS HIS HIS HIS HIS SEQRES 1 H 294 ARG SER GLU VAL GLN LEU VAL GLU SER GLY GLY ASP LEU SEQRES 2 H 294 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 294 SER GLY PHE THR PHE SER GLY TYR ALA MET ALA TRP VAL SEQRES 4 H 294 ARG GLN ALA PRO GLY LYS GLU MET GLN TRP VAL SER SER SEQRES 5 H 294 ILE SER ASP ASP GLY GLY THR SER TYR TYR ALA ASP SER SEQRES 6 H 294 VAL GLU GLY ARG PHE THR VAL SER ARG ASP ASN SER ARG SEQRES 7 H 294 SER SER LEU TYR LEU GLN ILE ASN ASN LEU ARG ALA GLY SEQRES 8 H 294 ASP THR ALA VAL TYR HIS CYS ALA ARG ASP HIS GLY GLY SEQRES 9 H 294 ASN ASP TYR GLY ASP PHE GLY HIS PHE ASP LEU TRP GLY SEQRES 10 H 294 ARG GLY THR LEU VAL THR VAL SER SER GLY THR GLY GLY SEQRES 11 H 294 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY SEQRES 12 H 294 GLY ALA SER GLU ILE VAL LEU THR GLN SER PRO GLY THR SEQRES 13 H 294 LEU SER LEU SER PRO GLY GLU GLY ALA THR LEU SER CYS SEQRES 14 H 294 ARG ALA SER GLN ARG VAL SER ASN ASN TYR LEU ALA TRP SEQRES 15 H 294 TYR GLN HIS ARG PRO GLY GLN ALA PRO ARG LEU LEU ILE SEQRES 16 H 294 TYR GLY ALA SER SER ARG ALA THR GLY ILE PRO ASP ARG SEQRES 17 H 294 PHE ARG GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 18 H 294 ILE SER ARG LEU GLU PRO GLU ASP PHE ALA VAL TYR PHE SEQRES 19 H 294 CYS GLN GLN TYR GLY SER ALA PRO PRO TRP THR PHE GLY SEQRES 20 H 294 GLN GLY THR LYS VAL GLU ILE LYS GLY PRO PHE GLU ASP SEQRES 21 H 294 ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE GLU SEQRES 22 H 294 LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER SEQRES 23 H 294 TRP SER HIS PRO GLN PHE GLU LYS HET GOL A 301 6 HET GOL B 201 6 HET GOL B 202 6 HET GOL B 203 6 HET GOL B 204 6 HET PO4 B 205 5 HET K B 206 1 HET GOL H 301 6 HET PO4 H 302 5 HETNAM GOL GLYCEROL HETNAM PO4 PHOSPHATE ION HETNAM K POTASSIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 6(C3 H8 O3) FORMUL 9 PO4 2(O4 P 3-) FORMUL 10 K K 1+ FORMUL 13 HOH *384(H2 O) HELIX 1 AA1 THR A 30 HIS A 34 5 5 HELIX 2 AA2 ARG A 89 THR A 93 5 5 HELIX 3 AA3 GLN A 223 PHE A 227 5 5 HELIX 4 AA4 LEU B 9 ARG B 22 1 14 HELIX 5 AA5 SER B 25 ARG B 33 5 9 HELIX 6 AA6 PRO B 39 PHE B 43 5 5 HELIX 7 AA7 THR B 52 SER B 68 1 17 HELIX 8 AA8 THR B 69 TRP B 76 1 8 HELIX 9 AA9 ASP B 77 CYS B 98 1 22 HELIX 10 AB1 PRO B 109 LYS B 133 1 25 HELIX 11 AB2 SER B 136 THR B 155 1 20 HELIX 12 AB3 THR H 30 TYR H 34 5 5 HELIX 13 AB4 ASN H 76 ARG H 78 5 3 HELIX 14 AB5 ARG H 89 THR H 93 5 5 HELIX 15 AB6 VAL H 175 ASN H 178 5 4 HELIX 16 AB7 GLU H 226 PHE H 230 5 5 SHEET 1 AA1 4 GLN A 5 SER A 9 0 SHEET 2 AA1 4 LEU A 20 SER A 27 -1 O ALA A 25 N VAL A 7 SHEET 3 AA1 4 THR A 80 MET A 85 -1 O MET A 85 N LEU A 20 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N THR A 71 O GLN A 84 SHEET 1 AA2 6 LEU A 13 VAL A 14 0 SHEET 2 AA2 6 THR A 118 VAL A 122 1 O THR A 121 N VAL A 14 SHEET 3 AA2 6 ALA A 94 GLU A 101 -1 N TYR A 96 O THR A 118 SHEET 4 AA2 6 MET A 36 GLN A 41 -1 N VAL A 39 O TYR A 97 SHEET 5 AA2 6 GLU A 48 ILE A 53 -1 O GLU A 48 N ARG A 40 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O TYR A 61 N SER A 52 SHEET 1 AA3 4 LEU A 13 VAL A 14 0 SHEET 2 AA3 4 THR A 118 VAL A 122 1 O THR A 121 N VAL A 14 SHEET 3 AA3 4 ALA A 94 GLU A 101 -1 N TYR A 96 O THR A 118 SHEET 4 AA3 4 PHE A 111 TRP A 114 -1 O ASP A 112 N LYS A 100 SHEET 1 AA4 4 MET A 148 SER A 151 0 SHEET 2 AA4 4 VAL A 163 ALA A 169 -1 O ARG A 168 N THR A 149 SHEET 3 AA4 4 ASP A 214 ILE A 219 -1 O ILE A 219 N VAL A 163 SHEET 4 AA4 4 PHE A 206 SER A 211 -1 N SER A 207 O THR A 218 SHEET 1 AA5 6 SER A 154 SER A 156 0 SHEET 2 AA5 6 THR A 246 GLU A 249 1 O GLU A 249 N LEU A 155 SHEET 3 AA5 6 THR A 229 GLN A 234 -1 N TYR A 230 O THR A 246 SHEET 4 AA5 6 LEU A 177 GLN A 182 -1 N ASN A 178 O GLN A 233 SHEET 5 AA5 6 LYS A 189 TYR A 193 -1 O LEU A 191 N TRP A 179 SHEET 6 AA5 6 SER A 197 LEU A 198 -1 O SER A 197 N TYR A 193 SHEET 1 AA6 4 SER A 154 SER A 156 0 SHEET 2 AA6 4 THR A 246 GLU A 249 1 O GLU A 249 N LEU A 155 SHEET 3 AA6 4 THR A 229 GLN A 234 -1 N TYR A 230 O THR A 246 SHEET 4 AA6 4 THR A 241 PHE A 242 -1 O THR A 241 N GLN A 234 SHEET 1 AA7 4 GLN H 5 SER H 9 0 SHEET 2 AA7 4 LEU H 20 SER H 27 -1 O ALA H 25 N VAL H 7 SHEET 3 AA7 4 SER H 80 ILE H 85 -1 O LEU H 83 N LEU H 22 SHEET 4 AA7 4 PHE H 70 ASP H 75 -1 N SER H 73 O TYR H 82 SHEET 1 AA8 6 LEU H 13 VAL H 14 0 SHEET 2 AA8 6 THR H 120 VAL H 124 1 O THR H 123 N VAL H 14 SHEET 3 AA8 6 ALA H 94 ASP H 101 -1 N TYR H 96 O THR H 120 SHEET 4 AA8 6 MET H 36 GLN H 41 -1 N VAL H 39 O HIS H 97 SHEET 5 AA8 6 MET H 47 ILE H 53 -1 O GLN H 48 N ARG H 40 SHEET 6 AA8 6 SER H 60 TYR H 62 -1 O TYR H 61 N SER H 52 SHEET 1 AA9 4 LEU H 13 VAL H 14 0 SHEET 2 AA9 4 THR H 120 VAL H 124 1 O THR H 123 N VAL H 14 SHEET 3 AA9 4 ALA H 94 ASP H 101 -1 N TYR H 96 O THR H 120 SHEET 4 AA9 4 PHE H 113 TRP H 116 -1 O LEU H 115 N ARG H 100 SHEET 1 AB1 4 LEU H 150 SER H 153 0 SHEET 2 AB1 4 ALA H 165 ALA H 171 -1 O ARG H 170 N THR H 151 SHEET 3 AB1 4 ASP H 217 ILE H 222 -1 O LEU H 220 N LEU H 167 SHEET 4 AB1 4 PHE H 209 SER H 214 -1 N ARG H 210 O THR H 221 SHEET 1 AB2 6 THR H 156 LEU H 159 0 SHEET 2 AB2 6 THR H 250 ILE H 254 1 O GLU H 253 N LEU H 157 SHEET 3 AB2 6 VAL H 232 GLN H 237 -1 N TYR H 233 O THR H 250 SHEET 4 AB2 6 LEU H 180 HIS H 185 -1 N ALA H 181 O GLN H 236 SHEET 5 AB2 6 ARG H 192 TYR H 196 -1 O LEU H 194 N TRP H 182 SHEET 6 AB2 6 SER H 200 ARG H 201 -1 O SER H 200 N TYR H 196 SHEET 1 AB3 4 THR H 156 LEU H 159 0 SHEET 2 AB3 4 THR H 250 ILE H 254 1 O GLU H 253 N LEU H 157 SHEET 3 AB3 4 VAL H 232 GLN H 237 -1 N TYR H 233 O THR H 250 SHEET 4 AB3 4 THR H 245 PHE H 246 -1 O THR H 245 N GLN H 237 SSBOND 1 CYS A 24 CYS A 98 1555 1555 2.08 SSBOND 2 CYS A 167 CYS A 232 1555 1555 2.11 SSBOND 3 CYS B 29 CYS B 138 1555 1555 2.07 SSBOND 4 CYS H 24 CYS H 98 1555 1555 2.05 SSBOND 5 CYS H 169 CYS H 235 1555 1555 2.11 LINK O HOH A 428 K K B 206 1555 1555 2.78 LINK K K B 206 O HOH H 490 1555 1555 3.37 LINK K K B 206 O HOH H 529 1555 1555 3.10 LINK K K B 206 O HOH H 554 1555 1555 2.95 CISPEP 1 ASP A 112 PRO A 113 0 -5.91 CISPEP 2 SER A 151 PRO A 152 0 -14.72 CISPEP 3 THR A 238 PRO A 239 0 -7.34 CISPEP 4 SER H 153 PRO H 154 0 -9.34 CISPEP 5 PRO H 242 PRO H 243 0 9.98 CRYST1 112.930 112.930 155.974 90.00 90.00 120.00 P 31 2 1 6 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 0.008855 0.005112 0.000000 0.00000 SCALE2 0.000000 0.010225 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006411 0.00000