HEADER IMMUNE SYSTEM 25-SEP-24 9GVL TITLE TYPE-I INTERFERONS AUTOANTIBODY PMAB15 IN COMPLEX WITH INTERFERON TITLE 2 ALPHA-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERFERON ALPHA-2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: IFN-ALPHA-2,INTERFERON ALPHA-A,LEIF A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SCFV TYPE-I INTERFERONS AUTOANTIBODY PMAB15; COMPND 8 CHAIN: H, I; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IFNA2, IFNA2A, IFNA2B, IFNA2C; SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2 CELL; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: IFNA2; SOURCE 13 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 15 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,M.MAHEVAS,P.CHAPPERT,O.AHOUZI REVDAT 1 08-OCT-25 9GVL 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. 2.01 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) : 2.01 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 46627 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) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2428 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) : 2.01 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.02 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.59 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) : 0.3880 REMARK 3 BIN FREE R VALUE : 0.3705 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 49 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 : 5645 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 21 REMARK 3 SOLVENT ATOMS : 287 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.83 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 6.01910 REMARK 3 B22 (A**2) : -0.93930 REMARK 3 B33 (A**2) : -5.07980 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.97950 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.310 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.217 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.190 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.219 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.193 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 : 0.951 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5793 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 7842 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1952 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 985 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5793 ; 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 : 735 ; 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 : 5061 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.91 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.25 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|8 - A|51 } REMARK 3 ORIGIN FOR THE GROUP (A): 43.6845 -3.5932 24.154 REMARK 3 T TENSOR REMARK 3 T11: -0.1458 T22: -0.0544 REMARK 3 T33: 0.1541 T12: -0.0521 REMARK 3 T13: 0.0612 T23: 0.0219 REMARK 3 L TENSOR REMARK 3 L11: 6.6241 L22: 0.6972 REMARK 3 L33: 1.3147 L12: -1.1125 REMARK 3 L13: -1.4089 L23: -1.2658 REMARK 3 S TENSOR REMARK 3 S11: 0.2242 S12: 0.3718 S13: -0.1822 REMARK 3 S21: 0.3718 S22: -0.1618 S23: 0.3815 REMARK 3 S31: -0.1822 S32: 0.3815 S33: -0.0624 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|52 - A|136 } REMARK 3 ORIGIN FOR THE GROUP (A): 53.753 -8.8808 24.8295 REMARK 3 T TENSOR REMARK 3 T11: -0.2201 T22: 0.0924 REMARK 3 T33: 0.1008 T12: -0.0009 REMARK 3 T13: 0.0497 T23: 0.0602 REMARK 3 L TENSOR REMARK 3 L11: 6.0942 L22: 0 REMARK 3 L33: 0.1954 L12: -0.8741 REMARK 3 L13: -1.086 L23: 0.3416 REMARK 3 S TENSOR REMARK 3 S11: -0.014 S12: 0.1179 S13: -0.0409 REMARK 3 S21: 0.1179 S22: -0.1681 S23: 0.3942 REMARK 3 S31: -0.0409 S32: 0.3942 S33: 0.1821 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|137 - A|156 } REMARK 3 ORIGIN FOR THE GROUP (A): 44.3608 -5.2267 24.5273 REMARK 3 T TENSOR REMARK 3 T11: -0.0701 T22: 0.0399 REMARK 3 T33: 0.142 T12: -0.0299 REMARK 3 T13: 0.1093 T23: -0.0358 REMARK 3 L TENSOR REMARK 3 L11: 6.6906 L22: 1.1349 REMARK 3 L33: 0.1251 L12: 3.6897 REMARK 3 L13: 0.6737 L23: -1.1533 REMARK 3 S TENSOR REMARK 3 S11: 0.3114 S12: 0.3601 S13: -0.4644 REMARK 3 S21: 0.3601 S22: -0.2359 S23: 0.1834 REMARK 3 S31: -0.4644 S32: 0.1834 S33: -0.0754 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { B|8 - B|77 } REMARK 3 ORIGIN FOR THE GROUP (A): 66.4317 -22.2713 58.5325 REMARK 3 T TENSOR REMARK 3 T11: -0.1845 T22: 0.0384 REMARK 3 T33: -0.0041 T12: -0.0555 REMARK 3 T13: 0.0147 T23: -0.0625 REMARK 3 L TENSOR REMARK 3 L11: 8.689 L22: 0.2897 REMARK 3 L33: 1.5001 L12: -0.2736 REMARK 3 L13: 1.0797 L23: -0.1137 REMARK 3 S TENSOR REMARK 3 S11: -0.1238 S12: 0.0101 S13: -0.3784 REMARK 3 S21: 0.0101 S22: 0.1814 S23: 0.2631 REMARK 3 S31: -0.3784 S32: 0.2631 S33: -0.0576 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { B|78 - B|99 } REMARK 3 ORIGIN FOR THE GROUP (A): 77.9111 -21.1856 52.499 REMARK 3 T TENSOR REMARK 3 T11: -0.2729 T22: 0.304 REMARK 3 T33: -0.0427 T12: -0.0737 REMARK 3 T13: 0.0975 T23: -0.1986 REMARK 3 L TENSOR REMARK 3 L11: 7.1904 L22: 0 REMARK 3 L33: 5.529 L12: 2.8764 REMARK 3 L13: -3.4067 L23: 0.6905 REMARK 3 S TENSOR REMARK 3 S11: 0.0487 S12: -0.0742 S13: 0.0611 REMARK 3 S21: -0.0742 S22: -0.4913 S23: 0.2897 REMARK 3 S31: 0.0611 S32: 0.2897 S33: 0.4426 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { B|112 - B|156 } REMARK 3 ORIGIN FOR THE GROUP (A): 65.5323 -21.2114 65.1486 REMARK 3 T TENSOR REMARK 3 T11: -0.145 T22: 0.1118 REMARK 3 T33: 0.0367 T12: 0.036 REMARK 3 T13: -0.0076 T23: 0.0001 REMARK 3 L TENSOR REMARK 3 L11: 7.0208 L22: 3.1155 REMARK 3 L33: 0.2314 L12: 2.5746 REMARK 3 L13: 1.4446 L23: 1.3747 REMARK 3 S TENSOR REMARK 3 S11: -0.1784 S12: -0.2432 S13: -0.4829 REMARK 3 S21: -0.2432 S22: 0.1814 S23: -0.2139 REMARK 3 S31: -0.4829 S32: -0.2139 S33: -0.0031 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { H|3 - H|126 } REMARK 3 ORIGIN FOR THE GROUP (A): 15.71 -3.5551 19.7519 REMARK 3 T TENSOR REMARK 3 T11: -0.0954 T22: -0.0697 REMARK 3 T33: 0.1814 T12: -0.0324 REMARK 3 T13: 0.0358 T23: -0.0195 REMARK 3 L TENSOR REMARK 3 L11: 4.1274 L22: 0.1014 REMARK 3 L33: 0.5657 L12: -0.0325 REMARK 3 L13: 1.1374 L23: -0.0294 REMARK 3 S TENSOR REMARK 3 S11: -0.1554 S12: 0.0642 S13: -0.0032 REMARK 3 S21: 0.0642 S22: 0.0072 S23: 0.0704 REMARK 3 S31: -0.0032 S32: 0.0704 S33: 0.1482 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { H|147 - H|255 } REMARK 3 ORIGIN FOR THE GROUP (A): 24.0446 4.5002 37.5399 REMARK 3 T TENSOR REMARK 3 T11: -0.0371 T22: -0.0887 REMARK 3 T33: 0.1826 T12: 0.0281 REMARK 3 T13: -0.0287 T23: -0.0452 REMARK 3 L TENSOR REMARK 3 L11: 1.8034 L22: 0.5077 REMARK 3 L33: 0.5521 L12: -0.0362 REMARK 3 L13: -0.0664 L23: 0.547 REMARK 3 S TENSOR REMARK 3 S11: -0.0976 S12: 0.068 S13: 0.0625 REMARK 3 S21: 0.068 S22: -0.0654 S23: -0.0375 REMARK 3 S31: 0.0625 S32: -0.0375 S33: 0.163 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: { I|3 - I|126 } REMARK 3 ORIGIN FOR THE GROUP (A): 34.2907 -24.361 54.2761 REMARK 3 T TENSOR REMARK 3 T11: -0.0509 T22: 0.1279 REMARK 3 T33: -0.0788 T12: 0.022 REMARK 3 T13: -0.0204 T23: 0.0767 REMARK 3 L TENSOR REMARK 3 L11: 3.7207 L22: 0.9826 REMARK 3 L33: 0.6432 L12: 0.4519 REMARK 3 L13: 0.6664 L23: 0.9648 REMARK 3 S TENSOR REMARK 3 S11: 0.1263 S12: -0.3151 S13: -0.2127 REMARK 3 S21: -0.3151 S22: -0.0196 S23: -0.1576 REMARK 3 S31: -0.2127 S32: -0.1576 S33: -0.1067 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: { I|147 - I|255 } REMARK 3 ORIGIN FOR THE GROUP (A): 42.2807 -5.1134 58.2881 REMARK 3 T TENSOR REMARK 3 T11: 0.0151 T22: 0.0884 REMARK 3 T33: -0.0261 T12: 0.0568 REMARK 3 T13: -0.0657 T23: -0.1411 REMARK 3 L TENSOR REMARK 3 L11: 3.3908 L22: 1.2673 REMARK 3 L33: -0.063 L12: -1.3279 REMARK 3 L13: 0.6764 L23: -0.1243 REMARK 3 S TENSOR REMARK 3 S11: -0.2337 S12: -0.2034 S13: -0.0148 REMARK 3 S21: -0.2034 S22: 0.1031 S23: -0.1639 REMARK 3 S31: -0.0148 S32: -0.1639 S33: 0.1307 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GVL 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_1292142024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.953721 REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL REMARK 200 OPTICS : CRYOGENICALLY COOLED CHANNEL CUT REMARK 200 CRYSTAL MONOCHROMATOR, A CONVEX REMARK 200 PREFOCUSSING MIRROR AND A REMARK 200 KIRKPATRICK-BAEZ PAIR OF REMARK 200 FOCUSSING MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 30, 2023 (BUILT REMARK 200 20230630), AUTOPROC 1.0.5 REMARK 200 (20240123) REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.15 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46986 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 65.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.20200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 2.61100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 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 (%): 31.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M (NH4)2SO4 0.1 M NAACETATE PH 4.6 REMARK 280 30 %W/W PEG 2000 MME, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 291K 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 41.85950 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I 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 CYS A 1 REMARK 465 ASP A 2 REMARK 465 LEU A 3 REMARK 465 PRO A 4 REMARK 465 GLN A 5 REMARK 465 THR A 6 REMARK 465 HIS A 7 REMARK 465 GLY A 44 REMARK 465 ASN A 45 REMARK 465 GLN A 46 REMARK 465 PHE A 47 REMARK 465 GLN A 48 REMARK 465 LYS A 49 REMARK 465 ALA A 97 REMARK 465 CYS A 98 REMARK 465 VAL A 99 REMARK 465 ILE A 100 REMARK 465 GLN A 101 REMARK 465 GLY A 102 REMARK 465 VAL A 103 REMARK 465 GLY A 104 REMARK 465 VAL A 105 REMARK 465 THR A 106 REMARK 465 GLU A 107 REMARK 465 THR A 108 REMARK 465 PRO A 109 REMARK 465 LEU A 110 REMARK 465 MET A 111 REMARK 465 LYS A 112 REMARK 465 LEU A 157 REMARK 465 GLN A 158 REMARK 465 GLU A 159 REMARK 465 SER A 160 REMARK 465 LEU A 161 REMARK 465 ARG A 162 REMARK 465 SER A 163 REMARK 465 LYS A 164 REMARK 465 GLU A 165 REMARK 465 GLY A 166 REMARK 465 GLY A 167 REMARK 465 GLY A 168 REMARK 465 GLY A 169 REMARK 465 SER A 170 REMARK 465 LEU A 171 REMARK 465 VAL A 172 REMARK 465 PRO A 173 REMARK 465 ARG A 174 REMARK 465 GLY A 175 REMARK 465 SER A 176 REMARK 465 GLY A 177 REMARK 465 GLY A 178 REMARK 465 GLY A 179 REMARK 465 SER A 180 REMARK 465 HIS A 181 REMARK 465 HIS A 182 REMARK 465 HIS A 183 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 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 PHE B 43 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 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 THR B 108 REMARK 465 PRO B 109 REMARK 465 LEU B 110 REMARK 465 MET B 111 REMARK 465 LEU B 157 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 SER H 146 REMARK 465 GLY H 256 REMARK 465 PRO H 257 REMARK 465 PHE H 258 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 465 ARG I 1 REMARK 465 SER I 2 REMARK 465 GLY I 129 REMARK 465 GLY I 130 REMARK 465 SER I 131 REMARK 465 GLY I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 GLY I 135 REMARK 465 SER I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 GLY I 139 REMARK 465 GLY I 140 REMARK 465 SER I 141 REMARK 465 GLY I 142 REMARK 465 GLY I 143 REMARK 465 GLY I 144 REMARK 465 ALA I 145 REMARK 465 SER I 146 REMARK 465 GLY I 256 REMARK 465 PRO I 257 REMARK 465 PHE I 258 REMARK 465 GLU I 259 REMARK 465 ASP I 260 REMARK 465 ASP I 261 REMARK 465 ASP I 262 REMARK 465 ASP I 263 REMARK 465 LYS I 264 REMARK 465 ALA I 265 REMARK 465 GLY I 266 REMARK 465 TRP I 267 REMARK 465 SER I 268 REMARK 465 HIS I 269 REMARK 465 PRO I 270 REMARK 465 GLN I 271 REMARK 465 PHE I 272 REMARK 465 GLU I 273 REMARK 465 LYS I 274 REMARK 465 GLY I 275 REMARK 465 GLY I 276 REMARK 465 GLY I 277 REMARK 465 SER I 278 REMARK 465 GLY I 279 REMARK 465 GLY I 280 REMARK 465 GLY I 281 REMARK 465 SER I 282 REMARK 465 GLY I 283 REMARK 465 GLY I 284 REMARK 465 GLY I 285 REMARK 465 SER I 286 REMARK 465 TRP I 287 REMARK 465 SER I 288 REMARK 465 HIS I 289 REMARK 465 PRO I 290 REMARK 465 GLN I 291 REMARK 465 PHE I 292 REMARK 465 GLU I 293 REMARK 465 LYS I 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 51 CG CD OE1 OE2 REMARK 470 GLU A 113 CG CD OE1 OE2 REMARK 470 ASP A 114 CG OD1 OD2 REMARK 470 ASN A 156 CG OD1 ND2 REMARK 470 ARG B 12 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 13 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 41 CG CD OE1 OE2 REMARK 470 GLU B 42 CG CD OE1 OE2 REMARK 470 GLU B 51 CG CD OE1 OE2 REMARK 470 CYS B 98 SG REMARK 470 VAL B 99 CG1 CG2 REMARK 470 ASN B 156 CG OD1 ND2 REMARK 470 GLU H 3 CG CD OE1 OE2 REMARK 470 SER H 126 OG REMARK 470 LYS H 255 CG CD CE NZ REMARK 470 SER I 126 OG REMARK 470 LYS I 255 CG CD CE NZ 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 GLU A 51 22.15 -74.36 REMARK 500 GLU B 41 34.85 -78.76 REMARK 500 GLU B 51 29.57 -77.67 REMARK 500 ALA H 198 -25.41 70.56 REMARK 500 SER H 199 -1.57 -142.01 REMARK 500 ALA I 198 -24.77 71.19 REMARK 500 SER I 199 -1.81 -141.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9GVO RELATED DB: PDB REMARK 900 RELATED ID: 9GW5 RELATED DB: PDB DBREF 9GVL A 1 165 UNP P01563 IFNA2_HUMAN 24 188 DBREF 9GVL B 1 165 UNP P01563 IFNA2_HUMAN 24 188 DBREF 9GVL H 1 294 PDB 9GVL 9GVL 1 294 DBREF 9GVL I 1 294 PDB 9GVL 9GVL 1 294 SEQADV 9GVL GLY A 166 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 167 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 168 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 169 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER A 170 UNP P01563 EXPRESSION TAG SEQADV 9GVL LEU A 171 UNP P01563 EXPRESSION TAG SEQADV 9GVL VAL A 172 UNP P01563 EXPRESSION TAG SEQADV 9GVL PRO A 173 UNP P01563 EXPRESSION TAG SEQADV 9GVL ARG A 174 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 175 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER A 176 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 177 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 178 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY A 179 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER A 180 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 181 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 182 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 183 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 184 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 185 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 186 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 187 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS A 188 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 166 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 167 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 168 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 169 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER B 170 UNP P01563 EXPRESSION TAG SEQADV 9GVL LEU B 171 UNP P01563 EXPRESSION TAG SEQADV 9GVL VAL B 172 UNP P01563 EXPRESSION TAG SEQADV 9GVL PRO B 173 UNP P01563 EXPRESSION TAG SEQADV 9GVL ARG B 174 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 175 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER B 176 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 177 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 178 UNP P01563 EXPRESSION TAG SEQADV 9GVL GLY B 179 UNP P01563 EXPRESSION TAG SEQADV 9GVL SER B 180 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 181 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 182 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 183 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 184 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 185 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 186 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 187 UNP P01563 EXPRESSION TAG SEQADV 9GVL HIS B 188 UNP P01563 EXPRESSION TAG SEQRES 1 A 188 CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG SEQRES 2 A 188 THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU SEQRES 3 A 188 PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO SEQRES 4 A 188 GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR SEQRES 5 A 188 ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN SEQRES 6 A 188 LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU SEQRES 7 A 188 THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN SEQRES 8 A 188 LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY SEQRES 9 A 188 VAL THR GLU THR PRO LEU MET LYS GLU ASP SER ILE LEU SEQRES 10 A 188 ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU SEQRES 11 A 188 LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL SEQRES 12 A 188 ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN SEQRES 13 A 188 LEU GLN GLU SER LEU ARG SER LYS GLU GLY GLY GLY GLY SEQRES 14 A 188 SER LEU VAL PRO ARG GLY SER GLY GLY GLY SER HIS HIS SEQRES 15 A 188 HIS HIS HIS HIS HIS HIS 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 SEQRES 1 I 294 ARG SER GLU VAL GLN LEU VAL GLU SER GLY GLY ASP LEU SEQRES 2 I 294 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 I 294 SER GLY PHE THR PHE SER GLY TYR ALA MET ALA TRP VAL SEQRES 4 I 294 ARG GLN ALA PRO GLY LYS GLU MET GLN TRP VAL SER SER SEQRES 5 I 294 ILE SER ASP ASP GLY GLY THR SER TYR TYR ALA ASP SER SEQRES 6 I 294 VAL GLU GLY ARG PHE THR VAL SER ARG ASP ASN SER ARG SEQRES 7 I 294 SER SER LEU TYR LEU GLN ILE ASN ASN LEU ARG ALA GLY SEQRES 8 I 294 ASP THR ALA VAL TYR HIS CYS ALA ARG ASP HIS GLY GLY SEQRES 9 I 294 ASN ASP TYR GLY ASP PHE GLY HIS PHE ASP LEU TRP GLY SEQRES 10 I 294 ARG GLY THR LEU VAL THR VAL SER SER GLY THR GLY GLY SEQRES 11 I 294 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY SEQRES 12 I 294 GLY ALA SER GLU ILE VAL LEU THR GLN SER PRO GLY THR SEQRES 13 I 294 LEU SER LEU SER PRO GLY GLU GLY ALA THR LEU SER CYS SEQRES 14 I 294 ARG ALA SER GLN ARG VAL SER ASN ASN TYR LEU ALA TRP SEQRES 15 I 294 TYR GLN HIS ARG PRO GLY GLN ALA PRO ARG LEU LEU ILE SEQRES 16 I 294 TYR GLY ALA SER SER ARG ALA THR GLY ILE PRO ASP ARG SEQRES 17 I 294 PHE ARG GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 18 I 294 ILE SER ARG LEU GLU PRO GLU ASP PHE ALA VAL TYR PHE SEQRES 19 I 294 CYS GLN GLN TYR GLY SER ALA PRO PRO TRP THR PHE GLY SEQRES 20 I 294 GLN GLY THR LYS VAL GLU ILE LYS GLY PRO PHE GLU ASP SEQRES 21 I 294 ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE GLU SEQRES 22 I 294 LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER SEQRES 23 I 294 TRP SER HIS PRO GLN PHE GLU LYS HET GOL B 201 6 HET SO4 B 202 5 HET SO4 H 301 5 HET SO4 I 301 5 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL C3 H8 O3 FORMUL 6 SO4 3(O4 S 2-) FORMUL 9 HOH *287(H2 O) HELIX 1 AA1 SER A 8 ARG A 22 1 15 HELIX 2 AA2 SER A 25 ARG A 33 5 9 HELIX 3 AA3 PRO A 39 PHE A 43 5 5 HELIX 4 AA4 GLU A 51 SER A 68 1 18 HELIX 5 AA5 THR A 69 TRP A 76 1 8 HELIX 6 AA6 ASP A 77 GLU A 96 1 20 HELIX 7 AA7 ASP A 114 LYS A 133 1 20 HELIX 8 AA8 SER A 136 THR A 155 1 20 HELIX 9 AA9 LEU B 9 ARG B 22 1 14 HELIX 10 AB1 SER B 25 ARG B 33 5 9 HELIX 11 AB2 THR B 52 SER B 68 1 17 HELIX 12 AB3 THR B 69 TRP B 76 1 8 HELIX 13 AB4 ASP B 77 VAL B 99 1 23 HELIX 14 AB5 GLU B 113 LYS B 133 1 21 HELIX 15 AB6 SER B 136 THR B 155 1 20 HELIX 16 AB7 THR H 30 TYR H 34 5 5 HELIX 17 AB8 ASN H 76 ARG H 78 5 3 HELIX 18 AB9 ARG H 89 THR H 93 5 5 HELIX 19 AC1 VAL H 175 ASN H 178 5 4 HELIX 20 AC2 GLU H 226 PHE H 230 5 5 HELIX 21 AC3 THR I 30 TYR I 34 5 5 HELIX 22 AC4 ASN I 76 ARG I 78 5 3 HELIX 23 AC5 ARG I 89 THR I 93 5 5 HELIX 24 AC6 VAL I 175 ASN I 178 5 4 HELIX 25 AC7 GLU I 226 PHE I 230 5 5 SHEET 1 AA1 4 GLN H 5 SER H 9 0 SHEET 2 AA1 4 LEU H 20 SER H 27 -1 O ALA H 25 N VAL H 7 SHEET 3 AA1 4 SER H 80 ILE H 85 -1 O LEU H 83 N LEU H 22 SHEET 4 AA1 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AA2 6 LEU H 13 VAL H 14 0 SHEET 2 AA2 6 THR H 120 VAL H 124 1 O THR H 123 N VAL H 14 SHEET 3 AA2 6 ALA H 94 ASP H 101 -1 N TYR H 96 O THR H 120 SHEET 4 AA2 6 MET H 36 GLN H 41 -1 N VAL H 39 O HIS H 97 SHEET 5 AA2 6 GLN H 48 ILE H 53 -1 O GLN H 48 N ARG H 40 SHEET 6 AA2 6 SER H 60 TYR H 62 -1 O TYR H 61 N SER H 52 SHEET 1 AA3 4 LEU H 13 VAL H 14 0 SHEET 2 AA3 4 THR H 120 VAL H 124 1 O THR H 123 N VAL H 14 SHEET 3 AA3 4 ALA H 94 ASP H 101 -1 N TYR H 96 O THR H 120 SHEET 4 AA3 4 PHE H 113 TRP H 116 -1 O LEU H 115 N ARG H 100 SHEET 1 AA4 4 LEU H 150 SER H 153 0 SHEET 2 AA4 4 ALA H 165 ALA H 171 -1 O SER H 168 N SER H 153 SHEET 3 AA4 4 ASP H 217 ILE H 222 -1 O LEU H 220 N LEU H 167 SHEET 4 AA4 4 PHE H 209 SER H 214 -1 N ARG H 210 O THR H 221 SHEET 1 AA5 6 THR H 156 SER H 158 0 SHEET 2 AA5 6 THR H 250 GLU H 253 1 O GLU H 253 N LEU H 157 SHEET 3 AA5 6 ALA H 231 GLN H 237 -1 N ALA H 231 O VAL H 252 SHEET 4 AA5 6 LEU H 180 HIS H 185 -1 N HIS H 185 O VAL H 232 SHEET 5 AA5 6 ARG H 192 TYR H 196 -1 O LEU H 194 N TRP H 182 SHEET 6 AA5 6 SER H 200 ARG H 201 -1 O SER H 200 N TYR H 196 SHEET 1 AA6 4 THR H 156 SER H 158 0 SHEET 2 AA6 4 THR H 250 GLU H 253 1 O GLU H 253 N LEU H 157 SHEET 3 AA6 4 ALA H 231 GLN H 237 -1 N ALA H 231 O VAL H 252 SHEET 4 AA6 4 THR H 245 PHE H 246 -1 O THR H 245 N GLN H 237 SHEET 1 AA7 4 GLN I 5 SER I 9 0 SHEET 2 AA7 4 LEU I 20 SER I 27 -1 O SER I 23 N SER I 9 SHEET 3 AA7 4 SER I 80 ILE I 85 -1 O LEU I 83 N LEU I 22 SHEET 4 AA7 4 PHE I 70 ASP I 75 -1 N THR I 71 O GLN I 84 SHEET 1 AA8 6 LEU I 13 VAL I 14 0 SHEET 2 AA8 6 THR I 120 VAL I 124 1 O THR I 123 N VAL I 14 SHEET 3 AA8 6 ALA I 94 ASP I 101 -1 N TYR I 96 O THR I 120 SHEET 4 AA8 6 MET I 36 GLN I 41 -1 N VAL I 39 O HIS I 97 SHEET 5 AA8 6 GLN I 48 ILE I 53 -1 O GLN I 48 N ARG I 40 SHEET 6 AA8 6 SER I 60 TYR I 62 -1 O TYR I 61 N SER I 52 SHEET 1 AA9 4 LEU I 13 VAL I 14 0 SHEET 2 AA9 4 THR I 120 VAL I 124 1 O THR I 123 N VAL I 14 SHEET 3 AA9 4 ALA I 94 ASP I 101 -1 N TYR I 96 O THR I 120 SHEET 4 AA9 4 PHE I 113 TRP I 116 -1 O LEU I 115 N ARG I 100 SHEET 1 AB1 4 LEU I 150 SER I 153 0 SHEET 2 AB1 4 ALA I 165 ALA I 171 -1 O SER I 168 N SER I 153 SHEET 3 AB1 4 ASP I 217 ILE I 222 -1 O LEU I 220 N LEU I 167 SHEET 4 AB1 4 PHE I 209 SER I 214 -1 N ARG I 210 O THR I 221 SHEET 1 AB2 6 THR I 156 SER I 158 0 SHEET 2 AB2 6 THR I 250 GLU I 253 1 O GLU I 253 N LEU I 157 SHEET 3 AB2 6 VAL I 232 GLN I 237 -1 N TYR I 233 O THR I 250 SHEET 4 AB2 6 LEU I 180 HIS I 185 -1 N HIS I 185 O VAL I 232 SHEET 5 AB2 6 ARG I 192 TYR I 196 -1 O LEU I 194 N TRP I 182 SHEET 6 AB2 6 SER I 200 ARG I 201 -1 O SER I 200 N TYR I 196 SHEET 1 AB3 4 THR I 156 SER I 158 0 SHEET 2 AB3 4 THR I 250 GLU I 253 1 O GLU I 253 N LEU I 157 SHEET 3 AB3 4 VAL I 232 GLN I 237 -1 N TYR I 233 O THR I 250 SHEET 4 AB3 4 THR I 245 PHE I 246 -1 O THR I 245 N GLN I 237 SSBOND 1 CYS A 29 CYS A 138 1555 1555 2.05 SSBOND 2 CYS B 29 CYS B 138 1555 1555 2.05 SSBOND 3 CYS H 24 CYS H 98 1555 1555 2.04 SSBOND 4 CYS H 169 CYS H 235 1555 1555 2.06 SSBOND 5 CYS I 24 CYS I 98 1555 1555 2.06 SSBOND 6 CYS I 169 CYS I 235 1555 1555 2.04 CISPEP 1 SER H 153 PRO H 154 0 0.10 CISPEP 2 PRO H 242 PRO H 243 0 10.37 CISPEP 3 SER I 153 PRO I 154 0 -1.88 CISPEP 4 PRO I 242 PRO I 243 0 11.36 CRYST1 66.159 83.719 70.264 90.00 113.80 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015115 0.000000 0.006667 0.00000 SCALE2 0.000000 0.011945 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015555 0.00000