HEADER IMMUNE SYSTEM 26-SEP-24 9GW5 TITLE TYPE-I INTERFERON AUTOANTIBODIES PMAB3, PMAB19 AND PMAB14 IN COMPLEX TITLE 2 WITH INTERFERON ALPHA-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERFERON ALPHA-2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IFN-ALPHA-2,INTERFERON ALPHA-A,LEIF A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TYPE-I INTERFERONS AUTOANTIBODY PAMB14 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: SINGLE CHAIN FRAGMENT VARIABLE (SCFV) POLYPEPTIDE COMPND 11 CHAIN WITH HEAVY AND LIGHT COMPONENTS PART OF THE SAME CHAIN.; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: SCFV TYPE-I INTERFERONS AUTOANTIBODY PAMB03; COMPND 14 CHAIN: U; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: SCFV TYPE-I INTERFERONS AUTOANTIBODY PAMB19; COMPND 18 CHAIN: V; COMPND 19 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 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 14 EXPRESSION_SYSTEM_CELL: 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: SCHNEIDER S2 CELL; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 26 EXPRESSION_SYSTEM_CELL: 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 9GW5 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,R.LEVY,T.LE VOYER, JRNL AUTH 7 O.DELMONTE,C.O'FARRELLY,J.RIVIERE,B.AMADOR BORRERO, JRNL AUTH 8 A.SERVETTAZ,E.CRICKX,M.MICHEL,A.PUEL,L.ABEL,C.E.LUYT, JRNL AUTH 9 A.MATHIAN,Z.AMOURA,J.C.WEILL,J.L.CASANOVA,F.A.REY, JRNL AUTH10 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. 4.00 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) : 4.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 13185 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) : 0.296 REMARK 3 R VALUE (WORKING SET) : 0.294 REMARK 3 FREE R VALUE : 0.324 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 645 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) : 4.00 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.07 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.87 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) : 0.2956 REMARK 3 BIN FREE R VALUE : 0.3061 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 17 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 : 6368 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 151.3 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.85660 REMARK 3 B22 (A**2) : -2.85660 REMARK 3 B33 (A**2) : 5.71310 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) : 0.670 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.899 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL 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 : 0.852 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.836 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 6510 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 8824 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2196 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1094 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 6510 ; 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 : 855 ; 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 : 4200 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 0.84 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.51 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.57 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|9 - A|157 } REMARK 3 ORIGIN FOR THE GROUP (A): -46.3586 -30.1250 11.4826 REMARK 3 T TENSOR REMARK 3 T11: 0.0581 T22: -0.0559 REMARK 3 T33: 0.1709 T12: -0.2053 REMARK 3 T13: 0.1369 T23: 0.0669 REMARK 3 L TENSOR REMARK 3 L11: 8.799 L22: 6.6484 REMARK 3 L33: 8.3155 L12: -1.3041 REMARK 3 L13: 1.7291 L23: 1.5853 REMARK 3 S TENSOR REMARK 3 S11: -0.1695 S12: 0.3085 S13: -0.1858 REMARK 3 S21: 0.3085 S22: 0.1026 S23: -0.0327 REMARK 3 S31: -0.1858 S32: -0.0327 S33: 0.0669 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { U|3 - U|251 } REMARK 3 ORIGIN FOR THE GROUP (A): -19.0034 -22.0301 2.3227 REMARK 3 T TENSOR REMARK 3 T11: -0.1061 T22: -0.122 REMARK 3 T33: -0.304 T12: 0.0388 REMARK 3 T13: 0.01 T23: 0.1554 REMARK 3 L TENSOR REMARK 3 L11: 2.8152 L22: 6.5137 REMARK 3 L33: 1.8735 L12: -2.046 REMARK 3 L13: -0.5539 L23: 0.6677 REMARK 3 S TENSOR REMARK 3 S11: 0.0843 S12: 0.1242 S13: 0.3553 REMARK 3 S21: 0.1242 S22: -0.1962 S23: 0.1736 REMARK 3 S31: 0.3553 S32: 0.1736 S33: 0.112 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { V|3 - V|244 } REMARK 3 ORIGIN FOR THE GROUP (A): -65.6734 -41.1509 26.2603 REMARK 3 T TENSOR REMARK 3 T11: 0.4301 T22: 0.1779 REMARK 3 T33: 0.304 T12: -0.0728 REMARK 3 T13: 0.1468 T23: 0.0497 REMARK 3 L TENSOR REMARK 3 L11: 8.3124 L22: 8.3185 REMARK 3 L33: 8.3155 L12: 0.0018 REMARK 3 L13: -1.5832 L23: -3.0787 REMARK 3 S TENSOR REMARK 3 S11: -0.1532 S12: 0.3086 S13: 0.6864 REMARK 3 S21: 0.3086 S22: 0.119 S23: -0.2022 REMARK 3 S31: 0.6864 S32: -0.2022 S33: 0.0342 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { H|4 - H|122 } REMARK 3 ORIGIN FOR THE GROUP (A): -57.7954 -1.6656 3.4931 REMARK 3 T TENSOR REMARK 3 T11: 0.269 T22: -0.1985 REMARK 3 T33: 0.1969 T12: 0.1009 REMARK 3 T13: 0.1922 T23: -0.0645 REMARK 3 L TENSOR REMARK 3 L11: 2.5409 L22: 8.6314 REMARK 3 L33: 8.1014 L12: 0.5464 REMARK 3 L13: 2.9031 L23: 0.7925 REMARK 3 S TENSOR REMARK 3 S11: -0.192 S12: 0.3864 S13: -0.6357 REMARK 3 S21: 0.3864 S22: 0.0783 S23: 0.0125 REMARK 3 S31: -0.6357 S32: 0.0125 S33: 0.1137 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { H|433 - H|542 } REMARK 3 ORIGIN FOR THE GROUP (A): -58.3663 -12.4688 -15.3776 REMARK 3 T TENSOR REMARK 3 T11: -0.1584 T22: -0.1825 REMARK 3 T33: 0.0835 T12: 0.1472 REMARK 3 T13: 0.0062 T23: -0.0701 REMARK 3 L TENSOR REMARK 3 L11: 5.5168 L22: 4.2275 REMARK 3 L33: 8.3155 L12: 0.5971 REMARK 3 L13: 0.9671 L23: -0.6305 REMARK 3 S TENSOR REMARK 3 S11: -0.0356 S12: -0.2114 S13: -0.2844 REMARK 3 S21: -0.2114 S22: -0.0114 S23: -0.2202 REMARK 3 S31: -0.2844 S32: -0.2202 S33: 0.047 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292142043. 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 : 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 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS, STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13477 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000 REMARK 200 RESOLUTION RANGE LOW (A) : 150.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 79.00 REMARK 200 R MERGE (I) : 0.78100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.13 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.9 REMARK 200 DATA REDUNDANCY IN SHELL : 81.50 REMARK 200 R MERGE FOR SHELL (I) : 8.86900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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 (%): 63.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5 1.9 (NH4)2SO4, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 126.75667 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 63.37833 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 95.06750 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.68917 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 158.44583 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 126.75667 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 63.37833 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 31.68917 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 95.06750 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 158.44583 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, U, V 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 SER A 8 REMARK 465 GLY A 102 REMARK 465 VAL A 103 REMARK 465 GLY A 104 REMARK 465 VAL A 105 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 ARG H 1 REMARK 465 SER H 2 REMARK 465 GLU H 3 REMARK 465 SER H 413 REMARK 465 SER H 414 REMARK 465 GLY H 415 REMARK 465 THR H 416 REMARK 465 GLY H 417 REMARK 465 GLY H 418 REMARK 465 SER H 419 REMARK 465 GLY H 420 REMARK 465 GLY H 421 REMARK 465 GLY H 422 REMARK 465 GLY H 423 REMARK 465 SER H 424 REMARK 465 GLY H 425 REMARK 465 GLY H 426 REMARK 465 GLY H 427 REMARK 465 GLY H 428 REMARK 465 SER H 429 REMARK 465 GLY H 430 REMARK 465 GLY H 431 REMARK 465 GLY H 432 REMARK 465 PRO H 543 REMARK 465 PHE H 544 REMARK 465 GLU H 545 REMARK 465 ASP H 546 REMARK 465 ASP H 547 REMARK 465 ASP H 548 REMARK 465 ASP H 549 REMARK 465 LYS H 550 REMARK 465 ALA H 551 REMARK 465 GLY H 552 REMARK 465 TRP H 553 REMARK 465 SER H 554 REMARK 465 HIS H 555 REMARK 465 PRO H 556 REMARK 465 GLN H 557 REMARK 465 PHE H 558 REMARK 465 GLU H 559 REMARK 465 LYS H 560 REMARK 465 GLY H 561 REMARK 465 GLY H 562 REMARK 465 GLY H 563 REMARK 465 SER H 564 REMARK 465 GLY H 565 REMARK 465 GLY H 566 REMARK 465 GLY H 567 REMARK 465 SER H 568 REMARK 465 GLY H 569 REMARK 465 GLY H 570 REMARK 465 GLY H 571 REMARK 465 SER H 572 REMARK 465 TRP H 573 REMARK 465 SER H 574 REMARK 465 HIS H 575 REMARK 465 PRO H 576 REMARK 465 GLN H 577 REMARK 465 PHE H 578 REMARK 465 GLU H 579 REMARK 465 LYS H 580 REMARK 465 ARG U 1 REMARK 465 SER U 2 REMARK 465 GLY U 123 REMARK 465 THR U 124 REMARK 465 GLY U 125 REMARK 465 GLY U 126 REMARK 465 SER U 127 REMARK 465 GLY U 128 REMARK 465 GLY U 129 REMARK 465 GLY U 130 REMARK 465 GLY U 131 REMARK 465 SER U 132 REMARK 465 GLY U 133 REMARK 465 GLY U 134 REMARK 465 GLY U 135 REMARK 465 PHE U 252 REMARK 465 GLU U 253 REMARK 465 ASP U 254 REMARK 465 ASP U 255 REMARK 465 ASP U 256 REMARK 465 ASP U 257 REMARK 465 LYS U 258 REMARK 465 ALA U 259 REMARK 465 GLY U 260 REMARK 465 TRP U 261 REMARK 465 SER U 262 REMARK 465 HIS U 263 REMARK 465 PRO U 264 REMARK 465 GLN U 265 REMARK 465 PHE U 266 REMARK 465 GLU U 267 REMARK 465 LYS U 268 REMARK 465 GLY U 269 REMARK 465 GLY U 270 REMARK 465 GLY U 271 REMARK 465 SER U 272 REMARK 465 GLY U 273 REMARK 465 GLY U 274 REMARK 465 GLY U 275 REMARK 465 SER U 276 REMARK 465 GLY U 277 REMARK 465 GLY U 278 REMARK 465 GLY U 279 REMARK 465 SER U 280 REMARK 465 TRP U 281 REMARK 465 SER U 282 REMARK 465 HIS U 283 REMARK 465 PRO U 284 REMARK 465 GLN U 285 REMARK 465 PHE U 286 REMARK 465 GLU U 287 REMARK 465 LYS U 288 REMARK 465 ARG V 1 REMARK 465 SER V 2 REMARK 465 SER V 118 REMARK 465 GLY V 119 REMARK 465 THR V 120 REMARK 465 GLY V 121 REMARK 465 GLY V 122 REMARK 465 SER V 123 REMARK 465 GLY V 124 REMARK 465 GLY V 125 REMARK 465 GLY V 126 REMARK 465 GLY V 127 REMARK 465 SER V 128 REMARK 465 GLY V 129 REMARK 465 GLY V 130 REMARK 465 GLY V 131 REMARK 465 GLY V 132 REMARK 465 SER V 133 REMARK 465 GLY V 134 REMARK 465 GLY V 135 REMARK 465 GLY V 136 REMARK 465 ALA V 137 REMARK 465 SER V 138 REMARK 465 GLU V 139 REMARK 465 ILE V 245 REMARK 465 LYS V 246 REMARK 465 GLY V 247 REMARK 465 PRO V 248 REMARK 465 PHE V 249 REMARK 465 GLU V 250 REMARK 465 ASP V 251 REMARK 465 ASP V 252 REMARK 465 ASP V 253 REMARK 465 ASP V 254 REMARK 465 LYS V 255 REMARK 465 ALA V 256 REMARK 465 GLY V 257 REMARK 465 TRP V 258 REMARK 465 SER V 259 REMARK 465 HIS V 260 REMARK 465 PRO V 261 REMARK 465 GLN V 262 REMARK 465 PHE V 263 REMARK 465 GLU V 264 REMARK 465 LYS V 265 REMARK 465 GLY V 266 REMARK 465 GLY V 267 REMARK 465 GLY V 268 REMARK 465 SER V 269 REMARK 465 GLY V 270 REMARK 465 GLY V 271 REMARK 465 GLY V 272 REMARK 465 SER V 273 REMARK 465 GLY V 274 REMARK 465 GLY V 275 REMARK 465 GLY V 276 REMARK 465 SER V 277 REMARK 465 TRP V 278 REMARK 465 SER V 279 REMARK 465 HIS V 280 REMARK 465 PRO V 281 REMARK 465 GLN V 282 REMARK 465 PHE V 283 REMARK 465 GLU V 284 REMARK 465 LYS V 285 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 SER U 137 OG REMARK 470 SER U 142 OG REMARK 470 ASP U 143 CG OD1 OD2 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 GLN A 48 33.48 -96.62 REMARK 500 THR H 107 152.51 83.57 REMARK 500 SER H 464 -121.07 57.21 REMARK 500 ALA H 485 -36.89 66.58 REMARK 500 TYR U 29 130.65 68.97 REMARK 500 THR U 30 115.21 -31.65 REMARK 500 SER U 137 159.58 -41.95 REMARK 500 ARG U 172 -100.68 45.84 REMARK 500 ALA U 193 -28.45 65.41 REMARK 500 SER U 218 -85.11 -91.39 REMARK 500 ILE U 225 95.60 -65.38 REMARK 500 TYR U 233 39.20 -146.21 REMARK 500 ASP U 235 154.14 165.63 REMARK 500 LEU V 141 99.12 -64.58 REMARK 500 THR V 158 66.31 -108.76 REMARK 500 ARG V 184 98.43 -67.68 REMARK 500 ALA V 190 -16.50 61.52 REMARK 500 SER V 204 -162.97 -112.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9GVO RELATED DB: PDB REMARK 900 RELATED ID: 9GVL RELATED DB: PDB DBREF 9GW5 A 1 165 UNP P01563 IFNA2_HUMAN 24 188 DBREF 9GW5 H 1 580 PDB 9GW5 9GW5 1 580 DBREF 9GW5 U 1 288 PDB 9GW5 9GW5 1 288 DBREF 9GW5 V 1 285 PDB 9GW5 9GW5 1 285 SEQADV 9GW5 GLY A 166 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 167 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 168 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 169 UNP P01563 EXPRESSION TAG SEQADV 9GW5 SER A 170 UNP P01563 EXPRESSION TAG SEQADV 9GW5 LEU A 171 UNP P01563 EXPRESSION TAG SEQADV 9GW5 VAL A 172 UNP P01563 EXPRESSION TAG SEQADV 9GW5 PRO A 173 UNP P01563 EXPRESSION TAG SEQADV 9GW5 ARG A 174 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 175 UNP P01563 EXPRESSION TAG SEQADV 9GW5 SER A 176 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 177 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 178 UNP P01563 EXPRESSION TAG SEQADV 9GW5 GLY A 179 UNP P01563 EXPRESSION TAG SEQADV 9GW5 SER A 180 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 181 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 182 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 183 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 184 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 185 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 186 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 187 UNP P01563 EXPRESSION TAG SEQADV 9GW5 HIS A 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 H 290 ARG SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 H 290 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 290 SER GLY PHE THR PHE SER SER HIS ALA MET SER TRP VAL SEQRES 4 H 290 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP VAL SER SER SEQRES 5 H 290 ILE SER ALA ALA GLY GLY SER THR TYR TYR ALA ALA SER SEQRES 6 H 290 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER ASN SEQRES 7 H 290 LYS THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 H 290 ASP THR ALA ILE TYR TYR CYS ALA LYS GLU SER ASP ARG SEQRES 9 H 290 VAL THR THR LEU ASP TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 H 290 THR LEU VAL THR VAL SER SER GLY THR GLY GLY SER GLY SEQRES 11 H 290 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA SEQRES 12 H 290 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 13 H 290 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 14 H 290 SER GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN SEQRES 15 H 290 LYS PRO GLY GLN ALA PRO LYS LEU LEU ILE TYR ALA ALA SEQRES 16 H 290 SER SER LEU GLN THR GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 H 290 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 18 H 290 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 19 H 290 SER TYR ILE THR PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 20 H 290 VAL GLU ILE LYS GLY PRO PHE GLU ASP ASP ASP ASP LYS SEQRES 21 H 290 ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SEQRES 22 H 290 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO SEQRES 23 H 290 GLN PHE GLU LYS SEQRES 1 U 288 ARG SER GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL SEQRES 2 U 288 LYS LYS PRO GLY ALA SER VAL LYS VAL SER CYS LYS THR SEQRES 3 U 288 SER GLY TYR THR PHE THR SER TYR ASP ILE ASN TRP VAL SEQRES 4 U 288 ARG GLN ALA THR GLY GLN GLY LEU GLU TRP MET GLY TRP SEQRES 5 U 288 MET ASN PRO ASN THR GLY ASN THR GLY TYR ALA GLN LYS SEQRES 6 U 288 PHE GLN GLY ARG VAL ALA MET THR ARG SER SER SER THR SEQRES 7 U 288 ARG THR ALA TYR MET GLU LEU SER SER LEU THR SER GLU SEQRES 8 U 288 ASP THR ALA VAL TYR TYR CYS ALA ARG ALA GLY LEU THR SEQRES 9 U 288 GLY ALA GLY LEU ASP ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 U 288 VAL THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY SEQRES 11 U 288 GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA SER ASP SEQRES 12 U 288 ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SER SEQRES 13 U 288 VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER GLN SEQRES 14 U 288 ASP ILE ARG LYS TYR LEU ASN TRP TYR GLN GLN LYS PRO SEQRES 15 U 288 GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER ASN SEQRES 16 U 288 LEU GLN THR GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 17 U 288 SER GLY THR ASP PHE THR LEU THR ILE SER ARG LEU GLN SEQRES 18 U 288 PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR GLY SEQRES 19 U 288 ASP LEU PRO LEU THR PHE GLY GLY GLY THR LYS VAL GLY SEQRES 20 U 288 ILE THR GLY PRO PHE GLU ASP ASP ASP ASP LYS ALA GLY SEQRES 21 U 288 TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER GLY SEQRES 22 U 288 GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO GLN PHE SEQRES 23 U 288 GLU LYS SEQRES 1 V 285 ARG SER GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL SEQRES 2 V 285 LYS LYS PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SEQRES 3 V 285 SER GLY TYR ASP PHE SER ARG PHE SER ILE HIS TRP VAL SEQRES 4 V 285 ARG GLN ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP SEQRES 5 V 285 LEU ILE THR GLY ASN GLY ASP ALA LYS TYR SER GLN LYS SEQRES 6 V 285 PHE GLN GLY ARG VAL THR ILE SER ARG ASN ILE SER ALA SEQRES 7 V 285 SER THR ALA TYR MET GLU VAL THR ASN LEU ARG SER GLU SEQRES 8 V 285 ASP SER ALA VAL TYR TYR CYS SER ARG ASP PRO VAL ALA SEQRES 9 V 285 ALA GLY LEU TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 V 285 SER GLY THR GLY GLY SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 V 285 GLY GLY SER GLY GLY GLY ALA SER GLU ILE LEU LEU THR SEQRES 12 V 285 GLN SER PRO GLY THR LEU SER LEU SER PRO GLY GLU ARG SEQRES 13 V 285 ALA THR LEU SER CYS ARG ALA SER GLN PHE VAL SER SER SEQRES 14 V 285 THR TYR LEU ALA TRP TYR GLN HIS LYS PRO GLY GLN ALA SEQRES 15 V 285 PRO ARG LEU LEU ILE TYR GLY ALA SER SER ARG ALA THR SEQRES 16 V 285 GLY ILE PRO ASP ARG PHE SER GLY SER GLY SER GLY THR SEQRES 17 V 285 ASP PHE THR LEU THR ILE ASN GLY LEU GLU PRO GLU ASP SEQRES 18 V 285 PHE ALA VAL TYR TYR CYS GLN GLN TYR GLY SER SER PRO SEQRES 19 V 285 ARG THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS GLY SEQRES 20 V 285 PRO PHE GLU ASP ASP ASP ASP LYS ALA GLY TRP SER HIS SEQRES 21 V 285 PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER SEQRES 22 V 285 GLY GLY GLY SER TRP SER HIS PRO GLN PHE GLU LYS HELIX 1 AA1 LEU A 9 ARG A 22 1 14 HELIX 2 AA2 SER A 25 ARG A 33 5 9 HELIX 3 AA3 PRO A 39 GLY A 44 5 6 HELIX 4 AA4 ASN A 45 LYS A 49 5 5 HELIX 5 AA5 THR A 52 SER A 68 1 17 HELIX 6 AA6 THR A 69 TRP A 76 1 8 HELIX 7 AA7 ASP A 77 GLN A 101 1 25 HELIX 8 AA8 LYS A 112 LYS A 133 1 22 HELIX 9 AA9 SER A 136 THR A 155 1 20 HELIX 10 AB1 THR H 30 HIS H 34 5 5 HELIX 11 AB2 ARG H 89 THR H 93 5 5 HELIX 12 AB3 GLN H 513 PHE H 517 5 5 HELIX 13 AB4 THR U 30 TYR U 34 5 5 HELIX 14 AB5 GLN U 64 GLN U 67 5 4 HELIX 15 AB6 THR U 89 ASP U 92 5 4 HELIX 16 AB7 GLN U 221 ILE U 225 5 5 HELIX 17 AB8 ASP V 30 ARG V 33 5 4 HELIX 18 AB9 GLN V 64 GLN V 67 5 4 HELIX 19 AC1 ARG V 89 SER V 93 5 5 HELIX 20 AC2 PRO V 102 GLY V 106 5 5 HELIX 21 AC3 SER V 168 THR V 170 5 3 HELIX 22 AC4 GLU V 218 PHE V 222 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 SER H 23 N SER H 9 SHEET 3 AA1 4 THR H 80 MET H 85 -1 O MET H 85 N LEU H 20 SHEET 4 AA1 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AA2 5 THR H 60 TYR H 62 0 SHEET 2 AA2 5 GLU H 48 ILE H 53 -1 N SER H 52 O TYR H 61 SHEET 3 AA2 5 MET H 36 GLN H 41 -1 N ARG H 40 O GLU H 48 SHEET 4 AA2 5 ALA H 94 GLU H 101 -1 O TYR H 97 N VAL H 39 SHEET 5 AA2 5 PHE H 111 TRP H 114 -1 O ASP H 112 N LYS H 100 SHEET 1 AA3 5 THR H 60 TYR H 62 0 SHEET 2 AA3 5 GLU H 48 ILE H 53 -1 N SER H 52 O TYR H 61 SHEET 3 AA3 5 MET H 36 GLN H 41 -1 N ARG H 40 O GLU H 48 SHEET 4 AA3 5 ALA H 94 GLU H 101 -1 O TYR H 97 N VAL H 39 SHEET 5 AA3 5 THR H 118 VAL H 120 -1 O THR H 118 N TYR H 96 SHEET 1 AA4 4 MET H 438 SER H 441 0 SHEET 2 AA4 4 VAL H 453 ALA H 459 -1 O ARG H 458 N THR H 439 SHEET 3 AA4 4 ASP H 504 ILE H 509 -1 O LEU H 507 N ILE H 455 SHEET 4 AA4 4 PHE H 496 SER H 501 -1 N SER H 497 O THR H 508 SHEET 1 AA5 6 SER H 444 ALA H 447 0 SHEET 2 AA5 6 THR H 536 ILE H 540 1 O GLU H 539 N LEU H 445 SHEET 3 AA5 6 THR H 519 GLN H 524 -1 N TYR H 520 O THR H 536 SHEET 4 AA5 6 LEU H 467 GLN H 472 -1 N GLN H 472 O THR H 519 SHEET 5 AA5 6 LYS H 479 TYR H 483 -1 O LEU H 481 N TRP H 469 SHEET 6 AA5 6 SER H 487 LEU H 488 -1 O SER H 487 N TYR H 483 SHEET 1 AA6 4 SER H 444 ALA H 447 0 SHEET 2 AA6 4 THR H 536 ILE H 540 1 O GLU H 539 N LEU H 445 SHEET 3 AA6 4 THR H 519 GLN H 524 -1 N TYR H 520 O THR H 536 SHEET 4 AA6 4 THR H 531 PHE H 532 -1 O THR H 531 N GLN H 524 SHEET 1 AA7 4 GLN U 5 GLN U 8 0 SHEET 2 AA7 4 VAL U 20 SER U 27 -1 O LYS U 25 N VAL U 7 SHEET 3 AA7 4 THR U 80 LEU U 85 -1 O MET U 83 N VAL U 22 SHEET 4 AA7 4 VAL U 70 SER U 75 -1 N THR U 73 O TYR U 82 SHEET 1 AA8 6 GLU U 12 LYS U 14 0 SHEET 2 AA8 6 THR U 116 VAL U 120 1 O LEU U 117 N GLU U 12 SHEET 3 AA8 6 ALA U 94 ARG U 100 -1 N ALA U 94 O VAL U 118 SHEET 4 AA8 6 ILE U 36 ALA U 42 -1 N VAL U 39 O TYR U 97 SHEET 5 AA8 6 LEU U 47 MET U 53 -1 O MET U 50 N TRP U 38 SHEET 6 AA8 6 THR U 60 TYR U 62 -1 O GLY U 61 N TRP U 52 SHEET 1 AA9 4 MET U 146 SER U 149 0 SHEET 2 AA9 4 VAL U 161 ALA U 167 -1 O THR U 164 N SER U 149 SHEET 3 AA9 4 ASP U 212 ILE U 217 -1 O LEU U 215 N ILE U 163 SHEET 4 AA9 4 PHE U 204 SER U 209 -1 N SER U 207 O THR U 214 SHEET 1 AB1 6 SER U 152 ALA U 155 0 SHEET 2 AB1 6 THR U 244 ILE U 248 1 O LYS U 245 N LEU U 153 SHEET 3 AB1 6 THR U 227 GLN U 232 -1 N TYR U 228 O THR U 244 SHEET 4 AB1 6 LEU U 175 GLN U 180 -1 N GLN U 180 O THR U 227 SHEET 5 AB1 6 PRO U 186 TYR U 191 -1 O LYS U 187 N GLN U 179 SHEET 6 AB1 6 ASN U 195 LEU U 196 -1 O ASN U 195 N TYR U 191 SHEET 1 AB2 4 GLN V 5 GLN V 8 0 SHEET 2 AB2 4 VAL V 20 SER V 27 -1 O LYS V 25 N VAL V 7 SHEET 3 AB2 4 THR V 80 VAL V 85 -1 O MET V 83 N VAL V 22 SHEET 4 AB2 4 VAL V 70 ASN V 75 -1 N SER V 73 O TYR V 82 SHEET 1 AB3 6 GLU V 12 LYS V 14 0 SHEET 2 AB3 6 THR V 112 VAL V 116 1 O THR V 115 N GLU V 12 SHEET 3 AB3 6 ALA V 94 ARG V 100 -1 N TYR V 96 O THR V 112 SHEET 4 AB3 6 SER V 35 GLN V 41 -1 N VAL V 39 O TYR V 97 SHEET 5 AB3 6 LEU V 47 ILE V 54 -1 O MET V 50 N TRP V 38 SHEET 6 AB3 6 ALA V 60 TYR V 62 -1 O LYS V 61 N TRP V 52 SHEET 1 AB4 3 THR V 143 SER V 145 0 SHEET 2 AB4 3 ALA V 157 VAL V 167 -1 O ARG V 162 N THR V 143 SHEET 3 AB4 3 SER V 204 ILE V 214 -1 O PHE V 210 N CYS V 161 SHEET 1 AB5 6 THR V 148 SER V 150 0 SHEET 2 AB5 6 THR V 241 GLU V 244 1 O LYS V 242 N LEU V 149 SHEET 3 AB5 6 VAL V 224 GLN V 229 -1 N TYR V 225 O THR V 241 SHEET 4 AB5 6 LEU V 172 HIS V 177 -1 N ALA V 173 O GLN V 228 SHEET 5 AB5 6 PRO V 183 TYR V 188 -1 O LEU V 186 N TRP V 174 SHEET 6 AB5 6 SER V 192 ARG V 193 -1 O SER V 192 N TYR V 188 SSBOND 1 CYS A 29 CYS A 138 1555 1555 2.04 SSBOND 2 CYS H 24 CYS H 98 1555 1555 2.04 SSBOND 3 CYS H 457 CYS H 522 1555 1555 2.04 SSBOND 4 CYS U 24 CYS U 98 1555 1555 2.05 SSBOND 5 CYS U 165 CYS U 230 1555 1555 2.05 SSBOND 6 CYS V 24 CYS V 98 1555 1555 2.04 SSBOND 7 CYS V 161 CYS V 227 1555 1555 2.05 CISPEP 1 ASP H 112 PRO H 113 0 -1.12 CISPEP 2 SER H 441 PRO H 442 0 -4.66 CISPEP 3 THR H 528 PRO H 529 0 1.01 CISPEP 4 SER U 149 PRO U 150 0 -1.30 CISPEP 5 LEU U 236 PRO U 237 0 -1.55 CISPEP 6 SER V 145 PRO V 146 0 -2.20 CISPEP 7 SER V 233 PRO V 234 0 2.96 CRYST1 166.216 166.216 190.135 90.00 90.00 120.00 P 65 2 2 12 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 0.006016 0.003473 0.000000 0.00000 SCALE2 0.000000 0.006947 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005259 0.00000