HEADER CYTOKINE 21-AUG-25 9SFX TITLE SECUKINUMAB FV IN COMPLEX WITH HUMAN IL-17A COMPND MOL_ID: 1; COMPND 2 MOLECULE: SECUKINUMAB FV LIGHT-CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: THE CONSTRUCT INCLUDED A STREP TAG (WSHPQFEK) FUSED COMPND 6 WITH THE CARBOXYTERMINUS OF THE LIGHT-CHAIN; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SECUKINUMAB FV HEAVY-CHAIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: THE CONSTRUCT INCLUDED A C-TERMINAL HIS6 TAG; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: INTERLEUKIN-17A; COMPND 14 CHAIN: C; COMPND 15 SYNONYM: IL-17,IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8, COMPND 16 CTLA-8; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: THE CONSTRUCT INCLUDED AMINO ACIDS 20 TO 155 OF HUMAN COMPND 19 IL-17A WITH A N-TERMINAL HIS6 TAG FOLLOWED BY A PRESCISSION CLEAVAGE COMPND 20 SITE. THE TAG WAS CLEAVED WITH PRESCISSION PROTEASE BEFORE COMPND 21 CRYSTALLISATION OF THE COMPLEX WITH THE SECUKINUMAB FV; COMPND 22 MOL_ID: 4; COMPND 23 MOLECULE: HEAVY-CHAIN OF ANTI-IL-17A ANTIBODY XAB5 FV COMPND 24 (CRYSTALLIZATION AID); COMPND 25 CHAIN: H; COMPND 26 ENGINEERED: YES; COMPND 27 OTHER_DETAILS: THE CONSTRUCT INCLUDED A C-TERMINAL HIS6 TAG; COMPND 28 MOL_ID: 5; COMPND 29 MOLECULE: LIGHT-CHAIN OF ANTI-IL-17A ANTIBODY XAB5 (CRYSTALLIZATION COMPND 30 AID); COMPND 31 CHAIN: L; COMPND 32 ENGINEERED: YES; COMPND 33 OTHER_DETAILS: THE CONSTRUCT INCLUDED A C-TERMINAL STREP TAG COMPND 34 (WSHPQFEK) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: IL17A, CTLA8, IL17; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 20 EXPRESSION_SYSTEM_VARIANT: STAR; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 32 EXPRESSION_SYSTEM_STRAIN: TG1 KEYWDS MONOCLONAL ANTIBODY, CYTOKINE, THERAPEUTIC ANTIBODY, FV FRAGMENT EXPDTA X-RAY DIFFRACTION AUTHOR J.-M.RONDEAU,S.LEHMANN REVDAT 1 29-OCT-25 9SFX 0 JRNL AUTH D.UNGAN,C.BE,P.BACZYK,S.MITTERMEIER,S.LEHMANN,C.WIESMANN, JRNL AUTH 2 T.HUBER,F.KOLBINGER,J.M.RONDEAU JRNL TITL IL-17A COMPLEXES WITH THERAPEUTIC ANTIBODIES EXHIBIT JRNL TITL 2 DISTINCT SIZE DISTRIBUTIONS, POTENTIALLY CONTRIBUTING TO JRNL TITL 3 CLINICALLY OBSERVED IMMUNOGENICITY. JRNL REF MABS V. 17 75840 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 41111004 JRNL DOI 10.1080/19420862.2025.2575840 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.4 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.68 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 34046 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) : 0.178 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.213 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1702 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 : 17 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.68 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2872 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2359 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2728 REMARK 3 BIN R VALUE (WORKING SET) : 0.2346 REMARK 3 BIN FREE R VALUE : 0.2616 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144 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 : 4384 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 24 REMARK 3 SOLVENT ATOMS : 35 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.35 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -9.77090 REMARK 3 B22 (A**2) : -9.77090 REMARK 3 B33 (A**2) : 19.54170 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) : 0.383 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.237 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.197 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.240 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.200 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 : 0.939 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 4521 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 6137 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1502 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 101 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 659 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 4521 ; 20.000 ; 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 : 564 ; 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 : 4782 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.09 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 33.6382 -108.0025 -6.3034 REMARK 3 T TENSOR REMARK 3 T11: 0.0233 T22: -0.0591 REMARK 3 T33: -0.1367 T12: -0.1540 REMARK 3 T13: -0.0207 T23: -0.0237 REMARK 3 L TENSOR REMARK 3 L11: 2.5457 L22: 6.1087 REMARK 3 L33: 0.5581 L12: 1.0715 REMARK 3 L13: -0.0514 L23: -0.7850 REMARK 3 S TENSOR REMARK 3 S11: 0.0442 S12: -0.1074 S13: -0.0542 REMARK 3 S21: 0.5978 S22: 0.0384 S23: 0.1236 REMARK 3 S31: 0.2965 S32: 0.0013 S33: -0.0826 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 28.5051 -95.8443 -24.3653 REMARK 3 T TENSOR REMARK 3 T11: -0.1984 T22: 0.0691 REMARK 3 T33: -0.0659 T12: -0.2058 REMARK 3 T13: -0.0728 T23: 0.0577 REMARK 3 L TENSOR REMARK 3 L11: 2.9075 L22: 4.2864 REMARK 3 L33: 4.9826 L12: 0.3527 REMARK 3 L13: -0.8262 L23: 0.6626 REMARK 3 S TENSOR REMARK 3 S11: -0.2275 S12: 0.4762 S13: 0.0851 REMARK 3 S21: -0.1994 S22: 0.1294 S23: 0.6070 REMARK 3 S31: 0.2834 S32: -0.5705 S33: 0.0981 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 38.3932 -63.4582 -12.2360 REMARK 3 T TENSOR REMARK 3 T11: -0.0368 T22: -0.0403 REMARK 3 T33: -0.0892 T12: -0.0535 REMARK 3 T13: 0.1364 T23: 0.0662 REMARK 3 L TENSOR REMARK 3 L11: 1.5758 L22: 0.9964 REMARK 3 L33: 1.9485 L12: -0.9626 REMARK 3 L13: -0.5066 L23: 0.3680 REMARK 3 S TENSOR REMARK 3 S11: 0.1664 S12: 0.0690 S13: 0.2009 REMARK 3 S21: 0.1033 S22: 0.0220 S23: -0.1055 REMARK 3 S31: -0.5638 S32: -0.1945 S33: -0.1884 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { H|* } REMARK 3 ORIGIN FOR THE GROUP (A): 30.2421 -55.8795 16.1775 REMARK 3 T TENSOR REMARK 3 T11: 0.0043 T22: -0.1058 REMARK 3 T33: -0.1858 T12: -0.0286 REMARK 3 T13: 0.1095 T23: -0.0337 REMARK 3 L TENSOR REMARK 3 L11: 2.5812 L22: 3.9211 REMARK 3 L33: 5.6097 L12: 0.8702 REMARK 3 L13: -1.1472 L23: -0.4377 REMARK 3 S TENSOR REMARK 3 S11: 0.1903 S12: -0.2673 S13: 0.4271 REMARK 3 S21: 0.6848 S22: -0.0539 S23: -0.0432 REMARK 3 S31: -0.8652 S32: -0.1106 S33: -0.1364 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { L|* } REMARK 3 ORIGIN FOR THE GROUP (A): 14.8096 -60.5658 0.5728 REMARK 3 T TENSOR REMARK 3 T11: -0.3110 T22: 0.2781 REMARK 3 T33: -0.2373 T12: 0.0700 REMARK 3 T13: 0.0381 T23: 0.1005 REMARK 3 L TENSOR REMARK 3 L11: 3.8786 L22: 5.7085 REMARK 3 L33: 4.0001 L12: 0.2333 REMARK 3 L13: -1.7414 L23: -0.2948 REMARK 3 S TENSOR REMARK 3 S11: 0.1552 S12: 0.5042 S13: 0.1666 REMARK 3 S21: -0.3556 S22: -0.0161 S23: 0.9758 REMARK 3 S31: -0.3003 S32: -1.4302 S33: -0.1391 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9SFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1292150350. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUN-12 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 : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99996 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE JULY 4, 2012 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34093 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 27.680 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 20.10 REMARK 200 R MERGE (I) : 0.13100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.4600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 21.00 REMARK 200 R MERGE FOR SHELL (I) : 2.88800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.730 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 (%): 68.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.6, 1.8M REMARK 280 AMMONIUM CITRATE DIBASIC, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 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 35.99000 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 71.98000 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 53.98500 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 89.97500 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 17.99500 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 35.99000 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 71.98000 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 89.97500 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 53.98500 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 17.99500 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, L REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -35.99000 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 PRO A 112 REMARK 465 GLN A 113 REMARK 465 PHE A 114 REMARK 465 GLU A 115 REMARK 465 LYS A 116 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 HIS B 133 REMARK 465 GLY C 18 REMARK 465 PRO C 19 REMARK 465 ILE C 20 REMARK 465 VAL C 21 REMARK 465 LYS C 22 REMARK 465 ALA C 23 REMARK 465 GLY C 24 REMARK 465 ILE C 25 REMARK 465 THR C 26 REMARK 465 ILE C 27 REMARK 465 PRO C 28 REMARK 465 ARG C 29 REMARK 465 ASN C 30 REMARK 465 PRO C 31 REMARK 465 GLY C 32 REMARK 465 CYS C 33 REMARK 465 PRO C 34 REMARK 465 ASN C 35 REMARK 465 SER C 36 REMARK 465 GLU C 37 REMARK 465 ASP C 38 REMARK 465 LYS C 39 REMARK 465 ASN C 40 REMARK 465 PHE C 41 REMARK 465 PRO C 42 REMARK 465 ILE C 51 REMARK 465 HIS C 52 REMARK 465 ASN C 53 REMARK 465 ARG C 54 REMARK 465 ASN C 55 REMARK 465 THR C 56 REMARK 465 ASN C 57 REMARK 465 THR C 58 REMARK 465 ASN C 59 REMARK 465 PRO C 60 REMARK 465 LYS C 61 REMARK 465 ARG C 62 REMARK 465 HIS C 128 REMARK 465 CYS C 129 REMARK 465 VAL C 154 REMARK 465 ALA C 155 REMARK 465 HIS H 118 REMARK 465 HIS H 119 REMARK 465 HIS H 120 REMARK 465 HIS H 121 REMARK 465 HIS H 122 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 TRP L 108 REMARK 465 SER L 109 REMARK 465 HIS L 110 REMARK 465 PRO L 111 REMARK 465 GLN L 112 REMARK 465 PHE L 113 REMARK 465 GLU L 114 REMARK 465 LYS L 115 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 ALA A 52 -37.72 67.93 REMARK 500 ARG B 67 -52.13 -120.08 REMARK 500 ASP C 65 64.47 35.70 REMARK 500 SER C 72 66.66 -118.07 REMARK 500 SER H 85 46.92 37.12 REMARK 500 ASP H 99 -174.68 78.43 REMARK 500 ARG H 100 -70.25 -106.39 REMARK 500 ASN L 30 -90.22 -90.51 REMARK 500 GLU L 32 58.68 -67.99 REMARK 500 ALA L 51 -31.42 68.49 REMARK 500 REMARK 500 REMARK: NULL DBREF 9SFX A 1 116 PDB 9SFX 9SFX 1 116 DBREF 9SFX B 1 133 PDB 9SFX 9SFX 1 133 DBREF 9SFX C 20 155 UNP Q16552 IL17_HUMAN 20 155 DBREF 9SFX H 1 122 PDB 9SFX 9SFX 1 122 DBREF 9SFX L 1 115 PDB 9SFX 9SFX 1 115 SEQADV 9SFX GLY C 18 UNP Q16552 EXPRESSION TAG SEQADV 9SFX PRO C 19 UNP Q16552 EXPRESSION TAG SEQRES 1 A 116 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 A 116 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 A 116 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 A 116 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 A 116 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 A 116 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 A 116 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 A 116 TYR GLY SER SER PRO CYS THR PHE GLY GLN GLY THR ARG SEQRES 9 A 116 LEU GLU ILE LYS TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 B 133 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 133 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 133 PHE THR PHE SER ASN TYR TRP MET ASN TRP VAL ARG GLN SEQRES 4 B 133 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE ASN SEQRES 5 B 133 GLN ASP GLY SER GLU LYS TYR TYR VAL GLY SER VAL LYS SEQRES 6 B 133 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 B 133 LEU TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 B 133 ALA VAL TYR TYR CYS VAL ARG ASP TYR TYR ASP ILE LEU SEQRES 9 B 133 THR ASP TYR TYR ILE HIS TYR TRP TYR PHE ASP LEU TRP SEQRES 10 B 133 GLY ARG GLY THR LEU VAL THR VAL SER SER HIS HIS HIS SEQRES 11 B 133 HIS HIS HIS SEQRES 1 C 138 GLY PRO ILE VAL LYS ALA GLY ILE THR ILE PRO ARG ASN SEQRES 2 C 138 PRO GLY CYS PRO ASN SER GLU ASP LYS ASN PHE PRO ARG SEQRES 3 C 138 THR VAL MET VAL ASN LEU ASN ILE HIS ASN ARG ASN THR SEQRES 4 C 138 ASN THR ASN PRO LYS ARG SER SER ASP TYR TYR ASN ARG SEQRES 5 C 138 SER THR SER PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO SEQRES 6 C 138 GLU ARG TYR PRO SER VAL ILE TRP GLU ALA LYS CYS ARG SEQRES 7 C 138 HIS LEU GLY CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR SEQRES 8 C 138 HIS MET ASN SER VAL PRO ILE GLN GLN GLU ILE LEU VAL SEQRES 9 C 138 LEU ARG ARG GLU PRO PRO HIS CYS PRO ASN SER PHE ARG SEQRES 10 C 138 LEU GLU LYS ILE LEU VAL SER VAL GLY CYS THR CYS VAL SEQRES 11 C 138 THR PRO ILE VAL HIS HIS VAL ALA SEQRES 1 H 122 GLU VAL GLN LEU VAL GLU SER GLY GLY ASP LEU VAL GLN SEQRES 2 H 122 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 122 PHE THR PHE SER SER TYR TRP MET SER TRP VAL ARG GLN SEQRES 4 H 122 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASN ILE LYS SEQRES 5 H 122 GLN ASP GLY SER GLU LYS TYR TYR VAL ASP SER VAL LYS SEQRES 6 H 122 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 122 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 122 ALA VAL TYR TYR CYS ALA ARG ASP ARG GLY SER LEU TYR SEQRES 9 H 122 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER HIS SEQRES 10 H 122 HIS HIS HIS HIS HIS SEQRES 1 L 115 ALA ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 115 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG PRO SER SEQRES 3 L 115 GLN GLY ILE ASN TRP GLU LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 115 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 115 SER LEU GLU ASN GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 115 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 115 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN PHE SEQRES 8 L 115 ASN SER TYR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 115 GLU ILE LYS TRP SER HIS PRO GLN PHE GLU LYS HET GOL B 201 6 HET GOL C 201 6 HET GOL C 202 6 HET GOL C 203 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 6 GOL 4(C3 H8 O3) FORMUL 10 HOH *35(H2 O) HELIX 1 AA1 SER A 30 SER A 32 5 3 HELIX 2 AA2 GLU A 80 PHE A 84 5 5 HELIX 3 AA3 THR B 28 TYR B 32 5 5 HELIX 4 AA4 GLY B 62 LYS B 65 5 4 HELIX 5 AA5 ARG B 87 THR B 91 5 5 HELIX 6 AA6 ASP C 65 SER C 70 1 6 HELIX 7 AA7 THR H 28 TYR H 32 5 5 HELIX 8 AA8 ASP H 62 LYS H 65 5 4 HELIX 9 AA9 ASN H 74 LYS H 76 5 3 HELIX 10 AB1 ARG H 87 THR H 91 5 5 HELIX 11 AB2 GLN L 79 PHE L 83 5 5 SHEET 1 AA1 3 LEU A 4 SER A 7 0 SHEET 2 AA1 3 ALA A 19 VAL A 29 -1 O SER A 22 N SER A 7 SHEET 3 AA1 3 PHE A 63 ILE A 76 -1 O ILE A 76 N ALA A 19 SHEET 1 AA2 6 THR A 10 LEU A 13 0 SHEET 2 AA2 6 THR A 103 ILE A 107 1 O ARG A 104 N LEU A 11 SHEET 3 AA2 6 ALA A 85 GLN A 91 -1 N TYR A 87 O THR A 103 SHEET 4 AA2 6 LEU A 34 GLN A 39 -1 N ALA A 35 O GLN A 90 SHEET 5 AA2 6 ARG A 46 TYR A 50 -1 O LEU A 48 N TRP A 36 SHEET 6 AA2 6 SER A 54 ARG A 55 -1 O SER A 54 N TYR A 50 SHEET 1 AA3 4 THR A 10 LEU A 13 0 SHEET 2 AA3 4 THR A 103 ILE A 107 1 O ARG A 104 N LEU A 11 SHEET 3 AA3 4 ALA A 85 GLN A 91 -1 N TYR A 87 O THR A 103 SHEET 4 AA3 4 THR A 98 PHE A 99 -1 O THR A 98 N GLN A 91 SHEET 1 AA4 4 GLN B 3 SER B 7 0 SHEET 2 AA4 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA4 4 SER B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA4 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA5 6 LEU B 11 VAL B 12 0 SHEET 2 AA5 6 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AA5 6 ALA B 92 LEU B 104 -1 N TYR B 94 O THR B 121 SHEET 4 AA5 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA5 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA5 6 LYS B 58 TYR B 60 -1 O TYR B 59 N ALA B 50 SHEET 1 AA6 4 LEU B 11 VAL B 12 0 SHEET 2 AA6 4 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AA6 4 ALA B 92 LEU B 104 -1 N TYR B 94 O THR B 121 SHEET 4 AA6 4 TYR B 107 TRP B 117 -1 O ILE B 109 N ASP B 102 SHEET 1 AA7 2 TRP C 74 GLU C 80 0 SHEET 2 AA7 2 VAL C 88 CYS C 94 -1 O GLU C 91 N HIS C 77 SHEET 1 AA8 3 ARG C 84 TYR C 85 0 SHEET 2 AA8 3 ASN C 111 ARG C 124 -1 O LEU C 122 N TYR C 85 SHEET 3 AA8 3 PHE C 133 VAL C 147 -1 O VAL C 142 N ILE C 115 SHEET 1 AA9 2 CYS C 99 ILE C 100 0 SHEET 2 AA9 2 VAL C 106 ASP C 107 -1 O ASP C 107 N CYS C 99 SHEET 1 AB1 4 GLN H 3 SER H 7 0 SHEET 2 AB1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB1 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AB2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 110 SHEET 4 AB2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N ASN H 50 SHEET 1 AB3 4 LEU L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 PRO L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB3 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB4 6 SER L 10 SER L 12 0 SHEET 2 AB4 6 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AB4 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB4 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB4 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB5 4 SER L 10 SER L 12 0 SHEET 2 AB5 4 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AB5 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SSBOND 1 CYS A 23 CYS A 89 1555 1555 2.06 SSBOND 2 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 3 CYS C 94 CYS C 144 1555 1555 2.07 SSBOND 4 CYS C 99 CYS C 146 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.07 CISPEP 1 SER A 7 PRO A 8 0 -13.50 CISPEP 2 SER A 95 PRO A 96 0 6.65 CISPEP 3 TYR C 85 PRO C 86 0 1.05 CISPEP 4 GLU C 125 PRO C 126 0 4.64 CISPEP 5 PRO C 126 PRO C 127 0 4.02 CISPEP 6 SER L 7 PRO L 8 0 0.52 CISPEP 7 TYR L 94 PRO L 95 0 -1.10 CRYST1 186.350 186.350 107.970 90.00 90.00 120.00 P 61 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 0.005366 0.003098 0.000000 0.00000 SCALE2 0.000000 0.006196 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009262 0.00000