HEADER SIGNALING PROTEIN / CYTOKINE 16-SEP-09 3JVF
TITLE CRYSTAL STRUCTURE OF AN INTERLEUKIN-17 RECEPTOR COMPLEX
CAVEAT 3JVF NAG C 302 HAS WRONG CHIRALITY AT ATOM C1 NAG C 304 HAS WRONG
CAVEAT 2 3JVF CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-17F;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IL-17F, INTERLEUKIN-24, IL-24, CYTOKINE ML-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTERLEUKIN-17 RECEPTOR A;
COMPND 8 CHAIN: C;
COMPND 9 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 10 SYNONYM: IL-17 RECEPTOR, CDW217;
COMPND 11 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: IL17F, IL24;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: IL17RA, IL17R;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 16 EXPRESSION_SYSTEM_CELL: BACMAM 293 CELLS;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS
KEYWDS CYTOKINE, INTERLEUKIN, CYSTEINE-KNOT GROWTH FACTOR, RECEPTOR-CYTOKINE
KEYWDS 2 COMPLEX, DISULFIDE BOND, GLYCOPROTEIN, SECRETED, MEMBRANE, RECEPTOR,
KEYWDS 3 TRANSMEMBRANE, SIGNALING PROTEIN, SIGNALING PROTEIN - CYTOKINE
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.K.ELY,K.C.GARCIA
REVDAT 4 29-JUL-20 3JVF 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 13-JUL-11 3JVF 1 VERSN
REVDAT 2 29-DEC-09 3JVF 1 JRNL
REVDAT 1 20-OCT-09 3JVF 0
JRNL AUTH L.K.ELY,S.FISCHER,K.C.GARCIA
JRNL TITL STRUCTURAL BASIS OF RECEPTOR SHARING BY INTERLEUKIN 17
JRNL TITL 2 CYTOKINES.
JRNL REF NAT.IMMUNOL. V. 10 1245 2009
JRNL REFN ISSN 1529-2908
JRNL PMID 19838198
JRNL DOI 10.1038/NI.1813
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 18479
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 948
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.8235 - 6.3061 0.95 2581 116 0.2358 0.2251
REMARK 3 2 6.3061 - 5.0085 0.99 2547 129 0.2094 0.2236
REMARK 3 3 5.0085 - 4.3763 0.99 2509 129 0.1863 0.2309
REMARK 3 4 4.3763 - 3.9766 0.99 2492 147 0.2180 0.2611
REMARK 3 5 3.9766 - 3.6918 0.99 2481 124 0.2430 0.3054
REMARK 3 6 3.6918 - 3.4742 0.99 2456 152 0.2715 0.3233
REMARK 3 7 3.4742 - 3.3003 1.00 2465 151 0.2999 0.3336
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 72.06
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3987
REMARK 3 ANGLE : 1.333 5428
REMARK 3 CHIRALITY : 0.079 631
REMARK 3 PLANARITY : 0.005 695
REMARK 3 DIHEDRAL : 19.892 1456
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3JVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-08; 16-APR-09; 17-JUL-08;
REMARK 200 10-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100
REMARK 200 PH : 9.2
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y; Y
REMARK 200 RADIATION SOURCE : SSRL; SSRL; SSRL; APS
REMARK 200 BEAMLINE : BL9-2; BL11-1; BL11-1; 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL; NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00; 1.07; 0.978; 1.03
REMARK 200 MONOCHROMATOR : NULL; NULL; NULL; NULL
REMARK 200 OPTICS : NULL; NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL; NULL; NULL; NULL
REMARK 200 DETECTOR MANUFACTURER : NULL; NULL; NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18749
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, 0.1M CAPSO, CALCIUM CHLORIDE,
REMARK 280 PH 9.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.95000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 85.36500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 85.36500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.47500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 85.36500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 85.36500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.42500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 85.36500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.36500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.47500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 85.36500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.36500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 61.42500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 40.95000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ARG A 1
REMARK 465 LYS A 2
REMARK 465 ILE A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 5
REMARK 465 VAL A 6
REMARK 465 GLY A 7
REMARK 465 HIS A 8
REMARK 465 THR A 9
REMARK 465 PHE A 10
REMARK 465 PHE A 11
REMARK 465 GLN A 12
REMARK 465 LYS A 13
REMARK 465 PRO A 14
REMARK 465 GLU A 15
REMARK 465 SER A 16
REMARK 465 CYS A 17
REMARK 465 PRO A 18
REMARK 465 PRO A 19
REMARK 465 VAL A 20
REMARK 465 PRO A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 GLN A 105
REMARK 465 GLY A 106
REMARK 465 CYS A 107
REMARK 465 SER A 108
REMARK 465 VAL A 109
REMARK 465 GLN A 133
REMARK 465 ARG B 1
REMARK 465 LYS B 2
REMARK 465 ILE B 3
REMARK 465 PRO B 4
REMARK 465 LYS B 5
REMARK 465 VAL B 6
REMARK 465 GLY B 7
REMARK 465 HIS B 8
REMARK 465 THR B 9
REMARK 465 PHE B 10
REMARK 465 PHE B 11
REMARK 465 GLN B 12
REMARK 465 LYS B 13
REMARK 465 PRO B 14
REMARK 465 GLU B 15
REMARK 465 SER B 16
REMARK 465 CYS B 17
REMARK 465 PRO B 18
REMARK 465 PRO B 19
REMARK 465 VAL B 20
REMARK 465 PRO B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 ILE B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 VAL B 132
REMARK 465 GLN B 133
REMARK 465 SER C 1
REMARK 465 PRO C 273
REMARK 465 GLU C 274
REMARK 465 MET C 275
REMARK 465 PRO C 276
REMARK 465 ASP C 277
REMARK 465 THR C 278
REMARK 465 PRO C 279
REMARK 465 GLU C 280
REMARK 465 PRO C 281
REMARK 465 ILE C 282
REMARK 465 PRO C 283
REMARK 465 ASP C 284
REMARK 465 TYR C 285
REMARK 465 MET C 286
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 SER A 24 OG
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 ASN A 35 CG OD1 ND2
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 SER A 41 OG
REMARK 470 LYS A 103 CG CD CE NZ
REMARK 470 HIS A 104 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 110 OG
REMARK 470 GLU B 34 CG CD OE1 OE2
REMARK 470 ASN B 35 CG OD1 ND2
REMARK 470 SER B 41 OG
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 GLN B 105 CG CD OE1 NE2
REMARK 470 CYS B 107 SG
REMARK 470 SER B 108 OG
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 VAL B 128 CG1 CG2
REMARK 470 ASP C 29 CG OD1 OD2
REMARK 470 SER C 30 OG
REMARK 470 LEU C 101 CG CD1 CD2
REMARK 470 VAL C 178 CG1 CG2
REMARK 470 SER C 189 OG
REMARK 470 GLN C 231 CG CD OE1 NE2
REMARK 470 LYS C 243 CG CD CE NZ
REMARK 470 SER C 267 OG
REMARK 470 CYS C 272 SG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 53 C2 NAG D 1 2.15
REMARK 500 ND2 ASN C 18 C2 NAG C 303 2.15
REMARK 500 ND2 ASN C 234 O5 NAG C 304 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 96 CG GLU A 96 CD 0.105
REMARK 500 GLU A 96 CD GLU A 96 OE1 0.101
REMARK 500 GLU A 96 CD GLU A 96 OE2 0.080
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS B 77 -177.26 -64.70
REMARK 500 ASN B 79 -176.86 -68.78
REMARK 500 PRO C 15 108.35 -46.37
REMARK 500 HIS C 33 63.00 61.48
REMARK 500 SER C 41 159.22 -43.13
REMARK 500 THR C 54 -169.65 -78.51
REMARK 500 ASN C 89 -83.40 -39.51
REMARK 500 ASN C 91 47.97 -77.75
REMARK 500 GLN C 145 109.50 -161.61
REMARK 500 LYS C 147 111.30 -163.07
REMARK 500 ASP C 153 176.85 -58.69
REMARK 500 CYS C 154 40.16 -79.02
REMARK 500 LEU C 181 -140.55 56.56
REMARK 500 ASN C 194 39.68 -95.47
REMARK 500 HIS C 198 -179.78 -66.82
REMARK 500 CYS C 245 45.14 -89.74
REMARK 500 LEU C 260 122.55 -35.66
REMARK 500 ASN C 261 -28.73 89.68
REMARK 500 CYS C 263 155.67 -47.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 134 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 43 OD1
REMARK 620 2 ASN B 43 ND2 61.3
REMARK 620 3 GLU B 45 OE1 97.0 65.7
REMARK 620 4 GLU B 45 OE2 62.9 76.9 46.2
REMARK 620 N 1 2 3
DBREF 3JVF A 1 133 UNP Q96PD4 IL17F_HUMAN 31 163
DBREF 3JVF B 1 133 UNP Q96PD4 IL17F_HUMAN 31 163
DBREF 3JVF C 1 286 UNP Q96F46 I17RA_HUMAN 32 317
SEQRES 1 A 133 ARG LYS ILE PRO LYS VAL GLY HIS THR PHE PHE GLN LYS
SEQRES 2 A 133 PRO GLU SER CYS PRO PRO VAL PRO GLY GLY SER MET LYS
SEQRES 3 A 133 LEU ASP ILE GLY ILE ILE ASN GLU ASN GLN ARG VAL SER
SEQRES 4 A 133 MET SER ARG ASN ILE GLU SER ARG SER THR SER PRO TRP
SEQRES 5 A 133 ASN TYR THR VAL THR TRP ASP PRO ASN ARG TYR PRO SER
SEQRES 6 A 133 GLU VAL VAL GLN ALA GLN CYS ARG ASN LEU GLY CYS ILE
SEQRES 7 A 133 ASN ALA GLN GLY LYS GLU ASP ILE SER MET ASN SER VAL
SEQRES 8 A 133 PRO ILE GLN GLN GLU THR LEU VAL VAL ARG ARG LYS HIS
SEQRES 9 A 133 GLN GLY CYS SER VAL SER PHE GLN LEU GLU LYS VAL LEU
SEQRES 10 A 133 VAL THR VAL GLY CYS THR CYS VAL THR PRO VAL ILE HIS
SEQRES 11 A 133 HIS VAL GLN
SEQRES 1 B 133 ARG LYS ILE PRO LYS VAL GLY HIS THR PHE PHE GLN LYS
SEQRES 2 B 133 PRO GLU SER CYS PRO PRO VAL PRO GLY GLY SER MET LYS
SEQRES 3 B 133 LEU ASP ILE GLY ILE ILE ASN GLU ASN GLN ARG VAL SER
SEQRES 4 B 133 MET SER ARG ASN ILE GLU SER ARG SER THR SER PRO TRP
SEQRES 5 B 133 ASN TYR THR VAL THR TRP ASP PRO ASN ARG TYR PRO SER
SEQRES 6 B 133 GLU VAL VAL GLN ALA GLN CYS ARG ASN LEU GLY CYS ILE
SEQRES 7 B 133 ASN ALA GLN GLY LYS GLU ASP ILE SER MET ASN SER VAL
SEQRES 8 B 133 PRO ILE GLN GLN GLU THR LEU VAL VAL ARG ARG LYS HIS
SEQRES 9 B 133 GLN GLY CYS SER VAL SER PHE GLN LEU GLU LYS VAL LEU
SEQRES 10 B 133 VAL THR VAL GLY CYS THR CYS VAL THR PRO VAL ILE HIS
SEQRES 11 B 133 HIS VAL GLN
SEQRES 1 C 286 SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER
SEQRES 2 C 286 GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS
SEQRES 3 C 286 LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO
SEQRES 4 C 286 SER SER PRO MLY ASP LEU GLN ILE GLN LEU HIS PHE ALA
SEQRES 5 C 286 HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE
SEQRES 6 C 286 GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU
SEQRES 7 C 286 GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN
SEQRES 8 C 286 GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU
SEQRES 9 C 286 ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS
SEQRES 10 C 286 PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL
SEQRES 11 C 286 HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN
SEQRES 12 C 286 HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS
SEQRES 13 C 286 ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY
SEQRES 14 C 286 SER LEU TRP ASP PRO ASN ILE THR VAL GLU THR LEU GLU
SEQRES 15 C 286 ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU
SEQRES 16 C 286 SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS
SEQRES 17 C 286 MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE
SEQRES 18 C 286 PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASN
SEQRES 19 C 286 VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG
SEQRES 20 C 286 HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU
SEQRES 21 C 286 ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO
SEQRES 22 C 286 GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET
MODRES 3JVF ASN A 53 ASN GLYCOSYLATION SITE
MODRES 3JVF ASN C 18 ASN GLYCOSYLATION SITE
MODRES 3JVF ASN C 23 ASN GLYCOSYLATION SITE
MODRES 3JVF ASN C 36 ASN GLYCOSYLATION SITE
MODRES 3JVF ASN C 194 ASN GLYCOSYLATION SITE
MODRES 3JVF ASN C 234 ASN GLYCOSYLATION SITE
MODRES 3JVF MLY C 43 LYS N-DIMETHYL-LYSINE
HET MLY C 43 11
HET NAG D 1 14
HET NAG D 2 14
HET CA B 134 1
HET NAG C 301 14
HET NAG C 302 14
HET NAG C 303 14
HET NAG C 304 14
HET NAG C 305 14
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
FORMUL 3 MLY C8 H18 N2 O2
FORMUL 4 NAG 7(C8 H15 N O6)
FORMUL 5 CA CA 2+
HELIX 1 1 ASN A 43 SER A 48 1 6
HELIX 2 2 ASN B 43 SER B 48 1 6
HELIX 3 3 ASP C 72 LEU C 76 5 5
HELIX 4 4 THR C 162 SER C 167 1 6
SHEET 1 A 5 MET A 25 LYS A 26 0
SHEET 2 A 5 LYS B 26 ASP B 28 -1 O LEU B 27 N MET A 25
SHEET 3 A 5 PHE A 111 VAL A 125 1 N PHE A 111 O ASP B 28
SHEET 4 A 5 ASN A 89 ARG A 102 -1 N VAL A 99 O GLU A 114
SHEET 5 A 5 ARG A 62 TYR A 63 -1 N TYR A 63 O VAL A 100
SHEET 1 B 2 TRP A 52 TRP A 58 0
SHEET 2 B 2 GLU A 66 CYS A 72 -1 O VAL A 67 N THR A 57
SHEET 1 C 2 CYS A 77 ILE A 78 0
SHEET 2 C 2 GLU A 84 ASP A 85 -1 O ASP A 85 N CYS A 77
SHEET 1 D 5 ILE A 129 HIS A 131 0
SHEET 2 D 5 ARG C 265 VAL C 270 1 O ARG C 265 N HIS A 130
SHEET 3 D 5 ARG C 247 PRO C 254 -1 N HIS C 248 O VAL C 270
SHEET 4 D 5 TYR C 199 PHE C 206 -1 N THR C 204 O GLN C 249
SHEET 5 D 5 PHE C 215 ILE C 221 -1 O HIS C 217 N LEU C 203
SHEET 1 E 2 TRP B 52 TRP B 58 0
SHEET 2 E 2 GLU B 66 CYS B 72 -1 O GLN B 69 N THR B 55
SHEET 1 F 3 ARG B 62 TYR B 63 0
SHEET 2 F 3 GLU B 84 LYS B 103 -1 O VAL B 100 N TYR B 63
SHEET 3 F 3 GLY B 76 ILE B 78 -1 N CYS B 77 O MET B 88
SHEET 1 G 3 ARG B 62 TYR B 63 0
SHEET 2 G 3 GLU B 84 LYS B 103 -1 O VAL B 100 N TYR B 63
SHEET 3 G 3 SER B 110 VAL B 125 -1 O SER B 110 N LYS B 103
SHEET 1 H 4 CYS C 19 VAL C 21 0
SHEET 2 H 4 PHE C 98 PHE C 100 -1 O GLU C 99 N THR C 20
SHEET 3 H 4 GLY C 80 GLN C 87 -1 N ALA C 81 O PHE C 98
SHEET 4 H 4 GLU C 92 CYS C 95 -1 O GLU C 92 N GLN C 87
SHEET 1 I 5 CYS C 19 VAL C 21 0
SHEET 2 I 5 PHE C 98 PHE C 100 -1 O GLU C 99 N THR C 20
SHEET 3 I 5 GLY C 80 GLN C 87 -1 N ALA C 81 O PHE C 98
SHEET 4 I 5 GLU C 125 LEU C 133 -1 O LEU C 133 N GLY C 80
SHEET 5 I 5 SER C 146 LEU C 150 -1 O PHE C 149 N TYR C 126
SHEET 1 J 3 PRO C 42 HIS C 53 0
SHEET 2 J 3 LEU C 59 LEU C 69 -1 O VAL C 62 N HIS C 50
SHEET 3 J 3 ARG C 112 VAL C 119 -1 O PHE C 113 N TRP C 67
SHEET 1 K 3 THR C 177 GLU C 179 0
SHEET 2 K 3 LEU C 186 PHE C 190 -1 O SER C 189 N THR C 177
SHEET 3 K 3 SER C 233 LEU C 237 -1 O LEU C 237 N LEU C 186
SSBOND 1 CYS A 72 CYS A 122 1555 1555 2.04
SSBOND 2 CYS A 77 CYS A 124 1555 1555 2.05
SSBOND 3 CYS B 72 CYS B 122 1555 1555 2.04
SSBOND 4 CYS B 77 CYS B 124 1555 1555 2.03
SSBOND 5 CYS C 12 CYS C 19 1555 1555 2.03
SSBOND 6 CYS C 26 CYS C 95 1555 1555 2.03
SSBOND 7 CYS C 154 CYS C 165 1555 1555 2.04
SSBOND 8 CYS C 214 CYS C 245 1555 1555 2.04
SSBOND 9 CYS C 259 CYS C 263 1555 1555 2.05
LINK ND2 ASN A 53 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN C 18 C1 NAG C 303 1555 1555 1.45
LINK ND2 ASN C 23 C1 NAG C 305 1555 1555 1.44
LINK ND2 ASN C 36 C1 NAG C 302 1555 1555 1.45
LINK C PRO C 42 N MLY C 43 1555 1555 1.32
LINK C MLY C 43 N ASP C 44 1555 1555 1.33
LINK ND2 ASN C 194 C1 NAG C 301 1555 1555 1.44
LINK ND2 ASN C 234 C1 NAG C 304 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK OD1 ASN B 43 CA CA B 134 1555 1555 2.02
LINK ND2 ASN B 43 CA CA B 134 1555 1555 2.38
LINK OE1 GLU B 45 CA CA B 134 1555 1555 2.69
LINK OE2 GLU B 45 CA CA B 134 1555 1555 2.90
CISPEP 1 TYR A 63 PRO A 64 0 2.41
CISPEP 2 TYR B 63 PRO B 64 0 4.47
CISPEP 3 LEU C 133 PRO C 134 0 4.74
CRYST1 170.730 170.730 81.900 90.00 90.00 90.00 P 41 21 2 16
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 0.005857 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012210 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
