HEADER TRANSCRIPTION 09-JUL-17 5OEN
TITLE CRYSTAL STRUCTURE OF STAT2 IN COMPLEX WITH IRF9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON REGULATORY FACTOR 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 206-376;
COMPND 5 SYNONYM: IRF-9,IFN-ALPHA-RESPONSIVE TRANSCRIPTION FACTOR SUBUNIT,
COMPND 6 ISGF3 P48 SUBUNIT,INTERFERON-STIMULATED GENE FACTOR 3 GAMMA,ISGF-3
COMPND 7 GAMMA,TRANSCRIPTIONAL REGULATOR ISGF3 SUBUNIT GAMMA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 141-315;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: IRF9, ISGF3G;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: STAT2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS STAT2, IRF9, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,D.PANNE
REVDAT 3 17-JAN-24 5OEN 1 REMARK
REVDAT 2 31-JAN-18 5OEN 1 JRNL
REVDAT 1 24-JAN-18 5OEN 0
JRNL AUTH S.RENGACHARI,S.GROISS,J.M.DEVOS,E.CARON,N.GRANDVAUX,D.PANNE
JRNL TITL STRUCTURAL BASIS OF STAT2 RECOGNITION BY IRF9 REVEALS
JRNL TITL 2 MOLECULAR INSIGHTS INTO ISGF3 FUNCTION.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E601 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29317535
JRNL DOI 10.1073/PNAS.1718426115
REMARK 2
REMARK 2 RESOLUTION. 2.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 3 NUMBER OF REFLECTIONS : 7469
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.260
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.190
REMARK 3 FREE R VALUE TEST SET COUNT : 761
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 32.1179 - 4.9545 0.95 1472 149 0.2468 0.2835
REMARK 3 2 4.9545 - 3.9348 0.96 1437 187 0.2279 0.2757
REMARK 3 3 3.9348 - 3.4381 0.93 1408 140 0.2621 0.3367
REMARK 3 4 3.4381 - 3.1240 0.85 1268 161 0.2847 0.3343
REMARK 3 5 3.1240 - 2.9003 0.74 1123 124 0.2982 0.3755
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.46
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 : 0.002 2754
REMARK 3 ANGLE : 0.463 3725
REMARK 3 CHIRALITY : 0.035 415
REMARK 3 PLANARITY : 0.003 486
REMARK 3 DIHEDRAL : 13.020 1689
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 5OEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7970
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.919
REMARK 200 RESOLUTION RANGE LOW (A) : 39.389
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.19400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.89800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1BF5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FORMATE AND 20%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 62.01850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER A 349
REMARK 465 PRO A 350
REMARK 465 GLY A 351
REMARK 465 SER A 352
REMARK 465 SER A 353
REMARK 465 HIS A 354
REMARK 465 LYS B 183
REMARK 465 THR B 184
REMARK 465 SER B 185
REMARK 465 SER B 186
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 NH1 ARG B 160 O HOH B 401 1.94
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 LEU A 259 -19.24 91.84
REMARK 500 ASP A 270 -103.60 62.57
REMARK 500 ASN A 278 -154.53 -130.40
REMARK 500 LYS A 312 117.65 -170.97
REMARK 500 PHE A 339 -16.90 -143.90
REMARK 500 LYS B 289 -48.01 73.82
REMARK 500 ARG B 314 69.23 -108.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5OEN A 206 376 UNP Q61179 IRF9_MOUSE 206 376
DBREF 5OEN B 141 315 UNP Q3UDU1 Q3UDU1_MOUSE 141 315
SEQADV 5OEN ALA A 347 UNP Q61179 GLU 347 ENGINEERED MUTATION
SEQADV 5OEN ALA A 348 UNP Q61179 GLU 348 ENGINEERED MUTATION
SEQADV 5OEN ALA B 242 UNP Q3UDU1 GLN 242 ENGINEERED MUTATION
SEQADV 5OEN ALA B 243 UNP Q3UDU1 LYS 243 ENGINEERED MUTATION
SEQRES 1 A 171 LEU PRO LEU ASN SER ASP TYR SER LEU LEU LEU THR PHE
SEQRES 2 A 171 ILE TYR GLY GLY ARG VAL VAL GLY LYS THR GLN VAL HIS
SEQRES 3 A 171 SER LEU ASP CYS ARG LEU VAL ALA GLU ARG SER ASP SER
SEQRES 4 A 171 GLU SER SER MET GLU GLN VAL GLU PHE PRO LYS PRO ASP
SEQRES 5 A 171 PRO LEU GLU PRO THR GLN HIS LEU LEU ASN GLN LEU ASP
SEQRES 6 A 171 ARG GLY VAL LEU VAL ALA SER ASN SER ARG GLY LEU PHE
SEQRES 7 A 171 VAL GLN ARG LEU CYS PRO ILE PRO ILE SER TRP ASN ALA
SEQRES 8 A 171 PRO GLU ALA PRO PRO GLY PRO GLY PRO HIS LEU LEU PRO
SEQRES 9 A 171 SER ASN LYS CYS VAL GLU LEU PHE LYS THR THR TYR PHE
SEQRES 10 A 171 CYS ARG ASP LEU ALA GLN TYR PHE GLN GLY GLN GLY PRO
SEQRES 11 A 171 PRO PRO LYS PHE GLN ALA THR LEU HIS PHE TRP ALA ALA
SEQRES 12 A 171 SER PRO GLY SER SER HIS SER GLN GLU ASN LEU ILE THR
SEQRES 13 A 171 VAL GLN MET GLU GLN ALA PHE ALA ARG HIS LEU LEU GLU
SEQRES 14 A 171 LYS ILE
SEQRES 1 B 175 GLN LEU GLU ILE GLU ASN ARG ILE GLN GLY LEU HIS VAL
SEQRES 2 B 175 ASP ILE GLU PHE LEU VAL ARG SER ILE ARG GLN LEU LYS
SEQRES 3 B 175 ASP GLU GLN ASP VAL PHE SER PHE ARG TYR THR VAL PHE
SEQRES 4 B 175 SER LEU LYS LYS THR SER SER SER ASP PRO HIS GLN SER
SEQRES 5 B 175 GLN GLN ALA GLN LEU VAL GLN ALA THR ALA ASN LYS VAL
SEQRES 6 B 175 ASP ARG MET ARG LYS GLU VAL LEU ASP ILE SER LYS GLY
SEQRES 7 B 175 LEU VAL GLY ARG LEU THR THR LEU VAL ASP LEU LEU LEU
SEQRES 8 B 175 PRO LYS LEU ASP GLU TRP LYS VAL GLN GLN ALA ALA SER
SEQRES 9 B 175 CYS ILE GLY ALA PRO PRO PRO GLU LEU GLN LEU GLU GLN
SEQRES 10 B 175 LEU GLU GLN TRP LEU THR ALA GLY ALA LYS PHE LEU PHE
SEQRES 11 B 175 HIS LEU ARG GLN LEU LEU LYS GLN LEU LYS GLU MET SER
SEQRES 12 B 175 HIS MET LEU ARG TYR LYS GLY ASP MET PHE GLY GLN GLY
SEQRES 13 B 175 VAL ASP LEU GLN ASN ALA GLN VAL MET GLU LEU LEU GLN
SEQRES 14 B 175 ARG LEU LEU GLN ARG SER
FORMUL 3 HOH *19(H2 O)
HELIX 1 AA1 PRO A 261 ASN A 267 1 7
HELIX 2 AA2 THR A 319 GLY A 332 1 14
HELIX 3 AA3 ALA A 367 GLU A 374 1 8
HELIX 4 AA4 LEU B 142 LEU B 181 1 40
HELIX 5 AA5 PRO B 189 CYS B 245 1 57
HELIX 6 AA6 GLN B 254 SER B 283 1 30
HELIX 7 AA7 HIS B 284 LEU B 286 5 3
HELIX 8 AA8 GLY B 290 ARG B 314 1 25
SHEET 1 AA1 5 VAL A 224 VAL A 230 0
SHEET 2 AA1 5 LEU A 214 TYR A 220 -1 N LEU A 216 O THR A 228
SHEET 3 AA1 5 GLU A 357 GLN A 366 -1 O THR A 361 N ILE A 219
SHEET 4 AA1 5 THR A 342 ALA A 347 -1 N LEU A 343 O VAL A 362
SHEET 5 AA1 5 ILE A 292 ASN A 295 -1 N SER A 293 O HIS A 344
SHEET 1 AA2 5 GLN A 250 GLU A 252 0
SHEET 2 AA2 5 ASP A 234 VAL A 238 1 N ARG A 236 O VAL A 251
SHEET 3 AA2 5 VAL A 273 ASN A 278 -1 O VAL A 273 N LEU A 237
SHEET 4 AA2 5 GLY A 281 ARG A 286 -1 O PHE A 283 N ALA A 276
SHEET 5 AA2 5 VAL A 314 LYS A 318 -1 O VAL A 314 N VAL A 284
CISPEP 1 GLU A 260 PRO A 261 0 -4.96
CRYST1 30.602 124.037 51.029 90.00 92.10 90.00 P 1 21 1 2
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 0.032678 0.000000 0.001196 0.00000
SCALE2 0.000000 0.008062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
