HEADER IMMUNE SYSTEM 18-APR-16 5JEJ
TITLE PHOSPHORYLATED STING IN COMPLEX WITH IRF-3 CTD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STIMULATOR OF INTERFERON GENES PROTEIN;
COMPND 3 CHAIN: C, D, E;
COMPND 4 FRAGMENT: UNP RESIDUES 342-379;
COMPND 5 SYNONYM: HSTING,ENDOPLASMIC RETICULUM INTERFERON STIMULATOR,ERIS,
COMPND 6 MEDIATOR OF IRF3 ACTIVATION,HMITA,TRANSMEMBRANE PROTEIN 173;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: PHOSPHOSERINE INCLUDED IN THE STRUCTURE;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: INTERFERON REGULATORY FACTOR 3;
COMPND 11 CHAIN: A, B;
COMPND 12 FRAGMENT: UNP RESIDUES 189-427;
COMPND 13 SYNONYM: IRF-3;
COMPND 14 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: TMEM173, ERIS, MITA, STING;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: IRF3;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INNATE IMMUNITY, SIGNALING, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.LI,C.SHU
REVDAT 2 29-JUN-16 5JEJ 1 JRNL
REVDAT 1 15-JUN-16 5JEJ 0
JRNL AUTH B.ZHAO,C.SHU,X.GAO,B.SANKARAN,F.DU,C.L.SHELTON,A.B.HERR,
JRNL AUTH 2 J.Y.JI,P.LI
JRNL TITL STRUCTURAL BASIS FOR CONCERTED RECRUITMENT AND ACTIVATION OF
JRNL TITL 2 IRF-3 BY INNATE IMMUNE ADAPTOR PROTEINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 E3403 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 27302953
JRNL DOI 10.1073/PNAS.1603269113
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 35068
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 44.6649 - 4.8060 1.00 2496 150 0.1570 0.1839
REMARK 3 2 4.8060 - 3.8153 1.00 2448 148 0.1297 0.1921
REMARK 3 3 3.8153 - 3.3332 1.00 2406 146 0.1449 0.1957
REMARK 3 4 3.3332 - 3.0285 1.00 2403 145 0.1774 0.2451
REMARK 3 5 3.0285 - 2.8115 1.00 2421 146 0.1875 0.2691
REMARK 3 6 2.8115 - 2.6457 1.00 2389 145 0.1816 0.2754
REMARK 3 7 2.6457 - 2.5132 1.00 2397 144 0.1840 0.2517
REMARK 3 8 2.5132 - 2.4039 1.00 2409 146 0.1903 0.2603
REMARK 3 9 2.4039 - 2.3113 1.00 2389 145 0.1920 0.2527
REMARK 3 10 2.3113 - 2.2316 1.00 2382 143 0.2386 0.3190
REMARK 3 11 2.2316 - 2.1618 0.99 2386 143 0.2307 0.3231
REMARK 3 12 2.1618 - 2.1000 0.98 2321 142 0.2381 0.2868
REMARK 3 13 2.1000 - 2.0447 0.93 2226 135 0.2503 0.3343
REMARK 3 14 2.0447 - 1.9948 0.84 1997 120 0.2729 0.3517
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760
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 : 0.007 4072
REMARK 3 ANGLE : 1.004 5552
REMARK 3 CHIRALITY : 0.041 592
REMARK 3 PLANARITY : 0.005 719
REMARK 3 DIHEDRAL : 14.791 1481
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 359 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.2300 29.1452 399.6199
REMARK 3 T TENSOR
REMARK 3 T11: 0.4819 T22: 0.6580
REMARK 3 T33: 0.3427 T12: 0.0899
REMARK 3 T13: -0.0162 T23: 0.1588
REMARK 3 L TENSOR
REMARK 3 L11: 4.5112 L22: 9.9936
REMARK 3 L33: 7.0389 L12: 1.4508
REMARK 3 L13: 2.8626 L23: -0.6216
REMARK 3 S TENSOR
REMARK 3 S11: 0.2381 S12: -0.6242 S13: -0.7020
REMARK 3 S21: 1.2135 S22: 0.0796 S23: 0.0081
REMARK 3 S31: 0.7604 S32: 0.3404 S33: -0.3135
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 372 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.9572 15.8712 409.8534
REMARK 3 T TENSOR
REMARK 3 T11: 0.4286 T22: 0.4589
REMARK 3 T33: 0.8878 T12: 0.0100
REMARK 3 T13: 0.1222 T23: 0.0767
REMARK 3 L TENSOR
REMARK 3 L11: 0.2824 L22: 1.3711
REMARK 3 L33: 4.2589 L12: -0.3421
REMARK 3 L13: 0.5260 L23: 1.1338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: 0.4116 S13: -1.4677
REMARK 3 S21: -0.4816 S22: -0.8614 S23: -1.8338
REMARK 3 S31: -0.4063 S32: 0.3789 S33: 0.9155
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 359 THROUGH 368 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.1487 68.1908 394.3349
REMARK 3 T TENSOR
REMARK 3 T11: 0.3987 T22: 0.4230
REMARK 3 T33: 0.3171 T12: -0.0071
REMARK 3 T13: 0.0243 T23: -0.1236
REMARK 3 L TENSOR
REMARK 3 L11: 2.1516 L22: 9.2692
REMARK 3 L33: 6.4454 L12: -0.2751
REMARK 3 L13: 0.4762 L23: 0.5641
REMARK 3 S TENSOR
REMARK 3 S11: 0.7745 S12: -1.4191 S13: 1.3330
REMARK 3 S21: 0.4676 S22: 0.0258 S23: -0.3304
REMARK 3 S31: -1.0455 S32: 0.5357 S33: -0.8011
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 376 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.0534 31.0636 392.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.4214 T22: 0.9819
REMARK 3 T33: 0.5737 T12: 0.1048
REMARK 3 T13: -0.0106 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 2.7479 L22: 5.8302
REMARK 3 L33: 8.2834 L12: 1.4096
REMARK 3 L13: -3.9913 L23: -5.6105
REMARK 3 S TENSOR
REMARK 3 S11: -0.1912 S12: -0.2053 S13: -0.6576
REMARK 3 S21: 0.0727 S22: -0.3916 S23: -0.7066
REMARK 3 S31: 0.3632 S32: 0.2262 S33: 0.5808
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.9165 50.2090 372.5470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1949 T22: 0.3329
REMARK 3 T33: 0.1753 T12: -0.0232
REMARK 3 T13: -0.0258 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 2.1952 L22: 3.5896
REMARK 3 L33: 1.5594 L12: -1.5454
REMARK 3 L13: -0.6813 L23: 0.3896
REMARK 3 S TENSOR
REMARK 3 S11: 0.1080 S12: 0.3774 S13: -0.0949
REMARK 3 S21: -0.2472 S22: -0.1038 S23: -0.0164
REMARK 3 S31: -0.0242 S32: -0.1074 S33: -0.0049
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 110.8615 67.4300 375.4124
REMARK 3 T TENSOR
REMARK 3 T11: 0.2615 T22: 0.3988
REMARK 3 T33: 0.4035 T12: -0.0076
REMARK 3 T13: -0.0263 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 9.9785 L22: 7.7776
REMARK 3 L33: 4.3927 L12: -8.1322
REMARK 3 L13: -4.2834 L23: 3.5891
REMARK 3 S TENSOR
REMARK 3 S11: 0.2790 S12: -0.6339 S13: 1.6651
REMARK 3 S21: -0.2589 S22: 0.2972 S23: -0.8660
REMARK 3 S31: -0.5826 S32: 0.3609 S33: -0.5851
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.9325 45.7267 381.1962
REMARK 3 T TENSOR
REMARK 3 T11: 0.1230 T22: 0.2474
REMARK 3 T33: 0.1254 T12: -0.0019
REMARK 3 T13: -0.0087 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.2385 L22: 3.0937
REMARK 3 L33: 1.2739 L12: 0.2864
REMARK 3 L13: 0.0753 L23: 1.1392
REMARK 3 S TENSOR
REMARK 3 S11: -0.0192 S12: -0.1018 S13: -0.0482
REMARK 3 S21: 0.1111 S22: 0.0107 S23: -0.0015
REMARK 3 S31: 0.0416 S32: 0.0573 S33: -0.0115
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 189 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.6198 49.0547 378.3988
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.2677
REMARK 3 T33: 0.1567 T12: 0.0053
REMARK 3 T13: 0.0171 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 3.5780 L22: 2.6560
REMARK 3 L33: 0.7774 L12: -2.1214
REMARK 3 L13: 0.4946 L23: 0.2865
REMARK 3 S TENSOR
REMARK 3 S11: 0.2741 S12: 0.2328 S13: -0.0054
REMARK 3 S21: -0.2935 S22: -0.2576 S23: 0.0803
REMARK 3 S31: 0.0426 S32: -0.0792 S33: -0.0257
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 230 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.3791 31.6161 379.7344
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.3427
REMARK 3 T33: 0.4504 T12: -0.0280
REMARK 3 T13: -0.0181 T23: 0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 2.0017 L22: 6.0983
REMARK 3 L33: 0.5136 L12: -9.0962
REMARK 3 L13: -1.7521 L23: 1.1995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: -0.0342 S13: -1.9896
REMARK 3 S21: 0.0073 S22: -0.1007 S23: 0.7756
REMARK 3 S31: 0.5444 S32: -0.1713 S33: 0.1389
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.7860 42.2408 390.8708
REMARK 3 T TENSOR
REMARK 3 T11: 0.1789 T22: 0.3431
REMARK 3 T33: 0.1364 T12: -0.0167
REMARK 3 T13: 0.0188 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 1.9321 L22: 4.9232
REMARK 3 L33: 1.4189 L12: -1.5320
REMARK 3 L13: 0.3433 L23: -0.7389
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.4566 S13: -0.1584
REMARK 3 S21: 0.2869 S22: 0.0740 S23: 0.1643
REMARK 3 S31: 0.1000 S32: 0.0281 S33: -0.0307
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 317 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.0418 60.0114 383.1770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1470 T22: 0.2824
REMARK 3 T33: 0.1787 T12: -0.0263
REMARK 3 T13: -0.0197 T23: -0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.3471 L22: 2.3154
REMARK 3 L33: 1.0308 L12: -0.6915
REMARK 3 L13: 0.0617 L23: -0.9571
REMARK 3 S TENSOR
REMARK 3 S11: -0.0545 S12: -0.1556 S13: 0.2183
REMARK 3 S21: 0.1643 S22: -0.0202 S23: -0.0819
REMARK 3 S31: -0.1275 S32: 0.0527 S33: 0.0791
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 5JEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35085
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.654
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
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
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 (%): 38.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 5.5, 200 MM MGCL2,
REMARK 280 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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 0.00000
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 657 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 673 LIES ON A SPECIAL POSITION.
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 C 341
REMARK 465 THR C 342
REMARK 465 VAL C 343
REMARK 465 GLY C 344
REMARK 465 SER C 345
REMARK 465 LEU C 346
REMARK 465 LYS C 347
REMARK 465 THR C 348
REMARK 465 SER C 349
REMARK 465 ALA C 350
REMARK 465 VAL C 351
REMARK 465 PRO C 352
REMARK 465 SER C 353
REMARK 465 THR C 354
REMARK 465 SER C 355
REMARK 465 THR C 356
REMARK 465 MET C 357
REMARK 465 SER C 358
REMARK 465 SER D 341
REMARK 465 THR D 342
REMARK 465 VAL D 343
REMARK 465 GLY D 344
REMARK 465 SER D 345
REMARK 465 LEU D 346
REMARK 465 LYS D 347
REMARK 465 THR D 348
REMARK 465 SER D 349
REMARK 465 ALA D 350
REMARK 465 VAL D 351
REMARK 465 PRO D 352
REMARK 465 SER D 353
REMARK 465 THR D 354
REMARK 465 SER D 355
REMARK 465 THR D 356
REMARK 465 MET D 357
REMARK 465 SER D 358
REMARK 465 GLU D 369
REMARK 465 LYS D 370
REMARK 465 PRO D 371
REMARK 465 LEU D 372
REMARK 465 PRO D 373
REMARK 465 LEU D 374
REMARK 465 ARG D 375
REMARK 465 THR D 376
REMARK 465 ASP D 377
REMARK 465 TRP D 378
REMARK 465 SER D 379
REMARK 465 SER E 341
REMARK 465 THR E 342
REMARK 465 VAL E 343
REMARK 465 GLY E 344
REMARK 465 SER E 345
REMARK 465 LEU E 346
REMARK 465 LYS E 347
REMARK 465 THR E 348
REMARK 465 SER E 349
REMARK 465 ALA E 350
REMARK 465 VAL E 351
REMARK 465 PRO E 352
REMARK 465 SER E 353
REMARK 465 THR E 354
REMARK 465 SER E 355
REMARK 465 THR E 356
REMARK 465 MET E 357
REMARK 465 SER E 358
REMARK 465 GLN E 359
REMARK 465 GLU E 360
REMARK 465 PRO E 361
REMARK 465 GLU E 362
REMARK 465 LEU E 363
REMARK 465 LEU E 364
REMARK 465 ILE E 365
REMARK 465 SEP E 366
REMARK 465 GLY E 367
REMARK 465 MET E 368
REMARK 465 GLU E 369
REMARK 465 LYS E 370
REMARK 465 PRO E 371
REMARK 465 LEU E 372
REMARK 465 PRO E 373
REMARK 465 LEU E 374
REMARK 465 ARG E 375
REMARK 465 SER A 186
REMARK 465 GLU A 187
REMARK 465 PHE A 188
REMARK 465 GLY A 423
REMARK 465 PRO A 424
REMARK 465 GLY A 425
REMARK 465 GLU A 426
REMARK 465 SER A 427
REMARK 465 SER B 186
REMARK 465 GLU B 187
REMARK 465 PHE B 188
REMARK 465 GLN B 422
REMARK 465 GLY B 423
REMARK 465 PRO B 424
REMARK 465 GLY B 425
REMARK 465 GLU B 426
REMARK 465 SER B 427
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 O HOH A 544 O HOH A 663 2.06
REMARK 500 O HOH A 564 O HOH A 663 2.15
REMARK 500 O HOH A 635 O HOH A 655 2.16
REMARK 500 OG SER B 303 O HOH B 501 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU C 360 NZ LYS C 370 11516 2.04
REMARK 500 O HOH A 575 O HOH B 668 1655 2.14
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 GLU C 369 130.48 65.46
REMARK 500 LYS C 370 155.34 -46.50
REMARK 500 VAL A 233 -83.21 78.10
REMARK 500 TYR A 342 -3.18 -146.41
REMARK 500 PHE B 216 139.58 -170.22
REMARK 500 THR B 237 1.87 -156.22
REMARK 500 TYR B 342 -3.27 -143.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 402 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH A 690 DISTANCE = 6.29 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JEL RELATED DB: PDB
REMARK 900 RELATED ID: 5JEK RELATED DB: PDB
REMARK 900 RELATED ID: 5JEM RELATED DB: PDB
REMARK 900 RELATED ID: 5JEO RELATED DB: PDB
REMARK 900 RELATED ID: 5JER RELATED DB: PDB
DBREF 5JEJ C 342 379 UNP Q86WV6 STING_HUMAN 342 379
DBREF 5JEJ D 342 379 UNP Q86WV6 STING_HUMAN 342 379
DBREF 5JEJ E 342 379 UNP Q86WV6 STING_HUMAN 342 379
DBREF 5JEJ A 189 427 UNP Q14653 IRF3_HUMAN 189 427
DBREF 5JEJ B 189 427 UNP Q14653 IRF3_HUMAN 189 427
SEQADV 5JEJ SER C 341 UNP Q86WV6 EXPRESSION TAG
SEQADV 5JEJ TRP C 378 UNP Q86WV6 PHE 378 CONFLICT
SEQADV 5JEJ SER D 341 UNP Q86WV6 EXPRESSION TAG
SEQADV 5JEJ TRP D 378 UNP Q86WV6 PHE 378 CONFLICT
SEQADV 5JEJ SER E 341 UNP Q86WV6 EXPRESSION TAG
SEQADV 5JEJ TRP E 378 UNP Q86WV6 PHE 378 CONFLICT
SEQADV 5JEJ SER A 186 UNP Q14653 EXPRESSION TAG
SEQADV 5JEJ GLU A 187 UNP Q14653 EXPRESSION TAG
SEQADV 5JEJ PHE A 188 UNP Q14653 EXPRESSION TAG
SEQADV 5JEJ SER B 186 UNP Q14653 EXPRESSION TAG
SEQADV 5JEJ GLU B 187 UNP Q14653 EXPRESSION TAG
SEQADV 5JEJ PHE B 188 UNP Q14653 EXPRESSION TAG
SEQRES 1 C 39 SER THR VAL GLY SER LEU LYS THR SER ALA VAL PRO SER
SEQRES 2 C 39 THR SER THR MET SER GLN GLU PRO GLU LEU LEU ILE SEP
SEQRES 3 C 39 GLY MET GLU LYS PRO LEU PRO LEU ARG THR ASP TRP SER
SEQRES 1 D 39 SER THR VAL GLY SER LEU LYS THR SER ALA VAL PRO SER
SEQRES 2 D 39 THR SER THR MET SER GLN GLU PRO GLU LEU LEU ILE SEP
SEQRES 3 D 39 GLY MET GLU LYS PRO LEU PRO LEU ARG THR ASP TRP SER
SEQRES 1 E 39 SER THR VAL GLY SER LEU LYS THR SER ALA VAL PRO SER
SEQRES 2 E 39 THR SER THR MET SER GLN GLU PRO GLU LEU LEU ILE SEP
SEQRES 3 E 39 GLY MET GLU LYS PRO LEU PRO LEU ARG THR ASP TRP SER
SEQRES 1 A 242 SER GLU PHE GLU ASN PRO LEU LYS ARG LEU LEU VAL PRO
SEQRES 2 A 242 GLY GLU GLU TRP GLU PHE GLU VAL THR ALA PHE TYR ARG
SEQRES 3 A 242 GLY ARG GLN VAL PHE GLN GLN THR ILE SER CYS PRO GLU
SEQRES 4 A 242 GLY LEU ARG LEU VAL GLY SER GLU VAL GLY ASP ARG THR
SEQRES 5 A 242 LEU PRO GLY TRP PRO VAL THR LEU PRO ASP PRO GLY MET
SEQRES 6 A 242 SER LEU THR ASP ARG GLY VAL MET SER TYR VAL ARG HIS
SEQRES 7 A 242 VAL LEU SER CYS LEU GLY GLY GLY LEU ALA LEU TRP ARG
SEQRES 8 A 242 ALA GLY GLN TRP LEU TRP ALA GLN ARG LEU GLY HIS CYS
SEQRES 9 A 242 HIS THR TYR TRP ALA VAL SER GLU GLU LEU LEU PRO ASN
SEQRES 10 A 242 SER GLY HIS GLY PRO ASP GLY GLU VAL PRO LYS ASP LYS
SEQRES 11 A 242 GLU GLY GLY VAL PHE ASP LEU GLY PRO PHE ILE VAL ASP
SEQRES 12 A 242 LEU ILE THR PHE THR GLU GLY SER GLY ARG SER PRO ARG
SEQRES 13 A 242 TYR ALA LEU TRP PHE CYS VAL GLY GLU SER TRP PRO GLN
SEQRES 14 A 242 ASP GLN PRO TRP THR LYS ARG LEU VAL MET VAL LYS VAL
SEQRES 15 A 242 VAL PRO THR CYS LEU ARG ALA LEU VAL GLU MET ALA ARG
SEQRES 16 A 242 VAL GLY GLY ALA SER SER LEU GLU ASN THR VAL ASP LEU
SEQRES 17 A 242 HIS ILE SER ASN SER HIS PRO LEU SER LEU THR SER ASP
SEQRES 18 A 242 GLN TYR LYS ALA TYR LEU GLN ASP LEU VAL GLU GLY MET
SEQRES 19 A 242 ASP PHE GLN GLY PRO GLY GLU SER
SEQRES 1 B 242 SER GLU PHE GLU ASN PRO LEU LYS ARG LEU LEU VAL PRO
SEQRES 2 B 242 GLY GLU GLU TRP GLU PHE GLU VAL THR ALA PHE TYR ARG
SEQRES 3 B 242 GLY ARG GLN VAL PHE GLN GLN THR ILE SER CYS PRO GLU
SEQRES 4 B 242 GLY LEU ARG LEU VAL GLY SER GLU VAL GLY ASP ARG THR
SEQRES 5 B 242 LEU PRO GLY TRP PRO VAL THR LEU PRO ASP PRO GLY MET
SEQRES 6 B 242 SER LEU THR ASP ARG GLY VAL MET SER TYR VAL ARG HIS
SEQRES 7 B 242 VAL LEU SER CYS LEU GLY GLY GLY LEU ALA LEU TRP ARG
SEQRES 8 B 242 ALA GLY GLN TRP LEU TRP ALA GLN ARG LEU GLY HIS CYS
SEQRES 9 B 242 HIS THR TYR TRP ALA VAL SER GLU GLU LEU LEU PRO ASN
SEQRES 10 B 242 SER GLY HIS GLY PRO ASP GLY GLU VAL PRO LYS ASP LYS
SEQRES 11 B 242 GLU GLY GLY VAL PHE ASP LEU GLY PRO PHE ILE VAL ASP
SEQRES 12 B 242 LEU ILE THR PHE THR GLU GLY SER GLY ARG SER PRO ARG
SEQRES 13 B 242 TYR ALA LEU TRP PHE CYS VAL GLY GLU SER TRP PRO GLN
SEQRES 14 B 242 ASP GLN PRO TRP THR LYS ARG LEU VAL MET VAL LYS VAL
SEQRES 15 B 242 VAL PRO THR CYS LEU ARG ALA LEU VAL GLU MET ALA ARG
SEQRES 16 B 242 VAL GLY GLY ALA SER SER LEU GLU ASN THR VAL ASP LEU
SEQRES 17 B 242 HIS ILE SER ASN SER HIS PRO LEU SER LEU THR SER ASP
SEQRES 18 B 242 GLN TYR LYS ALA TYR LEU GLN ASP LEU VAL GLU GLY MET
SEQRES 19 B 242 ASP PHE GLN GLY PRO GLY GLU SER
MODRES 5JEJ SEP C 366 SER MODIFIED RESIDUE
MODRES 5JEJ SEP D 366 SER MODIFIED RESIDUE
HET SEP C 366 10
HET SEP D 366 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 6 HOH *380(H2 O)
HELIX 1 AA1 PRO C 371 ARG C 375 5 5
HELIX 2 AA2 ASN A 190 LEU A 196 5 7
HELIX 3 AA3 ASP A 254 SER A 266 1 13
HELIX 4 AA4 LEU A 322 GLU A 334 1 13
HELIX 5 AA5 PRO A 357 ARG A 361 5 5
HELIX 6 AA6 THR A 370 GLY A 383 1 14
HELIX 7 AA7 THR A 404 GLU A 417 1 14
HELIX 8 AA8 ASN B 190 VAL B 197 5 8
HELIX 9 AA9 ASP B 254 SER B 266 1 13
HELIX 10 AB1 LEU B 322 GLU B 334 1 13
HELIX 11 AB2 PRO B 357 ARG B 361 5 5
HELIX 12 AB3 THR B 370 GLY B 383 1 14
HELIX 13 AB4 THR B 404 GLY B 418 1 15
SHEET 1 AA1 6 ARG A 213 ILE A 220 0
SHEET 2 AA1 6 PHE A 204 TYR A 210 -1 N VAL A 206 O GLN A 218
SHEET 3 AA1 6 MET A 364 PRO A 369 -1 O VAL A 368 N GLU A 205
SHEET 4 AA1 6 ALA A 343 VAL A 348 -1 N LEU A 344 O VAL A 367
SHEET 5 AA1 6 THR A 291 SER A 296 -1 N SER A 296 O ALA A 343
SHEET 6 AA1 6 GLY A 309 GLU A 310 -1 O GLY A 309 N TRP A 293
SHEET 1 AA2 5 TRP A 241 THR A 244 0
SHEET 2 AA2 5 LEU A 226 VAL A 229 1 N ARG A 227 O VAL A 243
SHEET 3 AA2 5 LEU A 272 ALA A 277 -1 O LEU A 272 N LEU A 228
SHEET 4 AA2 5 TRP A 280 ARG A 285 -1 O TRP A 282 N TRP A 275
SHEET 5 AA2 5 GLY A 317 ASP A 321 -1 O PHE A 320 N LEU A 281
SHEET 1 AA3 2 ASN A 389 VAL A 391 0
SHEET 2 AA3 2 LEU A 401 LEU A 403 -1 O LEU A 401 N VAL A 391
SHEET 1 AA4 6 ARG B 213 SER B 221 0
SHEET 2 AA4 6 GLU B 203 TYR B 210 -1 N VAL B 206 O GLN B 218
SHEET 3 AA4 6 MET B 364 PRO B 369 -1 O LYS B 366 N THR B 207
SHEET 4 AA4 6 ALA B 343 VAL B 348 -1 N LEU B 344 O VAL B 367
SHEET 5 AA4 6 THR B 291 SER B 296 -1 N TYR B 292 O CYS B 347
SHEET 6 AA4 6 GLY B 309 GLU B 310 -1 O GLY B 309 N TRP B 293
SHEET 1 AA5 5 TRP B 241 THR B 244 0
SHEET 2 AA5 5 LEU B 226 VAL B 229 1 N ARG B 227 O VAL B 243
SHEET 3 AA5 5 LEU B 272 ALA B 277 -1 O LEU B 274 N LEU B 226
SHEET 4 AA5 5 TRP B 280 ARG B 285 -1 O TRP B 282 N TRP B 275
SHEET 5 AA5 5 GLY B 317 ASP B 321 -1 O VAL B 319 N LEU B 281
SHEET 1 AA6 2 ASN B 389 VAL B 391 0
SHEET 2 AA6 2 LEU B 401 LEU B 403 -1 O LEU B 403 N ASN B 389
LINK C ILE C 365 N SEP C 366 1555 1555 1.33
LINK C SEP C 366 N GLY C 367 1555 1555 1.33
LINK C ILE D 365 N SEP D 366 1555 1555 1.33
LINK C SEP D 366 N GLY D 367 1555 1555 1.33
CISPEP 1 VAL A 233 GLY A 234 0 -16.72
CRYST1 64.076 56.401 75.548 90.00 104.64 90.00 P 1 2 1 6
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 0.015606 0.000000 0.004076 0.00000
SCALE2 0.000000 0.017730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013681 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
