HEADER IMMUNE SYSTEM 06-JUN-18 6DNK
TITLE HUMAN STIMULATOR OF INTERFERON GENES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STIMULATOR OF INTERFERON GENES PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HSTING,ENDOPLASMIC RETICULUM INTERFERON STIMULATOR,ERIS,
COMPND 5 MEDIATOR OF IRF3 ACTIVATION,HMITA,TRANSMEMBRANE PROTEIN 173;
COMPND 6 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: 562
KEYWDS HUMAN STING, COMPLEX, 2', 3'-CGAMP, TMEM173, ALA230 ALLELLE,
KEYWDS 2 230A/232R, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.FERNANDEZ,L.LI,S.L.ERGUN
REVDAT 5 11-OCT-23 6DNK 1 JRNL HETSYN
REVDAT 4 07-AUG-19 6DNK 1 JRNL
REVDAT 3 24-JUL-19 6DNK 1 JRNL
REVDAT 2 17-JUL-19 6DNK 1 JRNL
REVDAT 1 13-MAR-19 6DNK 0
JRNL AUTH S.L.ERGUN,D.FERNANDEZ,T.M.WEISS,L.LI
JRNL TITL STING POLYMER STRUCTURE REVEALS MECHANISMS FOR ACTIVATION,
JRNL TITL 2 HYPERACTIVATION, AND INHIBITION.
JRNL REF CELL V. 178 290 2019
JRNL REFN ISSN 1097-4172
JRNL PMID 31230712
JRNL DOI 10.1016/J.CELL.2019.05.036
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.L.ERGUN,D.FERNANDEZ,T.M.WEISS,L.LI
REMARK 1 TITL STING POLYMER STRUCTURE REVEALS MECHANISMS FOR ACTIVATION,
REMARK 1 TITL 2 HYPERACTIVATION, AND INHIBITION
REMARK 1 REF BIORXIV 2019
REMARK 1 REFN ISSN 2692-8205
REMARK 1 DOI 10.1101/552166
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 15683
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 876
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1140
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.52
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.16000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.065
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1480 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1375 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2014 ; 1.771 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3126 ; 1.050 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 7.604 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;35.252 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 243 ;17.662 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;22.211 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 225 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1675 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 357 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 693 ; 2.780 ; 3.814
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 692 ; 2.781 ; 3.809
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 862 ; 4.270 ; 5.671
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 863 ; 4.268 ; 5.678
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 787 ; 3.571 ; 4.259
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 788 ; 3.569 ; 4.258
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1151 ; 5.747 ; 6.221
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1629 ; 8.466 ;30.601
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1595 ; 8.404 ;30.521
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6DNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1000234993.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL, NON FIXED EXIT SLIT
REMARK 200 OPTICS : RH COATED COLLIMATING MIRRORS, K
REMARK 200 -B FOCUSING MIRRORS
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16624
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 39.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.71800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 6CY7
REMARK 200
REMARK 200 REMARK: NEEDLE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM SULFATE, PEG 3350, PH 6.7,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K
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 17.93150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.20700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.20700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 8.96575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.20700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.20700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.89725
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.20700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.20700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 8.96575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.20700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.20700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.89725
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 17.93150
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: 4900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 0.000000 1.000000 0.000000 110.41400
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -110.41400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -71.72600
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 A 557 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 ASN A 187
REMARK 465 ASN A 188
REMARK 465 LEU A 189
REMARK 465 LEU A 190
REMARK 465 ARG A 191
REMARK 465 GLY A 192
REMARK 465 ASP A 319
REMARK 465 ASP A 320
REMARK 465 SER A 321
REMARK 465 GLU A 336
REMARK 465 GLU A 337
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 OG1 THR A 263 O HOH A 502 2.15
REMARK 500 O HOH A 526 O HOH A 559 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 232 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
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 TYR A 167 -67.28 -147.23
REMARK 500 HIS A 185 -42.01 179.42
REMARK 500 ASP A 216 119.94 -166.05
REMARK 500 SER A 305 -105.51 -143.82
REMARK 500 GLN A 306 -55.79 17.80
REMARK 500 ARG A 334 89.87 -64.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 305 GLN A 306 -126.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1SY A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1SY A 401
DBREF 6DNK A 154 337 UNP Q86WV6 STING_HUMAN 154 337
SEQADV 6DNK ALA A 230 UNP Q86WV6 GLY 230 CONFLICT
SEQADV 6DNK ARG A 232 UNP Q86WV6 HIS 232 CONFLICT
SEQRES 1 A 184 ASN VAL ALA HIS GLY LEU ALA TRP SER TYR TYR ILE GLY
SEQRES 2 A 184 TYR LEU ARG LEU ILE LEU PRO GLU LEU GLN ALA ARG ILE
SEQRES 3 A 184 ARG THR TYR ASN GLN HIS TYR ASN ASN LEU LEU ARG GLY
SEQRES 4 A 184 ALA VAL SER GLN ARG LEU TYR ILE LEU LEU PRO LEU ASP
SEQRES 5 A 184 CYS GLY VAL PRO ASP ASN LEU SER MET ALA ASP PRO ASN
SEQRES 6 A 184 ILE ARG PHE LEU ASP LYS LEU PRO GLN GLN THR ALA ASP
SEQRES 7 A 184 ARG ALA GLY ILE LYS ASP ARG VAL TYR SER ASN SER ILE
SEQRES 8 A 184 TYR GLU LEU LEU GLU ASN GLY GLN ARG ALA GLY THR CYS
SEQRES 9 A 184 VAL LEU GLU TYR ALA THR PRO LEU GLN THR LEU PHE ALA
SEQRES 10 A 184 MET SER GLN TYR SER GLN ALA GLY PHE SER ARG GLU ASP
SEQRES 11 A 184 ARG LEU GLU GLN ALA LYS LEU PHE CYS ARG THR LEU GLU
SEQRES 12 A 184 ASP ILE LEU ALA ASP ALA PRO GLU SER GLN ASN ASN CYS
SEQRES 13 A 184 ARG LEU ILE ALA TYR GLN GLU PRO ALA ASP ASP SER SER
SEQRES 14 A 184 PHE SER LEU SER GLN GLU VAL LEU ARG HIS LEU ARG GLN
SEQRES 15 A 184 GLU GLU
HET 1SY A 401 45
HETNAM 1SY CGAMP
HETSYN 1SY 2',3' CGAMP; C-GMP-AMP; C[G(2',5')PA(3',5')P]
FORMUL 2 1SY C20 H24 N10 O13 P2
FORMUL 3 HOH *67(H2 O)
HELIX 1 AA1 ASN A 154 GLY A 166 1 13
HELIX 2 AA2 TYR A 167 GLN A 184 1 18
HELIX 3 AA3 ASN A 211 ALA A 215 5 5
HELIX 4 AA4 THR A 263 TYR A 274 1 12
HELIX 5 AA5 SER A 275 GLY A 278 5 4
HELIX 6 AA6 SER A 280 GLU A 282 5 3
HELIX 7 AA7 ASP A 283 ASP A 301 1 19
HELIX 8 AA8 SER A 324 ARG A 334 1 11
SHEET 1 AA1 5 ILE A 219 LYS A 224 0
SHEET 2 AA1 5 SER A 243 GLU A 249 -1 O ILE A 244 N ASP A 223
SHEET 3 AA1 5 GLN A 252 TYR A 261 -1 O ALA A 254 N LEU A 247
SHEET 4 AA1 5 LEU A 198 PRO A 203 1 N LEU A 201 O GLU A 260
SHEET 5 AA1 5 CYS A 309 TYR A 314 1 O ILE A 312 N LEU A 202
SHEET 1 AA2 2 GLN A 228 ARG A 232 0
SHEET 2 AA2 2 ILE A 235 TYR A 240 -1 O TYR A 240 N GLN A 228
SITE 1 AC1 20 SER A 162 TYR A 163 GLY A 166 TYR A 167
SITE 2 AC1 20 ARG A 232 ILE A 235 ARG A 238 VAL A 239
SITE 3 AC1 20 TYR A 240 THR A 263 PRO A 264 HOH A 501
SITE 4 AC1 20 HOH A 502 HOH A 506 HOH A 508 HOH A 511
SITE 5 AC1 20 HOH A 513 HOH A 520 HOH A 538 HOH A 545
CRYST1 110.414 110.414 35.863 90.00 90.00 90.00 P 41 21 2 8
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 0.009057 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009057 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027884 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
