HEADER TRANSFERASE/DNA 19-APR-13 4K9B
TITLE STRUCTURE OF TERNARY COMPLEX OF CGAS WITH DSDNA AND BOUND C[G(2 ,5 )
TITLE 2 PA(3 ,5 )P]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 147-507;
COMPND 5 SYNONYM: CGAMP SYNTHASE, CGAS, M-CGAS, MAB-21 DOMAIN-CONTAINING
COMPND 6 PROTEIN 1;
COMPND 7 EC: 2.7.7.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA-F;
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA-R;
COMPND 15 CHAIN: E;
COMPND 16 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: MB21D1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: THIS SEQUENCE WAS SYNTHESIZED BY REGULAR PROTOCOL;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE WAS SYNTHESIZED BY REGULAR PROTOCOL
KEYWDS NUCLEOTIDYLTRANSFERASE FOLD, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GAO,Y.WU,D.J.PATEL
REVDAT 3 28-FEB-24 4K9B 1 REMARK SEQADV LINK
REVDAT 2 28-AUG-13 4K9B 1 JRNL
REVDAT 1 15-MAY-13 4K9B 0
JRNL AUTH P.GAO,M.ASCANO,Y.WU,W.BARCHET,B.L.GAFFNEY,T.ZILLINGER,
JRNL AUTH 2 A.A.SERGANOV,Y.LIU,R.A.JONES,G.HARTMANN,T.TUSCHL,D.J.PATEL
JRNL TITL CYCLIC [G(2',5')PA(3',5')P] IS THE METAZOAN SECOND MESSENGER
JRNL TITL 2 PRODUCED BY DNA-ACTIVATED CYCLIC GMP-AMP SYNTHASE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 153 1094 2013
JRNL REFN ISSN 0092-8674
JRNL PMID 23647843
JRNL DOI 10.1016/J.CELL.2013.04.046
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25950
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.710
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 42.6631 - 5.4437 0.99 1811 152 0.1753 0.2040
REMARK 3 2 5.4437 - 4.3222 1.00 1753 146 0.1387 0.1984
REMARK 3 3 4.3222 - 3.7762 1.00 1734 145 0.1507 0.1768
REMARK 3 4 3.7762 - 3.4311 1.00 1709 142 0.1565 0.1932
REMARK 3 5 3.4311 - 3.1853 1.00 1708 143 0.1692 0.2076
REMARK 3 6 3.1853 - 2.9975 1.00 1725 144 0.1995 0.2517
REMARK 3 7 2.9975 - 2.8474 1.00 1697 142 0.2000 0.2432
REMARK 3 8 2.8474 - 2.7235 1.00 1689 141 0.1950 0.2681
REMARK 3 9 2.7235 - 2.6187 1.00 1692 141 0.1962 0.2383
REMARK 3 10 2.6187 - 2.5283 1.00 1684 141 0.1848 0.2817
REMARK 3 11 2.5283 - 2.4493 1.00 1691 141 0.1881 0.2837
REMARK 3 12 2.4493 - 2.3793 1.00 1699 141 0.2023 0.2606
REMARK 3 13 2.3793 - 2.3166 1.00 1681 141 0.2249 0.2644
REMARK 3 14 2.3166 - 2.2601 1.00 1677 140 0.2452 0.3307
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.770
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 : 0.010 3706
REMARK 3 ANGLE : 1.933 5114
REMARK 3 CHIRALITY : 0.149 555
REMARK 3 PLANARITY : 0.004 539
REMARK 3 DIHEDRAL : 20.378 1465
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 183.0612 319.2490 170.7980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2758 T22: 0.2174
REMARK 3 T33: 0.4399 T12: -0.1183
REMARK 3 T13: 0.0349 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.0195 L22: 2.3563
REMARK 3 L33: 7.2086 L12: -0.9343
REMARK 3 L13: -0.5327 L23: 0.2088
REMARK 3 S TENSOR
REMARK 3 S11: 0.2098 S12: 0.0680 S13: 0.3599
REMARK 3 S21: 0.0408 S22: 0.0704 S23: 0.1284
REMARK 3 S31: -1.2731 S32: -0.4562 S33: -0.1651
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): 185.4193 309.0271 161.9726
REMARK 3 T TENSOR
REMARK 3 T11: 0.2666 T22: 0.2079
REMARK 3 T33: 0.3025 T12: -0.0252
REMARK 3 T13: 0.0125 T23: 0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 2.9524 L22: 4.9686
REMARK 3 L33: 8.4600 L12: -0.0803
REMARK 3 L13: -0.6621 L23: 4.4573
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: 0.2721 S13: 0.0498
REMARK 3 S21: -0.2216 S22: -0.0609 S23: -0.0002
REMARK 3 S31: -0.3478 S32: -0.0139 S33: 0.0558
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 220 THROUGH 376 )
REMARK 3 ORIGIN FOR THE GROUP (A): 192.6127 300.4706 161.5935
REMARK 3 T TENSOR
REMARK 3 T11: 0.2706 T22: 0.3162
REMARK 3 T33: 0.3019 T12: 0.0199
REMARK 3 T13: 0.0798 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.5824 L22: 2.4522
REMARK 3 L33: 1.8183 L12: 0.7993
REMARK 3 L13: -0.3594 L23: -1.2562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: 0.2206 S13: -0.1306
REMARK 3 S21: -0.3684 S22: -0.1725 S23: -0.4640
REMARK 3 S31: 0.0056 S32: 0.4248 S33: 0.1267
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 377 THROUGH 506 )
REMARK 3 ORIGIN FOR THE GROUP (A): 193.0083 303.9679 185.8648
REMARK 3 T TENSOR
REMARK 3 T11: 0.2133 T22: 0.3724
REMARK 3 T33: 0.3081 T12: -0.0781
REMARK 3 T13: 0.0018 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 2.5560 L22: 2.4511
REMARK 3 L33: 2.3960 L12: -0.0220
REMARK 3 L13: 0.1988 L23: 1.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0636 S12: -0.4008 S13: 0.1234
REMARK 3 S21: 0.1208 S22: 0.1184 S23: -0.4699
REMARK 3 S31: -0.1471 S32: 0.6599 S33: -0.1023
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 169.0731 314.6758 168.6682
REMARK 3 T TENSOR
REMARK 3 T11: 0.5561 T22: 0.3239
REMARK 3 T33: 0.3809 T12: 0.0190
REMARK 3 T13: 0.0784 T23: 0.0879
REMARK 3 L TENSOR
REMARK 3 L11: 5.8287 L22: 3.7077
REMARK 3 L33: 2.8707 L12: 0.4850
REMARK 3 L13: -1.0700 L23: 0.1939
REMARK 3 S TENSOR
REMARK 3 S11: 0.2400 S12: 0.7437 S13: 0.4585
REMARK 3 S21: -0.5169 S22: 0.2444 S23: -0.0075
REMARK 3 S31: -1.2916 S32: -0.2889 S33: -0.2178
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 4 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 167.3470 313.1241 169.8164
REMARK 3 T TENSOR
REMARK 3 T11: 0.3956 T22: 0.4533
REMARK 3 T33: 0.3718 T12: -0.0437
REMARK 3 T13: 0.0421 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 5.5874 L22: 6.9987
REMARK 3 L33: 7.0864 L12: 0.4624
REMARK 3 L13: 0.8949 L23: 1.9848
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: 0.1259 S13: 0.3902
REMARK 3 S21: 0.2203 S22: 0.1612 S23: 0.5477
REMARK 3 S31: 0.0921 S32: -1.2245 S33: -0.0986
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 4K9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000079053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 0.2 M MGCL2, 30% PEG300,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.65550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.13900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.01600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.65550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.13900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.01600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.65550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.13900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.01600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.65550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.13900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.01600
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: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E
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 A 773 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 780 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 A 146
REMARK 465 PRO A 147
REMARK 465 ASP A 148
REMARK 465 ARG A 241
REMARK 465 ILE A 242
REMARK 465 PRO A 243
REMARK 465 LEU A 507
REMARK 465 DA D 16
REMARK 465 DA D 17
REMARK 465 DT E 1
REMARK 465 DT E 2
REMARK 465 DT E 3
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 ARG A 244 CG CD NE CZ NH1 NH2
REMARK 470 DC E 4 P OP1 OP2
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 DC D 8 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DG E 11 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DG E 11 N9 - C4 - C5 ANGL. DEV. = -2.5 DEGREES
REMARK 500 DA E 14 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT E 17 O4' - C1' - N1 ANGL. DEV. = 4.5 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 ARG A 185 -56.64 -136.28
REMARK 500 GLU A 186 49.11 -81.85
REMARK 500 SER A 207 -56.81 70.12
REMARK 500 TYR A 229 -126.91 61.69
REMARK 500 TRP A 331 -74.41 -121.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 GTP AND ATP WAS ADDED TO THE CRYSTALLIZATION CONDITION AND A C[G(2',
REMARK 600 5')PA(3',5')P LIGAND WAS OBSERVED WHICH HAS BEEN REPRESENTED AS G
REMARK 600 AND A WITH A 2' TO 5' AND A 3' TO 5' LINK
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 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 378 NE2
REMARK 620 2 CYS A 384 SG 113.7
REMARK 620 3 CYS A 385 SG 103.9 131.0
REMARK 620 4 CYS A 392 SG 97.8 100.0 104.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A A 604
DBREF 4K9B A 147 507 UNP Q8C6L5 CGAS_MOUSE 147 507
DBREF 4K9B D 1 17 PDB 4K9B 4K9B 1 17
DBREF 4K9B E 1 17 PDB 4K9B 4K9B 1 17
SEQADV 4K9B SER A 146 UNP Q8C6L5 EXPRESSION TAG
SEQRES 1 A 362 SER PRO ASP LYS LEU LYS LYS VAL LEU ASP LYS LEU ARG
SEQRES 2 A 362 LEU LYS ARG LYS ASP ILE SER GLU ALA ALA GLU THR VAL
SEQRES 3 A 362 ASN LYS VAL VAL GLU ARG LEU LEU ARG ARG MET GLN LYS
SEQRES 4 A 362 ARG GLU SER GLU PHE LYS GLY VAL GLU GLN LEU ASN THR
SEQRES 5 A 362 GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN
SEQRES 6 A 362 GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE
SEQRES 7 A 362 GLU LEU GLN GLU TYR TYR GLU THR GLY ALA PHE TYR LEU
SEQRES 8 A 362 VAL LYS PHE LYS ARG ILE PRO ARG GLY ASN PRO LEU SER
SEQRES 9 A 362 HIS PHE LEU GLU GLY GLU VAL LEU SER ALA THR LYS MET
SEQRES 10 A 362 LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU VAL LYS
SEQRES 11 A 362 GLU ILE LYS ASP ILE ASP VAL SER VAL GLU LYS GLU LYS
SEQRES 12 A 362 PRO GLY SER PRO ALA VAL THR LEU LEU ILE ARG ASN PRO
SEQRES 13 A 362 GLU GLU ILE SER VAL ASP ILE ILE LEU ALA LEU GLU SER
SEQRES 14 A 362 LYS GLY SER TRP PRO ILE SER THR LYS GLU GLY LEU PRO
SEQRES 15 A 362 ILE GLN GLY TRP LEU GLY THR LYS VAL ARG THR ASN LEU
SEQRES 16 A 362 ARG ARG GLU PRO PHE TYR LEU VAL PRO LYS ASN ALA LYS
SEQRES 17 A 362 ASP GLY ASN SER PHE GLN GLY GLU THR TRP ARG LEU SER
SEQRES 18 A 362 PHE SER HIS THR GLU LYS TYR ILE LEU ASN ASN HIS GLY
SEQRES 19 A 362 ILE GLU LYS THR CYS CYS GLU SER SER GLY ALA LYS CYS
SEQRES 20 A 362 CYS ARG LYS GLU CYS LEU LYS LEU MET LYS TYR LEU LEU
SEQRES 21 A 362 GLU GLN LEU LYS LYS GLU PHE GLN GLU LEU ASP ALA PHE
SEQRES 22 A 362 CYS SER TYR HIS VAL LYS THR ALA ILE PHE HIS MET TRP
SEQRES 23 A 362 THR GLN ASP PRO GLN ASP SER GLN TRP ASP PRO ARG ASN
SEQRES 24 A 362 LEU SER SER CYS PHE ASP LYS LEU LEU ALA PHE PHE LEU
SEQRES 25 A 362 GLU CYS LEU ARG THR GLU LYS LEU ASP HIS TYR PHE ILE
SEQRES 26 A 362 PRO LYS PHE ASN LEU PHE SER GLN GLU LEU ILE ASP ARG
SEQRES 27 A 362 LYS SER LYS GLU PHE LEU SER LYS LYS ILE GLU TYR GLU
SEQRES 28 A 362 ARG ASN ASN GLY PHE PRO ILE PHE ASP LYS LEU
SEQRES 1 D 17 DA DA DA DT DT DG DC DC DG DA DA DG DA
SEQRES 2 D 17 DC DG DA DA
SEQRES 1 E 17 DT DT DT DC DG DT DC DT DT DC DG DG DC
SEQRES 2 E 17 DA DA DT DT
HET ZN A 601 1
HET PO4 A 602 5
HET G A 603 23
HET A A 604 22
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM G GUANOSINE-5'-MONOPHOSPHATE
HETNAM A ADENOSINE-5'-MONOPHOSPHATE
FORMUL 4 ZN ZN 2+
FORMUL 5 PO4 O4 P 3-
FORMUL 6 G C10 H14 N5 O8 P
FORMUL 7 A C10 H14 N5 O7 P
FORMUL 8 HOH *165(H2 O)
HELIX 1 1 LYS A 149 ARG A 158 1 10
HELIX 2 2 LYS A 160 GLN A 183 1 24
HELIX 3 3 SER A 258 GLU A 276 1 19
HELIX 4 4 PRO A 319 LYS A 323 5 5
HELIX 5 5 GLY A 333 ARG A 342 1 10
HELIX 6 6 PHE A 367 ASN A 377 1 11
HELIX 7 7 CYS A 393 PHE A 412 1 20
HELIX 8 8 GLN A 413 ASP A 416 5 4
HELIX 9 9 CYS A 419 ASP A 434 1 16
HELIX 10 10 GLN A 436 ARG A 443 5 8
HELIX 11 11 ASN A 444 THR A 462 1 19
HELIX 12 12 ASP A 482 ASN A 499 1 18
HELIX 13 13 PHE A 501 LYS A 506 5 6
SHEET 1 A 7 GLU A 193 THR A 197 0
SHEET 2 A 7 GLU A 211 GLU A 219 -1 O LYS A 217 N GLU A 193
SHEET 3 A 7 GLU A 303 SER A 314 1 O ALA A 311 N LEU A 218
SHEET 4 A 7 PHE A 345 VAL A 348 -1 O LEU A 347 N LEU A 312
SHEET 5 A 7 TRP A 363 SER A 366 -1 O ARG A 364 N VAL A 348
SHEET 6 A 7 PHE A 234 PHE A 239 -1 N TYR A 235 O TRP A 363
SHEET 7 A 7 ILE A 223 GLU A 227 -1 N GLN A 226 O LEU A 236
SHEET 1 B 5 GLU A 193 THR A 197 0
SHEET 2 B 5 GLU A 211 GLU A 219 -1 O LYS A 217 N GLU A 193
SHEET 3 B 5 GLU A 303 SER A 314 1 O ALA A 311 N LEU A 218
SHEET 4 B 5 ALA A 293 ARG A 299 -1 N LEU A 296 O VAL A 306
SHEET 5 B 5 ASP A 281 VAL A 284 -1 N SER A 283 O LEU A 297
SHEET 1 C 2 LEU A 252 GLU A 253 0
SHEET 2 C 2 VAL A 256 LEU A 257 -1 O VAL A 256 N GLU A 253
SHEET 1 D 2 ALA A 352 ASP A 354 0
SHEET 2 D 2 SER A 357 GLN A 359 -1 O GLN A 359 N ALA A 352
LINK O2' G A 603 P A A 604 1555 1555 1.58
LINK P G A 603 O3' A A 604 1555 1555 1.59
LINK NE2 HIS A 378 ZN ZN A 601 1555 1555 2.13
LINK SG CYS A 384 ZN ZN A 601 1555 1555 2.37
LINK SG CYS A 385 ZN ZN A 601 1555 1555 2.37
LINK SG CYS A 392 ZN ZN A 601 1555 1555 2.39
CISPEP 1 LYS A 184 ARG A 185 0 2.90
CISPEP 2 ASN A 300 PRO A 301 0 2.65
SITE 1 AC1 4 HIS A 378 CYS A 384 CYS A 385 CYS A 392
SITE 1 AC2 7 HIS A 203 HOH A 793 HOH A 813 DG D 9
SITE 2 AC2 7 DA D 10 DC E 10 DG E 11
SITE 1 AC3 9 ASP A 213 LYS A 288 GLY A 290 SER A 291
SITE 2 AC3 9 ASP A 307 ILE A 309 LYS A 350 ARG A 364
SITE 3 AC3 9 A A 604
SITE 1 AC4 4 ARG A 364 CYS A 419 TYR A 421 G A 603
CRYST1 85.311 98.278 130.032 90.00 90.00 90.00 I 2 2 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 0.011722 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007690 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
