HEADER TRANSCRIPTION 13-APR-17 5XGE
TITLE CRYSTAL STRUCTURE OF THE PAS-GGDEF-EAL DOMAIN OF PA0861 FROM
TITLE 2 PSEUDOMONAS AERUGINOSA IN COMPLEX WITH CYCLIC DI-GMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN PA0861;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 233-800;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: PA0861;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PNIC-CH2
KEYWDS PAS DOMAIN, GGDEF-EAL DOMAIN, PSEUDOMONAS AERUGINOSA, BIOFILM, RBDA,
KEYWDS 2 PA0861, CYCLIC DI-GMP, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.LIU,C.W.LIEW,R.SREEKANTH,J.LESCAR
REVDAT 5 27-MAR-24 5XGE 1 HETSYN
REVDAT 4 03-APR-19 5XGE 1 JRNL
REVDAT 3 04-APR-18 5XGE 1 JRNL
REVDAT 2 28-FEB-18 5XGE 1 JRNL
REVDAT 1 20-DEC-17 5XGE 0
JRNL AUTH C.LIU,C.W.LIEW,Y.H.WONG,S.T.TAN,W.H.POH,M.S.S.MANIMEKALAI,
JRNL AUTH 2 S.RAJAN,L.XIN,Z.X.LIANG,G.GRUBER,S.A.RICE,J.LESCAR
JRNL TITL INSIGHTS INTO BIOFILM DISPERSAL REGULATION FROM THE CRYSTAL
JRNL TITL 2 STRUCTURE OF THE PAS-GGDEF-EAL REGION OF RBDA FROM
JRNL TITL 3 PSEUDOMONAS AERUGINOSA.
JRNL REF J. BACTERIOL. V. 200 2018
JRNL REFN ESSN 1098-5530
JRNL PMID 29109186
JRNL DOI 10.1128/JB.00515-17
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11285
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 565
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2663
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1789
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2530
REMARK 3 BIN R VALUE (WORKING SET) : 0.1753
REMARK 3 BIN FREE R VALUE : 0.2468
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.99
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4295
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 93.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.83990
REMARK 3 B22 (A**2) : -0.83990
REMARK 3 B33 (A**2) : 1.67990
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.360
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.528
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.852
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4424 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6001 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1556 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 114 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 644 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4424 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 578 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5175 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.35
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.18
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0572 0.9174 91.3356
REMARK 3 T TENSOR
REMARK 3 T11: -0.1673 T22: -0.1296
REMARK 3 T33: -0.0996 T12: 0.0236
REMARK 3 T13: 0.0752 T23: -0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 0.9129 L22: 0.4578
REMARK 3 L33: 1.3899 L12: 0.1135
REMARK 3 L13: 0.2635 L23: 0.0153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: 0.0591 S13: 0.0228
REMARK 3 S21: -0.0690 S22: 0.0410 S23: -0.0903
REMARK 3 S31: -0.1044 S32: 0.1876 S33: -0.0610
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5XGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11308
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.310
REMARK 200 RESOLUTION RANGE LOW (A) : 48.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.19100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 0.61800
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES/IMIDAZOLE AT PH 6.5, 0.1M
REMARK 280 CARBOXYLIC ACID, 10% (W/V) PEG 4000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 67.44050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 38.93679
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 70.40800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 67.44050
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 38.93679
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 70.40800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 67.44050
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 38.93679
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 70.40800
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 67.44050
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 38.93679
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 70.40800
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 67.44050
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 38.93679
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 70.40800
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 67.44050
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 38.93679
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 70.40800
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.87358
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 140.81600
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 77.87358
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 140.81600
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 77.87358
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 140.81600
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 77.87358
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 140.81600
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 77.87358
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 140.81600
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 77.87358
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 140.81600
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: 9410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 211.22400
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 233
REMARK 465 GLN A 234
REMARK 465 GLU A 235
REMARK 465 VAL A 236
REMARK 465 GLU A 237
REMARK 465 ASN A 238
REMARK 465 ALA A 239
REMARK 465 LEU A 240
REMARK 465 GLU A 299
REMARK 465 SER A 300
REMARK 465 SER A 301
REMARK 465 ARG A 302
REMARK 465 GLU A 303
REMARK 465 GLU A 304
REMARK 465 GLY A 305
REMARK 465 MET A 306
REMARK 465 LEU A 307
REMARK 465 GLN A 798
REMARK 465 PRO A 799
REMARK 465 PRO A 800
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 SER A 292 33.32 -92.31
REMARK 500 LEU A 293 -78.40 -137.11
REMARK 500 GLU A 310 35.09 -70.16
REMARK 500 GLN A 311 -28.50 -144.36
REMARK 500 ASP A 318 -101.16 45.41
REMARK 500 HIS A 330 -2.41 83.47
REMARK 500 ASP A 331 -63.26 -138.06
REMARK 500 SER A 333 -151.87 39.40
REMARK 500 ARG A 346 55.10 -148.94
REMARK 500 TYR A 366 96.11 -59.16
REMARK 500 LEU A 452 32.18 -89.43
REMARK 500 ASN A 463 72.22 47.35
REMARK 500 LYS A 527 22.20 -79.90
REMARK 500 ARG A 529 162.28 63.84
REMARK 500 ASP A 538 -74.56 -98.55
REMARK 500 GLU A 541 -27.22 -155.55
REMARK 500 GLU A 579 -88.91 -88.82
REMARK 500 GLU A 580 170.42 62.09
REMARK 500 ASP A 737 42.47 -108.82
REMARK 500 GLU A 740 -66.15 -103.44
REMARK 500 PHE A 795 -60.37 -108.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C2E A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XGB RELATED DB: PDB
REMARK 900 RELATED ID: 5XGD RELATED DB: PDB
DBREF 5XGE A 233 800 UNP Q9I580 Q9I580_PSEAE 233 800
SEQRES 1 A 568 ARG GLN GLU VAL GLU ASN ALA LEU ASP ALA GLU ARG GLU
SEQRES 2 A 568 ARG ALA GLN ILE THR LEU ALA SER ILE GLY ASP GLY VAL
SEQRES 3 A 568 ILE THR ALA ASP THR GLN GLY GLY ILE SER TYR LEU ASN
SEQRES 4 A 568 PRO ALA ALA GLU GLN MET THR ASN TRP THR LEU ASP LYS
SEQRES 5 A 568 ALA ARG GLY LEU PRO LEU ALA SER LEU PHE ARG ILE VAL
SEQRES 6 A 568 ASP GLU SER SER ARG GLU GLU GLY MET LEU LEU ILE GLU
SEQRES 7 A 568 GLN ILE LEU SER GLY GLU ILE ASP GLY GLY ARG GLU HIS
SEQRES 8 A 568 SER LYS LEU VAL LEU ARG HIS ASP GLY SER SER VAL PRO
SEQRES 9 A 568 VAL THR LEU VAL GLY ALA PRO ILE HIS ARG GLY ALA GLU
SEQRES 10 A 568 ILE THR GLY VAL VAL LEU VAL LEU HIS ASP MET THR ARG
SEQRES 11 A 568 GLU ARG GLN TYR MET ALA ARG LEU SER TRP GLN ALA THR
SEQRES 12 A 568 HIS ASP ALA LEU THR GLY LEU THR ASN ARG ARG GLU PHE
SEQRES 13 A 568 GLU TYR ARG LEU GLN ILE ALA LEU GLU ARG LEU GLU ARG
SEQRES 14 A 568 ASN SER GLY ARG HIS ALA LEU MET PHE LEU ASP LEU ASP
SEQRES 15 A 568 GLN PHE LYS LEU VAL ASN ASP THR CYS GLY HIS ALA ALA
SEQRES 16 A 568 GLY ASP GLU LEU LEU ARG GLN VAL CYS THR LEU LEU GLN
SEQRES 17 A 568 GLN GLY LEU ARG GLU GLY ASP THR LEU ALA ARG LEU GLY
SEQRES 18 A 568 GLY ASP GLU PHE GLY ILE LEU LEU GLU ASN CYS PRO ALA
SEQRES 19 A 568 GLU LYS ALA VAL GLU ILE ALA ASP HIS LEU ARG LYS THR
SEQRES 20 A 568 ILE GLN ASP LEU HIS PHE THR TRP SER GLY GLN PRO PHE
SEQRES 21 A 568 ASN CYS THR VAL SER VAL GLY LEU VAL HIS LEU LEU PRO
SEQRES 22 A 568 GLY ILE SER THR LEU GLU GLU ALA LEU ARG SER ALA ASP
SEQRES 23 A 568 MET ALA CYS TYR MET ALA LYS GLU LYS GLY ARG ASN ARG
SEQRES 24 A 568 VAL GLN VAL PHE HIS GLN ASP ASP VAL GLU LEU SER MET
SEQRES 25 A 568 ARG PHE GLY GLU MET THR TRP VAL GLN ARG ILE HIS LEU
SEQRES 26 A 568 ALA LEU GLU GLU ASP ARG PHE SER LEU TYR ALA GLN PRO
SEQRES 27 A 568 ILE VAL PRO LEU GLY GLU GLY ALA GLU GLU GLY LEU HIS
SEQRES 28 A 568 VAL GLU LEU LEU LEU ARG LEU ARG ASP GLU GLY GLY ARG
SEQRES 29 A 568 LEU VAL PRO PRO LEU SER PHE ILE PRO ALA ALA GLU ARG
SEQRES 30 A 568 TYR GLY LEU MET THR LEU ILE ASP ARG TRP VAL VAL GLU
SEQRES 31 A 568 ASN ALA PHE ARG THR LEU VAL GLU ARG ALA GLN ASP PRO
SEQRES 32 A 568 ARG ALA GLU PRO ILE GLY THR CYS ALA ILE ASN LEU SER
SEQRES 33 A 568 GLY ALA THR ILE GLY ASP GLU SER PHE LEU GLN PHE LEU
SEQRES 34 A 568 THR GLU LEU PHE ALA ARG TYR ARG ILE PRO PRO GLN THR
SEQRES 35 A 568 ILE CYS PHE GLU VAL THR GLU THR VAL ALA VAL ALA ASN
SEQRES 36 A 568 LEU ALA SER ALA ILE ARG PHE ILE ASN GLU LEU LYS ASP
SEQRES 37 A 568 THR GLY CYS ARG PHE SER LEU ASP ASP PHE CYS ALA GLY
SEQRES 38 A 568 MET SER SER PHE ILE TYR LEU LYS HIS LEU PRO VAL ASP
SEQRES 39 A 568 TYR LEU LYS ILE ASP GLY SER PHE VAL LYS ASP MET LEU
SEQRES 40 A 568 GLU ASP PRO ILE ASP ARG ALA MET VAL GLN VAL ILE ASN
SEQRES 41 A 568 HIS ILE GLY HIS VAL MET GLY LYS ARG THR ILE ALA GLU
SEQRES 42 A 568 PHE VAL GLU THR VAL GLU VAL MET GLU ALA LEU ARG GLU
SEQRES 43 A 568 ILE GLY ILE ASP TYR ALA GLN GLY LEU ALA ILE GLY ALA
SEQRES 44 A 568 PRO LEU PRO PHE SER ARG GLN PRO PRO
HET C2E A 901 46
HETNAM C2E 9,9'-[(2R,3R,3AS,5S,7AR,9R,10R,10AS,12S,14AR)-3,5,10,
HETNAM 2 C2E 12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,
HETNAM 3 C2E 2-D:3',2'-J][1,3,7,9,2,
HETNAM 4 C2E 8]TETRAOXADIPHOSPHACYCLODODECINE-2,9-DIYL]BIS(2-AMINO-
HETNAM 5 C2E 1,9-DIHYDRO-6H-PURIN-6-ONE)
HETSYN C2E C-DI-GMP; CYCLIC DIGUANOSINE MONOPHOSPHATE
FORMUL 2 C2E C20 H24 N10 O14 P2
FORMUL 3 HOH *141(H2 O)
HELIX 1 AA1 ALA A 242 ILE A 254 1 13
HELIX 2 AA2 ASN A 271 ASN A 279 1 9
HELIX 3 AA3 THR A 281 ARG A 286 1 6
HELIX 4 AA4 THR A 361 GLN A 365 5 5
HELIX 5 AA5 TYR A 366 ALA A 374 1 9
HELIX 6 AA6 ASN A 384 ARG A 398 1 15
HELIX 7 AA7 GLN A 415 GLY A 424 1 10
HELIX 8 AA8 GLY A 424 GLY A 442 1 19
HELIX 9 AA9 PRO A 465 ASP A 482 1 18
HELIX 10 AB1 THR A 509 LYS A 527 1 19
HELIX 11 AB2 GLU A 541 GLU A 561 1 21
HELIX 12 AB3 PRO A 599 TYR A 610 1 12
HELIX 13 AB4 LEU A 612 GLN A 633 1 22
HELIX 14 AB5 SER A 648 ASP A 654 1 7
HELIX 15 AB6 SER A 656 ARG A 669 1 14
HELIX 16 AB7 PRO A 671 GLN A 673 5 3
HELIX 17 AB8 GLU A 681 ASN A 687 1 7
HELIX 18 AB9 ASN A 687 ASP A 700 1 14
HELIX 19 AC1 GLY A 713 LEU A 723 1 11
HELIX 20 AC2 ASP A 731 ASP A 737 1 7
HELIX 21 AC3 ASP A 741 MET A 758 1 18
HELIX 22 AC4 THR A 769 GLY A 780 1 12
SHEET 1 AA1 6 ILE A 267 LEU A 270 0
SHEET 2 AA1 6 GLY A 257 ASP A 262 -1 N THR A 260 O SER A 268
SHEET 3 AA1 6 GLY A 352 ASP A 359 -1 O VAL A 353 N ALA A 261
SHEET 4 AA1 6 PRO A 336 ILE A 344 -1 N ALA A 342 O VAL A 354
SHEET 5 AA1 6 HIS A 323 LEU A 328 -1 N HIS A 323 O LEU A 339
SHEET 6 AA1 6 ARG A 295 VAL A 297 -1 N ARG A 295 O LEU A 328
SHEET 1 AA2 5 THR A 448 ARG A 451 0
SHEET 2 AA2 5 GLU A 456 LEU A 461 -1 O LEU A 460 N THR A 448
SHEET 3 AA2 5 HIS A 406 LEU A 413 -1 N ALA A 407 O LEU A 461
SHEET 4 AA2 5 VAL A 496 LEU A 503 -1 O SER A 497 N ASP A 412
SHEET 5 AA2 5 VAL A 532 VAL A 534 1 O GLN A 533 N LEU A 500
SHEET 1 AA3 2 PHE A 485 TRP A 487 0
SHEET 2 AA3 2 GLN A 490 PHE A 492 -1 O PHE A 492 N PHE A 485
SHEET 1 AA4 4 LEU A 597 VAL A 598 0
SHEET 2 AA4 4 LEU A 582 ARG A 591 -1 N LEU A 590 O VAL A 598
SHEET 3 AA4 4 PHE A 564 PRO A 573 -1 N SER A 565 O ARG A 589
SHEET 4 AA4 4 LEU A 793 PRO A 794 -1 O LEU A 793 N ALA A 568
SHEET 1 AA510 LEU A 597 VAL A 598 0
SHEET 2 AA510 LEU A 582 ARG A 591 -1 N LEU A 590 O VAL A 598
SHEET 3 AA510 ILE A 640 ASN A 646 1 O ALA A 644 N VAL A 584
SHEET 4 AA510 ILE A 675 THR A 680 1 O GLU A 678 N ILE A 645
SHEET 5 AA510 ARG A 704 PHE A 710 1 O ARG A 704 N PHE A 677
SHEET 6 AA510 TYR A 727 ILE A 730 1 O LYS A 729 N PHE A 710
SHEET 7 AA510 ARG A 761 ALA A 764 1 O ILE A 763 N LEU A 728
SHEET 8 AA510 TYR A 783 ALA A 784 1 O TYR A 783 N ALA A 764
SHEET 9 AA510 PHE A 564 PRO A 573 -1 N VAL A 572 O ALA A 784
SHEET 10 AA510 LEU A 793 PRO A 794 -1 O LEU A 793 N ALA A 568
SITE 1 AC1 15 GLN A 569 GLU A 585 LEU A 587 LEU A 588
SITE 2 AC1 15 ARG A 589 ASP A 617 VAL A 620 ASN A 646
SITE 3 AC1 15 ASP A 708 GLU A 765 PHE A 766 GLU A 768
SITE 4 AC1 15 GLY A 786 LEU A 787 HOH A1023
CRYST1 134.881 134.881 211.224 90.00 90.00 120.00 H 3 2 18
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 0.007414 0.004280 0.000000 0.00000
SCALE2 0.000000 0.008561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004734 0.00000
(ATOM LINES ARE NOT SHOWN.)
END