HEADER TRANSCRIPTION/DNA 12-FEB-10 3LSR
TITLE CRYSTAL STRUCTURE OF DEST IN COMPLEX WITH DUPLEX DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEST;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (27-MER);
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: DEST, PA4890;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES
KEYWDS TRANSCRIPTIONAL REPRESSOR, DEST-DNA COMPLEX, TETR FAMILY, DNA-
KEYWDS 2 BINDING, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSCRIPTION-DNA
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.MILLER,S.W.WHITE
REVDAT 4 06-SEP-23 3LSR 1 REMARK
REVDAT 3 13-OCT-21 3LSR 1 REMARK SEQADV
REVDAT 2 18-AUG-10 3LSR 1 JRNL
REVDAT 1 04-AUG-10 3LSR 0
JRNL AUTH D.J.MILLER,Y.M.ZHANG,C.SUBRAMANIAN,C.O.ROCK,S.W.WHITE
JRNL TITL STRUCTURAL BASIS FOR THE TRANSCRIPTIONAL REGULATION OF
JRNL TITL 2 MEMBRANE LIPID HOMEOSTASIS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 971 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20639888
JRNL DOI 10.1038/NSMB.1847
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 13546
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 709
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 781
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1470
REMARK 3 NUCLEIC ACID ATOMS : 548
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 15
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
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): 0.367
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.269
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.218
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.223
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2118 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2977 ; 1.423 ; 2.288
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 190 ; 5.268 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;33.952 ;21.765
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 246 ;16.644 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.940 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1410 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 816 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1385 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 45 ; 0.128 ; 0.200
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): 58 ; 0.130 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.171 ; 0.200
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): 978 ; 0.769 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1504 ; 1.385 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1466 ; 1.304 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1473 ; 2.246 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 3LSR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000057683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14862
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.4000
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: PDB ENTRY 3LSP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ML- 0.1M MES PH7.0, 9% PEG 20K.
REMARK 280 PROTEIN SAMPLE- 0.3 MM PROTEIN, 0.3 MM OLIGO, 0.3 MM 18:1DELTA9-
REMARK 280 COA. DROP- 2UL ML + 2 UL PROTEIN + 0.5 UL 1M AMMONIUM SULFATE.,
REMARK 280 GROWN UNDER MINERAL OIL, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 39.67900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 39.67900
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.72900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.67900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.36450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.67900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.09350
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.67900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.67900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 72.72900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 39.67900
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 109.09350
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 39.67900
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.36450
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -79.35800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 79.35800
REMARK 350 BIOMT3 2 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 PRO A 176
REMARK 465 ALA A 177
REMARK 465 ALA A 178
REMARK 465 ASP A 179
REMARK 465 LEU A 180
REMARK 465 PRO A 181
REMARK 465 PRO A 182
REMARK 465 HIS A 183
REMARK 465 LEU A 184
REMARK 465 MET A 185
REMARK 465 GLY A 206
REMARK 465 LEU A 207
REMARK 465 PRO A 208
REMARK 465 GLY A 209
REMARK 465 SER A 210
REMARK 465 SER A 211
REMARK 465 VAL A 212
REMARK 465 ASP A 213
REMARK 465 LYS A 214
REMARK 465 LEU A 215
REMARK 465 ALA A 216
REMARK 465 ALA A 217
REMARK 465 ALA A 218
REMARK 465 LEU A 219
REMARK 465 GLU A 220
REMARK 465 DT B 0
REMARK 465 DG B 1
REMARK 465 DT B 2
REMARK 465 DA B 3
REMARK 465 DA B 31
REMARK 465 DC B 32
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 GLU A 7 CG CD OE1 OE2
REMARK 470 GLN A 11 CG CD OE1 NE2
REMARK 470 LEU A 85 CG CD1 CD2
REMARK 470 TYR A 115 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 DC B 4 P OP1 OP2 O5' C5'
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 B 4 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC B 7 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DG B 9 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA B 12 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC B 14 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DC B 16 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG B 17 O4' - C1' - N9 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DT B 20 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT B 21 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT B 21 C3' - O3' - P ANGL. DEV. = 8.9 DEGREES
REMARK 500 DC B 24 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 DC B 24 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC B 24 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DT B 28 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DG B 29 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DT B 30 O4' - C1' - N1 ANGL. DEV. = 3.1 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 5 47.91 -100.95
REMARK 500 GLU A 25 4.14 -58.47
REMARK 500 ASN A 103 38.90 -147.36
REMARK 500 SER A 118 -168.28 -79.21
REMARK 500 HIS A 148 1.35 -69.21
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 SO4 A 221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LSP RELATED DB: PDB
REMARK 900 PSEDOPALINDROME DNA BOUND TO DEST
REMARK 900 RELATED ID: 3LSJ RELATED DB: PDB
REMARK 900 SAME PROTEIN WITHOUT DNA
DBREF 3LSR A 1 209 UNP Q9HUS3 Q9HUS3_PSEAE 1 209
DBREF 3LSR B 0 32 PDB 3LSR 3LSR 0 32
SEQADV 3LSR ALA A 2 UNP Q9HUS3 SER 2 ENGINEERED MUTATION
SEQADV 3LSR SER A 210 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR SER A 211 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR VAL A 212 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR ASP A 213 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR LYS A 214 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR LEU A 215 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR ALA A 216 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR ALA A 217 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR ALA A 218 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR LEU A 219 UNP Q9HUS3 EXPRESSION TAG
SEQADV 3LSR GLU A 220 UNP Q9HUS3 EXPRESSION TAG
SEQRES 1 A 220 MET ALA SER PRO ARG ALA GLU GLN LYS GLN GLN THR ARG
SEQRES 2 A 220 HIS ALA LEU MET SER ALA ALA ARG HIS LEU MET GLU SER
SEQRES 3 A 220 GLY ARG GLY PHE GLY SER LEU SER LEU ARG GLU VAL THR
SEQRES 4 A 220 ARG ALA ALA GLY ILE VAL PRO ALA GLY PHE TYR ARG HIS
SEQRES 5 A 220 PHE SER ASP MET ASP GLN LEU GLY LEU ALA LEU VAL ALA
SEQRES 6 A 220 GLU VAL ASP GLU THR PHE ARG ALA THR LEU ARG ALA VAL
SEQRES 7 A 220 ARG ARG ASN GLU PHE GLU LEU GLY GLY LEU ILE ASP ALA
SEQRES 8 A 220 SER VAL ARG ILE PHE LEU ASP ALA VAL GLY ALA ASN ARG
SEQRES 9 A 220 SER GLN PHE LEU PHE LEU ALA ARG GLU GLN TYR GLY GLY
SEQRES 10 A 220 SER LEU PRO ILE ARG GLN ALA ILE ALA SER LEU ARG GLN
SEQRES 11 A 220 ARG ILE THR ASP ASP LEU ALA ALA ASP LEU ALA LEU LEU
SEQRES 12 A 220 ASN LYS MET PRO HIS LEU ASP GLY ALA ALA LEU ASP VAL
SEQRES 13 A 220 PHE ALA ASP LEU VAL VAL LYS THR VAL PHE ALA THR LEU
SEQRES 14 A 220 PRO GLU LEU ILE ASP PRO PRO ALA ALA ASP LEU PRO PRO
SEQRES 15 A 220 HIS LEU MET PRO ALA ALA LYS ILE THR HIS GLN LEU ARG
SEQRES 16 A 220 PHE ILE MET ILE GLY GLY LYS HIS TRP HIS GLY LEU PRO
SEQRES 17 A 220 GLY SER SER VAL ASP LYS LEU ALA ALA ALA LEU GLU
SEQRES 1 B 33 DT DG DT DA DC DA DT DC DA DG DT DG DA
SEQRES 2 B 33 DA DC DG DC DG DC DG DT DT DC DA DC DT
SEQRES 3 B 33 DG DA DT DG DT DA DC
HET SO4 A 221 5
HET SO4 A 222 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *15(H2 O)
HELIX 1 1 ALA A 6 LEU A 23 1 18
HELIX 2 2 GLY A 29 LEU A 33 5 5
HELIX 3 3 SER A 34 GLY A 43 1 10
HELIX 4 4 VAL A 45 HIS A 52 5 8
HELIX 5 5 ASP A 55 ASN A 81 1 27
HELIX 6 6 GLY A 87 ALA A 102 1 16
HELIX 7 7 ASN A 103 GLY A 117 1 15
HELIX 8 8 SER A 118 LEU A 143 1 26
HELIX 9 9 ASP A 150 ASP A 174 1 25
HELIX 10 10 PRO A 186 HIS A 203 1 18
SITE 1 AC1 6 HIS A 14 SER A 18 ARG A 21 HIS A 22
SITE 2 AC1 6 SER A 105 HOH A 230
SITE 1 AC2 6 GLY A 87 LEU A 88 ILE A 89 ARG A 195
SITE 2 AC2 6 HOH A 233 HOH A 234
CRYST1 79.358 79.358 145.458 90.00 90.00 90.00 I 41 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 0.012601 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
