HEADER LYASE/DNA 20-APR-08 3CVY
TITLE DROSOPHILA MELANOGASTER (6-4) PHOTOLYASE BOUND TO REPAIRED DS DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*DAP*DCP*DAP*DGP*DCP*DGP*DGP*DTP*DTP*DGP*DCP*DAP*DGP*DGP*DT)-3');
COMPND 4 CHAIN: C;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(*DTP*DAP*DCP*DCP*DTP*DGP*DCP*DAP*DAP*DCP*DCP*DGP*DCP*DTP*DG)-3');
COMPND 9 CHAIN: D;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: RE11660P;
COMPND 13 CHAIN: A;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 7 ORGANISM_TAXID: 7227;
SOURCE 8 GENE: PHR64-520;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI PLYSS (DE-3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: DERIVED FROM PDEST007
KEYWDS DNA REPAIR, LYASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.MAUL,T.R.M.BARENDS,A.F.GLAS,M.J.CRYLE,I.SCHLICHTING,T.CARELL
REVDAT 6 21-FEB-24 3CVY 1 REMARK SEQADV
REVDAT 5 25-OCT-17 3CVY 1 REMARK
REVDAT 4 09-JUN-09 3CVY 1 REVDAT
REVDAT 3 24-FEB-09 3CVY 1 VERSN
REVDAT 2 30-DEC-08 3CVY 1 JRNL
REVDAT 1 04-NOV-08 3CVY 0
JRNL AUTH M.J.MAUL,T.R.BARENDS,A.F.GLAS,M.J.CRYLE,T.DOMRATCHEVA,
JRNL AUTH 2 S.SCHNEIDER,I.SCHLICHTING,T.CARELL
JRNL TITL CRYSTAL STRUCTURE AND MECHANISM OF A DNA (6-4) PHOTOLYASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 47 10076 2008
JRNL REFN ISSN 1433-7851
JRNL PMID 18956392
JRNL DOI 10.1002/ANIE.200804268
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 17285
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 886
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1245
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4110
REMARK 3 NUCLEIC ACID ATOMS : 609
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 9
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : -3.46000
REMARK 3 B33 (A**2) : 3.25000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.384
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.270
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.273
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4973 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4140 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6882 ; 1.112 ; 2.121
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9686 ; 0.776 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 500 ; 5.808 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;34.164 ;22.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 723 ;15.460 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;11.373 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 724 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4993 ; 0.000 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 905 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1114 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4330 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2353 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2546 ; 0.079 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 106 ; 0.138 ; 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): 7 ; 0.170 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.237 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.194 ; 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): 3276 ; 0.476 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 996 ; 0.042 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4071 ; 0.514 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3160 ; 0.619 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2811 ; 1.120 ; 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 : BABINET MODEL WITH 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 3CVY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17459
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG1500, 0.1 M MIB BUFFER, PH
REMARK 280 8.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 41.68000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.29500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.42000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.29500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.68000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.42000
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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 -22
REMARK 465 ALA A -21
REMARK 465 SER A -20
REMARK 465 TRP A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 PRO A -16
REMARK 465 GLN A -15
REMARK 465 PHE A -14
REMARK 465 GLU A -13
REMARK 465 LYS A -12
REMARK 465 GLY A -11
REMARK 465 ALA A -10
REMARK 465 SER A -9
REMARK 465 THR A -8
REMARK 465 SER A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 LYS A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 THR A 506
REMARK 465 GLY A 507
REMARK 465 LYS A 508
REMARK 465 GLU A 509
REMARK 465 GLU A 510
REMARK 465 GLU A 511
REMARK 465 SER A 512
REMARK 465 SER A 513
REMARK 465 PHE A 514
REMARK 465 GLU A 515
REMARK 465 GLU A 516
REMARK 465 LYS A 517
REMARK 465 SER A 518
REMARK 465 GLU A 519
REMARK 465 THR A 520
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 C 2 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG C 13 O4' - C1' - N9 ANGL. DEV. = 5.4 DEGREES
REMARK 500 DT C 15 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT D 1 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC D 3 O4' - C1' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DC D 3 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DT D 5 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 DT D 5 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC D 7 O4' - C4' - C3' ANGL. DEV. = -3.9 DEGREES
REMARK 500 DC D 7 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DA D 8 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA D 8 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES
REMARK 500 DA D 9 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC D 10 O4' - C1' - N1 ANGL. DEV. = 2.1 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 13 -68.39 -129.85
REMARK 500 LYS A 14 -153.11 -98.23
REMARK 500 SER A 80 -160.18 -129.23
REMARK 500 ARG A 101 73.04 49.21
REMARK 500 ASN A 151 35.69 -96.88
REMARK 500 LYS A 210 31.05 -83.95
REMARK 500 ARG A 211 48.24 -167.77
REMARK 500 HIS A 333 83.44 -156.03
REMARK 500 THR A 376 -112.11 -97.17
REMARK 500 ASP A 379 -62.19 -130.99
REMARK 500 PHE A 415 -51.99 71.84
REMARK 500 CYS A 453 15.84 -145.67
REMARK 500 TRP A 458 -2.38 -57.27
REMARK 500 CYS A 470 96.84 -162.99
REMARK 500 THR A 474 -62.61 -130.39
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 FAD A 521
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CVU RELATED DB: PDB
REMARK 900 DROSOPHILA MELANOGASTER (6-4) PHOTOLYASE BOUND TO DS DNA WITH A T-T
REMARK 900 (6-4) PHOTOLESION
REMARK 900 RELATED ID: 3CVV RELATED DB: PDB
REMARK 900 DROSOPHILA MELANOGASTER (6-4) PHOTOLYASE BOUND TO DS DNA WITH A T-T
REMARK 900 (6-4) PHOTOLESION AND F0 COFACTOR
REMARK 900 RELATED ID: 3CVW RELATED DB: PDB
REMARK 900 DROSOPHILA MELANOGASTER (6-4) PHOTOLYASE H365N MUTANT BOUND TO DS
REMARK 900 DNA WITH A T-T (6-4) PHOTOLESION AND COFACTOR F0
REMARK 900 RELATED ID: 3CVX RELATED DB: PDB
REMARK 900 DROSOPHILA MELANOGASTER (6-4) PHOTOLYASE H369M MUTANT BOUND TO DS
REMARK 900 DNA WITH A T-T (6-4) PHOTOLESION
DBREF 3CVY A 1 520 UNP Q8SXK5 Q8SXK5_DROME 1 520
DBREF 3CVY C 1 15 PDB 3CVY 3CVY 1 15
DBREF 3CVY D 1 15 PDB 3CVY 3CVY 1 15
SEQADV 3CVY MET A -22 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY ALA A -21 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY SER A -20 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY TRP A -19 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY SER A -18 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY HIS A -17 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY PRO A -16 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY GLN A -15 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY PHE A -14 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY GLU A -13 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY LYS A -12 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY GLY A -11 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY ALA A -10 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY SER A -9 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY THR A -8 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY SER A -7 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY LEU A -6 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY TYR A -5 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY LYS A -4 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY LYS A -3 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY ALA A -2 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY GLY A -1 UNP Q8SXK5 EXPRESSION TAG
SEQADV 3CVY LEU A 0 UNP Q8SXK5 EXPRESSION TAG
SEQRES 1 C 15 DA DC DA DG DC DG DG DT DT DG DC DA DG
SEQRES 2 C 15 DG DT
SEQRES 1 D 15 DT DA DC DC DT DG DC DA DA DC DC DG DC
SEQRES 2 D 15 DT DG
SEQRES 1 A 543 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 543 SER THR SER LEU TYR LYS LYS ALA GLY LEU MET ASP SER
SEQRES 3 A 543 GLN ARG SER THR LEU VAL HIS TRP PHE ARG LYS GLY LEU
SEQRES 4 A 543 ARG LEU HIS ASP ASN PRO ALA LEU SER HIS ILE PHE THR
SEQRES 5 A 543 ALA ALA ASN ALA ALA PRO GLY ARG TYR PHE VAL ARG PRO
SEQRES 6 A 543 ILE PHE ILE LEU ASP PRO GLY ILE LEU ASP TRP MET GLN
SEQRES 7 A 543 VAL GLY ALA ASN ARG TRP ARG PHE LEU GLN GLN THR LEU
SEQRES 8 A 543 GLU ASP LEU ASP ASN GLN LEU ARG LYS LEU ASN SER ARG
SEQRES 9 A 543 LEU PHE VAL VAL ARG GLY LYS PRO ALA GLU VAL PHE PRO
SEQRES 10 A 543 ARG ILE PHE LYS SER TRP ARG VAL GLU MET LEU THR PHE
SEQRES 11 A 543 GLU THR ASP ILE GLU PRO TYR SER VAL THR ARG ASP ALA
SEQRES 12 A 543 ALA VAL GLN LYS LEU ALA LYS ALA GLU GLY VAL ARG VAL
SEQRES 13 A 543 GLU THR HIS CYS SER HIS THR ILE TYR ASN PRO GLU LEU
SEQRES 14 A 543 VAL ILE ALA LYS ASN LEU GLY LYS ALA PRO ILE THR TYR
SEQRES 15 A 543 GLN LYS PHE LEU GLY ILE VAL GLU GLN LEU LYS VAL PRO
SEQRES 16 A 543 LYS VAL LEU GLY VAL PRO GLU LYS LEU LYS ASN MET PRO
SEQRES 17 A 543 THR PRO PRO LYS ASP GLU VAL GLU GLN LYS ASP SER ALA
SEQRES 18 A 543 ALA TYR ASP CYS PRO THR MET LYS GLN LEU VAL LYS ARG
SEQRES 19 A 543 PRO GLU GLU LEU GLY PRO ASN LYS PHE PRO GLY GLY GLU
SEQRES 20 A 543 THR GLU ALA LEU ARG ARG MET GLU GLU SER LEU LYS ASP
SEQRES 21 A 543 GLU ILE TRP VAL ALA ARG PHE GLU LYS PRO ASN THR ALA
SEQRES 22 A 543 PRO ASN SER LEU GLU PRO SER THR THR VAL LEU SER PRO
SEQRES 23 A 543 TYR LEU LYS PHE GLY CYS LEU SER ALA ARG LEU PHE ASN
SEQRES 24 A 543 GLN LYS LEU LYS GLU ILE ILE LYS ARG GLN PRO LYS HIS
SEQRES 25 A 543 SER GLN PRO PRO VAL SER LEU ILE GLY GLN LEU MET TRP
SEQRES 26 A 543 ARG GLU PHE TYR TYR THR VAL ALA ALA ALA GLU PRO ASN
SEQRES 27 A 543 PHE ASP ARG MET LEU GLY ASN VAL TYR CYS MET GLN ILE
SEQRES 28 A 543 PRO TRP GLN GLU HIS PRO ASP HIS LEU GLU ALA TRP THR
SEQRES 29 A 543 HIS GLY ARG THR GLY TYR PRO PHE ILE ASP ALA ILE MET
SEQRES 30 A 543 ARG GLN LEU ARG GLN GLU GLY TRP ILE HIS HIS LEU ALA
SEQRES 31 A 543 ARG HIS ALA VAL ALA CYS PHE LEU THR ARG GLY ASP LEU
SEQRES 32 A 543 TRP ILE SER TRP GLU GLU GLY GLN ARG VAL PHE GLU GLN
SEQRES 33 A 543 LEU LEU LEU ASP GLN ASP TRP ALA LEU ASN ALA GLY ASN
SEQRES 34 A 543 TRP MET TRP LEU SER ALA SER ALA PHE PHE HIS GLN TYR
SEQRES 35 A 543 PHE ARG VAL TYR SER PRO VAL ALA PHE GLY LYS LYS THR
SEQRES 36 A 543 ASP PRO GLN GLY HIS TYR ILE ARG LYS TYR VAL PRO GLU
SEQRES 37 A 543 LEU SER LYS TYR PRO ALA GLY CYS ILE TYR GLU PRO TRP
SEQRES 38 A 543 LYS ALA SER LEU VAL ASP GLN ARG ALA TYR GLY CYS VAL
SEQRES 39 A 543 LEU GLY THR ASP TYR PRO HIS ARG ILE VAL LYS HIS GLU
SEQRES 40 A 543 VAL VAL HIS LYS GLU ASN ILE LYS ARG MET GLY ALA ALA
SEQRES 41 A 543 TYR LYS VAL ASN ARG GLU VAL ARG THR GLY LYS GLU GLU
SEQRES 42 A 543 GLU SER SER PHE GLU GLU LYS SER GLU THR
HET FAD A 521 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 4 FAD C27 H33 N9 O15 P2
FORMUL 5 HOH *9(H2 O)
HELIX 1 1 ASN A 21 ALA A 34 1 14
HELIX 2 2 GLY A 57 LEU A 78 1 22
HELIX 3 3 LYS A 88 ARG A 101 1 14
HELIX 4 4 GLU A 112 GLU A 129 1 18
HELIX 5 5 ASN A 143 ASN A 151 1 9
HELIX 6 6 THR A 158 GLU A 167 1 10
HELIX 7 7 ASP A 190 ASP A 196 1 7
HELIX 8 8 THR A 204 VAL A 209 1 6
HELIX 9 9 ARG A 211 LEU A 215 5 5
HELIX 10 10 GLY A 223 LEU A 235 1 13
HELIX 11 11 ASP A 237 PHE A 244 1 8
HELIX 12 12 GLU A 245 THR A 249 5 5
HELIX 13 13 LEU A 261 PHE A 267 1 7
HELIX 14 14 SER A 271 GLN A 286 1 16
HELIX 15 15 SER A 295 ALA A 312 1 18
HELIX 16 16 HIS A 333 HIS A 342 1 10
HELIX 17 17 TYR A 347 GLY A 361 1 15
HELIX 18 18 HIS A 364 THR A 376 1 13
HELIX 19 19 SER A 383 LEU A 395 1 13
HELIX 20 20 ASP A 399 SER A 411 1 13
HELIX 21 21 ALA A 427 THR A 432 5 6
HELIX 22 22 GLY A 436 VAL A 443 1 8
HELIX 23 23 PRO A 444 SER A 447 5 4
HELIX 24 24 PRO A 450 TYR A 455 1 6
HELIX 25 25 GLU A 456 ALA A 460 5 5
HELIX 26 26 SER A 461 TYR A 468 1 8
HELIX 27 27 LYS A 482 GLU A 503 1 22
SHEET 1 A 5 PHE A 83 ARG A 86 0
SHEET 2 A 5 TYR A 38 LEU A 46 1 N LEU A 46 O VAL A 85
SHEET 3 A 5 SER A 6 PHE A 12 1 N PHE A 12 O ILE A 43
SHEET 4 A 5 VAL A 102 GLU A 108 1 O MET A 104 N VAL A 9
SHEET 5 A 5 ARG A 132 HIS A 136 1 O ARG A 132 N LEU A 105
CISPEP 1 PRO A 292 PRO A 293 0 3.81
SITE 1 AC1 25 PHE A 244 LYS A 246 THR A 258 THR A 259
SITE 2 AC1 25 LEU A 261 SER A 262 LEU A 265 GLN A 299
SITE 3 AC1 25 LEU A 300 ARG A 303 TYR A 306 TRP A 362
SITE 4 AC1 25 HIS A 365 ARG A 368 PHE A 391 LEU A 395
SITE 5 AC1 25 ASP A 397 GLN A 398 ASP A 399 LEU A 402
SITE 6 AC1 25 ASN A 403 ASN A 406 TRP A 407 LEU A 410
SITE 7 AC1 25 DT C 8
CRYST1 83.360 88.840 86.590 90.00 90.00 90.00 P 21 21 21 4
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 0.011996 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END