HEADER LIGASE/DNA 12-NOV-08 3F8I
TITLE MOUSE UHRF1 SRA DOMAIN BOUND WITH HEMI-METHYLATED CPG, CRYSTAL
TITLE 2 STRUCTURE IN SPACE GROUP P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE UHRF1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: YDG DOMAIN: UNP RESIDUES 419-628;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*DCP*DCP*DAP*DTP*DGP*(5CM)P*DGP*DCP*DTP*DGP*DAP*DC)-
COMPND 8 3';
COMPND 9 CHAIN: D, F;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: 5'-D(*DGP*DTP*DCP*DAP*DGP*DCP*DGP*DCP*DAP*DTP*DGP*DG)-3';
COMPND 13 CHAIN: E, G;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: UHRF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PXC666;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: SYNTHETIC DNA OLIGO;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 OTHER_DETAILS: SYNTHETIC DNA OLIGO
KEYWDS UHRF1, BASE FLIPPING, 5-METHYLCYTOSINE, CPG METHYLATION, CELL CYCLE,
KEYWDS 2 DEVELOPMENTAL PROTEIN, DNA DAMAGE, DNA REPAIR, DNA-BINDING, LIGASE,
KEYWDS 3 METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 4 REGULATION, UBL CONJUGATION, UBL CONJUGATION PATHWAY, ZINC, ZINC-
KEYWDS 5 FINGER, LIGASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HASHIMOTO,J.R.HORTON,X.ZHANG,X.CHENG
REVDAT 4 06-SEP-23 3F8I 1 COMPND SOURCE DBREF SEQADV
REVDAT 4 2 1 LINK
REVDAT 3 24-MAR-09 3F8I 1 JRNL
REVDAT 2 20-JAN-09 3F8I 1 JRNL
REVDAT 1 06-JAN-09 3F8I 0
JRNL AUTH H.HASHIMOTO,J.R.HORTON,X.ZHANG,X.CHENG
JRNL TITL UHRF1, A MODULAR MULTI-DOMAIN PROTEIN, REGULATES
JRNL TITL 2 REPLICATION-COUPLED CROSSTALK BETWEEN DNA METHYLATION AND
JRNL TITL 3 HISTONE MODIFICATIONS.
JRNL REF EPIGENETICS V. 4 8 2009
JRNL REFN ISSN 1559-2294
JRNL PMID 19077538
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.HASHIMOTO,J.R.HORTON,X.ZHANG,M.BOSTICK,S.E.JACOBSEN,
REMARK 1 AUTH 2 X.CHENG
REMARK 1 TITL THE SRA DOMAIN OF UHRF1 FLIPS 5-METHYLCYTOSINE OUT OF THE
REMARK 1 TITL 2 DNA HELIX.
REMARK 1 REF NATURE V. 455 826 2008
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 18772888
REMARK 1 DOI 10.1038/NATURE07280
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 622448.070
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 27777
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1351
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.29
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1869
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE : 0.4220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 101
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3204
REMARK 3 NUCLEIC ACID ATOMS : 974
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.56000
REMARK 3 B22 (A**2) : -17.03000
REMARK 3 B33 (A**2) : -2.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 35.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 32.01
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3F8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30041
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 34.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 2ZO0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.4M NACL, PH 7.0, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 31.20800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: ASYMMETRIC UNIT CONTAINS TWO SRA-DNA COMPLEXES.
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: 3030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.3 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 350
REMARK 350 BIOMOLECULE: 2
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: 3050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, G
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 GLU A 623
REMARK 465 LYS A 624
REMARK 465 SER A 625
REMARK 465 ARG A 626
REMARK 465 LYS A 627
REMARK 465 ARG A 628
REMARK 465 GLU B 623
REMARK 465 LYS B 624
REMARK 465 SER B 625
REMARK 465 ARG B 626
REMARK 465 LYS B 627
REMARK 465 ARG B 628
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 529 CG CD OE1 OE2
REMARK 470 LYS A 547 CG CD CE NZ
REMARK 470 GLU A 597 CG CD OE1 OE2
REMARK 470 GLU A 613 CG CD OE1 OE2
REMARK 470 GLU A 617 CG CD OE1 OE2
REMARK 470 LYS A 622 CG CD CE NZ
REMARK 470 GLU B 529 CG CD OE1 OE2
REMARK 470 LYS B 547 CG CD CE NZ
REMARK 470 ARG B 596 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 597 CD OE1 OE2
REMARK 470 GLU B 613 CG CD OE1 OE2
REMARK 470 GLU B 617 CG CD OE1 OE2
REMARK 470 ASN B 621 CG OD1 ND2
REMARK 470 LYS B 622 CG CD CE NZ
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 VAL A 451 -54.42 -124.52
REMARK 500 ASP A 460 -56.92 -137.99
REMARK 500 ASN A 508 -127.40 39.75
REMARK 500 ASP A 530 70.75 87.44
REMARK 500 TRP A 531 -39.92 -36.29
REMARK 500 ASN B 421 30.91 -97.19
REMARK 500 VAL B 451 -57.07 -126.26
REMARK 500 ASP B 460 -56.02 -131.46
REMARK 500 ASN B 508 -125.70 44.28
REMARK 500 ASP B 530 84.71 75.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DG E 433 0.08 SIDE CHAIN
REMARK 500 DG G 433 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZO0 RELATED DB: PDB
REMARK 900 SRA-DNA COMPLEX IN P2(1)2(1)2(1) SPACE GROUP
REMARK 900 RELATED ID: 2ZO1 RELATED DB: PDB
REMARK 900 SRA-DNA COMPLEX IN P4(1)2(1)2 SPACE GROUP
REMARK 900 RELATED ID: 2ZO2 RELATED DB: PDB
REMARK 900 SRA-DNA NON-SPECIFIC COMPLEX IN P6(1)22 SPACE GROUP
REMARK 900 RELATED ID: 3F8J RELATED DB: PDB
REMARK 900 SRA-DNA COMPLEX IN C222(1) SPACE GROUP
DBREF 3F8I A 418 628 UNP Q8VDF2 UHRF1_MOUSE 418 628
DBREF 3F8I B 418 628 UNP Q8VDF2 UHRF1_MOUSE 418 628
DBREF 3F8I D 402 413 PDB 3F8I 3F8I 402 413
DBREF 3F8I E 421 433 PDB 3F8I 3F8I 421 433
DBREF 3F8I F 402 413 PDB 3F8I 3F8I 402 413
DBREF 3F8I G 421 433 PDB 3F8I 3F8I 421 433
SEQADV 3F8I HIS A 417 UNP Q8VDF2 EXPRESSION TAG
SEQADV 3F8I MET A 418 UNP Q8VDF2 VAL 418 CONFLICT
SEQADV 3F8I HIS B 417 UNP Q8VDF2 EXPRESSION TAG
SEQADV 3F8I MET B 418 UNP Q8VDF2 VAL 418 CONFLICT
SEQRES 1 A 212 HIS MET PRO ALA ASN HIS PHE GLY PRO ILE PRO GLY VAL
SEQRES 2 A 212 PRO VAL GLY THR MET TRP ARG PHE ARG VAL GLN VAL SER
SEQRES 3 A 212 GLU SER GLY VAL HIS ARG PRO HIS VAL ALA GLY ILE HIS
SEQRES 4 A 212 GLY ARG SER ASN ASP GLY ALA TYR SER LEU VAL LEU ALA
SEQRES 5 A 212 GLY GLY TYR GLU ASP ASP VAL ASP ASN GLY ASN TYR PHE
SEQRES 6 A 212 THR TYR THR GLY SER GLY GLY ARG ASP LEU SER GLY ASN
SEQRES 7 A 212 LYS ARG THR ALA GLY GLN SER SER ASP GLN LYS LEU THR
SEQRES 8 A 212 ASN ASN ASN ARG ALA LEU ALA LEU ASN CYS HIS SER PRO
SEQRES 9 A 212 ILE ASN GLU LYS GLY ALA GLU ALA GLU ASP TRP ARG GLN
SEQRES 10 A 212 GLY LYS PRO VAL ARG VAL VAL ARG ASN MET LYS GLY GLY
SEQRES 11 A 212 LYS HIS SER LYS TYR ALA PRO ALA GLU GLY ASN ARG TYR
SEQRES 12 A 212 ASP GLY ILE TYR LYS VAL VAL LYS TYR TRP PRO GLU ARG
SEQRES 13 A 212 GLY LYS SER GLY PHE LEU VAL TRP ARG TYR LEU LEU ARG
SEQRES 14 A 212 ARG ASP ASP THR GLU PRO GLU PRO TRP THR ARG GLU GLY
SEQRES 15 A 212 LYS ASP ARG THR ARG GLN LEU GLY LEU THR MET GLN TYR
SEQRES 16 A 212 PRO GLU GLY TYR LEU GLU ALA LEU ALA ASN LYS GLU LYS
SEQRES 17 A 212 SER ARG LYS ARG
SEQRES 1 B 212 HIS MET PRO ALA ASN HIS PHE GLY PRO ILE PRO GLY VAL
SEQRES 2 B 212 PRO VAL GLY THR MET TRP ARG PHE ARG VAL GLN VAL SER
SEQRES 3 B 212 GLU SER GLY VAL HIS ARG PRO HIS VAL ALA GLY ILE HIS
SEQRES 4 B 212 GLY ARG SER ASN ASP GLY ALA TYR SER LEU VAL LEU ALA
SEQRES 5 B 212 GLY GLY TYR GLU ASP ASP VAL ASP ASN GLY ASN TYR PHE
SEQRES 6 B 212 THR TYR THR GLY SER GLY GLY ARG ASP LEU SER GLY ASN
SEQRES 7 B 212 LYS ARG THR ALA GLY GLN SER SER ASP GLN LYS LEU THR
SEQRES 8 B 212 ASN ASN ASN ARG ALA LEU ALA LEU ASN CYS HIS SER PRO
SEQRES 9 B 212 ILE ASN GLU LYS GLY ALA GLU ALA GLU ASP TRP ARG GLN
SEQRES 10 B 212 GLY LYS PRO VAL ARG VAL VAL ARG ASN MET LYS GLY GLY
SEQRES 11 B 212 LYS HIS SER LYS TYR ALA PRO ALA GLU GLY ASN ARG TYR
SEQRES 12 B 212 ASP GLY ILE TYR LYS VAL VAL LYS TYR TRP PRO GLU ARG
SEQRES 13 B 212 GLY LYS SER GLY PHE LEU VAL TRP ARG TYR LEU LEU ARG
SEQRES 14 B 212 ARG ASP ASP THR GLU PRO GLU PRO TRP THR ARG GLU GLY
SEQRES 15 B 212 LYS ASP ARG THR ARG GLN LEU GLY LEU THR MET GLN TYR
SEQRES 16 B 212 PRO GLU GLY TYR LEU GLU ALA LEU ALA ASN LYS GLU LYS
SEQRES 17 B 212 SER ARG LYS ARG
SEQRES 1 D 12 DC DC DA DT DG 5CM DG DC DT DG DA DC
SEQRES 1 E 12 DG DT DC DA DG DC DG DC DA DT DG DG
SEQRES 1 F 12 DC DC DA DT DG 5CM DG DC DT DG DA DC
SEQRES 1 G 12 DG DT DC DA DG DC DG DC DA DT DG DG
MODRES 3F8I 5CM D 407 DC
MODRES 3F8I 5CM F 407 DC
HET 5CM D 407 20
HET 5CM F 407 20
HETNAM 5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE
FORMUL 3 5CM 2(C10 H16 N3 O7 P)
FORMUL 7 HOH *135(H2 O)
HELIX 1 1 PHE A 437 SER A 444 1 8
HELIX 2 2 THR A 507 LEU A 515 1 9
HELIX 3 3 ASP A 530 GLY A 534 5 5
HELIX 4 4 LYS A 544 LYS A 547 5 4
HELIX 5 5 THR A 595 LEU A 605 1 11
HELIX 6 6 GLY A 614 ASN A 621 1 8
HELIX 7 7 PHE B 437 SER B 444 1 8
HELIX 8 8 THR B 507 LEU B 515 1 9
HELIX 9 9 ASP B 530 GLY B 534 5 5
HELIX 10 10 LYS B 544 HIS B 548 5 5
HELIX 11 11 THR B 595 LEU B 605 1 11
HELIX 12 12 GLY B 614 LYS B 622 1 9
SHEET 1 A 5 MET A 434 TRP A 435 0
SHEET 2 A 5 ASN A 557 ARG A 572 -1 O ASN A 557 N TRP A 435
SHEET 3 A 5 LEU A 578 ARG A 586 -1 O LEU A 583 N LYS A 567
SHEET 4 A 5 TYR A 480 THR A 484 -1 N TYR A 483 O TYR A 582
SHEET 5 A 5 VAL A 475 ASN A 477 -1 N VAL A 475 O THR A 482
SHEET 1 B 5 ILE A 454 ARG A 457 0
SHEET 2 B 5 GLY A 461 LEU A 467 -1 O TYR A 463 N HIS A 455
SHEET 3 B 5 VAL A 537 ASN A 542 1 O ASN A 542 N LEU A 467
SHEET 4 B 5 ASN A 557 ARG A 572 -1 O ARG A 558 N ARG A 541
SHEET 5 B 5 ALA A 526 GLU A 527 -1 N ALA A 526 O TYR A 568
SHEET 1 C 5 MET B 434 TRP B 435 0
SHEET 2 C 5 ASN B 557 ARG B 572 -1 O ASN B 557 N TRP B 435
SHEET 3 C 5 LEU B 578 ARG B 586 -1 O LEU B 583 N LYS B 567
SHEET 4 C 5 TYR B 480 THR B 484 -1 N PHE B 481 O LEU B 584
SHEET 5 C 5 VAL B 475 ASP B 476 -1 N VAL B 475 O THR B 482
SHEET 1 D 5 ILE B 454 ARG B 457 0
SHEET 2 D 5 GLY B 461 LEU B 467 -1 O TYR B 463 N HIS B 455
SHEET 3 D 5 VAL B 537 ASN B 542 1 O ARG B 538 N TYR B 463
SHEET 4 D 5 ASN B 557 ARG B 572 -1 O ASP B 560 N VAL B 539
SHEET 5 D 5 ALA B 526 GLU B 527 -1 N ALA B 526 O TYR B 568
LINK O3' DG D 406 P 5CM D 407 1555 1555 1.61
LINK O3' 5CM D 407 P DG D 408 1555 1555 1.60
LINK O3' DG F 406 P 5CM F 407 1555 1555 1.61
LINK O3' 5CM F 407 P DG F 408 1555 1555 1.61
CRYST1 50.084 62.416 113.447 90.00 98.92 90.00 P 1 21 1 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 0.019966 0.000000 0.003134 0.00000
SCALE2 0.000000 0.016022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008923 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
