HEADER LIGASE 22-JUL-08 3DWH
TITLE STRUCTURAL AND FUNCTIONAL ANALYSIS OF SRA DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE UHRF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SRA DOMAIN, YDG DOMAIN, RESIDUES 414-617;
COMPND 5 SYNONYM: UBIQUITIN-LIKE PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN
COMPND 6 1, UBIQUITIN-LIKE-CONTAINING PHD AND RING FINGER DOMAINS PROTEIN 1,
COMPND 7 INVERTED CCAAT BOX-BINDING PROTEIN OF 90 KDA, TRANSCRIPTION FACTOR
COMPND 8 ICBP90, NUCLEAR ZINC FINGER PROTEIN NP95, NUCLEAR PROTEIN 95, HUNP95,
COMPND 9 RING FINGER PROTEIN 106;
COMPND 10 EC: 6.3.2.-;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: UHRF1, ICBP90, NP95, RNF106;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA BARREL, CELL CYCLE, DNA DAMAGE, DNA REPAIR, DNA-BINDING, LIGASE,
KEYWDS 2 METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 3 REGULATION, UBL CONJUGATION PATHWAY, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR C.QIAN,J.JAKONCIC,M.ZHOU
REVDAT 7 13-MAR-24 3DWH 1 COMPND SOURCE
REVDAT 6 21-FEB-24 3DWH 1 REMARK SEQADV
REVDAT 5 13-JUL-11 3DWH 1 VERSN
REVDAT 4 09-JUN-09 3DWH 1 REVDAT
REVDAT 3 24-FEB-09 3DWH 1 VERSN
REVDAT 2 13-JAN-09 3DWH 1 JRNL
REVDAT 1 21-OCT-08 3DWH 0
JRNL AUTH C.QIAN,S.LI,J.JAKONCIC,L.ZENG,M.J.WALSH,M.M.ZHOU
JRNL TITL STRUCTURE AND HEMIMETHYLATED CPG BINDING OF THE SRA DOMAIN
JRNL TITL 2 FROM HUMAN UHRF1.
JRNL REF J.BIOL.CHEM. V. 283 34490 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18945682
JRNL DOI 10.1074/JBC.C800169200
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 16701
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 894
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1219
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1500
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.47000
REMARK 3 B12 (A**2) : 0.16000
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): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.474
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1568 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2125 ; 1.608 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 195 ; 5.424 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;34.986 ;23.026
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 240 ;14.487 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;20.908 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 207 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1238 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 684 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1051 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 118 ; 0.146 ; 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): 41 ; 0.243 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.134 ; 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 ; 1.151 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1521 ; 1.864 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 690 ; 2.597 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 602 ; 3.952 ; 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 3DWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-08; 18-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X4C; X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM; ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17595
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08300
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) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
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; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 51.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL 1.2M AMMONIUM SULFATE
REMARK 280 0.2M NACL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 31.78733
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 63.57467
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 63.57467
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 31.78733
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 484
REMARK 465 ASP A 485
REMARK 465 LEU A 486
REMARK 465 SER A 487
REMARK 465 GLY A 488
REMARK 465 ASN A 489
REMARK 465 LYS A 490
REMARK 465 ARG A 491
REMARK 465 THR A 492
REMARK 465 ALA A 493
REMARK 465 GLU A 494
REMARK 465 GLN A 495
REMARK 465 LEU A 615
REMARK 465 ALA A 616
REMARK 465 ASN A 617
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 467 CG CD OE1 OE2
REMARK 470 LYS A 568 CD CE NZ
REMARK 470 LYS A 595 CE NZ
REMARK 470 LYS A 599 CD CE NZ
REMARK 470 LYS A 600 CD CE NZ
REMARK 470 ALA A 614 CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASN A 474 O HOH A 687 2.08
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 ASN A 416 23.19 -76.29
REMARK 500 ASP A 455 -69.19 -137.22
REMARK 500 ALA A 463 37.51 -141.27
REMARK 500 TYR A 466 101.42 57.73
REMARK 500 ASN A 503 -129.14 53.07
REMARK 500 ASP A 526 61.46 -104.11
REMARK 500 ASP A 583 80.92 -151.63
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 619
DBREF 3DWH A 414 617 UNP Q96T88 UHRF1_HUMAN 414 617
SEQADV 3DWH GLY A 410 UNP Q96T88 EXPRESSION TAG
SEQADV 3DWH SER A 411 UNP Q96T88 EXPRESSION TAG
SEQADV 3DWH HIS A 412 UNP Q96T88 EXPRESSION TAG
SEQADV 3DWH MET A 413 UNP Q96T88 EXPRESSION TAG
SEQRES 1 A 208 GLY SER HIS MET PRO SER ASN HIS TYR GLY PRO ILE PRO
SEQRES 2 A 208 GLY ILE PRO VAL GLY THR MET TRP ARG PHE ARG VAL GLN
SEQRES 3 A 208 VAL SER GLU SER GLY VAL HIS ARG PRO HIS VAL ALA GLY
SEQRES 4 A 208 ILE HIS GLY ARG SER ASN ASP GLY ALA TYR SER LEU VAL
SEQRES 5 A 208 LEU ALA GLY GLY TYR GLU ASP ASP VAL ASP HIS GLY ASN
SEQRES 6 A 208 PHE PHE THR TYR THR GLY SER GLY GLY ARG ASP LEU SER
SEQRES 7 A 208 GLY ASN LYS ARG THR ALA GLU GLN SER CYS ASP GLN LYS
SEQRES 8 A 208 LEU THR ASN THR ASN ARG ALA LEU ALA LEU ASN CYS PHE
SEQRES 9 A 208 ALA PRO ILE ASN ASP GLN GLU GLY ALA GLU ALA LYS ASP
SEQRES 10 A 208 TRP ARG SER GLY LYS PRO VAL ARG VAL VAL ARG ASN VAL
SEQRES 11 A 208 LYS GLY GLY LYS ASN SER LYS TYR ALA PRO ALA GLU GLY
SEQRES 12 A 208 ASN ARG TYR ASP GLY ILE TYR LYS VAL VAL LYS TYR TRP
SEQRES 13 A 208 PRO GLU LYS GLY LYS SER GLY PHE LEU VAL TRP ARG TYR
SEQRES 14 A 208 LEU LEU ARG ARG ASP ASP ASP GLU PRO GLY PRO TRP THR
SEQRES 15 A 208 LYS GLU GLY LYS ASP ARG ILE LYS LYS LEU GLY LEU THR
SEQRES 16 A 208 MET GLN TYR PRO GLU GLY TYR LEU GLU ALA LEU ALA ASN
HET SO4 A 1 5
HET SO4 A 618 5
HET GOL A 619 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *131(H2 O)
HELIX 1 1 PHE A 432 SER A 439 1 8
HELIX 2 2 THR A 502 CYS A 512 1 11
HELIX 3 3 ASP A 526 GLY A 530 5 5
HELIX 4 4 LYS A 540 SER A 545 5 6
HELIX 5 5 THR A 591 GLY A 602 1 12
SHEET 1 A 4 MET A 429 TRP A 430 0
SHEET 2 A 4 ASN A 553 LYS A 568 -1 O ASN A 553 N TRP A 430
SHEET 3 A 4 LEU A 574 ARG A 582 -1 O VAL A 575 N GLU A 567
SHEET 4 A 4 PHE A 475 THR A 479 -1 N PHE A 476 O LEU A 580
SHEET 1 B 5 ILE A 449 ARG A 452 0
SHEET 2 B 5 GLY A 456 LEU A 462 -1 O TYR A 458 N HIS A 450
SHEET 3 B 5 VAL A 533 ASN A 538 1 O ASN A 538 N LEU A 462
SHEET 4 B 5 ASN A 553 LYS A 568 -1 O ASP A 556 N VAL A 535
SHEET 5 B 5 ALA A 522 GLU A 523 -1 N ALA A 522 O TYR A 564
CISPEP 1 LEU A 612 GLU A 613 0 16.87
SITE 1 AC1 5 ARG A 431 PHE A 432 TRP A 527 ARG A 528
SITE 2 AC1 5 ARG A 581
SITE 1 AC2 6 HIS A 412 SER A 415 ASN A 416 ARG A 443
SITE 2 AC2 6 LYS A 592 HOH A 695
SITE 1 AC3 4 PHE A 432 ARG A 433 ARG A 528 HOH A 701
CRYST1 65.557 65.557 95.362 90.00 90.00 120.00 P 31 2 1 6
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 0.015254 0.008807 0.000000 0.00000
SCALE2 0.000000 0.017614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010486 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
