HEADER LIGASE/NUCLEAR PROTEIN 16-JUN-11 3SHB
TITLE CRYSTAL STRUCTURE OF PHD DOMAIN OF UHRF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE UHRF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHD DOMAIN (UNP RESIDUES 298-366);
COMPND 5 SYNONYM: INVERTED CCAAT BOX-BINDING PROTEIN OF 90 KDA, NUCLEAR
COMPND 6 PROTEIN 95, NUCLEAR ZINC FINGER PROTEIN NP95, HUNP95, RING FINGER
COMPND 7 PROTEIN 106, TRANSCRIPTION FACTOR ICBP90, UBIQUITIN-LIKE PHD AND RING
COMPND 8 FINGER DOMAIN-CONTAINING PROTEIN 1, UBIQUITIN-LIKE-CONTAINING PHD AND
COMPND 9 RING FINGER DOMAINS PROTEIN 1;
COMPND 10 EC: 6.3.2.-;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: HISTONE H3 PEPTIDE;
COMPND 14 CHAIN: B;
COMPND 15 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: PETDUET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS UNMODIFIED HISTONE, METHYLATION, UHRF1, PHD, H3, LIGASE-NUCLEAR
KEYWDS 2 PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.HU,Z.LI,P.WANG,Y.LIN,Y.XU
REVDAT 2 20-MAR-24 3SHB 1 REMARK SEQADV LINK
REVDAT 1 24-AUG-11 3SHB 0
JRNL AUTH L.HU,Z.LI,P.WANG,Y.LIN,Y.XU
JRNL TITL CRYSTAL STRUCTURE OF PHD DOMAIN OF UHRF1 AND INSIGHTS INTO
JRNL TITL 2 RECOGNITION OF UNMODIFIED HISTONE H3 ARGININE RESIDUE 2.
JRNL REF CELL RES. 2011
JRNL REFN ISSN 1001-0602
JRNL PMID 21808300
JRNL DOI 10.1038/CR.2011.124
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.240
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 8535
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670
REMARK 3 FREE R VALUE TEST SET COUNT : 399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.7092 - 2.5960 0.99 2986 143 0.2108 0.2013
REMARK 3 2 2.5960 - 2.0606 0.96 2687 118 0.2022 0.2771
REMARK 3 3 2.0606 - 1.8002 0.90 2463 138 0.2196 0.2708
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 49.01
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.58160
REMARK 3 B22 (A**2) : -7.58160
REMARK 3 B33 (A**2) : -16.67040
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 586
REMARK 3 ANGLE : 1.322 790
REMARK 3 CHIRALITY : 0.086 82
REMARK 3 PLANARITY : 0.006 106
REMARK 3 DIHEDRAL : 16.448 223
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066201.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2823
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8535
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 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: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HYDROCHLORIDE (PH8.5), 30%
REMARK 280 W/V POLYETHYLENE GLYCEROL 4000, 0.2M MGCL2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 73.25500
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 146.51000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.88250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 183.13750
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 36.62750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.25500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 146.51000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 183.13750
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 109.88250
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.62750
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: 880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A1004 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2037 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2064 LIES ON A SPECIAL POSITION.
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 GLY A 303
REMARK 465 PRO A 304
REMARK 465 LEU A 305
REMARK 465 GLY A 306
REMARK 465 SER A 307
REMARK 465 PRO A 308
REMARK 465 GLU A 309
REMARK 465 PHE A 310
REMARK 465 ASN A 378
REMARK 465 ASP A 379
REMARK 465 ARG B 8
REMARK 465 LYS B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 GLY B 12
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2016 O HOH A 2016 8555 2.06
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 ASP A 320 19.59 56.80
REMARK 500 ALA A 330 -155.99 -117.23
REMARK 500 GLU A 348 -60.96 -100.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 315 SG
REMARK 620 2 CYS A 318 SG 108.9
REMARK 620 3 CYS A 326 SG 115.1 113.7
REMARK 620 4 CYS A 329 SG 109.5 96.0 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 331 SG
REMARK 620 2 CYS A 334 SG 110.2
REMARK 620 3 HIS A 354 ND1 100.9 101.4
REMARK 620 4 CYS A 357 SG 120.3 108.2 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 332 NE2
REMARK 620 2 GLU A 375 OE2 98.5
REMARK 620 3 GLU A 375 OE1 115.9 55.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 346 SG
REMARK 620 2 CYS A 349 SG 108.5
REMARK 620 3 CYS A 373 SG 110.6 109.3
REMARK 620 4 CYS A 376 SG 108.2 107.0 113.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1004
DBREF 3SHB A 311 379 UNP Q96T88 UHRF1_HUMAN 298 366
DBREF 3SHB B 1 12 PDB 3SHB 3SHB 1 12
SEQADV 3SHB GLY A 303 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB PRO A 304 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB LEU A 305 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB GLY A 306 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB SER A 307 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB PRO A 308 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB GLU A 309 UNP Q96T88 EXPRESSION TAG
SEQADV 3SHB PHE A 310 UNP Q96T88 EXPRESSION TAG
SEQRES 1 A 77 GLY PRO LEU GLY SER PRO GLU PHE SER GLY PRO SER CYS
SEQRES 2 A 77 LYS HIS CYS LYS ASP ASP VAL ASN ARG LEU CYS ARG VAL
SEQRES 3 A 77 CYS ALA CYS HIS LEU CYS GLY GLY ARG GLN ASP PRO ASP
SEQRES 4 A 77 LYS GLN LEU MET CYS ASP GLU CYS ASP MET ALA PHE HIS
SEQRES 5 A 77 ILE TYR CYS LEU ASP PRO PRO LEU SER SER VAL PRO SER
SEQRES 6 A 77 GLU ASP GLU TRP TYR CYS PRO GLU CYS ARG ASN ASP
SEQRES 1 B 12 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
HET ZN A1001 1
HET ZN A1002 1
HET ZN A1003 1
HET ZN A1004 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 HOH *66(H2 O)
HELIX 1 1 ASP A 339 ASP A 341 5 3
SHEET 1 A 2 GLN A 343 MET A 345 0
SHEET 2 A 2 ALA A 352 HIS A 354 -1 O PHE A 353 N LEU A 344
LINK SG CYS A 315 ZN ZN A1001 1555 1555 2.40
LINK SG CYS A 318 ZN ZN A1001 1555 1555 2.45
LINK SG CYS A 326 ZN ZN A1001 1555 1555 2.30
LINK SG CYS A 329 ZN ZN A1001 1555 1555 2.35
LINK SG CYS A 331 ZN ZN A1002 1555 1555 2.31
LINK NE2 HIS A 332 ZN ZN A1004 1555 1555 2.07
LINK SG CYS A 334 ZN ZN A1002 1555 1555 2.41
LINK SG CYS A 346 ZN ZN A1003 1555 1555 2.27
LINK SG CYS A 349 ZN ZN A1003 1555 1555 2.38
LINK ND1 HIS A 354 ZN ZN A1002 1555 1555 2.18
LINK SG CYS A 357 ZN ZN A1002 1555 1555 2.29
LINK SG CYS A 373 ZN ZN A1003 1555 1555 2.38
LINK OE2 GLU A 375 ZN ZN A1004 1555 1555 2.22
LINK OE1 GLU A 375 ZN ZN A1004 1555 1555 2.43
LINK SG CYS A 376 ZN ZN A1003 1555 1555 2.34
CISPEP 1 GLY A 312 PRO A 313 0 6.60
CISPEP 2 ASP A 359 PRO A 360 0 0.89
SITE 1 AC1 4 CYS A 315 CYS A 318 CYS A 326 CYS A 329
SITE 1 AC2 4 CYS A 331 CYS A 334 HIS A 354 CYS A 357
SITE 1 AC3 4 CYS A 346 CYS A 349 CYS A 373 CYS A 376
SITE 1 AC4 2 HIS A 332 GLU A 375
CRYST1 36.609 36.609 219.765 90.00 90.00 120.00 P 61 2 2 12
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 0.027316 0.015771 0.000000 0.00000
SCALE2 0.000000 0.031541 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004550 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
