HEADER LIGASE 18-DEC-08 3FL2
TITLE CRYSTAL STRUCTURE OF THE RING DOMAIN OF THE E3 UBIQUITIN-PROTEIN
TITLE 2 LIGASE UHRF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE UHRF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING DOMAIN (UNP RESIDUES 672-793);
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: ICBP90, NP95, RNF106, UHRF1;
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-LIC
KEYWDS CELL CYCLE, DNA DAMAGE, DNA REPAIR, RING FINGER DOMAIN, LIGASE, METAL
KEYWDS 2 BINDING, DNA REPLICATION, TRANSCRIPTIONAL SILENCING, CHROMATIN,
KEYWDS 3 PHOSPHORYLATION, TRANSCRIPTION, TRANSCRIPTION REGULATION, UBL
KEYWDS 4 CONJUGATION, UBL CONJUGATION PATHWAY, ZINC, ZINC-FINGER,
KEYWDS 5 EPIGENETICS, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 6 SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,G.V.AVVAKUMOV,S.XUE,Y.LI,C.BOUNTRA,J.WEIGELT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3FL2 1 SEQADV
REVDAT 2 01-NOV-17 3FL2 1 REMARK
REVDAT 1 20-JAN-09 3FL2 0
JRNL AUTH J.R.WALKER,G.V.AVVAKUMOV,S.XUE,Y.LI,C.BOUNTRA,J.WEIGELT,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON
JRNL TITL STRUCTURE OF THE RING DOMAIN OF THE E3 UBIQUITIN-PROTEIN
JRNL TITL 2 LIGASE UHRF1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0063
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 10426
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 525
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.2020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 907
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.94000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : 1.56000
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): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.655
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 932 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1250 ; 1.500 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 114 ; 5.859 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 44 ;37.206 ;24.091
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 155 ;11.981 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;11.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 139 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 708 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 580 ; 1.727 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 935 ; 2.419 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 352 ; 3.951 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 315 ; 5.665 ; 7.000
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 : 13
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 675 A 680
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9815 15.2735 2.6265
REMARK 3 T TENSOR
REMARK 3 T11: 0.2150 T22: 0.3401
REMARK 3 T33: 0.2441 T12: -0.0244
REMARK 3 T13: 0.0119 T23: -0.0850
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 10.9231
REMARK 3 L33: 20.7779 L12: 1.0348
REMARK 3 L13: -0.5350 L23: -0.8833
REMARK 3 S TENSOR
REMARK 3 S11: -0.0945 S12: 0.1958 S13: -0.1522
REMARK 3 S21: -0.2294 S22: -0.0592 S23: -0.1880
REMARK 3 S31: 0.2276 S32: 0.3448 S33: 0.1536
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 681 A 693
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6760 21.7238 12.9025
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.0978
REMARK 3 T33: 0.1584 T12: -0.0014
REMARK 3 T13: 0.0004 T23: 0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 5.2810 L22: 4.4344
REMARK 3 L33: 9.0049 L12: 0.5563
REMARK 3 L13: 1.6003 L23: -0.1472
REMARK 3 S TENSOR
REMARK 3 S11: -0.1344 S12: 0.4740 S13: 0.1745
REMARK 3 S21: -0.1597 S22: -0.0413 S23: 0.2118
REMARK 3 S31: -0.3526 S32: 0.3543 S33: 0.1757
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 694 A 711
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0875 11.4813 5.8139
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.2641
REMARK 3 T33: 0.2518 T12: 0.0194
REMARK 3 T13: 0.0216 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.2923 L22: 5.0884
REMARK 3 L33: 2.6207 L12: -0.5320
REMARK 3 L13: -0.6331 L23: 3.4181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: -0.1010 S13: 0.0067
REMARK 3 S21: -0.2982 S22: 0.2274 S23: -0.4159
REMARK 3 S31: -0.1849 S32: 0.2218 S33: -0.2541
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 712 A 725
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4847 8.2038 14.2880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.1392
REMARK 3 T33: 0.1774 T12: 0.0430
REMARK 3 T13: 0.0326 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.6879 L22: 1.3327
REMARK 3 L33: 8.8535 L12: -0.4589
REMARK 3 L13: -0.2636 L23: 1.4153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0704 S12: 0.0955 S13: -0.0070
REMARK 3 S21: -0.1283 S22: -0.1333 S23: -0.1887
REMARK 3 S31: 0.3080 S32: 0.1755 S33: 0.0629
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 726 A 731
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8315 5.2700 24.1930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.1375
REMARK 3 T33: 0.1726 T12: -0.0091
REMARK 3 T13: 0.0194 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 6.0461 L22: 7.1059
REMARK 3 L33: 20.4486 L12: -1.4442
REMARK 3 L13: 7.6894 L23: -3.4873
REMARK 3 S TENSOR
REMARK 3 S11: 0.2852 S12: -0.0104 S13: -0.5213
REMARK 3 S21: -0.0176 S22: -0.1334 S23: -0.2532
REMARK 3 S31: 0.9210 S32: 0.4155 S33: -0.1518
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 732 A 740
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4802 16.8317 25.3834
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.0578
REMARK 3 T33: 0.0899 T12: 0.0172
REMARK 3 T13: 0.0338 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 8.3805 L22: 4.9709
REMARK 3 L33: 1.5620 L12: 4.1290
REMARK 3 L13: 3.2821 L23: 2.1504
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: -0.1753 S13: 0.2693
REMARK 3 S21: 0.0702 S22: -0.0822 S23: 0.1596
REMARK 3 S31: -0.0055 S32: -0.1398 S33: 0.0467
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 741 A 745
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9575 14.2293 26.7629
REMARK 3 T TENSOR
REMARK 3 T11: 0.1106 T22: 0.1032
REMARK 3 T33: 0.1100 T12: 0.0102
REMARK 3 T13: 0.0050 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 7.9780 L22: 4.0860
REMARK 3 L33: 1.2527 L12: 3.6333
REMARK 3 L13: -0.2954 L23: -0.7881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: -0.3345 S13: 0.1489
REMARK 3 S21: 0.0923 S22: -0.0205 S23: -0.0724
REMARK 3 S31: 0.0558 S32: -0.0830 S33: 0.0640
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 746 A 751
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9907 10.2448 33.8324
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.1446
REMARK 3 T33: 0.1456 T12: 0.0047
REMARK 3 T13: 0.0148 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 9.9313 L22: 4.7459
REMARK 3 L33: 16.3730 L12: -0.6046
REMARK 3 L13: 2.8428 L23: 1.7204
REMARK 3 S TENSOR
REMARK 3 S11: 0.0799 S12: -0.3412 S13: -0.2355
REMARK 3 S21: 0.2934 S22: -0.1060 S23: 0.3882
REMARK 3 S31: 0.3993 S32: -0.6512 S33: 0.0261
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 752 A 757
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4188 13.6469 40.5327
REMARK 3 T TENSOR
REMARK 3 T11: 0.1855 T22: 0.2267
REMARK 3 T33: 0.1345 T12: -0.0178
REMARK 3 T13: 0.0159 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 5.0618 L22: 9.3367
REMARK 3 L33: 11.9961 L12: -0.5487
REMARK 3 L13: -4.0219 L23: -5.0798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: -0.2175 S13: -0.2011
REMARK 3 S21: -0.0124 S22: -0.0507 S23: 0.4297
REMARK 3 S31: 0.3891 S32: -0.4409 S33: 0.0490
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 758 A 767
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3781 17.6341 34.3644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1278 T22: 0.1250
REMARK 3 T33: 0.1317 T12: -0.0089
REMARK 3 T13: 0.0173 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 7.7393 L22: 4.1404
REMARK 3 L33: 3.8305 L12: -3.0225
REMARK 3 L13: -1.7065 L23: -0.5675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: -0.4435 S13: 0.2658
REMARK 3 S21: 0.2667 S22: 0.0787 S23: -0.0038
REMARK 3 S31: -0.1884 S32: -0.0217 S33: -0.1271
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 768 A 773
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7845 21.4042 34.5975
REMARK 3 T TENSOR
REMARK 3 T11: 0.1758 T22: 0.2042
REMARK 3 T33: 0.2083 T12: -0.0113
REMARK 3 T13: 0.0244 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.9233 L22: 6.5947
REMARK 3 L33: 14.8664 L12: -0.0140
REMARK 3 L13: -2.3100 L23: 2.5416
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: -0.2141 S13: -0.1944
REMARK 3 S21: 0.0340 S22: -0.0750 S23: 0.1266
REMARK 3 S31: 0.3534 S32: -0.4345 S33: 0.0544
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 774 A 781
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1475 16.5782 17.9303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.1042
REMARK 3 T33: 0.1352 T12: 0.0240
REMARK 3 T13: 0.0208 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.2945 L22: 5.8722
REMARK 3 L33: 9.8270 L12: 0.5351
REMARK 3 L13: 2.6180 L23: 1.2095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0291 S12: -0.0030 S13: 0.1285
REMARK 3 S21: 0.0664 S22: -0.0039 S23: 0.2241
REMARK 3 S31: -0.2154 S32: -0.3515 S33: 0.0329
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 782 A 793
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5590 6.5216 15.9121
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.0810
REMARK 3 T33: 0.1214 T12: 0.0134
REMARK 3 T13: -0.0014 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 7.1164 L22: 2.2881
REMARK 3 L33: 2.4719 L12: 1.0416
REMARK 3 L13: -2.0197 L23: 0.3536
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: 0.2760 S13: -0.2324
REMARK 3 S21: -0.1665 S22: -0.0725 S23: -0.0948
REMARK 3 S31: 0.1458 S32: 0.0361 S33: 0.0690
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS, ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS.
REMARK 4
REMARK 4 3FL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11019
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.76
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: 1Z6U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG MME 2000, 0.1 M TRIS-HCL, PH
REMARK 280 8.5, 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 22.86800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 24.20450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.45800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 24.20450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.86800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.45800
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: 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 GLY A 670
REMARK 465 SER A 671
REMARK 465 GLU A 672
REMARK 465 PRO A 673
REMARK 465 TYR A 674
REMARK 465 LEU A 701
REMARK 465 LYS A 702
REMARK 465 ASP A 703
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 ARG A 704 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 773 CD OE1 NE2
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 724 SG
REMARK 620 2 CYS A 727 SG 110.7
REMARK 620 3 CYS A 744 SG 102.9 105.7
REMARK 620 4 CYS A 747 SG 114.0 109.0 114.2
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 739 SG
REMARK 620 2 HIS A 741 ND1 120.5
REMARK 620 3 CYS A 759 SG 103.0 111.6
REMARK 620 4 CYS A 762 SG 103.0 104.5 114.3
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 A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BI7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SRA DOMAIN OF E3 UBIQUITIN-PROTEIN LIGASE
REMARK 900 UHRF1
REMARK 900 RELATED ID: 3CLZ RELATED DB: PDB
REMARK 900 THE SET AND RING ASSOCIATED (SRA) DOMAIN OF UHRF1 BOUND TO
REMARK 900 METHYLATED DNA
REMARK 900 RELATED ID: 2FAZ RELATED DB: PDB
REMARK 900 UBIQUITIN-LIKE DOMAIN OF HUMAN NUCLEAR ZINC FINGER PROTEIN NP95
REMARK 900 RELATED ID: 3DB4 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE TANDEM TUDOR DOMAINS OF THE E3 UBIQUITIN- PROTEIN
REMARK 900 LIGASE UHRF1
REMARK 900 RELATED ID: 3DB3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TANDEM TUDOR DOMAINS OF THE E3 UBIQUITIN-
REMARK 900 PROTEIN LIGASE UHRF1 IN COMPLEX WITH TRIMETHYLATED HISTONE H3-K9
REMARK 900 PEPTIDE
DBREF 3FL2 A 672 793 UNP Q96T88 UHRF1_HUMAN 672 793
SEQADV 3FL2 GLY A 670 UNP Q96T88 EXPRESSION TAG
SEQADV 3FL2 SER A 671 UNP Q96T88 EXPRESSION TAG
SEQRES 1 A 124 GLY SER GLU PRO TYR SER LEU THR ALA GLN GLN SER SER
SEQRES 2 A 124 LEU ILE ARG GLU ASP LYS SER ASN ALA LYS LEU TRP ASN
SEQRES 3 A 124 GLU VAL LEU ALA SER LEU LYS ASP ARG PRO ALA SER GLY
SEQRES 4 A 124 SER PRO PHE GLN LEU PHE LEU SER LYS VAL GLU GLU THR
SEQRES 5 A 124 PHE GLN CYS ILE CYS CYS GLN GLU LEU VAL PHE ARG PRO
SEQRES 6 A 124 ILE THR THR VAL CYS GLN HIS ASN VAL CYS LYS ASP CYS
SEQRES 7 A 124 LEU ASP ARG SER PHE ARG ALA GLN VAL PHE SER CYS PRO
SEQRES 8 A 124 ALA CYS ARG TYR ASP LEU GLY ARG SER TYR ALA MET GLN
SEQRES 9 A 124 VAL ASN GLN PRO LEU GLN THR VAL LEU ASN GLN LEU PHE
SEQRES 10 A 124 PRO GLY TYR GLY ASN GLY ARG
HET ZN A1001 1
HET ZN A1002 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 HOH *96(H2 O)
HELIX 1 1 THR A 677 ASP A 687 1 11
HELIX 2 2 ASN A 690 SER A 700 1 11
HELIX 3 3 SER A 709 PHE A 722 1 14
HELIX 4 4 LYS A 745 ALA A 754 1 10
HELIX 5 5 ASN A 775 PHE A 786 1 12
SHEET 1 A 2 PRO A 734 THR A 736 0
SHEET 2 A 2 ASN A 742 CYS A 744 -1 O VAL A 743 N ILE A 735
LINK SG CYS A 724 ZN ZN A1001 1555 1555 2.40
LINK SG CYS A 727 ZN ZN A1001 1555 1555 2.35
LINK SG CYS A 739 ZN ZN A1002 1555 1555 2.34
LINK ND1 HIS A 741 ZN ZN A1002 1555 1555 2.11
LINK SG CYS A 744 ZN ZN A1001 1555 1555 2.39
LINK SG CYS A 747 ZN ZN A1001 1555 1555 2.37
LINK SG CYS A 759 ZN ZN A1002 1555 1555 2.35
LINK SG CYS A 762 ZN ZN A1002 1555 1555 2.35
SITE 1 AC1 4 CYS A 724 CYS A 727 CYS A 744 CYS A 747
SITE 1 AC2 4 CYS A 739 HIS A 741 CYS A 759 CYS A 762
CRYST1 45.736 46.916 48.409 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 0.021865 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020657 0.00000
(ATOM LINES ARE NOT SHOWN.)
END