HEADER LIGASE/DNA BINDING PROTEIN 16-DEC-10 3ASL
TITLE STRUCTURE OF UHRF1 IN COMPLEX WITH HISTONE TAIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE UHRF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHD FINGER DOMAIN;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H3.3;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES IN UNP 2-12;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS HISTONE READER MODULE, EPIGENETIC REGULATION, HISTONE H3, LIGASE-DNA
KEYWDS 2 BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ARITA,K.SUGITA,M.UNOKI,R.HAMAMOTO,N.SEKIYAMA,H.TOCHIO,M.ARIYOSHI,
AUTHOR 2 M.SHIRAKAWA
REVDAT 4 13-MAR-24 3ASL 1 REMARK LINK
REVDAT 3 05-JUN-13 3ASL 1 JRNL
REVDAT 2 15-AUG-12 3ASL 1 JRNL
REVDAT 1 25-JAN-12 3ASL 0
JRNL AUTH K.ARITA,S.ISOGAI,T.ODA,M.UNOKI,K.SUGITA,N.SEKIYAMA,K.KUWATA,
JRNL AUTH 2 R.HAMAMOTO,H.TOCHIO,M.SATO,M.ARIYOSHI,M.SHIRAKAWA
JRNL TITL RECOGNITION OF MODIFICATION STATUS ON A HISTONE H3 TAIL BY
JRNL TITL 2 LINKED HISTONE READER MODULES OF THE EPIGENETIC REGULATOR
JRNL TITL 3 UHRF1
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 12950 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22837395
JRNL DOI 10.1073/PNAS.1203701109
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 13317
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 702
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) : 1.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 856
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.1670
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.1820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.46000
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): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.917
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 628 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 461 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 837 ; 1.512 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1115 ; 0.954 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 75 ; 5.550 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 31 ;30.248 ;23.871
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 108 ;11.245 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;23.990 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 85 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 684 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 117 ; 0.001 ; 0.020
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): 386 ; 1.239 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 149 ; 0.374 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 621 ; 1.913 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 242 ; 3.104 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 216 ; 4.341 ; 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): 1089 ; 1.176 ; 3.000
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 : 12
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 299 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6161 5.0809 -4.4428
REMARK 3 T TENSOR
REMARK 3 T11: 0.1630 T22: 0.0884
REMARK 3 T33: 0.0861 T12: -0.0591
REMARK 3 T13: -0.0034 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 10.2775 L22: 8.0260
REMARK 3 L33: 13.1448 L12: -6.5767
REMARK 3 L13: -0.2578 L23: 1.1835
REMARK 3 S TENSOR
REMARK 3 S11: 0.1879 S12: -0.3118 S13: -0.7173
REMARK 3 S21: 0.2959 S22: 0.0181 S23: 0.4645
REMARK 3 S31: 1.0213 S32: -0.3201 S33: -0.2060
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 305 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1521 6.9578 -12.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.1031
REMARK 3 T33: 0.0669 T12: -0.0285
REMARK 3 T13: 0.0129 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.3544 L22: 8.9009
REMARK 3 L33: 11.9230 L12: 3.1211
REMARK 3 L13: -2.3173 L23: -1.6552
REMARK 3 S TENSOR
REMARK 3 S11: -0.1449 S12: 0.0883 S13: 0.0051
REMARK 3 S21: -0.1410 S22: 0.1541 S23: 0.0217
REMARK 3 S31: 0.5669 S32: -0.1997 S33: -0.0092
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 311 A 315
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7552 14.9403 -9.6025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0341 T22: 0.1041
REMARK 3 T33: 0.0813 T12: 0.0120
REMARK 3 T13: 0.0082 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 3.9102 L22: 2.1558
REMARK 3 L33: 13.4497 L12: 1.5266
REMARK 3 L13: 2.6204 L23: 0.9786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: -0.0387 S13: 0.2396
REMARK 3 S21: 0.0111 S22: -0.1066 S23: 0.2242
REMARK 3 S31: -0.1688 S32: -0.6332 S33: 0.1297
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 316 A 321
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7877 18.5812 -6.4981
REMARK 3 T TENSOR
REMARK 3 T11: 0.0623 T22: 0.1054
REMARK 3 T33: 0.0785 T12: -0.0226
REMARK 3 T13: 0.0359 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 2.2106 L22: 3.8339
REMARK 3 L33: 7.6273 L12: 2.1429
REMARK 3 L13: -2.3005 L23: 0.7755
REMARK 3 S TENSOR
REMARK 3 S11: 0.1161 S12: -0.0315 S13: 0.1165
REMARK 3 S21: -0.0694 S22: 0.0416 S23: 0.0719
REMARK 3 S31: -0.3139 S32: 0.0262 S33: -0.1577
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 322 A 327
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5106 13.8244 -11.8972
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.0873
REMARK 3 T33: 0.0683 T12: -0.0041
REMARK 3 T13: 0.0129 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 3.2012 L22: 0.5962
REMARK 3 L33: 3.4918 L12: 0.3528
REMARK 3 L13: 0.3375 L23: 1.2875
REMARK 3 S TENSOR
REMARK 3 S11: 0.1076 S12: 0.1854 S13: 0.0264
REMARK 3 S21: 0.0497 S22: 0.0462 S23: -0.0401
REMARK 3 S31: 0.1143 S32: 0.0167 S33: -0.1538
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 328 A 332
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8151 16.3400 -5.3290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0734 T22: 0.0939
REMARK 3 T33: 0.0868 T12: -0.0024
REMARK 3 T13: 0.0094 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 3.4295 L22: 3.0691
REMARK 3 L33: 8.2159 L12: -1.9074
REMARK 3 L13: -0.5793 L23: 2.7132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0987 S12: 0.0569 S13: 0.0922
REMARK 3 S21: 0.0478 S22: 0.0012 S23: -0.1561
REMARK 3 S31: 0.1557 S32: 0.1247 S33: -0.1000
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 333 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4579 17.6068 4.9347
REMARK 3 T TENSOR
REMARK 3 T11: 0.2368 T22: 0.1300
REMARK 3 T33: 0.1124 T12: -0.1032
REMARK 3 T13: 0.0075 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 11.3672 L22: 5.4146
REMARK 3 L33: 9.8475 L12: 0.6878
REMARK 3 L13: 4.8806 L23: 2.9274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: -0.3316 S13: -0.2808
REMARK 3 S21: 0.3923 S22: 0.0734 S23: 0.1887
REMARK 3 S31: 0.3404 S32: -0.4853 S33: -0.0674
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 339 A 345
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8460 22.0256 -7.2026
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.0760
REMARK 3 T33: 0.1122 T12: -0.0171
REMARK 3 T13: 0.0354 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 2.1873 L22: 2.8674
REMARK 3 L33: 3.0495 L12: 2.4684
REMARK 3 L13: 0.7608 L23: 1.3176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0515 S12: 0.0269 S13: 0.2148
REMARK 3 S21: -0.1329 S22: 0.0323 S23: 0.2108
REMARK 3 S31: -0.3716 S32: -0.0328 S33: 0.0192
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 346 A 351
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8647 27.6825 -6.4922
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.0890
REMARK 3 T33: 0.1373 T12: -0.0564
REMARK 3 T13: 0.0018 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 9.0145 L22: 13.3287
REMARK 3 L33: 6.0176 L12: -9.9325
REMARK 3 L13: 0.2081 L23: -1.9039
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0125 S13: 0.3717
REMARK 3 S21: -0.0364 S22: -0.0079 S23: -0.2922
REMARK 3 S31: -0.5667 S32: 0.2311 S33: 0.0505
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 352 A 357
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9954 20.3399 3.5807
REMARK 3 T TENSOR
REMARK 3 T11: 0.0656 T22: 0.0922
REMARK 3 T33: 0.1289 T12: -0.0063
REMARK 3 T13: -0.0179 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 6.9250 L22: 8.0103
REMARK 3 L33: 14.6387 L12: -0.9552
REMARK 3 L13: -3.3947 L23: 3.1016
REMARK 3 S TENSOR
REMARK 3 S11: -0.2401 S12: -0.1708 S13: -0.1154
REMARK 3 S21: 0.5175 S22: 0.0394 S23: -0.0725
REMARK 3 S31: -0.0318 S32: 0.1556 S33: 0.2008
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 358 A 366
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0767 26.2117 4.7952
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.1116
REMARK 3 T33: 0.1152 T12: -0.0259
REMARK 3 T13: 0.0054 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 9.4354 L22: 8.1776
REMARK 3 L33: 4.8147 L12: 1.2365
REMARK 3 L13: 1.0641 L23: 2.8358
REMARK 3 S TENSOR
REMARK 3 S11: 0.0695 S12: 0.0152 S13: 0.3887
REMARK 3 S21: 0.4705 S22: -0.1271 S23: -0.0267
REMARK 3 S31: -0.0826 S32: -0.2942 S33: 0.0576
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 : B 1 B 9
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1145 10.3716 -5.1104
REMARK 3 T TENSOR
REMARK 3 T11: 0.0271 T22: 0.0488
REMARK 3 T33: 0.0283 T12: 0.0101
REMARK 3 T13: 0.0026 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.6995 L22: 5.0857
REMARK 3 L33: 4.6894 L12: -1.3128
REMARK 3 L13: 1.4491 L23: 1.4951
REMARK 3 S TENSOR
REMARK 3 S11: 0.1637 S12: 0.0287 S13: 0.0368
REMARK 3 S21: -0.2606 S22: -0.0815 S23: -0.0132
REMARK 3 S31: 0.0781 S32: 0.2596 S33: -0.0822
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 : 1.40
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 3ASL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000029644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-08; 22-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A; BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.28221; 1
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14019
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
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) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.5
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: SAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM SODIUM CITRATE, 42% PEGMME2000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.60500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.06850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.60500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.06850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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 SER A 298
REMARK 465 ALA A 367
REMARK 465 SER B 10
REMARK 465 THR B 11
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 ALA A 317 -155.54 -119.72
REMARK 500 GLU A 335 -64.16 -102.47
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 A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 302 SG
REMARK 620 2 CYS A 305 SG 107.1
REMARK 620 3 CYS A 313 SG 114.6 112.9
REMARK 620 4 CYS A 316 SG 111.5 100.8 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 318 SG
REMARK 620 2 CYS A 321 SG 109.0
REMARK 620 3 HIS A 341 ND1 99.7 99.4
REMARK 620 4 CYS A 344 SG 122.5 112.7 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 3 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 333 SG
REMARK 620 2 CYS A 336 SG 105.6
REMARK 620 3 CYS A 360 SG 109.4 114.5
REMARK 620 4 CYS A 363 SG 109.1 110.8 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 4 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 319 NE2
REMARK 620 2 GLU A 362 OE1 102.7
REMARK 620 N 1
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FL2 RELATED DB: PDB
REMARK 900 RELATED ID: 3DB3 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZKD RELATED DB: PDB
REMARK 900 RELATED ID: 2ZO0 RELATED DB: PDB
REMARK 900 RELATED ID: 3CLZ RELATED DB: PDB
REMARK 900 RELATED ID: 2FAZ RELATED DB: PDB
REMARK 900 RELATED ID: 3ASK RELATED DB: PDB
DBREF 3ASL A 298 367 UNP Q96T88 UHRF1_HUMAN 298 367
DBREF 3ASL B 1 11 UNP P84243 H33_HUMAN 2 12
SEQRES 1 A 70 SER GLY PRO SER CYS LYS HIS CYS LYS ASP ASP VAL ASN
SEQRES 2 A 70 ARG LEU CYS ARG VAL CYS ALA CYS HIS LEU CYS GLY GLY
SEQRES 3 A 70 ARG GLN ASP PRO ASP LYS GLN LEU MET CYS ASP GLU CYS
SEQRES 4 A 70 ASP MET ALA PHE HIS ILE TYR CYS LEU ASP PRO PRO LEU
SEQRES 5 A 70 SER SER VAL PRO SER GLU ASP GLU TRP TYR CYS PRO GLU
SEQRES 6 A 70 CYS ARG ASN ASP ALA
SEQRES 1 B 11 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR
HET ZN A 1 1
HET ZN A 2 1
HET ZN A 3 1
HET ZN A 4 1
HET EDO A 368 4
HET EDO A 369 4
HET EDO A 370 4
HET EDO B 12 4
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 EDO 4(C2 H6 O2)
FORMUL 11 HOH *72(H2 O)
HELIX 1 1 ASP A 326 ASP A 328 5 3
HELIX 2 2 TYR A 343 LEU A 345 5 3
SHEET 1 A 2 GLN A 330 MET A 332 0
SHEET 2 A 2 ALA A 339 HIS A 341 -1 O PHE A 340 N LEU A 331
LINK ZN ZN A 1 SG CYS A 302 1555 1555 2.34
LINK ZN ZN A 1 SG CYS A 305 1555 1555 2.36
LINK ZN ZN A 1 SG CYS A 313 1555 1555 2.31
LINK ZN ZN A 1 SG CYS A 316 1555 1555 2.31
LINK ZN ZN A 2 SG CYS A 318 1555 1555 2.33
LINK ZN ZN A 2 SG CYS A 321 1555 1555 2.36
LINK ZN ZN A 2 ND1 HIS A 341 1555 1555 2.12
LINK ZN ZN A 2 SG CYS A 344 1555 1555 2.30
LINK ZN ZN A 3 SG CYS A 333 1555 1555 2.36
LINK ZN ZN A 3 SG CYS A 336 1555 1555 2.34
LINK ZN ZN A 3 SG CYS A 360 1555 1555 2.30
LINK ZN ZN A 3 SG CYS A 363 1555 1555 2.33
LINK ZN ZN A 4 NE2 HIS A 319 1555 1555 1.97
LINK ZN ZN A 4 OE1 GLU A 362 1555 1555 2.39
CISPEP 1 ASP A 346 PRO A 347 0 -1.47
SITE 1 AC1 4 CYS A 302 CYS A 305 CYS A 313 CYS A 316
SITE 1 AC2 4 CYS A 318 CYS A 321 HIS A 341 CYS A 344
SITE 1 AC3 4 CYS A 333 CYS A 336 CYS A 360 CYS A 363
SITE 1 AC4 2 HIS A 319 GLU A 362
SITE 1 AC5 3 HOH A 15 CYS A 305 ARG A 311
SITE 1 AC6 4 HOH A 6 HOH A 15 LEU A 312 HOH A 371
SITE 1 AC7 8 HOH A 58 HOH A 63 LEU A 312 GLY A 323
SITE 2 AC7 8 ARG A 324 GLN A 325 HIS A 341 TYR A 343
SITE 1 AC8 5 PRO A 347 ARG A 364 ALA B 1 THR B 3
SITE 2 AC8 5 HOH B 52
CRYST1 67.210 36.137 34.175 90.00 110.69 90.00 C 1 2 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 0.014879 0.000000 0.005620 0.00000
SCALE2 0.000000 0.027672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.031279 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
