HEADER LIGASE 05-JUL-13 4LJP
TITLE STRUCTURE OF AN ACTIVE LIGASE (HOIP-H889A)/UBIQUITIN TRANSFER COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF31;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: E3 LIGASE HOIP CATALYTIC CORE (UNP RESIDUES 853-1072);
COMPND 5 SYNONYM: HOIL-1-INTERACTING PROTEIN, HOIP, RING FINGER PROTEIN 31,
COMPND 6 ZINC IN-BETWEEN-RING-FINGER UBIQUITIN-ASSOCIATED DOMAIN PROTEIN;
COMPND 7 EC: 6.3.2.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: POLYUBIQUITIN-C;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: UNP RESIDUES 77-152
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RNF31, ZIBRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-49B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 14 ORGANISM_TAXID: 9913
KEYWDS E3 LIGASE-UBIQUITIN COMPLEX, LIGASE, HOIP, RNF31, UBIQUITIN, RBR
KEYWDS 2 LIGASE, E3 LIGASE, RING DOMAIN, IBR DOMAIN, ZINC FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR R.R.RANA,B.STIEGLITZ,M.G.KOLIOPOULOS,A.C.MORRIS-DAVIES,
AUTHOR 2 E.CHRISTODOULOU,S.HOWELL,N.R.BROWN,K.RITTINGER
REVDAT 7 20-SEP-23 4LJP 1 REMARK SEQADV LINK
REVDAT 6 17-JUL-19 4LJP 1 REMARK
REVDAT 5 15-NOV-17 4LJP 1 REMARK
REVDAT 4 10-DEC-14 4LJP 1 REMARK
REVDAT 3 18-DEC-13 4LJP 1 JRNL
REVDAT 2 13-NOV-13 4LJP 1 JRNL
REVDAT 1 16-OCT-13 4LJP 0
JRNL AUTH B.STIEGLITZ,R.R.RANA,M.G.KOLIOPOULOS,A.C.MORRIS-DAVIES,
JRNL AUTH 2 V.SCHAEFFER,E.CHRISTODOULOU,S.HOWELL,N.R.BROWN,I.DIKIC,
JRNL AUTH 3 K.RITTINGER
JRNL TITL STRUCTURAL BASIS FOR LIGASE-SPECIFIC CONJUGATION OF LINEAR
JRNL TITL 2 UBIQUITIN CHAINS BY HOIP.
JRNL REF NATURE V. 503 422 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 24141947
JRNL DOI 10.1038/NATURE12638
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 17070
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 865
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 38.1768 - 4.9191 0.98 2670 152 0.1250 0.1607
REMARK 3 2 4.9191 - 3.9057 0.96 2575 152 0.1264 0.1545
REMARK 3 3 3.9057 - 3.4123 0.96 2654 142 0.1550 0.1631
REMARK 3 4 3.4123 - 3.1005 0.97 2623 130 0.1874 0.2679
REMARK 3 5 3.1005 - 2.8784 0.97 2539 151 0.2110 0.2545
REMARK 3 6 2.8784 - 2.7087 0.95 2576 158 0.2137 0.3141
REMARK 3 7 2.7087 - 2.5731 0.98 2639 143 0.2271 0.3056
REMARK 3 8 2.5731 - 2.4611 0.98 2800 84 0.2173 0.3490
REMARK 3 9 2.4611 - 2.3664 0.99 2664 171 0.2318 0.2869
REMARK 3 10 2.3664 - 2.2847 0.98 2570 151 0.2410 0.2613
REMARK 3 11 2.2847 - 2.2133 0.97 2682 122 0.2666 0.3317
REMARK 3 12 2.2133 - 2.1500 0.98 2697 132 0.2666 0.2965
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 2340
REMARK 3 ANGLE : 1.115 3163
REMARK 3 CHIRALITY : 0.071 340
REMARK 3 PLANARITY : 0.006 421
REMARK 3 DIHEDRAL : 16.864 900
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 857 THROUGH 895 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1544 46.8080 17.3213
REMARK 3 T TENSOR
REMARK 3 T11: 0.4082 T22: 0.3121
REMARK 3 T33: 0.2815 T12: 0.1075
REMARK 3 T13: 0.0626 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 3.2813 L22: 8.4769
REMARK 3 L33: 6.2392 L12: -4.3493
REMARK 3 L13: -1.6660 L23: 2.8500
REMARK 3 S TENSOR
REMARK 3 S11: -0.2512 S12: -0.1126 S13: 0.1807
REMARK 3 S21: 0.5493 S22: 0.0696 S23: -0.0410
REMARK 3 S31: -0.1156 S32: 0.1193 S33: 0.1905
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 896 THROUGH 938 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9879 50.1785 0.8215
REMARK 3 T TENSOR
REMARK 3 T11: 0.3259 T22: 0.3129
REMARK 3 T33: 0.2879 T12: 0.0895
REMARK 3 T13: -0.0359 T23: 0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 7.4308 L22: 2.8978
REMARK 3 L33: 4.6080 L12: -1.2919
REMARK 3 L13: -0.7063 L23: 0.7702
REMARK 3 S TENSOR
REMARK 3 S11: -0.0298 S12: 0.5963 S13: 0.2553
REMARK 3 S21: -0.2045 S22: -0.0370 S23: 0.5624
REMARK 3 S31: -0.3459 S32: -0.6010 S33: 0.0750
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 939 THROUGH 1012 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8153 33.1396 11.7477
REMARK 3 T TENSOR
REMARK 3 T11: 0.5578 T22: 0.3988
REMARK 3 T33: 0.3673 T12: 0.2556
REMARK 3 T13: 0.0657 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 3.2305 L22: 3.2007
REMARK 3 L33: 3.7752 L12: 0.5525
REMARK 3 L13: -0.8910 L23: -0.0276
REMARK 3 S TENSOR
REMARK 3 S11: -0.2732 S12: -0.3719 S13: -0.7253
REMARK 3 S21: 0.3886 S22: -0.0928 S23: -0.2067
REMARK 3 S31: 0.8663 S32: 0.6626 S33: 0.2949
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1013 THROUGH 1060 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2669 51.5709 -12.0920
REMARK 3 T TENSOR
REMARK 3 T11: 0.4972 T22: 0.4953
REMARK 3 T33: 0.3222 T12: 0.0614
REMARK 3 T13: 0.0547 T23: 0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 3.2761 L22: 3.1328
REMARK 3 L33: 5.4621 L12: 0.5522
REMARK 3 L13: -2.6105 L23: -2.1083
REMARK 3 S TENSOR
REMARK 3 S11: 0.1291 S12: 0.6358 S13: 0.4333
REMARK 3 S21: -0.5508 S22: 0.1745 S23: 0.0160
REMARK 3 S31: -0.9803 S32: -0.5737 S33: -0.2743
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1061 THROUGH 1071 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7607 54.3204 7.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.5467 T22: 0.4919
REMARK 3 T33: 0.3128 T12: -0.0210
REMARK 3 T13: 0.0010 T23: -0.0559
REMARK 3 L TENSOR
REMARK 3 L11: 9.2478 L22: 2.3366
REMARK 3 L33: 3.3106 L12: -0.0773
REMARK 3 L13: -5.5385 L23: 0.0353
REMARK 3 S TENSOR
REMARK 3 S11: 0.2661 S12: -0.9347 S13: -0.1150
REMARK 3 S21: 0.8162 S22: 0.0901 S23: -0.0179
REMARK 3 S31: -1.4920 S32: 1.2225 S33: 0.0208
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9424 34.0321 -3.7097
REMARK 3 T TENSOR
REMARK 3 T11: 0.3760 T22: 0.3618
REMARK 3 T33: 0.2904 T12: 0.1185
REMARK 3 T13: -0.0194 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 9.4767 L22: 4.3487
REMARK 3 L33: 1.9897 L12: 0.5903
REMARK 3 L13: 0.4481 L23: 0.0320
REMARK 3 S TENSOR
REMARK 3 S11: -0.1867 S12: 0.2015 S13: -0.2740
REMARK 3 S21: 0.4327 S22: 0.0141 S23: -0.3353
REMARK 3 S31: 0.2238 S32: 0.0338 S33: 0.1624
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8293 42.6363 -6.1267
REMARK 3 T TENSOR
REMARK 3 T11: 0.3055 T22: 0.4438
REMARK 3 T33: 0.3493 T12: 0.1824
REMARK 3 T13: -0.0759 T23: -0.0958
REMARK 3 L TENSOR
REMARK 3 L11: 7.7810 L22: 5.0357
REMARK 3 L33: 6.5382 L12: 5.8802
REMARK 3 L13: -1.6499 L23: -2.1213
REMARK 3 S TENSOR
REMARK 3 S11: -0.2722 S12: 0.3032 S13: 0.4405
REMARK 3 S21: 0.1858 S22: 0.0139 S23: 0.2479
REMARK 3 S31: -0.5391 S32: -0.7405 S33: 0.1736
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8015 38.6168 -15.6378
REMARK 3 T TENSOR
REMARK 3 T11: 0.2324 T22: 0.6422
REMARK 3 T33: 0.3720 T12: -0.0051
REMARK 3 T13: -0.0310 T23: -0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 6.1056 L22: 3.6808
REMARK 3 L33: 6.5816 L12: 3.3154
REMARK 3 L13: -2.1568 L23: -4.2848
REMARK 3 S TENSOR
REMARK 3 S11: -0.3597 S12: 1.3697 S13: 0.1221
REMARK 3 S21: -0.5751 S22: 0.3059 S23: 0.4126
REMARK 3 S31: 0.2213 S32: -0.5640 S33: -0.1019
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.4015 32.7316 -10.5229
REMARK 3 T TENSOR
REMARK 3 T11: 0.2915 T22: 0.7216
REMARK 3 T33: 0.5503 T12: -0.1079
REMARK 3 T13: 0.0220 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 6.4128 L22: 8.1259
REMARK 3 L33: 6.9809 L12: -5.8453
REMARK 3 L13: -0.2711 L23: 0.0466
REMARK 3 S TENSOR
REMARK 3 S11: -0.1362 S12: 1.1194 S13: -0.5332
REMARK 3 S21: -0.4724 S22: 0.0057 S23: 1.0551
REMARK 3 S31: 0.6014 S32: -1.1130 S33: 0.2627
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8568 33.2329 -0.4311
REMARK 3 T TENSOR
REMARK 3 T11: 0.3890 T22: 0.6032
REMARK 3 T33: 0.3188 T12: 0.0208
REMARK 3 T13: 0.0637 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 3.7796 L22: 7.0845
REMARK 3 L33: 6.9730 L12: -3.8225
REMARK 3 L13: 4.8861 L23: -3.4841
REMARK 3 S TENSOR
REMARK 3 S11: -0.2526 S12: -1.3428 S13: 0.1801
REMARK 3 S21: 0.6756 S22: 0.0611 S23: 0.4520
REMARK 3 S31: 0.0863 S32: -1.1994 S33: 0.2220
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 66 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4001 31.4395 -10.8243
REMARK 3 T TENSOR
REMARK 3 T11: 0.3251 T22: 0.5347
REMARK 3 T33: 0.2157 T12: 0.0112
REMARK 3 T13: -0.0187 T23: -0.1092
REMARK 3 L TENSOR
REMARK 3 L11: 5.0387 L22: 1.2614
REMARK 3 L33: 6.0837 L12: -0.3963
REMARK 3 L13: -5.4776 L23: 0.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.6698 S12: 1.1530 S13: -1.1425
REMARK 3 S21: -0.2585 S22: 0.0013 S23: -0.0421
REMARK 3 S31: 0.8181 S32: -0.5396 S33: 0.5783
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4993 37.5597 -26.7189
REMARK 3 T TENSOR
REMARK 3 T11: 0.2962 T22: 0.5281
REMARK 3 T33: 0.2892 T12: -0.1336
REMARK 3 T13: -0.0221 T23: -0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 7.4947 L22: 5.3668
REMARK 3 L33: 6.8911 L12: -4.6580
REMARK 3 L13: -5.2781 L23: 5.8967
REMARK 3 S TENSOR
REMARK 3 S11: -0.0325 S12: -0.2493 S13: 0.0901
REMARK 3 S21: -0.3676 S22: -0.1569 S23: 0.5199
REMARK 3 S31: -0.3795 S32: 1.0719 S33: 0.4119
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 4LJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CCP4
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17108
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 38.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.2
REMARK 200 STARTING MODEL: PDB ENTRY 4LJO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMINO ACIDS, 0.1 M IMIDAZOLE,
REMARK 280 MES, 30 % P550 MME_P20K , PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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 44.45667
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 88.91333
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: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 GLY A 850
REMARK 465 PRO A 851
REMARK 465 GLY A 852
REMARK 465 PRO A 853
REMARK 465 GLU A 854
REMARK 465 TYR A 855
REMARK 465 GLN A 856
REMARK 465 LYS A 1072
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 PRO A 958 158.22 -47.28
REMARK 500 ASN A 979 41.60 70.92
REMARK 500 ALA A 995 19.00 59.27
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 A1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 871 SG
REMARK 620 2 CYS A 874 SG 106.3
REMARK 620 3 CYS A 890 SG 109.6 107.0
REMARK 620 4 CYS A 893 SG 106.6 118.3 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 898 SG
REMARK 620 2 CYS A 901 SG 112.0
REMARK 620 3 HIS A 926 ND1 98.0 110.0
REMARK 620 4 CYS A 930 SG 106.0 112.4 117.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1103 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 911 SG
REMARK 620 2 CYS A 916 SG 129.5
REMARK 620 3 HIS A 923 NE2 103.9 97.4
REMARK 620 4 HIS A 925 NE2 93.6 117.7 115.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1104 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 969 SG
REMARK 620 2 CYS A 986 SG 113.4
REMARK 620 3 CYS A 998 SG 116.7 111.2
REMARK 620 4 HIS A1001 ND1 104.7 107.6 102.0
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 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LJO RELATED DB: PDB
REMARK 900 RELATED ID: 4LJQ RELATED DB: PDB
DBREF 4LJP A 853 1072 UNP Q96EP0 RNF31_HUMAN 853 1072
DBREF 4LJP B 1 76 UNP E1B9K1 E1B9K1_BOVIN 77 152
SEQADV 4LJP GLY A 850 UNP Q96EP0 EXPRESSION TAG
SEQADV 4LJP PRO A 851 UNP Q96EP0 EXPRESSION TAG
SEQADV 4LJP GLY A 852 UNP Q96EP0 EXPRESSION TAG
SEQADV 4LJP ALA A 889 UNP Q96EP0 HIS 889 ENGINEERED MUTATION
SEQRES 1 A 223 GLY PRO GLY PRO GLU TYR GLN ALA GLN GLY LEU ALA MET
SEQRES 2 A 223 TYR LEU GLN GLU ASN GLY ILE ASP CYS PRO LYS CYS LYS
SEQRES 3 A 223 PHE SER TYR ALA LEU ALA ARG GLY GLY CYS MET HIS PHE
SEQRES 4 A 223 ALA CYS THR GLN CYS ARG HIS GLN PHE CYS SER GLY CYS
SEQRES 5 A 223 TYR ASN ALA PHE TYR ALA LYS ASN LYS CYS PRO GLU PRO
SEQRES 6 A 223 ASN CYS ARG VAL LYS LYS SER LEU HIS GLY HIS HIS PRO
SEQRES 7 A 223 ARG ASP CYS LEU PHE TYR LEU ARG ASP TRP THR ALA LEU
SEQRES 8 A 223 ARG LEU GLN LYS LEU LEU GLN ASP ASN ASN VAL MET PHE
SEQRES 9 A 223 ASN THR GLU PRO PRO ALA GLY ALA ARG ALA VAL PRO GLY
SEQRES 10 A 223 GLY GLY CYS ARG VAL ILE GLU GLN LYS GLU VAL PRO ASN
SEQRES 11 A 223 GLY LEU ARG ASP GLU ALA CYS GLY LYS GLU THR PRO ALA
SEQRES 12 A 223 GLY TYR ALA GLY LEU CYS GLN ALA HIS TYR LYS GLU TYR
SEQRES 13 A 223 LEU VAL SER LEU ILE ASN ALA HIS SER LEU ASP PRO ALA
SEQRES 14 A 223 THR LEU TYR GLU VAL GLU GLU LEU GLU THR ALA THR GLU
SEQRES 15 A 223 ARG TYR LEU HIS VAL ARG PRO GLN PRO LEU ALA GLY GLU
SEQRES 16 A 223 ASP PRO PRO ALA TYR GLN ALA ARG LEU LEU GLN LYS LEU
SEQRES 17 A 223 THR GLU GLU VAL PRO LEU GLY GLN SER ILE PRO ARG ARG
SEQRES 18 A 223 ARG LYS
SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HET ZN A1101 1
HET ZN A1102 1
HET ZN A1103 1
HET ZN A1104 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 HOH *120(H2 O)
HELIX 1 1 ALA A 857 GLN A 865 1 9
HELIX 2 2 CYS A 930 ARG A 935 1 6
HELIX 3 3 THR A 938 ASN A 949 1 12
HELIX 4 4 CYS A 998 HIS A 1013 1 16
HELIX 5 5 ASP A 1016 TYR A 1021 5 6
HELIX 6 6 GLU A 1022 HIS A 1035 1 14
HELIX 7 7 ASP A 1045 VAL A 1061 1 17
HELIX 8 8 THR B 22 GLY B 35 1 14
HELIX 9 9 PRO B 37 ASP B 39 5 3
HELIX 10 10 LEU B 56 ASN B 60 5 5
SHEET 1 A 2 GLY A 868 ASP A 870 0
SHEET 2 A 2 SER A 877 ALA A 879 -1 O TYR A 878 N ILE A 869
SHEET 1 B 2 HIS A 887 ALA A 889 0
SHEET 2 B 2 GLN A 896 CYS A 898 -1 O PHE A 897 N PHE A 888
SHEET 1 C 2 ILE A 972 VAL A 977 0
SHEET 2 C 2 GLY A 980 ALA A 985 -1 O GLU A 984 N GLU A 973
SHEET 1 D 5 THR B 12 GLU B 16 0
SHEET 2 D 5 GLN B 2 LYS B 6 -1 N ILE B 3 O LEU B 15
SHEET 3 D 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4
SHEET 4 D 5 GLN B 41 PHE B 45 -1 N ILE B 44 O HIS B 68
SHEET 5 D 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
LINK SG CYS A 871 ZN ZN A1101 1555 1555 2.49
LINK SG CYS A 874 ZN ZN A1101 1555 1555 2.50
LINK SG CYS A 890 ZN ZN A1101 1555 1555 2.28
LINK SG CYS A 893 ZN ZN A1101 1555 1555 2.30
LINK SG CYS A 898 ZN ZN A1102 1555 1555 2.43
LINK SG CYS A 901 ZN ZN A1102 1555 1555 2.25
LINK SG CYS A 911 ZN ZN A1103 1555 1555 2.32
LINK SG CYS A 916 ZN ZN A1103 1555 1555 2.22
LINK NE2 HIS A 923 ZN ZN A1103 1555 1555 2.14
LINK NE2 HIS A 925 ZN ZN A1103 1555 1555 2.12
LINK ND1 HIS A 926 ZN ZN A1102 1555 1555 2.09
LINK SG CYS A 930 ZN ZN A1102 1555 1555 2.42
LINK SG CYS A 969 ZN ZN A1104 1555 1555 2.38
LINK SG CYS A 986 ZN ZN A1104 1555 1555 2.25
LINK SG CYS A 998 ZN ZN A1104 1555 1555 2.41
LINK ND1 HIS A1001 ZN ZN A1104 1555 1555 2.14
SITE 1 AC1 4 CYS A 871 CYS A 874 CYS A 890 CYS A 893
SITE 1 AC2 4 CYS A 898 CYS A 901 HIS A 926 CYS A 930
SITE 1 AC3 4 CYS A 911 CYS A 916 HIS A 923 HIS A 925
SITE 1 AC4 4 CYS A 969 CYS A 986 CYS A 998 HIS A1001
CRYST1 46.000 46.000 133.370 90.00 90.00 120.00 P 31 3
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 0.021739 0.012551 0.000000 0.00000
SCALE2 0.000000 0.025102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007498 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
