HEADER LIGASE 26-NOV-13 4NRG
TITLE CRYSTAL STRUCTURE OF A HUMAN MMS2/UBC13 D118G MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1,
COMPND 5 EDAF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2
COMPND 6 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBCH13,
COMPND 12 UBIQUITIN CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;
COMPND 13 EC: 6.3.2.19;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMS2, UBE2V2, UEV2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS-P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: BLU, UBE2N;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHIS-P1
KEYWDS UBC13, MMS2, E2, UBIQUITIN CONJUGATING ENZYME, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.HODGE,R.A.EDWARDS,J.N.M.GLOVER
REVDAT 2 31-DEC-14 4NRG 1 JRNL
REVDAT 1 10-DEC-14 4NRG 0
JRNL AUTH M.K.ROUT,C.D.HODGE,C.J.MARKIN,X.XU,J.N.GLOVER,W.XIAO,
JRNL AUTH 2 L.SPYRACOPOULOS
JRNL TITL STOCHASTIC GATE DYNAMICS REGULATE THE CATALYTIC ACTIVITY OF
JRNL TITL 2 UBIQUITINATION ENZYMES.
JRNL REF J.AM.CHEM.SOC. V. 136 17446 2014
JRNL REFN ISSN 0002-7863
JRNL PMID 25423605
JRNL DOI 10.1021/JA505440B
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 21572
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 1126
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 22.1374 - 3.8908 0.99 2828 140 0.1542 0.1708
REMARK 3 2 3.8908 - 3.0910 0.98 2655 138 0.1694 0.1917
REMARK 3 3 3.0910 - 2.7010 0.97 2600 149 0.1938 0.2395
REMARK 3 4 2.7010 - 2.4544 0.96 2517 153 0.1985 0.2267
REMARK 3 5 2.4544 - 2.2787 0.95 2552 135 0.1858 0.2453
REMARK 3 6 2.2787 - 2.1445 0.94 2458 165 0.1900 0.2311
REMARK 3 7 2.1445 - 2.0371 0.93 2479 118 0.2099 0.2747
REMARK 3 8 2.0371 - 1.9485 0.89 2357 128 0.2374 0.2905
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.11
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 : 0.005 2394
REMARK 3 ANGLE : 0.860 3256
REMARK 3 CHIRALITY : 0.059 350
REMARK 3 PLANARITY : 0.003 432
REMARK 3 DIHEDRAL : 11.801 936
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 6 through 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8344 13.9803 18.9881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.1497
REMARK 3 T33: 0.1864 T12: -0.0136
REMARK 3 T13: -0.0243 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 3.4792 L22: 2.4590
REMARK 3 L33: 7.7705 L12: -0.9644
REMARK 3 L13: 0.4972 L23: 1.6907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: -0.0370 S13: -0.1723
REMARK 3 S21: 0.3387 S22: -0.1105 S23: -0.1506
REMARK 3 S31: 0.5303 S32: 0.0574 S33: 0.2149
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 36 through 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7650 19.9963 11.1504
REMARK 3 T TENSOR
REMARK 3 T11: 0.1151 T22: 0.1194
REMARK 3 T33: 0.1848 T12: 0.0172
REMARK 3 T13: 0.0025 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 3.0423 L22: 1.3719
REMARK 3 L33: 5.0151 L12: 0.0554
REMARK 3 L13: 1.8975 L23: 0.1390
REMARK 3 S TENSOR
REMARK 3 S11: -0.2306 S12: 0.0040 S13: 0.0802
REMARK 3 S21: 0.1374 S22: 0.0087 S23: -0.0339
REMARK 3 S31: -0.1811 S32: 0.1367 S33: 0.1677
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 79 through 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9811 16.3273 10.3556
REMARK 3 T TENSOR
REMARK 3 T11: 0.0966 T22: 0.1504
REMARK 3 T33: 0.1354 T12: 0.0228
REMARK 3 T13: 0.0208 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 3.6354 L22: 2.6702
REMARK 3 L33: 4.7275 L12: 0.7020
REMARK 3 L13: 1.7854 L23: -1.2423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0706 S12: -0.2848 S13: 0.0142
REMARK 3 S21: 0.1339 S22: 0.1271 S23: 0.1395
REMARK 3 S31: 0.0264 S32: -0.3642 S33: -0.0638
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 128 through 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8742 19.3085 -1.9960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.1836
REMARK 3 T33: 0.1555 T12: 0.0237
REMARK 3 T13: -0.0497 T23: -0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 7.6025 L22: 7.4418
REMARK 3 L33: 8.2037 L12: 0.2343
REMARK 3 L13: -1.0764 L23: -1.1938
REMARK 3 S TENSOR
REMARK 3 S11: -0.3555 S12: 0.2842 S13: 0.3000
REMARK 3 S21: -0.1745 S22: 0.2693 S23: 0.2644
REMARK 3 S31: -0.1486 S32: 0.2542 S33: 0.0843
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'B' and (resid 2 through 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2218 12.0223 48.1338
REMARK 3 T TENSOR
REMARK 3 T11: 0.5095 T22: 0.4180
REMARK 3 T33: 0.4898 T12: 0.0821
REMARK 3 T13: 0.0352 T23: 0.0878
REMARK 3 L TENSOR
REMARK 3 L11: 5.0616 L22: 8.3017
REMARK 3 L33: 9.6406 L12: 2.1621
REMARK 3 L13: 0.4389 L23: 5.2709
REMARK 3 S TENSOR
REMARK 3 S11: 0.3577 S12: -0.0871 S13: 0.5695
REMARK 3 S21: 0.2270 S22: -0.3037 S23: -0.3793
REMARK 3 S31: 0.1890 S32: 0.7698 S33: -0.0193
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resid 18 through 27 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2361 25.0097 46.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.6202 T22: 0.5211
REMARK 3 T33: 0.2838 T12: -0.1044
REMARK 3 T13: -0.0290 T23: 0.0918
REMARK 3 L TENSOR
REMARK 3 L11: 4.3433 L22: 5.1458
REMARK 3 L33: 4.8413 L12: 2.3263
REMARK 3 L13: 4.3550 L23: 3.0163
REMARK 3 S TENSOR
REMARK 3 S11: -0.8436 S12: -1.0462 S13: -0.1704
REMARK 3 S21: 0.5191 S22: 0.5109 S23: 0.1445
REMARK 3 S31: 0.0252 S32: -1.4138 S33: 0.2165
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resid 28 through 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8444 26.0011 37.6355
REMARK 3 T TENSOR
REMARK 3 T11: 0.3193 T22: 0.1568
REMARK 3 T33: 0.1180 T12: 0.0571
REMARK 3 T13: -0.0548 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 9.3955 L22: 9.5831
REMARK 3 L33: 2.4727 L12: 7.1250
REMARK 3 L13: -1.7910 L23: -0.0586
REMARK 3 S TENSOR
REMARK 3 S11: 0.3728 S12: 0.0041 S13: 0.2798
REMARK 3 S21: 0.8183 S22: -0.0329 S23: 0.2267
REMARK 3 S31: 0.1393 S32: 0.0119 S33: -0.3052
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resid 58 through 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3662 17.5121 32.5592
REMARK 3 T TENSOR
REMARK 3 T11: 0.3566 T22: 0.1928
REMARK 3 T33: 0.1915 T12: 0.0631
REMARK 3 T13: 0.0067 T23: -0.0628
REMARK 3 L TENSOR
REMARK 3 L11: 4.6380 L22: 6.7551
REMARK 3 L33: 2.8061 L12: 0.9208
REMARK 3 L13: 0.2033 L23: -2.2469
REMARK 3 S TENSOR
REMARK 3 S11: -0.1254 S12: 0.0841 S13: -0.6279
REMARK 3 S21: -0.0080 S22: 0.1907 S23: 0.2577
REMARK 3 S31: 0.7155 S32: 0.2116 S33: -0.0983
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resid 77 through 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0987 16.6562 30.8206
REMARK 3 T TENSOR
REMARK 3 T11: 0.4313 T22: 0.3842
REMARK 3 T33: 0.3951 T12: 0.2185
REMARK 3 T13: 0.0440 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.8011 L22: 5.1512
REMARK 3 L33: 2.6077 L12: 0.0877
REMARK 3 L13: 1.6268 L23: -2.7312
REMARK 3 S TENSOR
REMARK 3 S11: -0.0780 S12: -0.0969 S13: -0.8935
REMARK 3 S21: -0.3720 S22: 0.0812 S23: -0.1591
REMARK 3 S31: 0.9834 S32: 0.4464 S33: 0.0667
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 101 through 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7531 21.4319 40.2244
REMARK 3 T TENSOR
REMARK 3 T11: 0.3816 T22: 0.4861
REMARK 3 T33: 0.3105 T12: 0.0850
REMARK 3 T13: -0.0956 T23: 0.1181
REMARK 3 L TENSOR
REMARK 3 L11: 4.7821 L22: 3.5936
REMARK 3 L33: 3.8454 L12: 3.9543
REMARK 3 L13: -4.2239 L23: -3.5699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -1.5902 S13: -1.0167
REMARK 3 S21: 0.7972 S22: -0.1694 S23: -0.7342
REMARK 3 S31: -0.5454 S32: 0.1864 S33: 0.1510
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 114 through 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2575 27.4013 22.9479
REMARK 3 T TENSOR
REMARK 3 T11: 0.4816 T22: 1.1196
REMARK 3 T33: 0.6482 T12: -0.0913
REMARK 3 T13: 0.1251 T23: -0.2541
REMARK 3 L TENSOR
REMARK 3 L11: 7.7489 L22: 1.9594
REMARK 3 L33: 5.4871 L12: 1.6871
REMARK 3 L13: 3.7200 L23: 1.3606
REMARK 3 S TENSOR
REMARK 3 S11: -0.1786 S12: 1.8645 S13: -1.4361
REMARK 3 S21: -0.8339 S22: 1.1475 S23: -0.6366
REMARK 3 S31: 0.4346 S32: -0.6829 S33: -0.7680
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 133 through 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2733 38.5369 28.3558
REMARK 3 T TENSOR
REMARK 3 T11: 0.1700 T22: 0.3262
REMARK 3 T33: 0.1721 T12: -0.0542
REMARK 3 T13: 0.0158 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 4.9447 L22: 6.7982
REMARK 3 L33: 4.6541 L12: -3.5808
REMARK 3 L13: 1.6936 L23: -0.6249
REMARK 3 S TENSOR
REMARK 3 S11: -0.1157 S12: 0.5239 S13: 0.4887
REMARK 3 S21: 0.1589 S22: 0.1767 S23: -0.3840
REMARK 3 S31: -0.6658 S32: 0.7433 S33: -0.1292
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 4NRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB083563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
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 : 21609
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
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) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
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
REMARK 200 STARTING MODEL: PDB ENTRY 1J7D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1 M SODIUM CITRATE, PH
REMARK 280 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 22.13600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.04650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.80800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.04650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.13600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.80800
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: 1520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 GLY B -7
REMARK 465 PRO B -6
REMARK 465 LEU B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 PRO B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 LEU B 121
REMARK 465 ALA B 122
REMARK 465 ASN B 151
REMARK 465 ILE B 152
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 LYS B 92 -78.21 -150.27
REMARK 500 ALA B 114 83.78 -150.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NR3 RELATED DB: PDB
REMARK 900 RELATED ID: 4NRI RELATED DB: PDB
DBREF 4NRG A 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 4NRG B 1 152 UNP P61088 UBE2N_HUMAN 1 152
SEQADV 4NRG GLY A -7 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG PRO A -6 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG LEU A -5 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG GLY A -4 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG SER A -3 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG PRO A -2 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG GLU A -1 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG PHE A 0 UNP Q15819 CLONING ARTIFACT
SEQADV 4NRG GLY B -7 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG PRO B -6 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG LEU B -5 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG GLY B -4 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG SER B -3 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG PRO B -2 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG GLU B -1 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG PHE B 0 UNP P61088 CLONING ARTIFACT
SEQADV 4NRG GLY B 118 UNP P61088 ASP 118 ENGINEERED MUTATION
SEQRES 1 A 153 GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR
SEQRES 2 A 153 GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU
SEQRES 3 A 153 LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL
SEQRES 4 A 153 SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR
SEQRES 5 A 153 ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN
SEQRES 6 A 153 TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY
SEQRES 7 A 153 PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL
SEQRES 8 A 153 THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY
SEQRES 9 A 153 MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP
SEQRES 10 A 153 GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU
SEQRES 11 A 153 ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO
SEQRES 12 A 153 GLN PRO PRO GLU GLY GLN THR TYR ASN ASN
SEQRES 1 B 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 B 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 B 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 B 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 B 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 B 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 B 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 B 160 GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 B 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 B 160 ALA LEU LEU SER ALA PRO ASN PRO GLY ASP PRO LEU ALA
SEQRES 11 B 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 B 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 B 160 MET ASN ASN ILE
FORMUL 3 HOH *165(H2 O)
HELIX 1 1 PRO A 10 GLY A 25 1 16
HELIX 2 2 ASP A 99 SER A 102 5 4
HELIX 3 3 ILE A 103 LYS A 108 1 6
HELIX 4 4 SER A 114 MET A 127 1 14
HELIX 5 5 SER A 128 LYS A 133 1 6
HELIX 6 6 PRO B 5 GLU B 18 1 14
HELIX 7 7 LEU B 88 LYS B 92 5 5
HELIX 8 8 GLN B 100 ALA B 114 1 15
HELIX 9 9 ASP B 124 ASN B 132 1 9
HELIX 10 10 ASN B 132 ALA B 148 1 17
SHEET 1 A 4 VAL A 31 LEU A 35 0
SHEET 2 A 4 ARG A 45 ILE A 51 -1 O THR A 47 N GLY A 34
SHEET 3 A 4 ILE A 62 GLU A 68 -1 O TYR A 63 N ILE A 50
SHEET 4 A 4 SER A 79 PHE A 82 -1 O SER A 79 N GLU A 68
SHEET 1 B 4 ILE B 23 PRO B 27 0
SHEET 2 B 4 TYR B 34 ALA B 40 -1 O HIS B 36 N GLU B 26
SHEET 3 B 4 THR B 51 PHE B 57 -1 O LEU B 56 N PHE B 35
SHEET 4 B 4 LYS B 68 PHE B 71 -1 O LYS B 68 N PHE B 57
CISPEP 1 TYR A 73 PRO A 74 0 1.33
CISPEP 2 TYR B 62 PRO B 63 0 8.16
CRYST1 44.272 73.616 92.093 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 0.022588 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013584 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
