HEADER LIGASE 26-NOV-13 4NR3
TITLE CRYSTAL STRUCTURE OF A HUMAN MMS2/UBC13 L121G 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 3 22-NOV-17 4NR3 1 REMARK
REVDAT 2 31-DEC-14 4NR3 1 JRNL
REVDAT 1 10-DEC-14 4NR3 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. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 27783
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.260
REMARK 3 FREE R VALUE TEST SET COUNT : 1461
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 22.1322 - 3.8761 1.00 2918 143 0.1487 0.1602
REMARK 3 2 3.8761 - 3.0792 0.99 2749 143 0.1770 0.2251
REMARK 3 3 3.0792 - 2.6908 0.98 2679 157 0.2078 0.2839
REMARK 3 4 2.6908 - 2.4451 0.98 2663 157 0.1955 0.2472
REMARK 3 5 2.4451 - 2.2700 0.96 2622 146 0.1953 0.2646
REMARK 3 6 2.2700 - 2.1363 0.96 2559 166 0.2036 0.2519
REMARK 3 7 2.1363 - 2.0294 0.96 2596 127 0.2213 0.2689
REMARK 3 8 2.0294 - 1.9411 0.95 2551 145 0.2203 0.3007
REMARK 3 9 1.9411 - 1.8664 0.94 2529 126 0.2463 0.3102
REMARK 3 10 1.8664 - 1.8020 0.92 2456 151 0.2439 0.2837
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.43
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 2431
REMARK 3 ANGLE : 1.127 3314
REMARK 3 CHIRALITY : 0.078 354
REMARK 3 PLANARITY : 0.005 442
REMARK 3 DIHEDRAL : 13.292 946
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8079 14.2434 18.9643
REMARK 3 T TENSOR
REMARK 3 T11: 0.1772 T22: 0.1619
REMARK 3 T33: 0.1639 T12: 0.0049
REMARK 3 T13: -0.0338 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 1.6824 L22: 1.5824
REMARK 3 L33: 7.1941 L12: -0.3993
REMARK 3 L13: 0.2624 L23: 1.2002
REMARK 3 S TENSOR
REMARK 3 S11: -0.1442 S12: -0.1370 S13: -0.1817
REMARK 3 S21: 0.4471 S22: -0.0501 S23: -0.0674
REMARK 3 S31: 0.5202 S32: 0.2891 S33: 0.1816
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6799 20.1809 11.1480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.1001
REMARK 3 T33: 0.1264 T12: 0.0013
REMARK 3 T13: -0.0044 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.4383 L22: 1.8476
REMARK 3 L33: 3.9139 L12: -0.2022
REMARK 3 L13: 0.7254 L23: 0.1143
REMARK 3 S TENSOR
REMARK 3 S11: -0.1595 S12: 0.0296 S13: 0.1156
REMARK 3 S21: 0.2091 S22: 0.0620 S23: -0.1050
REMARK 3 S31: -0.1086 S32: 0.3005 S33: 0.0550
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9975 23.4429 5.0652
REMARK 3 T TENSOR
REMARK 3 T11: 0.0716 T22: 0.0595
REMARK 3 T33: 0.1056 T12: 0.0099
REMARK 3 T13: 0.0018 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 5.9166 L22: 3.0702
REMARK 3 L33: 7.8429 L12: 0.1732
REMARK 3 L13: -0.9604 L23: -3.5516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: -0.0303 S13: 0.4366
REMARK 3 S21: 0.1843 S22: -0.0833 S23: 0.0390
REMARK 3 S31: -0.3650 S32: 0.2559 S33: 0.1093
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0579 19.7973 9.5467
REMARK 3 T TENSOR
REMARK 3 T11: 0.0932 T22: 0.1963
REMARK 3 T33: 0.1831 T12: 0.0461
REMARK 3 T13: 0.0034 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 2.3737 L22: 5.0528
REMARK 3 L33: 7.0268 L12: 2.0026
REMARK 3 L13: -0.4663 L23: -2.6072
REMARK 3 S TENSOR
REMARK 3 S11: -0.1807 S12: -0.1991 S13: 0.3308
REMARK 3 S21: 0.2156 S22: 0.1755 S23: 0.6105
REMARK 3 S31: -0.2546 S32: -0.3800 S33: 0.0111
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9808 10.8095 13.2977
REMARK 3 T TENSOR
REMARK 3 T11: 0.1115 T22: 0.1100
REMARK 3 T33: 0.1592 T12: 0.0046
REMARK 3 T13: 0.0221 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 3.1912 L22: 2.8130
REMARK 3 L33: 3.0147 L12: 1.0208
REMARK 3 L13: 3.0316 L23: 0.5084
REMARK 3 S TENSOR
REMARK 3 S11: 0.1444 S12: -0.0341 S13: -0.2214
REMARK 3 S21: 0.3007 S22: 0.0680 S23: 0.0631
REMARK 3 S31: 0.2314 S32: -0.0406 S33: -0.1997
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8159 19.5816 -1.9912
REMARK 3 T TENSOR
REMARK 3 T11: 0.0671 T22: 0.1960
REMARK 3 T33: 0.1143 T12: 0.0377
REMARK 3 T13: -0.0263 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 7.4353 L22: 7.2398
REMARK 3 L33: 7.7861 L12: 1.3988
REMARK 3 L13: -0.1196 L23: -0.3977
REMARK 3 S TENSOR
REMARK 3 S11: -0.2655 S12: 0.2483 S13: 0.2094
REMARK 3 S21: -0.3086 S22: 0.2831 S23: 0.1519
REMARK 3 S31: -0.2606 S32: 0.2068 S33: 0.0324
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1668 11.3606 47.8444
REMARK 3 T TENSOR
REMARK 3 T11: 0.5140 T22: 0.4787
REMARK 3 T33: 0.4729 T12: 0.0660
REMARK 3 T13: 0.0246 T23: 0.1801
REMARK 3 L TENSOR
REMARK 3 L11: 3.9503 L22: 9.4262
REMARK 3 L33: 3.4613 L12: 5.1949
REMARK 3 L13: -3.2103 L23: -2.8213
REMARK 3 S TENSOR
REMARK 3 S11: 0.1387 S12: -0.2354 S13: 0.6607
REMARK 3 S21: 0.3833 S22: -0.4947 S23: -0.3127
REMARK 3 S31: -0.1992 S32: 1.0768 S33: 0.3851
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5027 22.0761 44.2117
REMARK 3 T TENSOR
REMARK 3 T11: 0.6361 T22: 0.3676
REMARK 3 T33: 0.3286 T12: -0.1315
REMARK 3 T13: -0.0015 T23: 0.0790
REMARK 3 L TENSOR
REMARK 3 L11: 2.4345 L22: 3.7561
REMARK 3 L33: 1.2335 L12: 3.0240
REMARK 3 L13: 1.7328 L23: 2.1522
REMARK 3 S TENSOR
REMARK 3 S11: 0.2969 S12: -0.3943 S13: 0.1653
REMARK 3 S21: 1.1243 S22: -0.3485 S23: 0.3309
REMARK 3 S31: -0.0656 S32: 0.0026 S33: 0.0389
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8607 28.6685 37.1523
REMARK 3 T TENSOR
REMARK 3 T11: 0.3071 T22: 0.1804
REMARK 3 T33: 0.1493 T12: 0.0296
REMARK 3 T13: -0.0701 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 5.6340 L22: 8.9560
REMARK 3 L33: 1.5829 L12: 5.8640
REMARK 3 L13: -1.4060 L23: 0.1044
REMARK 3 S TENSOR
REMARK 3 S11: 0.3593 S12: -0.2226 S13: -0.0481
REMARK 3 S21: 0.6399 S22: -0.1080 S23: -0.2301
REMARK 3 S31: 0.1235 S32: -0.0194 S33: -0.2475
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 58 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3598 17.9973 32.5187
REMARK 3 T TENSOR
REMARK 3 T11: 0.4147 T22: 0.2108
REMARK 3 T33: 0.2258 T12: 0.0541
REMARK 3 T13: 0.0006 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 3.4985 L22: 5.2202
REMARK 3 L33: 1.9397 L12: 0.6499
REMARK 3 L13: -0.9536 L23: -1.8628
REMARK 3 S TENSOR
REMARK 3 S11: -0.3524 S12: -0.1763 S13: -0.5747
REMARK 3 S21: -0.5250 S22: 0.3170 S23: 0.2412
REMARK 3 S31: 0.8333 S32: 0.0412 S33: -0.0116
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4160 18.9340 33.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.3195 T22: 0.3153
REMARK 3 T33: 0.3526 T12: 0.1136
REMARK 3 T13: -0.0472 T23: 0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 3.2890 L22: 5.4490
REMARK 3 L33: 4.0270 L12: 0.4258
REMARK 3 L13: -0.0010 L23: -2.1271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0704 S12: -0.5549 S13: -0.8328
REMARK 3 S21: 0.3397 S22: -0.0203 S23: -0.4323
REMARK 3 S31: 0.4479 S32: 0.3133 S33: 0.0627
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0325 27.4697 22.9244
REMARK 3 T TENSOR
REMARK 3 T11: 0.2765 T22: 0.4230
REMARK 3 T33: 0.6477 T12: 0.0566
REMARK 3 T13: 0.0263 T23: -0.1039
REMARK 3 L TENSOR
REMARK 3 L11: 3.8715 L22: 7.8753
REMARK 3 L33: 7.4325 L12: 2.0017
REMARK 3 L13: -0.1529 L23: 1.3216
REMARK 3 S TENSOR
REMARK 3 S11: 0.2113 S12: 0.5803 S13: -0.8397
REMARK 3 S21: -0.6617 S22: -0.0506 S23: -0.7835
REMARK 3 S31: 0.5276 S32: 0.1154 S33: -0.1809
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2026 39.1395 28.3549
REMARK 3 T TENSOR
REMARK 3 T11: 0.2229 T22: 0.1434
REMARK 3 T33: 0.2045 T12: 0.0029
REMARK 3 T13: 0.0134 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 3.1838 L22: 3.5894
REMARK 3 L33: 8.9244 L12: -3.2982
REMARK 3 L13: -2.8262 L23: 2.1217
REMARK 3 S TENSOR
REMARK 3 S11: 0.2147 S12: -0.2662 S13: 0.2283
REMARK 3 S21: -0.0132 S22: 0.2075 S23: -0.3854
REMARK 3 S31: -0.2707 S32: 0.2319 S33: -0.4139
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 4NR3 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 DEPOSITION ID IS D_1000083550.
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27834
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.58800
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 (%): 47.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
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 22.13050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.88050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.38100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.88050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.13050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.38100
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: 15230 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 -2
REMARK 465 PRO A -1
REMARK 465 LEU A 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 GLU A 4
REMARK 465 PHE A 5
REMARK 465 GLY B -6
REMARK 465 PRO B -5
REMARK 465 LEU B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 PRO B -1
REMARK 465 GLU B 0
REMARK 465 PHE B 1
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 -91.74 -140.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NRI RELATED DB: PDB
REMARK 900 RELATED ID: 4NRG RELATED DB: PDB
DBREF 4NR3 A 6 145 UNP Q15819 UB2V2_HUMAN 6 145
DBREF 4NR3 B 2 150 UNP P61088 UBE2N_HUMAN 2 150
SEQADV 4NR3 GLY A -2 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 PRO A -1 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 LEU A 0 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 GLY A 1 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 SER A 2 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 PRO A 3 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 GLU A 4 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 PHE A 5 UNP Q15819 CLONING ARTIFACT
SEQADV 4NR3 GLY B -6 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 PRO B -5 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 LEU B -4 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 GLY B -3 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 SER B -2 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 PRO B -1 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 GLU B 0 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 PHE B 1 UNP P61088 CLONING ARTIFACT
SEQADV 4NR3 GLY B 121 UNP P61088 LEU 121 ENGINEERED MUTATION
SEQRES 1 A 148 GLY PRO LEU GLY SER PRO GLU PHE GLY VAL LYS VAL PRO
SEQRES 2 A 148 ARG ASN PHE ARG LEU LEU GLU GLU LEU GLU GLU GLY GLN
SEQRES 3 A 148 LYS GLY VAL GLY ASP GLY THR VAL SER TRP GLY LEU GLU
SEQRES 4 A 148 ASP ASP GLU ASP MET THR LEU THR ARG TRP THR GLY MET
SEQRES 5 A 148 ILE ILE GLY PRO PRO ARG THR ASN TYR GLU ASN ARG ILE
SEQRES 6 A 148 TYR SER LEU LYS VAL GLU CYS GLY PRO LYS TYR PRO GLU
SEQRES 7 A 148 ALA PRO PRO SER VAL ARG PHE VAL THR LYS ILE ASN MET
SEQRES 8 A 148 ASN GLY ILE ASN ASN SER SER GLY MET VAL ASP ALA ARG
SEQRES 9 A 148 SER ILE PRO VAL LEU ALA LYS TRP GLN ASN SER TYR SER
SEQRES 10 A 148 ILE LYS VAL VAL LEU GLN GLU LEU ARG ARG LEU MET MET
SEQRES 11 A 148 SER LYS GLU ASN MET LYS LEU PRO GLN PRO PRO GLU GLY
SEQRES 12 A 148 GLN THR TYR ASN ASN
SEQRES 1 B 157 GLY PRO LEU GLY SER PRO GLU PHE ALA GLY LEU PRO ARG
SEQRES 2 B 157 ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU PRO
SEQRES 3 B 157 VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN ALA
SEQRES 4 B 157 ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP SER
SEQRES 5 B 157 PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE LEU
SEQRES 6 B 157 PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG PHE
SEQRES 7 B 157 MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU GLY
SEQRES 8 B 157 ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER PRO
SEQRES 9 B 157 ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN ALA
SEQRES 10 B 157 LEU LEU SER ALA PRO ASN PRO ASP ASP PRO GLY ALA ASN
SEQRES 11 B 157 ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN ALA
SEQRES 12 B 157 ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA MET
SEQRES 13 B 157 ASN
FORMUL 3 HOH *161(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 VAL A 67 N TRP A 46
SHEET 4 A 4 SER A 79 PHE A 82 -1 O ARG A 81 N LYS A 66
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 -0.12
CISPEP 2 TYR B 62 PRO B 63 0 8.70
CRYST1 44.261 74.762 91.761 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 0.022593 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
