HEADER LIGASE 18-NOV-14 4WZ3
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN LUBX/LEGU2/LPP2887 U-BOX 1
TITLE 2 AND HOMO SAPIENS UBE2D2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UBIQUITIN CARRIER PROTEIN D2,UBIQUITIN-CONJUGATING ENZYME
COMPND 5 E2(17)KB 2,UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2,UBIQUITIN-PROTEIN
COMPND 6 LIGASE D2,P53-REGULATED UBIQUITIN-CONJUGATING ENZYME 1;
COMPND 7 EC: 6.3.2.19;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE LUBX;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: LEGIONELLA U-BOX PROTEIN;
COMPND 14 EC: 6.3.2.-;
COMPND 15 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: UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P15TV-LIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA;
SOURCE 13 ORGANISM_TAXID: 297246;
SOURCE 14 STRAIN: PARIS;
SOURCE 15 GENE: LUBX, LPP2887;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: P15TV-LIC
KEYWDS ALPHA/BETA PROTEIN, EFFECTOR, ACTIVATING ENZYME, STRUCTURAL GENOMICS,
KEYWDS 2 PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,A.T.QUAILE,T.SKARINA,B.NOCEK,R.DI LEO,V.YIM,A.SAVCHENKO,
AUTHOR 2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 7 15-NOV-23 4WZ3 1 REMARK
REVDAT 6 27-SEP-23 4WZ3 1 REMARK
REVDAT 5 04-DEC-19 4WZ3 1 REMARK
REVDAT 4 20-SEP-17 4WZ3 1 REMARK
REVDAT 3 19-AUG-15 4WZ3 1 JRNL REMARK
REVDAT 2 29-JUL-15 4WZ3 1 JRNL
REVDAT 1 07-JAN-15 4WZ3 0
JRNL AUTH A.T.QUAILE,M.L.URBANUS,P.J.STOGIOS,B.NOCEK,T.SKARINA,
JRNL AUTH 2 A.W.ENSMINGER,A.SAVCHENKO
JRNL TITL MOLECULAR CHARACTERIZATION OF LUBX: FUNCTIONAL DIVERGENCE OF
JRNL TITL 2 THE U-BOX FOLD BY LEGIONELLA PNEUMOPHILA.
JRNL REF STRUCTURE V. 23 1459 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26146184
JRNL DOI 10.1016/J.STR.2015.05.020
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.7
REMARK 3 NUMBER OF REFLECTIONS : 10884
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 968
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 35.8584 - 5.1570 0.95 2805 143 0.1569 0.1782
REMARK 3 2 5.1570 - 4.0952 0.97 2890 141 0.1283 0.1964
REMARK 3 3 4.0952 - 3.5781 0.98 2895 152 0.1467 0.1959
REMARK 3 4 3.5781 - 3.2512 0.98 2912 159 0.1831 0.2300
REMARK 3 5 3.2512 - 3.0183 0.91 2699 158 0.2112 0.2829
REMARK 3 6 3.0183 - 2.8404 0.74 2170 128 0.2306 0.2851
REMARK 3 7 2.8404 - 2.7000 0.53 1563 87 0.2443 0.3660
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2746
REMARK 3 ANGLE : 0.903 3737
REMARK 3 CHIRALITY : 0.044 417
REMARK 3 PLANARITY : 0.007 484
REMARK 3 DIHEDRAL : 13.874 1055
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 0:18
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0447 13.4072 10.1917
REMARK 3 T TENSOR
REMARK 3 T11: 0.3713 T22: 0.4776
REMARK 3 T33: 0.5333 T12: 0.0216
REMARK 3 T13: 0.0903 T23: 0.1134
REMARK 3 L TENSOR
REMARK 3 L11: 3.1130 L22: 3.2676
REMARK 3 L33: 3.0972 L12: 1.6507
REMARK 3 L13: 2.4143 L23: -0.4040
REMARK 3 S TENSOR
REMARK 3 S11: 0.2494 S12: -1.0676 S13: -0.3933
REMARK 3 S21: 0.4166 S22: -0.1271 S23: -0.8479
REMARK 3 S31: -0.5462 S32: -0.1519 S33: -0.0797
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 19:38
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6781 4.1993 11.3687
REMARK 3 T TENSOR
REMARK 3 T11: 0.2786 T22: 0.3968
REMARK 3 T33: 0.4997 T12: -0.0109
REMARK 3 T13: -0.1012 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 8.7445 L22: 8.3195
REMARK 3 L33: 8.2605 L12: 6.0095
REMARK 3 L13: -5.4911 L23: -6.6932
REMARK 3 S TENSOR
REMARK 3 S11: -0.1546 S12: -1.3015 S13: -0.7860
REMARK 3 S21: -0.4905 S22: -0.2480 S23: -1.2897
REMARK 3 S31: 0.6995 S32: 1.4969 S33: 0.2197
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESI 39:116
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8599 9.5298 8.8761
REMARK 3 T TENSOR
REMARK 3 T11: 0.2162 T22: 0.2492
REMARK 3 T33: 0.1197 T12: 0.0425
REMARK 3 T13: -0.0127 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 5.7845 L22: 4.6928
REMARK 3 L33: 2.1108 L12: 2.5585
REMARK 3 L13: -0.8116 L23: -2.4642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0647 S12: -0.0643 S13: 0.0572
REMARK 3 S21: 0.1190 S22: -0.0305 S23: 0.0750
REMARK 3 S31: -0.2893 S32: -0.3685 S33: -0.0364
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESI 117:147
REMARK 3 ORIGIN FOR THE GROUP (A): -68.5512 3.1306 15.2142
REMARK 3 T TENSOR
REMARK 3 T11: 0.2474 T22: 0.4609
REMARK 3 T33: 0.3259 T12: -0.0330
REMARK 3 T13: 0.0403 T23: 0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 6.4539 L22: 7.7887
REMARK 3 L33: 2.8351 L12: -3.2774
REMARK 3 L13: 0.5669 L23: -1.5971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: -0.8599 S13: -0.7663
REMARK 3 S21: 0.7147 S22: 0.2822 S23: 1.1747
REMARK 3 S31: -0.4717 S32: -0.3510 S33: -0.1957
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESI 4:94
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1305 31.9078 5.1980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2390 T22: 0.2234
REMARK 3 T33: 0.2851 T12: -0.0391
REMARK 3 T13: 0.0762 T23: 0.1187
REMARK 3 L TENSOR
REMARK 3 L11: 3.1044 L22: 3.1385
REMARK 3 L33: 4.3426 L12: 0.8909
REMARK 3 L13: 1.5405 L23: 0.5635
REMARK 3 S TENSOR
REMARK 3 S11: -0.1789 S12: 0.1493 S13: 0.3520
REMARK 3 S21: -0.3036 S22: 0.1131 S23: 0.1467
REMARK 3 S31: 0.0174 S32: -0.2409 S33: 0.0141
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESI 95:122
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1653 16.0065 20.9715
REMARK 3 T TENSOR
REMARK 3 T11: 0.2446 T22: 0.2764
REMARK 3 T33: 0.2757 T12: 0.0293
REMARK 3 T13: 0.0914 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 5.6280 L22: 6.9491
REMARK 3 L33: 9.2877 L12: -4.1611
REMARK 3 L13: 6.6930 L23: -7.3053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: -0.1728 S13: 0.1510
REMARK 3 S21: -0.1741 S22: -0.2681 S23: -0.2508
REMARK 3 S31: 0.1977 S32: 0.0273 S33: 0.2123
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND RESI 123:186
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9392 14.7119 33.3483
REMARK 3 T TENSOR
REMARK 3 T11: 0.7866 T22: 0.4795
REMARK 3 T33: 0.5992 T12: 0.0500
REMARK 3 T13: 0.3506 T23: 0.0889
REMARK 3 L TENSOR
REMARK 3 L11: 7.6716 L22: 3.1542
REMARK 3 L33: 1.1748 L12: -4.1121
REMARK 3 L13: -1.1678 L23: 0.9486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: -0.7006 S13: -0.3260
REMARK 3 S21: 1.1661 S22: 0.2846 S23: 0.7242
REMARK 3 S31: -0.8705 S32: -0.2821 S33: -0.2099
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 4WZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789897
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11243
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.66500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4DDI, LUBX U-BOX 1 WT PDB CODE 4WZ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML OF E2D2.(C85S)-UB CONJUGATE
REMARK 280 AND AN EQUIMOLAR CONCENTRATION OF LUBX (1-186), 0.2 M SODIUM
REMARK 280 TARTRATE, 0.1 M TRIS-CL (PH 8.5) AND 25% PEG3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 16.60300
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 33.20600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.90450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.50750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 8.30150
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 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 MSE B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 GLN B 187
REMARK 465 ILE B 188
REMARK 465 LYS B 189
REMARK 465 VAL B 190
REMARK 465 TYR B 191
REMARK 465 ASN B 192
REMARK 465 PHE B 193
REMARK 465 TYR B 194
REMARK 465 ARG B 195
REMARK 465 LYS B 196
REMARK 465 ARG B 197
REMARK 465 GLU B 198
REMARK 465 VAL B 199
REMARK 465 GLN B 200
REMARK 465 LYS B 201
REMARK 465 ASN B 202
REMARK 465 GLN B 203
REMARK 465 ILE B 204
REMARK 465 GLN B 205
REMARK 465 PRO B 206
REMARK 465 SER B 207
REMARK 465 VAL B 208
REMARK 465 SER B 209
REMARK 465 ASN B 210
REMARK 465 GLY B 211
REMARK 465 PHE B 212
REMARK 465 GLY B 213
REMARK 465 PHE B 214
REMARK 465 PHE B 215
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 ASP A 16 73.78 -117.47
REMARK 500 GLN A 20 33.80 -98.39
REMARK 500 SER A 22 117.19 -169.67
REMARK 500 ALA A 23 -166.22 -121.15
REMARK 500 ASP A 28 108.45 -43.70
REMARK 500 ARG A 90 -117.68 -128.78
REMARK 500 ASP A 130 77.44 -161.45
REMARK 500 SER B 41 -2.87 66.15
REMARK 500 LYS B 69 48.74 -98.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WZ0 RELATED DB: PDB
REMARK 900 U-BOX 1
REMARK 900 RELATED ID: MCSG-APC108251 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4WZ1 RELATED DB: PDB
REMARK 900 U-BOX 2 (WILD-TYPE)
REMARK 900 RELATED ID: 4WZ2 RELATED DB: PDB
REMARK 900 U-BOX 2, ILE175MET MUTANT
DBREF 4WZ3 A 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 4WZ3 B 1 215 UNP Q5X159 LUBX_LEGPA 1 215
SEQADV 4WZ3 GLY A 0 UNP P62837 EXPRESSION TAG
SEQADV 4WZ3 SER A 85 UNP P62837 CYS 85 ENGINEERED MUTATION
SEQRES 1 A 148 GLY MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN ASP
SEQRES 2 A 148 LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY PRO
SEQRES 3 A 148 VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE MET
SEQRES 4 A 148 GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE PHE
SEQRES 5 A 148 LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS PRO
SEQRES 6 A 148 PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO ASN
SEQRES 7 A 148 ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU ARG
SEQRES 8 A 148 SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL LEU
SEQRES 9 A 148 LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO ASP
SEQRES 10 A 148 ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS THR
SEQRES 11 A 148 ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP THR
SEQRES 12 A 148 GLN LYS TYR ALA MET
SEQRES 1 B 215 MSE ALA THR ARG ASN PRO PHE ASP ILE ASP HIS LYS SER
SEQRES 2 B 215 LYS TYR LEU ARG GLU ALA ALA LEU GLU ALA ASN LEU SER
SEQRES 3 B 215 HIS PRO GLU THR THR PRO THR MSE LEU THR CYS PRO ILE
SEQRES 4 B 215 ASP SER GLY PHE LEU LYS ASP PRO VAL ILE THR PRO GLU
SEQRES 5 B 215 GLY PHE VAL TYR ASN LYS SER SER ILE LEU LYS TRP LEU
SEQRES 6 B 215 GLU THR LYS LYS GLU ASP PRO GLN SER ARG LYS PRO LEU
SEQRES 7 B 215 THR ALA LYS ASP LEU GLN PRO PHE PRO GLU LEU LEU ILE
SEQRES 8 B 215 ILE VAL ASN ARG PHE VAL GLU THR GLN THR ASN TYR GLU
SEQRES 9 B 215 LYS LEU LYS ASN ARG LEU VAL GLN ASN ALA ARG VAL ALA
SEQRES 10 B 215 ALA ARG GLN LYS GLU TYR THR GLU ILE PRO ASP ILE PHE
SEQRES 11 B 215 LEU CYS PRO ILE SER LYS THR LEU ILE LYS THR PRO VAL
SEQRES 12 B 215 ILE THR ALA GLN GLY LYS VAL TYR ASP GLN GLU ALA LEU
SEQRES 13 B 215 SER ASN PHE LEU ILE ALA THR GLY ASN LYS ASP GLU THR
SEQRES 14 B 215 GLY LYS LYS LEU SER ILE ASP ASP VAL VAL VAL PHE ASP
SEQRES 15 B 215 GLU LEU TYR GLN GLN ILE LYS VAL TYR ASN PHE TYR ARG
SEQRES 16 B 215 LYS ARG GLU VAL GLN LYS ASN GLN ILE GLN PRO SER VAL
SEQRES 17 B 215 SER ASN GLY PHE GLY PHE PHE
MODRES 4WZ3 MSE B 34 MET MODIFIED RESIDUE
HET MSE B 34 8
HETNAM MSE SELENOMETHIONINE
FORMUL 2 MSE C5 H11 N O2 SE
FORMUL 3 HOH *53(H2 O)
HELIX 1 AA1 MET A 1 LEU A 13 1 13
HELIX 2 AA2 LEU A 86 ARG A 90 5 5
HELIX 3 AA3 THR A 98 ASP A 112 1 15
HELIX 4 AA4 VAL A 120 ASP A 130 1 11
HELIX 5 AA5 ASP A 130 ALA A 146 1 17
HELIX 6 AA6 ASP B 10 SER B 26 1 17
HELIX 7 AA7 PRO B 32 THR B 36 5 5
HELIX 8 AA8 LYS B 58 GLU B 66 1 9
HELIX 9 AA9 THR B 79 LEU B 83 5 5
HELIX 10 AB1 LEU B 89 ARG B 119 1 31
HELIX 11 AB2 PRO B 127 LEU B 131 5 5
HELIX 12 AB3 GLN B 153 THR B 163 1 11
HELIX 13 AB4 ASP B 182 TYR B 185 5 4
SHEET 1 AA1 4 CYS A 21 SER A 22 0
SHEET 2 AA1 4 HIS A 32 MET A 38 -1 O THR A 36 N SER A 22
SHEET 3 AA1 4 VAL A 49 HIS A 55 -1 O PHE A 50 N ILE A 37
SHEET 4 AA1 4 LYS A 66 PHE A 69 -1 O LYS A 66 N HIS A 55
SHEET 1 AA2 3 VAL B 55 ASN B 57 0
SHEET 2 AA2 3 PRO B 47 ILE B 49 -1 N VAL B 48 O TYR B 56
SHEET 3 AA2 3 GLN B 84 PRO B 85 -1 O GLN B 84 N ILE B 49
SHEET 1 AA3 3 VAL B 150 ASP B 152 0
SHEET 2 AA3 3 PRO B 142 ILE B 144 -1 N VAL B 143 O TYR B 151
SHEET 3 AA3 3 VAL B 179 VAL B 180 -1 O VAL B 179 N ILE B 144
SHEET 1 AA4 2 LYS B 166 ASP B 167 0
SHEET 2 AA4 2 LYS B 171 LYS B 172 -1 O LYS B 171 N ASP B 167
LINK C THR B 33 N MSE B 34 1555 1555 1.33
LINK C MSE B 34 N LEU B 35 1555 1555 1.33
CISPEP 1 GLY A 0 MET A 1 0 -2.15
CISPEP 2 ASP A 28 ASP A 29 0 21.02
CISPEP 3 TYR A 60 PRO A 61 0 4.08
CISPEP 4 GLU B 168 THR B 169 0 13.49
CRYST1 119.293 119.293 49.809 90.00 90.00 120.00 P 61 6
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 0.008383 0.004840 0.000000 0.00000
SCALE2 0.000000 0.009680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
