HEADER TRANSFERASE/PROTEIN BINDING 29-MAY-17 5VZW
TITLE TRIM23 RING DOMAIN IN COMPLEX WITH UBCH5-UB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME D2, E2
COMPND 5 UBIQUITIN-CONJUGATING ENZYME D2, UBIQUITIN CARRIER PROTEIN D2,
COMPND 6 UBIQUITIN-CONJUGATING ENZYME E2(17)KB 2, UBIQUITIN-CONJUGATING ENZYME
COMPND 7 E2-17 KDA 2, UBIQUITIN-PROTEIN LIGASE D2, P53-REGULATED UBIQUITIN-
COMPND 8 CONJUGATING ENZYME 1;
COMPND 9 EC: 2.3.2.23, 2.3.2.24;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: UBIQUITIN;
COMPND 14 CHAIN: C, D;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE TRIM23;
COMPND 18 CHAIN: F, G;
COMPND 19 FRAGMENT: RING DOMAIN (UNP RESIDUES 1-123);
COMPND 20 SYNONYM: ADP-RIBOSYLATION FACTOR DOMAIN-CONTAINING PROTEIN 1, GTP-
COMPND 21 BINDING PROTEIN ARD-1, RING FINGER PROTEIN 46, RING-TYPE E3 UBIQUITIN
COMPND 22 TRANSFERASE TRIM23, TRIPARTITE MOTIF-CONTAINING PROTEIN 23;
COMPND 23 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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: TRIM23, ARD1, ARFD1, RNF46;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS RING DOMAIN, E3 LIGASE, TRANSFERASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PORNILLOS,D.DAWIDZIAK
REVDAT 4 04-OCT-23 5VZW 1 REMARK
REVDAT 3 01-JAN-20 5VZW 1 REMARK
REVDAT 2 20-SEP-17 5VZW 1 JRNL
REVDAT 1 09-AUG-17 5VZW 0
JRNL AUTH D.M.DAWIDZIAK,J.G.SANCHEZ,J.M.WAGNER,B.K.GANSER-PORNILLOS,
JRNL AUTH 2 O.PORNILLOS
JRNL TITL STRUCTURE AND CATALYTIC ACTIVATION OF THE TRIM23 RING E3
JRNL TITL 2 UBIQUITIN LIGASE.
JRNL REF PROTEINS V. 85 1957 2017
JRNL REFN ESSN 1097-0134
JRNL PMID 28681414
JRNL DOI 10.1002/PROT.25348
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 33021
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 47.5800 - 5.4880 1.00 2411 155 0.1850 0.1952
REMARK 3 2 5.4880 - 4.3569 1.00 2288 148 0.1610 0.1846
REMARK 3 3 4.3569 - 3.8064 1.00 2255 145 0.1780 0.1945
REMARK 3 4 3.8064 - 3.4585 1.00 2253 145 0.2235 0.2930
REMARK 3 5 3.4585 - 3.2107 1.00 2245 146 0.2397 0.2617
REMARK 3 6 3.2107 - 3.0214 1.00 2241 144 0.2554 0.2946
REMARK 3 7 3.0214 - 2.8701 1.00 2211 142 0.2481 0.2838
REMARK 3 8 2.8701 - 2.7452 1.00 2209 143 0.2511 0.3255
REMARK 3 9 2.7452 - 2.6395 1.00 2196 141 0.2606 0.3059
REMARK 3 10 2.6395 - 2.5485 1.00 2241 144 0.2626 0.2966
REMARK 3 11 2.5485 - 2.4688 1.00 2188 142 0.2754 0.3040
REMARK 3 12 2.4688 - 2.3982 1.00 2203 142 0.2744 0.3838
REMARK 3 13 2.3982 - 2.3351 1.00 2207 143 0.2811 0.3176
REMARK 3 14 2.3351 - 2.2781 0.85 1873 120 0.2834 0.2976
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.80
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 : 0.003 4788
REMARK 3 ANGLE : 0.595 6511
REMARK 3 CHIRALITY : 0.043 743
REMARK 3 PLANARITY : 0.004 847
REMARK 3 DIHEDRAL : 13.950 2901
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5VZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228211.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.278
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.20000
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: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 5EYA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 5.5, 0.2 M CALCIUM
REMARK 280 CHLORIDE, 17% W/V PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
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 26.41500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.48150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.67750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.48150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.41500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.67750
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F, G, B, D
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 MET A 1
REMARK 465 GLY C -2
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 THR F 3
REMARK 465 LEU F 4
REMARK 465 VAL F 5
REMARK 465 VAL F 6
REMARK 465 ASN F 7
REMARK 465 LYS F 8
REMARK 465 LEU F 9
REMARK 465 GLY F 10
REMARK 465 ALA F 11
REMARK 465 GLY F 12
REMARK 465 VAL F 13
REMARK 465 ASP F 14
REMARK 465 SER F 15
REMARK 465 GLY F 16
REMARK 465 ARG F 17
REMARK 465 GLN F 18
REMARK 465 GLY F 19
REMARK 465 SER F 20
REMARK 465 ARG F 21
REMARK 465 GLY F 22
REMARK 465 THR F 23
REMARK 465 ALA F 24
REMARK 465 VAL F 25
REMARK 465 VAL F 26
REMARK 465 LYS F 27
REMARK 465 GLY F 105
REMARK 465 PRO F 106
REMARK 465 ILE F 107
REMARK 465 GLY F 108
REMARK 465 GLN F 109
REMARK 465 TYR F 110
REMARK 465 GLY F 111
REMARK 465 ALA F 112
REMARK 465 ALA F 113
REMARK 465 GLU F 114
REMARK 465 GLU F 115
REMARK 465 SER F 116
REMARK 465 ILE F 117
REMARK 465 GLY F 118
REMARK 465 ILE F 119
REMARK 465 SER F 120
REMARK 465 GLY F 121
REMARK 465 GLU F 122
REMARK 465 SER F 123
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 THR G 3
REMARK 465 LEU G 4
REMARK 465 VAL G 5
REMARK 465 VAL G 6
REMARK 465 ASN G 7
REMARK 465 LYS G 8
REMARK 465 LEU G 9
REMARK 465 GLY G 10
REMARK 465 ALA G 11
REMARK 465 GLY G 12
REMARK 465 VAL G 13
REMARK 465 ASP G 14
REMARK 465 SER G 15
REMARK 465 GLY G 16
REMARK 465 ARG G 17
REMARK 465 GLN G 18
REMARK 465 GLY G 19
REMARK 465 SER G 20
REMARK 465 ARG G 21
REMARK 465 GLY G 22
REMARK 465 THR G 23
REMARK 465 ALA G 24
REMARK 465 VAL G 25
REMARK 465 VAL G 26
REMARK 465 LYS G 27
REMARK 465 GLY G 105
REMARK 465 PRO G 106
REMARK 465 ILE G 107
REMARK 465 GLY G 108
REMARK 465 GLN G 109
REMARK 465 TYR G 110
REMARK 465 GLY G 111
REMARK 465 ALA G 112
REMARK 465 ALA G 113
REMARK 465 GLU G 114
REMARK 465 GLU G 115
REMARK 465 SER G 116
REMARK 465 ILE G 117
REMARK 465 GLY G 118
REMARK 465 ILE G 119
REMARK 465 SER G 120
REMARK 465 GLY G 121
REMARK 465 GLU G 122
REMARK 465 SER G 123
REMARK 465 MET B 1
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ASN F 104 CG OD1 ND2
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 ASP B 28 CG OD1 OD2
REMARK 470 LYS B 66 CG CD CE NZ
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 ARG B 125 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 128 CG CD CE NZ
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 144 CG CD CE NZ
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 24 CG CD OE1 OE2
REMARK 470 ASP D 32 CG OD1 OD2
REMARK 470 ARG D 54 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 60 CG OD1 ND2
REMARK 470 GLN D 62 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C GLY C 76 NZ LYS B 85 1.32
REMARK 500 NZ LYS A 85 C GLY D 76 1.32
REMARK 500 HH21 ARG F 68 O GLY F 82 1.57
REMARK 500
REMARK 500 REMARK: NULL
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 79.50 -150.40
REMARK 500 ARG A 90 -106.61 -121.12
REMARK 500 VAL F 33 -69.31 -104.75
REMARK 500 ASP F 75 -0.41 -141.27
REMARK 500 VAL G 33 -69.36 -105.37
REMARK 500 ASP G 75 -0.16 -141.42
REMARK 500 ARG B 90 -105.03 -117.43
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 F 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 31 SG
REMARK 620 2 CYS F 34 SG 107.9
REMARK 620 3 CYS F 56 SG 116.9 113.5
REMARK 620 4 CYS F 59 SG 117.8 102.2 97.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 51 SG
REMARK 620 2 HIS F 53 ND1 113.7
REMARK 620 3 CYS F 72 SG 109.9 113.7
REMARK 620 4 ASP F 75 OD2 117.7 87.4 113.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 31 SG
REMARK 620 2 CYS G 34 SG 108.2
REMARK 620 3 CYS G 56 SG 119.6 112.6
REMARK 620 4 CYS G 59 SG 117.3 99.5 97.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 51 SG
REMARK 620 2 HIS G 53 ND1 111.3
REMARK 620 3 CYS G 72 SG 109.7 112.1
REMARK 620 4 ASP G 75 OD2 122.8 86.0 112.7
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 F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 302
DBREF 5VZW A 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 5VZW C 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5VZW F 1 123 UNP P36406 TRI23_HUMAN 1 123
DBREF 5VZW G 1 123 UNP P36406 TRI23_HUMAN 1 123
DBREF 5VZW B 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 5VZW D 1 76 UNP P0CG47 UBB_HUMAN 1 76
SEQADV 5VZW ARG A 22 UNP P62837 SER 22 ENGINEERED MUTATION
SEQADV 5VZW LYS A 85 UNP P62837 CYS 85 ENGINEERED MUTATION
SEQADV 5VZW GLY C -2 UNP P0CG47 EXPRESSION TAG
SEQADV 5VZW SER C -1 UNP P0CG47 EXPRESSION TAG
SEQADV 5VZW HIS C 0 UNP P0CG47 EXPRESSION TAG
SEQADV 5VZW ARG B 22 UNP P62837 SER 22 ENGINEERED MUTATION
SEQADV 5VZW LYS B 85 UNP P62837 CYS 85 ENGINEERED MUTATION
SEQADV 5VZW GLY D -2 UNP P0CG47 EXPRESSION TAG
SEQADV 5VZW SER D -1 UNP P0CG47 EXPRESSION TAG
SEQADV 5VZW HIS D 0 UNP P0CG47 EXPRESSION TAG
SEQRES 1 A 147 MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN ASP LEU
SEQRES 2 A 147 ALA ARG ASP PRO PRO ALA GLN CYS ARG ALA GLY PRO VAL
SEQRES 3 A 147 GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE MET GLY
SEQRES 4 A 147 PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE PHE LEU
SEQRES 5 A 147 THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS PRO PRO
SEQRES 6 A 147 LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO ASN ILE
SEQRES 7 A 147 ASN SER ASN GLY SER ILE LYS LEU ASP ILE LEU ARG SER
SEQRES 8 A 147 GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL LEU LEU
SEQRES 9 A 147 SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO ASP ASP
SEQRES 10 A 147 PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS THR ASP
SEQRES 11 A 147 ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP THR GLN
SEQRES 12 A 147 LYS TYR ALA MET
SEQRES 1 C 79 GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY
SEQRES 2 C 79 LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE
SEQRES 3 C 79 GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE
SEQRES 4 C 79 PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN
SEQRES 5 C 79 LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN
SEQRES 6 C 79 LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 7 C 79 GLY
SEQRES 1 F 123 MET ALA THR LEU VAL VAL ASN LYS LEU GLY ALA GLY VAL
SEQRES 2 F 123 ASP SER GLY ARG GLN GLY SER ARG GLY THR ALA VAL VAL
SEQRES 3 F 123 LYS VAL LEU GLU CYS GLY VAL CYS GLU ASP VAL PHE SER
SEQRES 4 F 123 LEU GLN GLY ASP LYS VAL PRO ARG LEU LEU LEU CYS GLY
SEQRES 5 F 123 HIS THR VAL CYS HIS ASP CYS LEU THR ARG LEU PRO LEU
SEQRES 6 F 123 HIS GLY ARG ALA ILE ARG CYS PRO PHE ASP ARG GLN VAL
SEQRES 7 F 123 THR ASP LEU GLY ASP SER GLY VAL TRP GLY LEU LYS LYS
SEQRES 8 F 123 ASN PHE ALA LEU LEU GLU LEU LEU GLU ARG LEU GLN ASN
SEQRES 9 F 123 GLY PRO ILE GLY GLN TYR GLY ALA ALA GLU GLU SER ILE
SEQRES 10 F 123 GLY ILE SER GLY GLU SER
SEQRES 1 G 123 MET ALA THR LEU VAL VAL ASN LYS LEU GLY ALA GLY VAL
SEQRES 2 G 123 ASP SER GLY ARG GLN GLY SER ARG GLY THR ALA VAL VAL
SEQRES 3 G 123 LYS VAL LEU GLU CYS GLY VAL CYS GLU ASP VAL PHE SER
SEQRES 4 G 123 LEU GLN GLY ASP LYS VAL PRO ARG LEU LEU LEU CYS GLY
SEQRES 5 G 123 HIS THR VAL CYS HIS ASP CYS LEU THR ARG LEU PRO LEU
SEQRES 6 G 123 HIS GLY ARG ALA ILE ARG CYS PRO PHE ASP ARG GLN VAL
SEQRES 7 G 123 THR ASP LEU GLY ASP SER GLY VAL TRP GLY LEU LYS LYS
SEQRES 8 G 123 ASN PHE ALA LEU LEU GLU LEU LEU GLU ARG LEU GLN ASN
SEQRES 9 G 123 GLY PRO ILE GLY GLN TYR GLY ALA ALA GLU GLU SER ILE
SEQRES 10 G 123 GLY ILE SER GLY GLU SER
SEQRES 1 B 147 MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN ASP LEU
SEQRES 2 B 147 ALA ARG ASP PRO PRO ALA GLN CYS ARG ALA GLY PRO VAL
SEQRES 3 B 147 GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE MET GLY
SEQRES 4 B 147 PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE PHE LEU
SEQRES 5 B 147 THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS PRO PRO
SEQRES 6 B 147 LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO ASN ILE
SEQRES 7 B 147 ASN SER ASN GLY SER ILE LYS LEU ASP ILE LEU ARG SER
SEQRES 8 B 147 GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL LEU LEU
SEQRES 9 B 147 SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO ASP ASP
SEQRES 10 B 147 PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS THR ASP
SEQRES 11 B 147 ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP THR GLN
SEQRES 12 B 147 LYS TYR ALA MET
SEQRES 1 D 79 GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY
SEQRES 2 D 79 LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE
SEQRES 3 D 79 GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE
SEQRES 4 D 79 PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN
SEQRES 5 D 79 LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN
SEQRES 6 D 79 LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 7 D 79 GLY
HET ZN F 301 1
HET ZN F 302 1
HET ZN G 301 1
HET ZN G 302 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 4(ZN 2+)
FORMUL 11 HOH *51(H2 O)
HELIX 1 AA1 ALA A 2 ASP A 16 1 15
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 MET A 147 1 18
HELIX 6 AA6 THR C 22 GLY C 35 1 14
HELIX 7 AA7 PRO C 37 ASP C 39 5 3
HELIX 8 AA8 GLN F 41 LYS F 44 5 4
HELIX 9 AA9 HIS F 57 LEU F 63 1 7
HELIX 10 AB1 SER F 84 LEU F 89 5 6
HELIX 11 AB2 ASN F 92 GLN F 103 1 12
HELIX 12 AB3 GLN G 41 LYS G 44 5 4
HELIX 13 AB4 HIS G 57 ARG G 62 1 6
HELIX 14 AB5 SER G 84 LEU G 89 5 6
HELIX 15 AB6 ASN G 92 ASN G 104 1 13
HELIX 16 AB7 LEU B 3 ASP B 16 1 14
HELIX 17 AB8 LEU B 86 ARG B 90 5 5
HELIX 18 AB9 THR B 98 ASP B 112 1 15
HELIX 19 AC1 VAL B 120 ASP B 130 1 11
HELIX 20 AC2 ASP B 130 MET B 147 1 18
HELIX 21 AC3 THR D 22 GLY D 35 1 14
HELIX 22 AC4 PRO D 37 ASP D 39 5 3
SHEET 1 AA1 4 CYS A 21 PRO A 25 0
SHEET 2 AA1 4 HIS A 32 MET A 38 -1 O GLN A 34 N GLY A 24
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 5 THR C 12 VAL C 17 0
SHEET 2 AA2 5 MET C 1 LYS C 6 -1 N VAL C 5 O ILE C 13
SHEET 3 AA2 5 THR C 66 LEU C 71 1 O LEU C 67 N PHE C 4
SHEET 4 AA2 5 GLN C 41 PHE C 45 -1 N ARG C 42 O VAL C 70
SHEET 5 AA2 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45
SHEET 1 AA3 2 PRO F 46 LEU F 48 0
SHEET 2 AA3 2 THR F 54 CYS F 56 -1 O VAL F 55 N ARG F 47
SHEET 1 AA4 2 ALA F 69 ARG F 71 0
SHEET 2 AA4 2 VAL F 78 ASP F 80 -1 O THR F 79 N ILE F 70
SHEET 1 AA5 2 PRO G 46 LEU G 48 0
SHEET 2 AA5 2 THR G 54 CYS G 56 -1 O VAL G 55 N ARG G 47
SHEET 1 AA6 2 ALA G 69 ARG G 71 0
SHEET 2 AA6 2 VAL G 78 ASP G 80 -1 O THR G 79 N ILE G 70
SHEET 1 AA7 4 CYS B 21 PRO B 25 0
SHEET 2 AA7 4 HIS B 32 MET B 38 -1 O GLN B 34 N GLY B 24
SHEET 3 AA7 4 VAL B 49 HIS B 55 -1 O PHE B 50 N ILE B 37
SHEET 4 AA7 4 LYS B 66 PHE B 69 -1 O LYS B 66 N HIS B 55
SHEET 1 AA8 5 THR D 12 VAL D 17 0
SHEET 2 AA8 5 MET D 1 LYS D 6 -1 N MET D 1 O VAL D 17
SHEET 3 AA8 5 THR D 66 LEU D 71 1 O LEU D 69 N LYS D 6
SHEET 4 AA8 5 GLN D 41 PHE D 45 -1 N ARG D 42 O VAL D 70
SHEET 5 AA8 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
LINK SG CYS F 31 ZN ZN F 302 1555 1555 2.40
LINK SG CYS F 34 ZN ZN F 302 1555 1555 2.42
LINK SG CYS F 51 ZN ZN F 301 1555 1555 2.25
LINK ND1 HIS F 53 ZN ZN F 301 1555 1555 2.09
LINK SG CYS F 56 ZN ZN F 302 1555 1555 2.39
LINK SG CYS F 59 ZN ZN F 302 1555 1555 2.31
LINK SG CYS F 72 ZN ZN F 301 1555 1555 2.28
LINK OD2 ASP F 75 ZN ZN F 301 1555 1555 2.05
LINK SG CYS G 31 ZN ZN G 302 1555 1555 2.27
LINK SG CYS G 34 ZN ZN G 302 1555 1555 2.44
LINK SG CYS G 51 ZN ZN G 301 1555 1555 2.20
LINK ND1 HIS G 53 ZN ZN G 301 1555 1555 2.12
LINK SG CYS G 56 ZN ZN G 302 1555 1555 2.39
LINK SG CYS G 59 ZN ZN G 302 1555 1555 2.24
LINK SG CYS G 72 ZN ZN G 301 1555 1555 2.23
LINK OD2 ASP G 75 ZN ZN G 301 1555 1555 1.94
CISPEP 1 TYR A 60 PRO A 61 0 5.08
CISPEP 2 TYR B 60 PRO B 61 0 5.06
SITE 1 AC1 4 CYS F 51 HIS F 53 CYS F 72 ASP F 75
SITE 1 AC2 4 CYS F 31 CYS F 34 CYS F 56 CYS F 59
SITE 1 AC3 4 CYS G 51 HIS G 53 CYS G 72 ASP G 75
SITE 1 AC4 4 CYS G 31 CYS G 34 CYS G 56 CYS G 59
CRYST1 52.830 109.355 122.963 90.00 90.00 90.00 P 21 21 21 8
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 0.018929 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
