HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-DEC-05 2DAH
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL UBA DOMAIN IN THE HUMAN UBIQUILIN
TITLE 2 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUILIN-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBA DOMAIN;
COMPND 5 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: UBQLN3;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050613-28;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS UBIQUILIN-3, UBA DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ZHAO,T.KIGAWA,M.SATO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAH 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DAH 1 VERSN
REVDAT 1 14-JUN-06 2DAH 0
JRNL AUTH C.ZHAO,T.KIGAWA,M.SATO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL UBA DOMAIN IN THE HUMAN
JRNL TITL 2 UBIQUILIN 3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DAH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025184.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.80MM UBA DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL (PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, CYANA 1.0.8
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O ARG A 24 H LEU A 28 1.51
REMARK 500 O ALA A 41 H LEU A 45 1.56
REMARK 500 O LEU A 31 H GLY A 35 1.57
REMARK 500 O ASN A 27 H LEU A 31 1.58
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 1 SER A 3 96.10 57.54
REMARK 500 1 SER A 5 163.31 -48.47
REMARK 500 1 HIS A 8 -76.62 -76.36
REMARK 500 1 PHE A 9 63.66 -106.57
REMARK 500 1 GLN A 10 -74.41 -81.41
REMARK 500 1 ASN A 23 51.22 -141.37
REMARK 500 1 SER A 49 103.05 -53.01
REMARK 500 1 SER A 52 80.98 66.23
REMARK 500 2 SER A 6 -59.34 -135.23
REMARK 500 2 HIS A 8 -168.73 -103.58
REMARK 500 2 PHE A 9 70.75 45.73
REMARK 500 2 GLN A 10 -70.57 -93.39
REMARK 500 2 LEU A 22 48.30 -86.87
REMARK 500 2 SER A 49 98.86 -167.06
REMARK 500 2 SER A 53 82.79 46.92
REMARK 500 3 HIS A 8 -168.73 -116.42
REMARK 500 3 PHE A 9 70.29 45.04
REMARK 500 3 GLN A 10 -72.33 -93.20
REMARK 500 3 LEU A 22 31.45 -92.80
REMARK 500 3 LEU A 28 -70.99 -57.50
REMARK 500 3 SER A 49 -57.41 -171.03
REMARK 500 3 SER A 53 -59.16 72.11
REMARK 500 4 SER A 5 78.66 43.06
REMARK 500 4 SER A 6 -58.81 -161.91
REMARK 500 4 HIS A 8 -173.42 -54.10
REMARK 500 4 GLN A 10 -72.68 -87.18
REMARK 500 4 LEU A 28 -70.84 -52.42
REMARK 500 4 THR A 34 35.56 -91.84
REMARK 500 4 VAL A 38 -60.87 -90.91
REMARK 500 4 SER A 53 -58.80 -165.22
REMARK 500 5 SER A 5 -59.64 -128.09
REMARK 500 5 SER A 6 88.49 45.63
REMARK 500 5 GLN A 10 -72.76 -87.78
REMARK 500 5 LEU A 22 40.94 -93.50
REMARK 500 5 LEU A 28 -70.79 -53.82
REMARK 500 5 SER A 52 -62.91 -101.57
REMARK 500 6 SER A 6 -60.07 -174.42
REMARK 500 6 HIS A 8 -81.93 -143.93
REMARK 500 6 PHE A 9 66.57 -100.98
REMARK 500 6 GLN A 10 -72.70 -84.85
REMARK 500 6 ARG A 17 -39.47 -39.91
REMARK 500 6 ASN A 23 52.67 -145.48
REMARK 500 6 SER A 49 -58.83 -168.70
REMARK 500 6 SER A 52 154.85 -47.65
REMARK 500 7 SER A 6 115.08 60.22
REMARK 500 7 HIS A 8 -79.89 -58.92
REMARK 500 7 PHE A 9 65.37 -100.13
REMARK 500 7 GLN A 10 -72.48 -84.91
REMARK 500 7 ASN A 23 57.04 -141.95
REMARK 500 7 LEU A 28 -70.62 -58.80
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSG002000983.1 RELATED DB: TARGETDB
DBREF 2DAH A 8 48 UNP Q9H347 UBQL3_HUMAN 615 655
SEQADV 2DAH GLY A 1 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 2 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 3 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH GLY A 4 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 5 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 6 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH GLY A 7 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 49 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH GLY A 50 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH PRO A 51 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 52 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH SER A 53 UNP Q9H347 CLONING ARTIFACT
SEQADV 2DAH GLY A 54 UNP Q9H347 CLONING ARTIFACT
SEQRES 1 A 54 GLY SER SER GLY SER SER GLY HIS PHE GLN VAL GLN LEU
SEQRES 2 A 54 GLU GLN LEU ARG SER MET GLY PHE LEU ASN ARG GLU ALA
SEQRES 3 A 54 ASN LEU GLN ALA LEU ILE ALA THR GLY GLY ASP VAL ASP
SEQRES 4 A 54 ALA ALA VAL GLU LYS LEU ARG GLN SER SER GLY PRO SER
SEQRES 5 A 54 SER GLY
HELIX 1 1 PHE A 9 GLY A 20 1 12
HELIX 2 2 ASN A 23 GLY A 35 1 13
HELIX 3 3 ASP A 37 SER A 49 1 13
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
