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HEADER TRANSFERASE 09-JUN-15 5A4H
TITLE SOLUTION STRUCTURE OF THE LIPID DROPLET ANCHORING PEPTIDE
TITLE 2 OF CGI-58 BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE ABHD5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL PEPTIDE, RESIDUES 10-43;
COMPND 5 SYNONYM: ABHYDROLASE DOMAIN-CONTAINING PROTEIN 5, LIPID DROPLET-
COMPND 6 BINDING PROTEIN CGI-58, PROTEIN CGI-58, WR10_43;
COMPND 7 EC: 2.3.1.51;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: N-TERMINAL LD BINDING MOTIF OF CGI-58
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSUMO
KEYWDS TRANSFERASE, CGI-58, ABHD5, LIPID DROPLET ANCHOR, SOLUTION STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.BOESZOERMENYI,H.ARTHANARI,G.WAGNER,H.M.NAGY,K.ZANGGER,H.LINDERMUTH,
AUTHOR 2 M.OBERER
REVDAT 1 16-SEP-15 5A4H 0
JRNL AUTH A.BOESZOERMENYI,H.M.NAGY,H.ARTHANARI,C.J.PHILLIP,
JRNL AUTH 2 H.LINDERMUTH,R.E.LUNA,G.WAGNER,R.ZECHNER,K.ZANGGER,M.OBERER
JRNL TITL STRUCTURE OF A CGI-58 MOTIF PROVIDES THE MOLECULAR BASIS OF
JRNL TITL 2 LIPID DROPLET ANCHORING
JRNL REF J.BIOL.CHEM. 2015
JRNL REFN ESSN 1083-351X
JRNL REF 10.1074/JBC.M115.682203
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND
REMARK 3 IN THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 5A4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-15.
REMARK 100 THE PDBE ID CODE IS EBI-63988.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310.0 ; 310.0 ; 310.0 ;
REMARK 210 310.0 ; 303.0 ; 310.0 ;
REMARK 210 303.0
REMARK 210 PH : 6.0 ; 6.0 ; 6.0 ; 6.0 ; 6.0 ;
REMARK 210 6.0 ; 6.0
REMARK 210 IONIC STRENGTH : 70.0 ; 70.0 ; 70.0 ; 70.0
REMARK 210 ; 70.0 ; 70.0 ; 70.0
REMARK 210 PRESSURE : 1.0 ATM ; 1.0 ATM ; 1.0 ATM ; 1.0
REMARK 210 ATM ; 1.0 ATM ; 1.0 ATM ; 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 93% H2O/7% D2O ; 100% D2O
REMARK 210 ; 93% H2O/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HNCACB, HNCACO, HSQC
REMARK 210 ; HSQC_ANOESY, NOESYHSQC ;
REMARK 210 HCCONH ; CCONH, HCCH_TOCSY
REMARK 210 ; TOCSY_90MS ;
REMARK 210 13CHSQC_B900, CNOESY_B900
REMARK 210 ; NOESY_200MS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ ; 700 MHZ ; 750 MHZ ; 500
REMARK 210 MHZ ; 900 MHZ ; 900 MHZ ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DD2
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER ; VARIAN ; BRUKER ;
REMARK 210 VARIAN ; BRUKER ; BRUKER ;
REMARK 210 BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRDRAW ANY, NMRPIPE ANY,
REMARK 210 CCPNMR ANALYSIS 2.4, TALOS 1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON THE DOUBLY LABELED PEPTIDE BOUND TO
REMARK 210 DPC MICELLES. HOMONOCULEAR NOESY AND TOCSY EXPERIMENTS ON
REMARK 210 A SHORTER UNLABELED PEPTIDE ALSO BOUND TO DPC MICELLES AND
REMARK 210 PARAMAGNETIC RELAXATION EXPERIMENTS TO ORIENT THE PEPTIDE
REMARK 210 WITH RESPECT TO THE MICELLE.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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: 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 9 -74.15 -148.88
REMARK 500 1 ALA A 13 142.47 -177.92
REMARK 500 1 ASP A 14 -52.02 -141.45
REMARK 500 1 SER A 19 -32.43 -157.35
REMARK 500 1 LEU A 22 4.25 -68.38
REMARK 500 1 PRO A 27 -165.30 -69.74
REMARK 500 1 TRP A 29 90.09 -63.53
REMARK 500 1 CYS A 30 74.71 -151.87
REMARK 500 1 SER A 33 98.99 -63.65
REMARK 500 1 SER A 35 -174.42 -59.27
REMARK 500 1 HIS A 36 -51.11 -179.64
REMARK 500 1 LEU A 37 61.75 -100.56
REMARK 500 1 GLU A 39 -169.94 -60.88
REMARK 500 1 ALA A 40 96.28 -60.54
REMARK 500 1 GLU A 41 -176.66 -179.31
REMARK 500 2 SER A 9 164.14 63.10
REMARK 500 2 ALA A 13 102.90 62.32
REMARK 500 2 ALA A 15 62.42 -178.51
REMARK 500 2 SER A 19 -32.73 -153.99
REMARK 500 2 LEU A 22 4.21 -68.13
REMARK 500 2 PRO A 27 -165.32 -69.77
REMARK 500 2 TRP A 29 89.98 -63.66
REMARK 500 2 CYS A 30 75.92 -152.09
REMARK 500 2 SER A 33 -169.96 52.30
REMARK 500 2 HIS A 36 -72.99 -179.01
REMARK 500 2 ALA A 40 -174.20 -175.37
REMARK 500 3 MET A 7 -72.88 -124.37
REMARK 500 3 SER A 9 103.82 63.12
REMARK 500 3 ASP A 14 -41.16 -131.37
REMARK 500 3 ALA A 15 62.09 -175.89
REMARK 500 3 SER A 19 -32.55 -157.02
REMARK 500 3 LEU A 22 4.30 -68.27
REMARK 500 3 PRO A 27 -165.25 -69.81
REMARK 500 3 TRP A 29 90.21 -63.50
REMARK 500 3 CYS A 30 74.05 -152.10
REMARK 500 3 PRO A 31 72.76 -69.75
REMARK 500 3 SER A 33 112.74 64.97
REMARK 500 3 SER A 35 -179.52 -57.77
REMARK 500 3 HIS A 36 -71.63 -176.03
REMARK 500 4 ASP A 14 -58.59 -120.37
REMARK 500 4 ALA A 15 60.38 -151.38
REMARK 500 4 SER A 19 -32.80 -155.29
REMARK 500 4 LEU A 22 4.45 -68.61
REMARK 500 4 PRO A 27 -165.45 -69.81
REMARK 500 4 TRP A 29 90.20 -63.26
REMARK 500 4 CYS A 30 75.12 -152.00
REMARK 500 4 PRO A 31 73.50 -69.68
REMARK 500 4 THR A 32 36.41 -94.64
REMARK 500 4 SER A 33 -178.74 -56.89
REMARK 500 4 SER A 35 72.72 -111.83
REMARK 500
REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL FRAMGENT (V10-K43). FIRST FIVE RESIDUES ARE
REMARK 999 ARTIFACTS FROM CLONING AND PROTEASE CLEAVAGE SITE. THEY
REMARK 999 ARE NOT PART OF NATIVE STRUCTURE.
DBREF 5A4H A 10 43 UNP Q9DBL9 ABHD5_MOUSE 10 43
SEQADV 5A4H GLY A 5 UNP Q9DBL9 EXPRESSION TAG
SEQADV 5A4H ALA A 6 UNP Q9DBL9 EXPRESSION TAG
SEQADV 5A4H MET A 7 UNP Q9DBL9 EXPRESSION TAG
SEQADV 5A4H GLY A 8 UNP Q9DBL9 EXPRESSION TAG
SEQADV 5A4H SER A 9 UNP Q9DBL9 EXPRESSION TAG
SEQRES 1 A 39 GLY ALA MET GLY SER VAL ASP SER ALA ASP ALA GLY GLY
SEQRES 2 A 39 GLY SER GLY TRP LEU THR GLY TRP LEU PRO THR TRP CYS
SEQRES 3 A 39 PRO THR SER THR SER HIS LEU LYS GLU ALA GLU GLU LYS
HELIX 1 1 GLY A 20 GLY A 24 5 5
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
TER 532 LYS A 43
ENDMDL
MODEL 2
TER 532 LYS A 43
ENDMDL
MODEL 3
TER 532 LYS A 43
ENDMDL
MODEL 4
TER 532 LYS A 43
ENDMDL
MODEL 5
TER 532 LYS A 43
ENDMDL
MODEL 6
TER 532 LYS A 43
ENDMDL
MODEL 7
TER 532 LYS A 43
ENDMDL
MODEL 8
TER 532 LYS A 43
ENDMDL
MODEL 9
TER 532 LYS A 43
ENDMDL
MODEL 10
TER 532 LYS A 43
ENDMDL
MODEL 11
TER 532 LYS A 43
ENDMDL
MODEL 12
TER 532 LYS A 43
ENDMDL
MODEL 13
TER 532 LYS A 43
ENDMDL
MODEL 14
TER 532 LYS A 43
ENDMDL
MODEL 15
TER 532 LYS A 43
ENDMDL
MODEL 16
TER 532 LYS A 43
ENDMDL
MODEL 17
TER 532 LYS A 43
ENDMDL
MODEL 18
TER 532 LYS A 43
ENDMDL
MODEL 19
TER 532 LYS A 43
ENDMDL
MODEL 20
TER 532 LYS A 43
ENDMDL
MASTER 160 0 0 1 0 0 0 6 531 20 0 3
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