HEADER MEMBRANE PROTEIN 31-MAR-11 2LBG
TITLE STRUCTURE OF THE CHR OF THE PRION PROTEIN IN DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PRP, ASCR, PRP27-30, PRP33-35C;
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: PRNP, PRIP, PRP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET19B-GST
KEYWDS PRION PROTEIN, CONSERVED HYDROPHOBIC REGION, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SAUVE,Y.AUBIN
REVDAT 3 14-JUN-23 2LBG 1 REMARK
REVDAT 2 01-FEB-12 2LBG 1 JRNL
REVDAT 1 07-DEC-11 2LBG 0
JRNL AUTH S.SAUVE,D.BUIJS,G.GINGRAS,Y.AUBIN
JRNL TITL INTERACTIONS BETWEEN THE CONSERVED HYDROPHOBIC REGION OF THE
JRNL TITL 2 PRION PROTEIN AND DODECYLPHOSPHOCHOLINE MICELLES.
JRNL REF J.BIOL.CHEM. V. 287 1915 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22128151
JRNL DOI 10.1074/JBC.M111.279364
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CYANA 2.1
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3 (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CYANA 2.1 BUILD-IN TAD ALGORITHM
REMARK 4
REMARK 4 2LBG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000102191.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MG [U-99% 13C; U-99% 15N]
REMARK 210 PRP CONSERVED HYDROPHOBIC DOMAIN,
REMARK 210 14 MG DODECYLPHOSPHOCHOLINE
REMARK 210 (DPC) MICELLE, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HNHA; 3D HCCH-
REMARK 210 TOCSY; 3D HCCH-COSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY; 3D
REMARK 210 CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE III
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, TALOS +, CYANA 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17558 RELATED DB: BMRB
DBREF 2LBG A 1 27 UNP P04156 PRIO_HUMAN 110 136
SEQRES 1 A 27 LYS HIS MET ALA GLY ALA ALA ALA ALA GLY ALA VAL VAL
SEQRES 2 A 27 GLY GLY LEU GLY GLY TYR MET LEU GLY SER ALA MET SER
SEQRES 3 A 27 ARG
HELIX 1 1 HIS A 2 ARG A 27 1 26
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.)
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