HEADER LIPID BINDING PROTEIN 11-MAY-16 2ND6
TITLE STRUCTURE OF DK17 IN GM1 LUVS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL PENETRATING PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 4 ORGANISM_COMMON: FRUIT FLY;
SOURCE 5 ORGANISM_TAXID: 7227;
SOURCE 6 OTHER_DETAILS: SYNTHETIC PEPTIDE, MODIFIED VERSION OF PENETRATIN
SOURCE 7 PEPTIDE, DERIVED FROM ANTENNAPEDIA HOMEODOMAIN PROTEIN (3RD HELIX)
SOURCE 8 OF DROSOPHILA MELANOGASTER
KEYWDS LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.BERA,A.BHUNIA
REVDAT 2 14-JUN-23 2ND6 1 REMARK
REVDAT 1 22-MAR-17 2ND6 0
JRNL AUTH S.BERA,R.K.KAR,S.MONDAL,K.PAHAN,A.BHUNIA
JRNL TITL STRUCTURAL ELUCIDATION OF THE CELL-PENETRATING PENETRATIN
JRNL TITL 2 PEPTIDE IN MODEL MEMBRANES AT THE ATOMIC LEVEL: PROBING
JRNL TITL 3 HYDROPHOBIC INTERACTIONS IN THE BLOOD-BRAIN BARRIER
JRNL REF BIOCHEMISTRY V. 55 4982 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27532224
JRNL DOI 10.1021/ACS.BIOCHEM.6B00518
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, CYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ND6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000104716.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM CELL PENETRATING PEPTIDES
REMARK 210 -1, 55.5 MM H2O-2, 50 MM D2O-3,
REMARK 210 0.5 MM DSS-4, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H TOCSY; 2D 1H-1H 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 : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 26049 RELATED DB: BMRB
REMARK 900 RELATED ID: 2ND7 RELATED DB: PDB
REMARK 900 RELATED ID: 2ND8 RELATED DB: PDB
DBREF 2ND6 A 1 17 PDB 2ND6 2ND6 1 17
SEQRES 1 A 17 ASP ARG GLN ILE LYS ILE TRP PHE GLN ASN ARG ARG MET
SEQRES 2 A 17 LYS TRP LYS LYS
HELIX 1 1 ARG A 2 MET A 13 1 12
HELIX 2 2 LYS A 14 LYS A 16 5 3
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
