Header list of 1ee7.pdb file
Complete list - 25 201 Bytes
HEADER ANTIBIOTIC 31-JAN-00 1EE7
TITLE NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHRYSOSPERMIN C;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYPOMYCES CHRYSOSPERMUS;
SOURCE 3 ORGANISM_TAXID: 5131
KEYWDS CHRYSOSPERMIN C, PEPTAIBOL, ANTIBACTERIAL, ANTIFUNGAL, ANTIBIOTIC
EXPDTA SOLUTION NMR
AUTHOR R.ANDERS,O.OHLENSCHLAGER,V.SOSKIC,H.WENSCHUH,B.HEISE,L.R.BROWN
REVDAT 4 27-JUL-11 1EE7 1 REMARK
REVDAT 3 13-JUL-11 1EE7 1 VERSN
REVDAT 2 24-FEB-09 1EE7 1 VERSN
REVDAT 1 10-MAY-00 1EE7 0
JRNL AUTH R.ANDERS,O.OHLENSCHLAGER,V.SOSKIC,H.WENSCHUH,B.HEISE,
JRNL AUTH 2 L.R.BROWN
JRNL TITL THE NMR SOLUTION STRUCTURE OF THE ION CHANNEL PEPTAIBOL
JRNL TITL 2 CHRYSOSPERMIN C BOUND TO DODECYLPHOSPHOCHOLINE MICELLES.
JRNL REF EUR.J.BIOCHEM. V. 267 1784 2000
JRNL REFN ISSN 0014-2956
JRNL PMID 10712611
JRNL DOI 10.1046/J.1432-1327.2000.01177.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL 2.6
REMARK 3 AUTHORS : LUGINBUEHL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 379 RESTRAINTS, 338 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 40
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 1 DISTANCE CONSTRAINT FOR A HYDROGEN
REMARK 3 BOND
REMARK 4
REMARK 4 1EE7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-00.
REMARK 100 THE RCSB ID CODE IS RCSB010486.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 6.0 MM NA-CHRYSOSPERMIN C IN DPC
REMARK 210 -MICELLES 1:50, 4.3 MM SEL. 13C/15N-LAB. CHRYSOSPERMIN C IN DPC-
REMARK 210 MISCELLES 1:50; 4.3 MM [[15N',13C']-AIB9,AIB10,AIB13; [13CB]-
REMARK 210 AIB15,AIB16,AIB17]-CHRYSOSPERMIN C IN DPC-MICELLES 1:50
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY; HET-
REMARK 210 TOCSY; HMBC; H(N)CO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS, INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED DG STRUCTURE, CLOSEST
REMARK 210 TO AVERAGE STRUCTURE
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 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 400
REMARK 400 COMPOUND
REMARK 400 CHRYSOSPERMIN C IS LINEAR PEPTIDE, A MEMBER OF THE PEPTAIBOL
REMARK 400 FAMILY OF MEMBRANE CHANNEL FORMING PEPTIDES.
REMARK 400 HERE, CHRYSOSPERMIN C IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: CHRYSOSPERMIN C
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 0 TO 19
REMARK 400 DESCRIPTION: CHRYSOSPERMIN C IS A NONADECAMERIC HELICAL PEPTIDE.
REMARK 400 THE N-TERM IS ACETYLATED (RESIDUE 0)
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 DIV A 5 H AIB A 9 1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M24 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL TRICHOTOXIN_A50E
REMARK 900 RELATED ID: 1R9U RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ZERVAMICIN IIB IN
REMARK 900 METHANOL
REMARK 900 RELATED ID: 1DLZ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTIABOL ZERVAMICIN IIB
REMARK 900 RELATED ID: 1IH9 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ZERVAMICIN IIB BOUND TO
REMARK 900 DPC MICELLES
REMARK 900 RELATED ID: 1GQ0 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ANTIAMOEBIN I
REMARK 900 RELATED ID: 1JOH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL ANTIAMOEBIN I
REMARK 900 RELATED ID: 1AMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL ALAMETHICIN
REMARK 900 RELATED ID: 1OB7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL C
REMARK 900 RELATED ID: 1OB6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL B
REMARK 900 RELATED ID: 1OB4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL A
DBREF 1EE7 A 0 19 NOR NOR00981 NOR00981 0 19
SEQRES 1 A 20 ACE PHE AIB SER AIB DIV LEU GLN GLY AIB AIB ALA ALA
SEQRES 2 A 20 AIB PRO AIB AIB AIB GLN TPL
HET ACE A 0 6
HET AIB A 2 13
HET AIB A 4 13
HET DIV A 5 16
HET AIB A 9 13
HET AIB A 10 13
HET AIB A 13 13
HET AIB A 15 13
HET AIB A 16 13
HET AIB A 17 13
HET TPL A 19 27
HETNAM ACE ACETYL GROUP
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM DIV D-ISOVALINE
HETNAM TPL TRYPTOPHANOL
HETSYN TPL 2-AMINO-3-(1H-INDOL-3-YL)-PROPAN-1-OL
FORMUL 1 ACE C2 H4 O
FORMUL 1 AIB 8(C4 H9 N O2)
FORMUL 1 DIV C5 H11 N O2
FORMUL 1 TPL C11 H14 N2 O
HELIX 1 1 PHE A 1 GLN A 18 1 18
LINK C ACE A 0 N PHE A 1 1555 1555 1.33
LINK C PHE A 1 N AIB A 2 1555 1555 1.35
LINK C AIB A 2 N SER A 3 1555 1555 1.33
LINK C SER A 3 N AIB A 4 1555 1555 1.35
LINK C AIB A 4 N DIV A 5 1555 1555 1.35
LINK C DIV A 5 N LEU A 6 1555 1555 1.33
LINK C GLY A 8 N AIB A 9 1555 1555 1.35
LINK C AIB A 9 N AIB A 10 1555 1555 1.34
LINK C AIB A 10 N ALA A 11 1555 1555 1.33
LINK C ALA A 12 N AIB A 13 1555 1555 1.35
LINK C AIB A 13 N PRO A 14 1555 1555 1.36
LINK C PRO A 14 N AIB A 15 1555 1555 1.35
LINK C AIB A 15 N AIB A 16 1555 1555 1.35
LINK C AIB A 16 N AIB A 17 1555 1555 1.34
LINK C AIB A 17 N GLN A 18 1555 1555 1.32
LINK C GLN A 18 N TPL A 19 1555 1555 1.36
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
Complete list - 25 201 Bytes