Header list of 1dlz.pdb file
Complete list - 25 20 Bytes
HEADER ANTIBIOTIC 13-DEC-99 1DLZ
TITLE SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB (PEPTAIBOL
TITLE 2 ANTIBIOTIC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZERVAMICIN IIB;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLOPSIS SALMOSYNNEMATA;
SOURCE 3 ORGANISM_TAXID: 118885
KEYWDS ZREVAMICIN, PEPTAIBOL, ANTIBACTERIAL, ANTIFUNGAL, ANTIBIOTIC, BENT
KEYWDS 2 HELIX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.A.BALASHOVA,Z.O.SHENKAREV,A.A.TAGAEV,T.V.OVCHINNIKOVA,J.RAAP,
AUTHOR 2 A.S.ARSENIEV
REVDAT 5 27-JUL-11 1DLZ 1 REMARK
REVDAT 4 13-JUL-11 1DLZ 1 VERSN
REVDAT 3 24-FEB-09 1DLZ 1 VERSN
REVDAT 2 26-SEP-01 1DLZ 1 HELIX
REVDAT 1 03-FEB-00 1DLZ 0
JRNL AUTH T.A.BALASHOVA,Z.O.SHENKAREV,A.A.TAGAEV,T.V.OVCHINNIKOVA,
JRNL AUTH 2 J.RAAP,A.S.ARSENIEV
JRNL TITL NMR STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB IN
JRNL TITL 2 ISOTROPIC SOLVENTS.
JRNL REF FEBS LETT. V. 466 333 2000
JRNL REFN ISSN 0014-5793
JRNL PMID 10682854
JRNL DOI 10.1016/S0014-5793(99)01707-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 3.1
REMARK 3 AUTHORS : INSIGHT II/95
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 335 NOESY PEAKS, 129 UPPER CONSTRAINTS,
REMARK 3 19 ADDITIONAL LOWER CONSTRAINTS, 48 ADDITIONAL CONSTRAINTS FOR
REMARK 3 HYDROGEN BONDS, 12 ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1DLZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-99.
REMARK 100 THE RCSB ID CODE IS RCSB010197.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 5.8; 5.8
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1ATM; 1ATM
REMARK 210 SAMPLE CONTENTS : 10MM ZERVAMICIN IIB; 3MM
REMARK 210 ZERVAMICIN IIB, UNIFORM LABELING
REMARK 210 WITH 15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
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 : BEST 20 OUT OF 100 WITH CA
REMARK 210 BACKBONE RMSD NO LESS THAN 0.05
REMARK 210 ANGSTROMS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NOESY SPECTRUM 200MS, WE DETERMINED N15HB CONSTANT FROM
REMARK 210 NOESY SPECTRA (N15 ENRICHED SAMPLE)
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 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 ZERVAMICIN IIB IS LINEAR PEPTIDE, A MEMBER OF THE PEPTAIBOL
REMARK 400 FAMILY OF MEMBRANE CHANNEL FORMING PEPTIDES.
REMARK 400 HERE, ZERVAMICIN IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ZERVAMICIN IIB
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 0 TO 16
REMARK 400 DESCRIPTION: ZERVAMICIN IS A HEXADECAMERIC HELICAL PEPTIDE.
REMARK 400 THE N-TERM IS ACETYLATED (RESIDUE 0)
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: 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: 1EE7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND
REMARK 900 TO DPC MICELLES
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 1DLZ A 0 16 NOR NOR01092 NOR01092 0 16
SEQRES 1 A 17 ACE TRP ILE GLN DIV ILE THR AIB LEU AIB HYP GLN AIB
SEQRES 2 A 17 HYP AIB PRO PHL
HET ACE A 0 6
HET DIV A 4 16
HET AIB A 7 13
HET AIB A 9 13
HET HYP A 10 15
HET AIB A 12 13
HET HYP A 13 15
HET AIB A 14 13
HET PHL A 16 23
HETNAM ACE ACETYL GROUP
HETNAM DIV D-ISOVALINE
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM HYP 4-HYDROXYPROLINE
HETNAM PHL L-PHENYLALANINOL
HETSYN HYP HYDROXYPROLINE
FORMUL 1 ACE C2 H4 O
FORMUL 1 DIV C5 H11 N O2
FORMUL 1 AIB 4(C4 H9 N O2)
FORMUL 1 HYP 2(C5 H9 N O3)
FORMUL 1 PHL C9 H13 N O
HELIX 1 1 TRP A 1 HYP A 10 1 10
LINK C ACE A 0 N TRP A 1 1555 1555 1.34
LINK C GLN A 3 N DIV A 4 1555 1555 1.36
LINK C DIV A 4 N ILE A 5 1555 1555 1.36
LINK C THR A 6 N AIB A 7 1555 1555 1.35
LINK C AIB A 7 N LEU A 8 1555 1555 1.36
LINK C LEU A 8 N AIB A 9 1555 1555 1.36
LINK C AIB A 9 N HYP A 10 1555 1555 1.38
LINK C HYP A 10 N GLN A 11 1555 1555 1.35
LINK C GLN A 11 N AIB A 12 1555 1555 1.37
LINK C AIB A 12 N HYP A 13 1555 1555 1.38
LINK C HYP A 13 N AIB A 14 1555 1555 1.36
LINK C AIB A 14 N PRO A 15 1555 1555 1.37
LINK C PRO A 15 N PHL A 16 1555 1555 1.35
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
Complete list - 25 20 Bytes