Header list of 1gq0.pdb file
Complete list - 20 20 Bytes
HEADER ANTIBIOTIC 16-NOV-01 1GQ0
TITLE SOLUTION STRUCTURE OF ANTIAMOEBIN I, A MEMBRANE CHANNEL-FORMING
TITLE 2 POLYPEPTIDE; NMR, 20 STRUCTURES
CAVEAT 1GQ0 HYP A 13 C-ALPHA WRONG HAND IN ALL MODELS, PHL A 16 C-ALPHA
CAVEAT 2 1GQ0 WRONG HAND IN ALL MODELS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIAMOEBIN I;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLOPSIS SP. 2723;
SOURCE 3 ORGANISM_TAXID: 489044
KEYWDS ANTIAMOEBIN I, PEPTAIBOL, ANTIBACTERIAL, ANTIFUNGAL, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.P.GALBRAITH,R.HARRIS,P.C.DRISCOLL,B.A.WALLACE
REVDAT 5 20-DEC-17 1GQ0 1 JRNL
REVDAT 4 13-JUL-11 1GQ0 1 VERSN
REVDAT 3 24-FEB-09 1GQ0 1 VERSN
REVDAT 2 03-FEB-03 1GQ0 1 SOURCE
REVDAT 1 24-JAN-03 1GQ0 0
JRNL AUTH T.P.GALBRAITH,R.HARRIS,P.C.DRISCOLL,B.A.WALLACE
JRNL TITL SOLUTION NMR STUDIES OF ANTIAMOEBIN, A MEMBRANE
JRNL TITL 2 CHANNEL-FORMING POLYPEPTIDE.
JRNL REF BIOPHYS. J. V. 84 185 2003
JRNL REFN ISSN 0006-3495
JRNL PMID 12524274
JRNL DOI 10.1016/S0006-3495(03)74841-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.F.SNOOK,G.A.WOOLLEY,G.OLIVA,V.PATTABHI,S.F.WOOD,
REMARK 1 AUTH 2 T.L.BLUNDELL,B.A.WALLACE
REMARK 1 TITL THE STRUCTURE AND FUNCTION OF ANTIAMOEBIN I, A PROLINE-RICH
REMARK 1 TITL 2 MEMBRANE-ACTIVE POLYPEPTIDE.
REMARK 1 REF STRUCTURE V. 6 783 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9655831
REMARK 1 DOI 10.1016/S0969-2126(98)00079-3
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.DUCLOHIER,C.F.SNOOK,B.A.WALLACE
REMARK 1 TITL ANTIAMOEBIN CAN FUNCTION AS A CARRIER OR AS A PORE-FORMING
REMARK 1 TITL 2 PEPTAIBOL.
REMARK 1 REF BIOCHIM. BIOPHYS. ACTA V.1415 255 1998
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 9858744
REMARK 1 DOI 10.1016/S0005-2736(98)00184-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 246 ATOMS USED IN SIMULATED ANNEALING
REMARK 3 (INCLUDING HYDROGENS) RMSD VALUES FROM IDEAL GEOMETRY FOR 20
REMARK 3 MODELS: BOND DISTANCES 0.013 ANGSTROMS, STANDARD DEVIATION
REMARK 3 0.0001 BOND ANGLES 2.92 DEGREES, STANDARD DEVIATION 0.017
REMARK 3 IMPROPER ANGLES 6.62 DEGREES, STANDARD DEVIATION 0.028
REMARK 4
REMARK 4 1GQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1290005778.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; ROESY; DQF-COSY; TOCSY;
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MARDIGRAS, XPLOR
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: 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: PISA
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 ANTIAMOEBIN I IS LINEAR PEPTIDE, A MEMBER OF THE PEPTAIBOL
REMARK 400 FAMILY OF MEMBRANE CHANNEL FORMING PEPTIDES.
REMARK 400 HERE, ANTIAMOEBIN I IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ANTIAMOEBIN I
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 0 TO 16
REMARK 400 DESCRIPTION: ANTIAMOEBIN I IS A HEXADECAMERIC HELICAL PEPTIDE.
REMARK 400 THE N-TERM IS ACETYLATED (RESIDUE 0)
REMARK 400
REMARK 400 THE ANTIAMOEBIN 1 IS PEPTAIBOL, A MEMBER OF ANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ANTIAMOEBIN 1
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: ANTIAMOEBIN I IS A HEXADECAMERIC 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
REMARK 500 REMARK: NULL
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 AIB A 2 56.39 -65.05
REMARK 500 1 AIB A 3 -33.54 -176.90
REMARK 500 1 AIB A 4 73.91 -8.73
REMARK 500 1 DIV A 5 65.98 27.51
REMARK 500 1 LEU A 7 45.84 22.77
REMARK 500 1 AIB A 8 -23.24 159.42
REMARK 500 1 DIV A 12 -37.20 -38.84
REMARK 500 1 HYP A 13 -59.22 -4.54
REMARK 500 1 AIB A 14 -79.87 -35.94
REMARK 500 2 AIB A 3 -23.25 164.94
REMARK 500 2 AIB A 4 86.26 -7.81
REMARK 500 2 DIV A 5 66.04 29.42
REMARK 500 2 LEU A 7 79.51 33.17
REMARK 500 2 HYP A 13 -62.92 -2.61
REMARK 500 2 AIB A 14 -79.86 14.75
REMARK 500 2 PRO A 15 -34.85 -38.93
REMARK 500 3 AIB A 2 58.72 -65.43
REMARK 500 3 AIB A 3 -27.29 178.45
REMARK 500 3 AIB A 4 85.92 -21.75
REMARK 500 3 LEU A 7 86.46 32.33
REMARK 500 3 DIV A 12 -38.36 -35.99
REMARK 500 3 HYP A 13 -58.12 -4.21
REMARK 500 3 AIB A 14 -67.18 -0.68
REMARK 500 3 PRO A 15 -35.66 -38.73
REMARK 500 4 AIB A 2 64.85 -64.32
REMARK 500 4 AIB A 3 -7.78 143.46
REMARK 500 4 AIB A 4 84.69 -24.77
REMARK 500 4 DIV A 5 60.07 29.61
REMARK 500 4 LEU A 7 65.41 35.81
REMARK 500 4 HYP A 10 35.78 -86.07
REMARK 500 4 DIV A 12 -60.90 -38.59
REMARK 500 4 HYP A 13 -66.14 18.97
REMARK 500 4 AIB A 14 -58.74 -23.00
REMARK 500 4 PRO A 15 -35.83 -39.53
REMARK 500 5 AIB A 2 68.65 -61.52
REMARK 500 5 AIB A 3 -26.50 172.60
REMARK 500 5 AIB A 4 83.79 -21.95
REMARK 500 5 LEU A 7 51.02 34.81
REMARK 500 5 DIV A 12 -35.01 -31.40
REMARK 500 5 HYP A 13 -61.34 -0.51
REMARK 500 5 AIB A 14 -72.47 6.63
REMARK 500 5 PRO A 15 -33.91 -33.76
REMARK 500 6 AIB A 2 68.22 -62.11
REMARK 500 6 AIB A 3 -33.10 -175.20
REMARK 500 6 AIB A 4 89.72 -24.40
REMARK 500 6 DIV A 5 70.21 35.55
REMARK 500 6 LEU A 7 58.31 36.49
REMARK 500 6 AIB A 8 29.92 40.83
REMARK 500 6 DIV A 12 -44.68 -38.06
REMARK 500 6 HYP A 13 -63.65 4.73
REMARK 500
REMARK 500 THIS ENTRY HAS 170 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JOH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL ANTIAMOEBIN I
REMARK 900 RELATED ID: 1EE7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1AMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL ALAMETHICIN
REMARK 900 RELATED ID: 1M24 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL TRICHOTOXIN_A50E
REMARK 900 RELATED ID: 1OB4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL A
REMARK 900 RELATED ID: 1OB6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL B
REMARK 900 RELATED ID: 1OB7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTAIBOL CEPHAIBOL C
REMARK 900 RELATED ID: 1R9U RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ZERVAMICIN IIB IN METHANOL
REMARK 900 RELATED ID: 1IH9 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ZERVAMICIN IIB BOUND TO DPC
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1DLZ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PEPTAIBOL ZERVAMICIN IIB IN ISOTROPIC
REMARK 900 SOLVENTS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE ANTIBIOTIC REPORTED HERE IS SIMILAR IN STRUCTURE TO THAT
REMARK 999 FOUND IN EMBL:AAB11467 FROM THE SPECIES ACREMONIUM TUBAKII
DBREF 1GQ0 A 0 16 NOR NOR00945 NOR00945 0 16
SEQRES 1 A 17 ACE PHE AIB AIB AIB DIV GLY LEU AIB AIB HYP GLN DIV
SEQRES 2 A 17 HYP AIB PRO PHL
MODRES 1GQ0 AIB A 2 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 AIB A 3 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 AIB A 4 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 AIB A 8 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 AIB A 9 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 HYP A 10 PRO 4-HYDROXYPROLINE
MODRES 1GQ0 HYP A 13 PRO 4-HYDROXYPROLINE
MODRES 1GQ0 AIB A 14 ALA ALPHA-AMINOISOBUTYRIC ACID
MODRES 1GQ0 PHL A 16 PHE L-PHENYLALANINOL
HET ACE A 0 6
HET AIB A 2 13
HET AIB A 3 13
HET AIB A 4 13
HET DIV A 5 16
HET AIB A 8 13
HET AIB A 9 13
HET HYP A 10 15
HET DIV A 12 16
HET HYP A 13 15
HET AIB A 14 13
HET PHL A 16 23
HETNAM ACE ACETYL GROUP
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM DIV D-ISOVALINE
HETNAM HYP 4-HYDROXYPROLINE
HETNAM PHL L-PHENYLALANINOL
HETSYN HYP HYDROXYPROLINE
FORMUL 1 ACE C2 H4 O
FORMUL 1 AIB 6(C4 H9 N O2)
FORMUL 1 DIV 2(C5 H11 N O2)
FORMUL 1 HYP 2(C5 H9 N O3)
FORMUL 1 PHL C9 H13 N O
HELIX 1 1 AIB A 3 AIB A 8 1 6
HELIX 2 2 AIB A 9 DIV A 12 5 4
LINK C ACE A 0 N PHE A 1 1555 1555 1.35
LINK C PHE A 1 N AIB A 2 1555 1555 1.35
LINK C AIB A 2 N AIB A 3 1555 1555 1.37
LINK C AIB A 3 N AIB A 4 1555 1555 1.37
LINK C AIB A 4 N DIV A 5 1555 1555 1.37
LINK C DIV A 5 N GLY A 6 1555 1555 1.35
LINK C LEU A 7 N AIB A 8 1555 1555 1.35
LINK C AIB A 8 N AIB A 9 1555 1555 1.37
LINK C AIB A 9 N HYP A 10 1555 1555 1.37
LINK C HYP A 10 N GLN A 11 1555 1555 1.33
LINK C GLN A 11 N DIV A 12 1555 1555 1.35
LINK C DIV A 12 N HYP A 13 1555 1555 1.38
LINK C HYP A 13 N AIB A 14 1555 1555 1.37
LINK C AIB A 14 N PRO A 15 1555 1555 1.37
LINK C PRO A 15 N PHL A 16 1555 1555 1.33
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 - 20 20 Bytes