Header list of 1f0e.pdb file
Complete list - 14 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 16-MAY-00 1F0E
TITLE CECROPIN A(1-8)-MAGAININ 2(1-12) MODIFIED GIG TO P IN
TITLE 2 DODECYLPHOSPHOCHOLINE MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CECROPIN A-MAGAININ 2 HYBRID PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 FOR THIS PEPTIDE IS A HYBRID OF SEQUENCES WHICH OCCUR NATURALLY IN
SOURCE 5 HYALOPHORA CECROPIA (CECROPIA MOTH) AND XENOPUS LAEVIS (AFRICAN
SOURCE 6 CLAWED FROG)
KEYWDS HELIX-TURN-HELIX, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.OH,S.Y.SHIN,S.LEE,Y.KIM
REVDAT 4 14-MAR-18 1F0E 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1F0E 1 VERSN
REVDAT 2 31-MAY-05 1F0E 1 JRNL REMARK
REVDAT 1 14-JUN-00 1F0E 0
JRNL AUTH D.OH,S.Y.SHIN,S.LEE,J.H.KANG,S.D.KIM,P.D.RYU,K.S.HAHM,Y.KIM
JRNL TITL ROLE OF THE HINGE REGION AND THE TRYPTOPHAN RESIDUE IN THE
JRNL TITL 2 SYNTHETIC ANTIMICROBIAL PEPTIDES, CECROPIN A(1-8)-MAGAININ
JRNL TITL 3 2(1-12) AND ITS ANALOGUES, ON THEIR ANTIBIOTIC ACTIVITIES
JRNL TITL 4 AND STRUCTURES.
JRNL REF BIOCHEMISTRY V. 39 11855 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11009597
JRNL DOI 10.1021/BI000453G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER, A.T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011090.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.78
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : DODECYLPHOSPHOCHOLINE-D38
REMARK 210 MICELLES
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 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-DYNAMICAL
REMARK 210 SIMULATED ANNEALING HYBRID METHOD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : NULL
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 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 LYS A 3 66.33 -164.98
REMARK 500 1 ILE A 8 107.93 -58.48
REMARK 500 2 LYS A 3 -76.34 -100.71
REMARK 500 3 TRP A 2 -45.07 -152.16
REMARK 500 3 LYS A 3 51.40 -140.64
REMARK 500 4 TRP A 2 -130.57 -165.74
REMARK 500 4 LYS A 3 69.56 -155.26
REMARK 500 5 PRO A 9 48.17 -76.82
REMARK 500 6 LYS A 3 4.54 -151.74
REMARK 500 8 LYS A 3 83.42 -163.15
REMARK 500 9 LYS A 3 40.40 -109.88
REMARK 500 10 TRP A 2 -123.84 -152.67
REMARK 500 10 ILE A 8 106.03 -51.88
REMARK 500 11 LYS A 3 -35.53 -162.78
REMARK 500 11 LYS A 17 -92.37 -85.56
REMARK 500 12 TRP A 2 -32.00 -165.49
REMARK 500 12 LYS A 3 45.87 -96.07
REMARK 500 12 PRO A 9 3.28 -68.54
REMARK 500 13 TRP A 2 -143.49 -144.22
REMARK 500 13 PRO A 9 44.48 -79.23
REMARK 500 14 TRP A 2 101.51 -165.36
REMARK 500 14 LYS A 3 13.19 -155.59
REMARK 500 16 PHE A 11 -70.78 -72.19
REMARK 500 17 LYS A 3 -52.14 -127.41
REMARK 500 18 LYS A 3 44.37 -93.07
REMARK 500 19 TRP A 2 -174.20 -51.75
REMARK 500 19 LYS A 3 -47.74 -158.67
REMARK 500 20 TRP A 2 55.79 -164.44
REMARK 500 20 PRO A 9 -159.99 -73.51
REMARK 500 20 LYS A 17 -89.52 -85.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 19
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D9J RELATED DB: PDB
REMARK 900 RELATED ID: 1D9L RELATED DB: PDB
REMARK 900 RELATED ID: 1D9M RELATED DB: PDB
REMARK 900 RELATED ID: 1D9O RELATED DB: PDB
REMARK 900 RELATED ID: 1D9P RELATED DB: PDB
REMARK 900 RELATED ID: 1F0D RELATED DB: PDB
REMARK 900 RELATED ID: 1F0F RELATED DB: PDB
REMARK 900 RELATED ID: 1F0G RELATED DB: PDB
REMARK 900 RELATED ID: 1F0H RELATED DB: PDB
DBREF 1F0E A 1 8 UNP P01507 CECA_HYACE 27 34
DBREF 1F0E A 10 18 UNP P11006 MAGA_XENLA 86 94
SEQADV 1F0E PRO A 9 UNP P11006 ENGINEERED MUTATION
SEQRES 1 A 19 LYS TRP LYS LEU PHE LYS LYS ILE PRO LYS PHE LEU HIS
SEQRES 2 A 19 SER ALA LYS LYS PHE NH2
HET NH2 A 19 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LYS A 3 ILE A 8 1 6
HELIX 2 2 ILE A 8 LYS A 17 1 10
LINK C PHE A 18 N NH2 A 19 1555 1555 1.31
SITE 1 AC1 1 PHE A 18
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 - 14 20 Bytes