Header list of 1vm2.pdb file
Complete list - 2 20 Bytes
HEADER ANTIBIOTIC 31-AUG-04 1VM2
TITLE SOLUTION STRUCTURE OF AN ANTICANCER PEPTIDE DESIGNED BASED ON THE N-
TITLE 2 TERMINAL SEQUENCE OF E. COLI ENZYME IIA (GLUCOSE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE A2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED USING THE SOLID-PHASE
SOURCE 4 METHOD AND PURIFIED BY HPLC.
KEYWDS ANTIMICROBIAL PEPTIDE, BACTERIAL MEMBRANE ANCHOR, AMPHIPATHIC HELIX,
KEYWDS 2 ANTI-TUMOR PEPTIDE, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR G.WANG,X.LI
REVDAT 4 02-MAR-22 1VM2 1 REMARK LINK
REVDAT 3 17-FEB-09 1VM2 1 AUTHOR VERSN
REVDAT 2 01-MAR-05 1VM2 1 JRNL
REVDAT 1 07-DEC-04 1VM2 0
JRNL AUTH G.WANG,Y.LI,X.LI
JRNL TITL CORRELATION OF THREE-DIMENSIONAL STRUCTURES WITH THE
JRNL TITL 2 ANTIBACTERIAL ACTIVITY OF A GROUP OF PEPTIDES DESIGNED BASED
JRNL TITL 3 ON A NONTOXIC BACTERIAL MEMBRANE ANCHOR.
JRNL REF J.BIOL.CHEM. V. 280 5803 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15572363
JRNL DOI 10.1074/JBC.M410116200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE/NMRDRAW 2.1, XPLOR-NIH 1.06
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE/NMRDRAW), SCHWIETERS, C.D.,
REMARK 3 KUSZEWSKI, J., TJANDRA, N, CLORE, G.M. (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 124
REMARK 3 DISTANCES DERIVED FROM THE NOESY SPECTRA, 20 BACKBONE DIHEDRAL
REMARK 3 ANGLES DERIVED FROM A SET OF CHEMICAL SHIFTS USING THE NMR
REMARK 3 PROGRAM TALOS, AND 4 CHI1 ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1VM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000001998.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE, 80MM SODIUM
REMARK 210 DODECYLSULFATE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY; DQF-COSY;
REMARK 210 ROESY; (1H,15N)HSQC; (1H,13C)HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 1.0, MOLMOL 2K.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS GREATER THAN
REMARK 210 0.50 A, RMS DIFFERENCE FOR BOND
REMARK 210 DEVIATIONS FROM IDEALITY LESS
REMARK 210 THAN 0.01 A, RMS DIFFERENCE FOR
REMARK 210 ANGLE DEVIATIONS FROM IDEALITY
REMARK 210 LESS THAN 5 DEGREES, STRUCTURES
REMARK 210 WITH THE LOWEREST ENERGIES IN
REMARK 210 THE ENSEMBLE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR NMR TECHNIQUES, PLUS THE USE OF BACKBONE ANGLE
REMARK 210 RESTRAINTS DERIVED FROM A SET OF HETERONUCLEAR CHEMICAL SHIFTS
REMARK 210 MEASURED ON THE NATURAL ABUNDANCE PEPTIDE BOUND TO MICELLES.
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 O LEU A 2 H LYS A 5 1.57
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 3 ASP A 12 -73.01 -82.20
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 14
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O53 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MEMBRANE ANCHOR
REMARK 900 RELATED ID: 1VM3 RELATED DB: PDB
REMARK 900 RELATED ID: 1VM4 RELATED DB: PDB
REMARK 900 RELATED ID: 1VM5 RELATED DB: PDB
DBREF 1VM2 A 1 14 PDB 1VM2 1VM2 1 14
SEQRES 1 A 14 GLY LEU PHE ASP LYS LEU LYS SER LEU VAL SER ASP PHE
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LEU A 2 PHE A 13 1 12
LINK C PHE A 13 N NH2 A 14 1555 1555 1.31
SITE 1 AC1 2 VAL A 10 PHE A 13
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 - 2 20 Bytes