Header list of 2mag.pdb file
Complete list - 26 20 Bytes
HEADER ANTIBIOTIC 19-DEC-97 2MAG TITLE NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAGAININ 2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 4 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 5 ORGANISM_TAXID: 8355; SOURCE 6 OTHER_DETAILS: THE PEPTIDE WAS PREPARED BY SOLID-PHASE SYNTHESIS KEYWDS ANTIBIOTIC, MAGAININ, MEMBRANE, AMPHIPATHIC HELIX, MICELLE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR J.J.GESELL,M.ZASLOFF,S.J.OPELLA REVDAT 3 26-OCT-16 2MAG 1 SOURCE VERSN REVDAT 2 24-FEB-09 2MAG 1 VERSN REVDAT 1 08-APR-98 2MAG 0 JRNL AUTH J.GESELL,M.ZASLOFF,S.J.OPELLA JRNL TITL TWO-DIMENSIONAL 1H NMR EXPERIMENTS SHOW THAT THE 23-RESIDUE JRNL TITL 2 MAGAININ ANTIBIOTIC PEPTIDE IS AN ALPHA-HELIX IN JRNL TITL 3 DODECYLPHOSPHOCHOLINE MICELLES, SODIUM DODECYLSULFATE JRNL TITL 4 MICELLES, AND TRIFLUOROETHANOL/WATER SOLUTION. JRNL REF J.BIOMOL.NMR V. 9 127 1997 JRNL REFN ISSN 0925-2738 JRNL PMID 9090128 JRNL DOI 10.1023/A:1018698002314 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR INTERFACED THROUGH NMRCOMPASS NMRCOMPASS REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 2MAG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.1 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : BIOSYM NMRCOMPASS NMRCOMPASS REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST 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: 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 ILE A 2 26.44 -76.69 REMARK 500 1 LYS A 10 -70.35 -63.61 REMARK 500 2 ASN A 22 -87.53 -72.20 REMARK 500 3 ILE A 2 27.79 -75.92 REMARK 500 5 ILE A 2 32.35 -82.28 REMARK 500 5 PHE A 5 -70.97 -47.38 REMARK 500 6 ASN A 22 -86.65 -39.69 REMARK 500 7 ASN A 22 -84.87 -69.12 REMARK 500 10 ASN A 22 52.45 96.24 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 24 DBREF 2MAG A 1 23 UNP P11006 MAGA_XENLA 267 289 SEQRES 1 A 24 GLY ILE GLY LYS PHE LEU HIS SER ALA LYS LYS PHE GLY SEQRES 2 A 24 LYS ALA PHE VAL GLY GLU ILE MET ASN SER NH2 HET NH2 A 24 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 LYS A 4 MET A 21 1 18 LINK N NH2 A 24 C SER A 23 1555 1555 1.35 SITE 1 AC1 1 SER A 23 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 - 26 20 Bytes