Header list of 2g9p.pdb file
Complete list - 9 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 07-MAR-06 2G9P TITLE NMR STRUCTURE OF A NOVEL ANTIMICROBIAL PEPTIDE, LATARCIN 2A, FROM TITLE 2 SPIDER (LACHESANA TARABAEVI) VENOM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIMICROBIAL PEPTIDE LATARCIN 2A; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 CAN BE NATURALLY FOUND IN SPIDER (LACHESANA TARABAEVI) VENOM KEYWDS HELIX-HINGE-HELIX, ANTIMICROBIAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.V.DUBOVSKII,P.E.VOLYNSKY,A.A.POLYANSKY,V.V.CHUPIN,R.G.EFREMOV, AUTHOR 2 A.S.ARSENIEV REVDAT 3 09-MAR-22 2G9P 1 REMARK REVDAT 2 24-FEB-09 2G9P 1 VERSN REVDAT 1 12-SEP-06 2G9P 0 JRNL AUTH P.V.DUBOVSKII,P.E.VOLYNSKY,A.A.POLYANSKY,V.V.CHUPIN, JRNL AUTH 2 R.G.EFREMOV,A.S.ARSENIEV JRNL TITL SPATIAL STRUCTURE AND ACTIVITY MECHANISM OF A NOVEL SPIDER JRNL TITL 2 ANTIMICROBIAL PEPTIDE. JRNL REF BIOCHEMISTRY V. 45 10759 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16939228 JRNL DOI 10.1021/BI060635W REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1.C., FANMEM REMARK 3 AUTHORS : VARIAN, CO (VNMR), VON FREYBERG, B., BRAUN, W., REMARK 3 NOLDE, D.E., VOLYNSKY, P.E., ARSENIEV, A.S., REMARK 3 EFREMOV, R.G. (FANMEM) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: IN TOTAL, 222 DISTANCE AND 123 TORSION REMARK 3 ANGLES CONSTRAINTS WERE USED FOR STRUCTURE CALCULATION REMARK 4 REMARK 4 2G9P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000036864. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318; 318 REMARK 210 PH : 6.8; 6.8 REMARK 210 IONIC STRENGTH : NO SALT; NO SALT REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7 MM LTC2A; 102 MM SDS-D25, REMARK 210 95% H2O, 5% D2O; 1.7 MM LTC2A; REMARK 210 102 MM SDS-D25, 100 % D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY; DRX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1.A, CYANA 1.0.6., REMARK 210 XEASY 40300000, MOLMOL 2K.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED REMARK 210 BY REFINEMENT IN IMPLICIT REMARK 210 MEMBRANE MODEL (WATER/OCTANOL/ REMARK 210 WATER SLAB) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 TECHNIQUES. 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 6 LEU A 2 -55.95 -162.54 REMARK 500 6 ARG A 23 87.43 -169.89 REMARK 500 7 LEU A 2 -56.16 -162.66 REMARK 500 7 ARG A 23 88.40 -169.79 REMARK 500 9 LYS A 25 -71.33 -92.52 REMARK 500 11 LEU A 2 -55.19 -162.41 REMARK 500 11 ARG A 23 83.69 -168.76 REMARK 500 13 LEU A 2 -55.96 -162.66 REMARK 500 13 ARG A 12 29.38 -164.64 REMARK 500 14 ARG A 12 29.75 -164.54 REMARK 500 14 ARG A 23 54.81 -140.50 REMARK 500 16 LEU A 2 -56.84 -161.81 REMARK 500 16 ARG A 12 29.80 -164.56 REMARK 500 16 ARG A 23 77.21 -162.66 REMARK 500 17 ARG A 23 88.54 -169.96 REMARK 500 18 ARG A 23 88.43 -169.68 REMARK 500 19 ARG A 12 32.12 -164.62 REMARK 500 19 ARG A 23 82.10 -165.85 REMARK 500 20 LEU A 2 -55.65 -162.23 REMARK 500 20 ARG A 12 30.19 -164.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF THE PROTEIN HAS NOT BEEN DEPOSITED REMARK 999 INTO ANY SEQUENCE DATABASE. DBREF 2G9P A 1 26 UNP Q1ELU1 Q1ELU1_9ARAC 59 84 SEQRES 1 A 26 GLY LEU PHE GLY LYS LEU ILE LYS LYS PHE GLY ARG LYS SEQRES 2 A 26 ALA ILE SER TYR ALA VAL LYS LYS ALA ARG GLY LYS HIS HELIX 1 1 GLY A 1 GLY A 11 1 11 HELIX 2 2 ARG A 12 ALA A 22 1 11 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 - 9 20 Bytes