Header list of 1wxn.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 27-JAN-05 1WXN TITLE SOLUTION STRUCTURE OF APETX2, A SPECIFIC PEPTIDE INHIBITOR OF ASIC3 TITLE 2 PROTON-GATED CHANNELS COMPND MOL_ID: 1; COMPND 2 MOLECULE: TOXIN APETX2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ANTHOPLEURA ELEGANTISSIMA TOXIN 2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANTHOPLEURA ELEGANTISSIMA; SOURCE 3 ORGANISM_COMMON: CLONAL ANEMONE; SOURCE 4 ORGANISM_TAXID: 6110 KEYWDS APETX2, ANTHOPLEURA ELEGANTISSIMA TOXIN 2, ASIC, ACID-SENSING ION KEYWDS 2 CHANNEL, TOXIN EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR B.CHAGOT,P.ESCOUBAS,S.DIOCHOT,C.BERNARD,M.LAZDUNSKI,H.DARBON REVDAT 3 02-MAR-22 1WXN 1 REMARK REVDAT 2 24-FEB-09 1WXN 1 VERSN REVDAT 1 16-AUG-05 1WXN 0 JRNL AUTH B.CHAGOT,P.ESCOUBAS,S.DIOCHOT,C.BERNARD,M.LAZDUNSKI,H.DARBON JRNL TITL SOLUTION STRUCTURE OF APETX2, A SPECIFIC PEPTIDE INHIBITOR JRNL TITL 2 OF ASIC3 PROTON-GATED CHANNELS JRNL REF PROTEIN SCI. V. 14 2003 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15987885 JRNL DOI 10.1110/PS.051378905 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.2 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WXN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000024123. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1.32MM APETX2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13, ARIA REMARK 210 1.2 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY, STRUCTURES WITH THE REMARK 210 LEAST RESTRAINT VIOLATIONS 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 1 TYR A 16 16.64 58.68 REMARK 500 1 PRO A 40 -105.44 -92.50 REMARK 500 1 ALA A 41 56.83 -160.24 REMARK 500 2 TYR A 16 76.27 54.39 REMARK 500 2 PRO A 21 74.19 -68.67 REMARK 500 2 PRO A 40 -98.44 -90.85 REMARK 500 2 ALA A 41 21.96 -153.96 REMARK 500 3 TYR A 16 78.63 51.60 REMARK 500 3 ARG A 24 33.57 -94.57 REMARK 500 3 PRO A 40 -93.34 -97.49 REMARK 500 3 ALA A 41 57.10 -157.62 REMARK 500 4 PRO A 40 -90.63 -95.39 REMARK 500 4 ALA A 41 50.90 -168.25 REMARK 500 5 TYR A 16 86.88 67.45 REMARK 500 5 THR A 22 29.18 -79.03 REMARK 500 5 PRO A 40 -94.68 -92.89 REMARK 500 5 ALA A 41 17.19 -151.06 REMARK 500 6 TYR A 16 77.96 62.36 REMARK 500 6 PRO A 40 -94.69 -98.98 REMARK 500 6 ALA A 41 45.50 -152.72 REMARK 500 7 TYR A 16 73.99 53.99 REMARK 500 7 PRO A 21 92.67 -62.42 REMARK 500 7 PRO A 40 -79.83 -97.14 REMARK 500 7 ALA A 41 43.08 -176.56 REMARK 500 8 TYR A 16 76.04 58.10 REMARK 500 8 PRO A 40 -90.33 -96.70 REMARK 500 8 ALA A 41 31.61 -163.85 REMARK 500 9 PRO A 21 98.12 -65.18 REMARK 500 9 PRO A 40 -90.11 -97.27 REMARK 500 9 ALA A 41 32.53 -157.24 REMARK 500 10 TYR A 16 64.43 63.52 REMARK 500 10 PRO A 21 108.85 -42.40 REMARK 500 10 PRO A 40 -93.60 -92.41 REMARK 500 10 ALA A 41 49.50 -163.64 REMARK 500 11 TYR A 16 74.46 58.73 REMARK 500 11 PRO A 21 90.24 -69.55 REMARK 500 11 PRO A 40 -95.14 -90.10 REMARK 500 11 ALA A 41 40.91 -154.60 REMARK 500 12 SER A 19 79.69 -152.77 REMARK 500 12 PRO A 40 -97.85 -97.97 REMARK 500 12 ALA A 41 38.43 -169.59 REMARK 500 13 PRO A 40 -77.49 -93.13 REMARK 500 13 ALA A 41 33.84 -177.89 REMARK 500 14 CYS A 6 75.05 -119.25 REMARK 500 14 ARG A 24 30.26 -94.33 REMARK 500 14 PRO A 40 -94.55 -99.11 REMARK 500 14 ALA A 41 48.46 -151.40 REMARK 500 15 TYR A 16 25.69 43.11 REMARK 500 15 PRO A 18 34.51 -83.49 REMARK 500 15 PRO A 40 -102.00 -98.79 REMARK 500 REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1WXN A 1 42 UNP P61542 APT2_ANTEL 1 42 SEQRES 1 A 42 GLY THR ALA CYS SER CYS GLY ASN SER LYS GLY ILE TYR SEQRES 2 A 42 TRP PHE TYR ARG PRO SER CYS PRO THR ASP ARG GLY TYR SEQRES 3 A 42 THR GLY SER CYS ARG TYR PHE LEU GLY THR CYS CYS THR SEQRES 4 A 42 PRO ALA ASP HELIX 1 1 PRO A 21 GLY A 25 5 5 SHEET 1 A 4 ALA A 3 CYS A 6 0 SHEET 2 A 4 SER A 9 PHE A 15 -1 O GLY A 11 N CYS A 4 SHEET 3 A 4 GLY A 35 THR A 39 -1 O THR A 36 N TRP A 14 SHEET 4 A 4 GLY A 28 TYR A 32 -1 N CYS A 30 O CYS A 37 SSBOND 1 CYS A 4 CYS A 37 1555 1555 2.03 SSBOND 2 CYS A 6 CYS A 30 1555 1555 2.03 SSBOND 3 CYS A 20 CYS A 38 1555 1555 2.03 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 - r 2 2 Bytes