Header list of 1wpd.pdb file
Complete list - 18 20 Bytes
HEADER TOXIN 01-SEP-04 1WPD TITLE EVIDENCE FOR DOMAIN-SPECIFIC RECOGNITION OF SK AND KV CHANNELS BY MTX TITLE 2 AND HSTX1 SCORPION TOXINS COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTASSIUM CHANNEL TOXIN ALPHA-KTX 6.2,POTASSIUM CHANNEL COMPND 3 TOXIN ALPHA-KTX 6.3; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: MAUROTOXIN,MTX,NEUROTOXIN HSTX1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCORPIO PALMATUS, HETEROMETRUS SPINIFER; SOURCE 3 ORGANISM_COMMON: ISRAELI GOLDEN SCORPION, ASIA GIANT FOREST SOURCE 4 SCORPION; SOURCE 5 ORGANISM_TAXID: 1662106, 118530; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS NEUROTOXIN, CHIMERA, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR I.REGAYA,C.BEETON,G.FERRAT,N.ANDREOTTI,G.K.CHANDY,H.DARBON,M.DE AUTHOR 2 WAARD,J.M.SABATIER REVDAT 4 18-DEC-19 1WPD 1 COMPND SOURCE REMARK DBREF REVDAT 3 24-FEB-09 1WPD 1 VERSN REVDAT 2 25-JAN-05 1WPD 1 JRNL REVDAT 1 19-OCT-04 1WPD 0 JRNL AUTH I.REGAYA,C.BEETON,G.FERRAT,N.ANDREOTTI,H.DARBON,M.DE WAARD, JRNL AUTH 2 J.M.SABATIER JRNL TITL EVIDENCE FOR DOMAIN-SPECIFIC RECOGNITION OF SK AND KV JRNL TITL 2 CHANNELS BY MTX AND HSTX1 SCORPION TOXINS JRNL REF J.BIOL.CHEM. V. 279 55690 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15498765 JRNL DOI 10.1074/JBC.M410055200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.0, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WPD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-04. REMARK 100 THE DEPOSITION ID IS D_1000023846. 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 : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, DIANA 2.8 REMARK 210 METHOD USED : DISTANCE GEOMETRY, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS 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 THR A 4 31.04 -164.07 REMARK 500 1 SER A 6 -158.18 -163.83 REMARK 500 1 ASP A 8 75.22 84.96 REMARK 500 1 CYS A 9 -65.61 -95.98 REMARK 500 1 CYS A 19 146.96 -25.13 REMARK 500 1 ASN A 26 -169.94 50.55 REMARK 500 1 ARG A 27 8.62 -64.47 REMARK 500 1 LYS A 30 85.27 172.07 REMARK 500 1 CYS A 31 170.84 -39.94 REMARK 500 2 SER A 2 139.42 -176.57 REMARK 500 2 THR A 4 33.76 -167.89 REMARK 500 2 SER A 6 -135.09 59.70 REMARK 500 2 ASP A 8 64.09 69.24 REMARK 500 2 CYS A 9 -68.15 -95.78 REMARK 500 2 CYS A 19 140.10 -23.01 REMARK 500 2 LYS A 28 93.04 174.02 REMARK 500 2 LYS A 30 83.83 168.87 REMARK 500 2 CYS A 31 172.18 -37.05 REMARK 500 3 SER A 2 139.88 -177.14 REMARK 500 3 THR A 4 40.08 -148.21 REMARK 500 3 SER A 6 -168.71 56.24 REMARK 500 3 ASP A 8 53.85 -179.78 REMARK 500 3 CYS A 9 -62.27 -105.73 REMARK 500 3 CYS A 19 147.16 -27.73 REMARK 500 3 LYS A 28 93.10 173.27 REMARK 500 3 LYS A 30 90.11 163.96 REMARK 500 3 CYS A 31 174.30 -40.31 REMARK 500 4 SER A 2 121.40 62.91 REMARK 500 4 CYS A 3 -179.82 61.25 REMARK 500 4 THR A 4 56.29 -99.93 REMARK 500 4 LYS A 7 -79.81 -154.84 REMARK 500 4 ALA A 11 -70.46 -71.22 REMARK 500 4 CYS A 19 147.14 -27.54 REMARK 500 4 PRO A 20 0.13 -68.87 REMARK 500 4 LYS A 28 97.75 176.19 REMARK 500 4 LYS A 30 81.41 173.84 REMARK 500 4 CYS A 31 171.37 -40.79 REMARK 500 4 ASN A 32 -169.65 -109.19 REMARK 500 5 SER A 2 140.13 63.60 REMARK 500 5 SER A 6 -137.96 -163.88 REMARK 500 5 LYS A 7 28.94 46.04 REMARK 500 5 ALA A 11 -70.12 -70.74 REMARK 500 5 CYS A 19 168.99 43.95 REMARK 500 5 LYS A 28 98.06 169.67 REMARK 500 5 LYS A 30 79.77 175.32 REMARK 500 5 CYS A 31 171.42 -38.14 REMARK 500 6 CYS A 9 -72.29 -104.48 REMARK 500 6 ALA A 11 -71.39 -71.73 REMARK 500 6 CYS A 19 137.84 -21.87 REMARK 500 6 LYS A 28 99.66 173.13 REMARK 500 REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1WPD A 1 20 UNP P80719 KAX62_SCOPA 1 20 DBREF 1WPD A 21 34 UNP P59867 KAX63_HETSP 21 34 SEQRES 1 A 34 VAL SER CYS THR GLY SER LYS ASP CYS TYR ALA PRO CYS SEQRES 2 A 34 ARG LYS GLN THR GLY CYS PRO TYR GLY LYS CYS MET ASN SEQRES 3 A 34 ARG LYS CYS LYS CYS ASN ARG CYS HELIX 1 1 CYS A 9 GLY A 18 1 10 SSBOND 1 CYS A 3 CYS A 24 1555 1555 2.03 SSBOND 2 CYS A 9 CYS A 29 1555 1555 2.03 SSBOND 3 CYS A 13 CYS A 31 1555 1555 2.03 SSBOND 4 CYS A 19 CYS A 34 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 - 18 20 Bytes