Header list of 1pe4.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 21-MAY-03 1PE4
TITLE SOLUTION STRUCTURE OF TOXIN CN12 FROM CENTRUROIDES NOXIUS ALFA
TITLE 2 SCORPION TOXIN ACTING ON SODIUM CHANNELS. NMR STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN CN11;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CN12
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CENTRUROIDES NOXIUS;
SOURCE 3 ORGANISM_COMMON: MEXICAN SCORPION;
SOURCE 4 ORGANISM_TAXID: 6878;
SOURCE 5 SECRETION: VENOM;
SOURCE 6 OTHER_DETAILS: TOXIN OBTAINED DIRECTLY FROM VENOM OF CENTRUROIDES
SOURCE 7 NOXIUS. ACTIVITY IS VERY LOW, HOWEVER CN12 HAS SOME REQUIREMENTS FOR
SOURCE 8 BEING A VERY ACTIVE TOXIN.
KEYWDS TOXIN, SCORPION TOXIN, CENTRUROIDES NOXIUS, SODIUM CHANNELS ALPHA
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 19
MDLTYP MINIMIZED AVERAGE
AUTHOR F.DEL RIO-PORTILLA,E.HERNANDEZ-MARIN,G.PIMIENTA,F.V.CORONAS,
AUTHOR 2 F.Z.ZAMUDIO,R.C.RODRGUEZ DE LA VEGA,E.WANKE,L.D.POSSANI
REVDAT 4 23-FEB-22 1PE4 1 REMARK
REVDAT 3 24-FEB-09 1PE4 1 VERSN
REVDAT 2 10-AUG-04 1PE4 1 JRNL
REVDAT 1 25-MAY-04 1PE4 0
JRNL AUTH F.DEL RIO-PORTILLA,E.HERNANDEZ-MARIN,G.PIMIENTA,F.V.CORONAS,
JRNL AUTH 2 F.Z.ZAMUDIO,R.C.RODRGUEZ DE LA VEGA,E.WANKE,L.D.POSSANI
JRNL TITL NMR SOLUTION STRUCTURE OF CN12, A NOVEL PEPTIDE FROM THE
JRNL TITL 2 MEXICAN SCORPION CENTRUROIDES NOXIUS WITH A TYPICAL
JRNL TITL 3 BETA-TOXIN SEQUENCE BUT WITH ALPHA-LIKE PHYSIOLOGICAL
JRNL TITL 4 ACTIVITY.
JRNL REF EUR.J.BIOCHEM. V. 271 2504 2004
JRNL REFN ISSN 0014-2956
JRNL PMID 15182366
JRNL DOI 10.1111/J.1432-1033.2004.04181.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE JOURNAL REFERENCE
REMARK 4
REMARK 4 1PE4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019265.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 3.1; 3.1
REMARK 210 IONIC STRENGTH : NONE; NONE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM IN H2O/D2O 90:10%;; 0.6
REMARK 210 MM IN 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF COSY, 2D TOCSY, AND 2D
REMARK 210 NOSEY; DQF-COSY, 2D TOCSY, AND
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, VNMR 6.1C
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 250
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO RESTRAINT VIOLATIONS LESS
REMARK 210 THAN 0.2 ANGSTROMS AND MIMINUM
REMARK 210 ENERGY LESS THAN 115.0 KCAL/MOL
REMARK 210 BEST REPRESENTATIVE CONFORMER IN
REMARK 210 THIS ENSEMBLE: 1
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR 1H-1H 2D
REMARK 210 NMR ON THE NATURAL TOXIN EXTRACTED FROM THE SCORPION VENOM
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 CYS A 11 149.36 -176.26
REMARK 500 1 LYS A 12 -70.65 -94.89
REMARK 500 1 PHE A 13 -154.28 -116.05
REMARK 500 1 CYS A 15 109.19 59.10
REMARK 500 1 SER A 16 111.64 -162.04
REMARK 500 1 ASN A 22 54.34 -117.25
REMARK 500 1 LYS A 31 -73.13 -103.58
REMARK 500 1 ASP A 36 32.06 -99.56
REMARK 500 1 TYR A 41 -57.92 -124.15
REMARK 500 1 ALA A 42 -148.12 -96.14
REMARK 500 1 THR A 54 -175.56 -60.75
REMARK 500 1 LEU A 56 85.93 -162.54
REMARK 500 1 TRP A 57 24.79 -146.20
REMARK 500 1 ASP A 59 -107.33 -94.45
REMARK 500 1 CYS A 65 -95.95 -56.23
REMARK 500 2 LEU A 6 85.13 42.96
REMARK 500 2 ALA A 7 -81.09 -38.91
REMARK 500 2 SER A 8 -161.28 -59.91
REMARK 500 2 LYS A 12 -82.26 -119.85
REMARK 500 2 CYS A 15 28.70 -179.86
REMARK 500 2 ASN A 22 59.09 -176.10
REMARK 500 2 PRO A 23 36.00 -86.60
REMARK 500 2 ASN A 26 -70.88 -61.86
REMARK 500 2 ASP A 36 -70.47 -173.41
REMARK 500 2 TYR A 41 -57.61 -123.84
REMARK 500 2 ALA A 42 -150.01 -91.37
REMARK 500 2 HIS A 49 67.84 65.53
REMARK 500 2 VAL A 50 -43.55 -156.87
REMARK 500 2 GLU A 52 30.27 -84.66
REMARK 500 2 TRP A 57 27.96 -158.87
REMARK 500 2 ASP A 59 -119.22 -94.31
REMARK 500 2 THR A 62 -175.29 -62.86
REMARK 500 2 CYS A 65 -155.12 -57.06
REMARK 500 2 ARG A 66 87.86 -62.57
REMARK 500 3 ASP A 2 170.64 -48.93
REMARK 500 3 ALA A 7 -95.81 -17.51
REMARK 500 3 SER A 8 -149.42 -63.39
REMARK 500 3 CYS A 11 121.71 -171.78
REMARK 500 3 LYS A 12 -80.38 -116.00
REMARK 500 3 PHE A 13 -163.15 -107.04
REMARK 500 3 CYS A 15 127.24 60.35
REMARK 500 3 SER A 16 -179.13 179.27
REMARK 500 3 ASN A 21 -138.42 -81.71
REMARK 500 3 LYS A 31 -66.13 -103.88
REMARK 500 3 TYR A 41 -95.33 -123.67
REMARK 500 3 ALA A 42 -116.75 -97.01
REMARK 500 3 TRP A 57 80.76 -160.82
REMARK 500 3 ASP A 59 -151.53 -94.45
REMARK 500 3 SER A 60 -75.84 -74.16
REMARK 500 3 CYS A 65 173.50 54.98
REMARK 500
REMARK 500 THIS ENTRY HAS 347 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CN2 RELATED DB: PDB
REMARK 900 SAME SECONDARY STRUCTURE AS NA+ CHANNEL TOXINS.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AT THE TIME OF PROCESSING, NO REFERENCE
REMARK 999 DATABASE SEQUENCE FOR THIS PROTEIN WAS
REMARK 999 AVAILABLE.
DBREF 1PE4 A 1 67 UNP P63019 SCX12_CENNO 1 67
SEQRES 1 A 67 ARG ASP GLY TYR PRO LEU ALA SER ASN GLY CYS LYS PHE
SEQRES 2 A 67 GLY CYS SER GLY LEU GLY GLU ASN ASN PRO THR CYS ASN
SEQRES 3 A 67 HIS VAL CYS GLU LYS LYS ALA GLY SER ASP TYR GLY TYR
SEQRES 4 A 67 CYS TYR ALA TRP THR CYS TYR CYS GLU HIS VAL ALA GLU
SEQRES 5 A 67 GLY THR VAL LEU TRP GLY ASP SER GLY THR GLY PRO CYS
SEQRES 6 A 67 ARG SER
HELIX 1 1 THR A 24 LYS A 32 1 9
SHEET 1 A 3 ASP A 2 GLY A 3 0
SHEET 2 A 3 TYR A 46 GLU A 48 -1 O CYS A 47 N GLY A 3
SHEET 3 A 3 GLY A 38 TYR A 39 -1 N TYR A 39 O TYR A 46
SSBOND 1 CYS A 11 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 15 CYS A 40 1555 1555 2.03
SSBOND 3 CYS A 25 CYS A 45 1555 1555 2.03
SSBOND 4 CYS A 29 CYS A 47 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 - b 23 2 Bytes