Header list of 1cn2.pdb file
Complete list - b 16 2 Bytes
HEADER NEUROTOXIN 21-JUN-98 1CN2
TITLE SOLUTION STRUCTURE OF TOXIN 2 FROM CENTRUROIDES NOXIUS HOFFMANN, A
TITLE 2 BETA SCORPION NEUROTOXIN ACTING ON SODIUM CHANNELS, NMR, 15
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOXIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CN2
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
KEYWDS NEUROTOXIN, SCORPION TOXIN, CENTRUROIDES NOXIUS, SODIUM CHANNELS
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR A.PINTAR,L.D.POSSANI,M.DELEPIERRE
REVDAT 3 16-FEB-22 1CN2 1 REMARK LINK
REVDAT 2 24-FEB-09 1CN2 1 VERSN
REVDAT 1 13-JAN-99 1CN2 0
JRNL AUTH A.PINTAR,L.D.POSSANI,M.DELEPIERRE
JRNL TITL SOLUTION STRUCTURE OF TOXIN 2 FROM CENTRUROIDES NOXIUS
JRNL TITL 2 HOFFMANN, A BETA-SCORPION NEUROTOXIN ACTING ON SODIUM
JRNL TITL 3 CHANNELS.
JRNL REF J.MOL.BIOL. V. 287 359 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10080898
JRNL DOI 10.1006/JMBI.1999.2611
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.VAZQUEZ,J.V.TAPIA,W.K.ELIASON,B.M.MARTIN,F.LEBRETON,
REMARK 1 AUTH 2 M.DELEPIERRE,L.D.POSSANI,B.BECERRIL
REMARK 1 TITL CLONING AND CHARACTERIZATION OF THE CDNAS ENCODING NA+
REMARK 1 TITL 2 CHANNEL-SPECIFIC TOXINS 1 AND 2 OF THE SCORPION CENTRUROIDES
REMARK 1 TITL 3 NOXIUS HOFFMANN
REMARK 1 REF TOXICON V. 33 1161 1995
REMARK 1 REFN ISSN 0041-0101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : VON FREYBERG,SCHAUMANN,BRAU
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE JRNL CITATION
REMARK 4
REMARK 4 1CN2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172404.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS
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: 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 ASN A 9 -77.90 -88.83
REMARK 500 1 LEU A 17 -149.32 -80.83
REMARK 500 1 ASN A 22 40.34 -88.74
REMARK 500 1 GLN A 31 46.07 -105.70
REMARK 500 1 GLN A 32 -40.18 -159.86
REMARK 500 1 ALA A 43 89.11 -52.85
REMARK 500 1 THR A 49 64.09 -154.99
REMARK 500 1 HIS A 50 31.87 -176.23
REMARK 500 1 GLN A 54 31.47 -92.15
REMARK 500 1 PRO A 59 -167.43 -75.04
REMARK 500 1 LYS A 63 67.43 -169.52
REMARK 500 2 ASN A 9 -77.88 -76.94
REMARK 500 2 LYS A 13 89.23 73.23
REMARK 500 2 LYS A 18 144.48 69.61
REMARK 500 2 ASP A 23 -66.41 -107.03
REMARK 500 2 GLN A 31 56.19 -107.40
REMARK 500 2 GLN A 32 -24.45 -177.67
REMARK 500 2 TYR A 33 47.04 -107.18
REMARK 500 2 ALA A 43 86.21 -54.73
REMARK 500 2 THR A 49 34.17 -148.70
REMARK 500 2 HIS A 50 34.30 -155.10
REMARK 500 2 TYR A 52 -167.78 -108.99
REMARK 500 2 GLN A 54 34.82 -93.73
REMARK 500 2 LYS A 63 64.50 -168.72
REMARK 500 3 ASN A 9 -78.50 -71.94
REMARK 500 3 CYS A 12 -169.68 -102.92
REMARK 500 3 LYS A 13 176.70 69.76
REMARK 500 3 TYR A 14 89.25 48.79
REMARK 500 3 GLU A 15 75.00 -158.27
REMARK 500 3 LYS A 18 77.41 61.51
REMARK 500 3 ASP A 21 95.90 -68.54
REMARK 500 3 ASN A 22 57.27 -96.09
REMARK 500 3 ASP A 23 -68.78 -106.01
REMARK 500 3 GLN A 31 48.26 -107.43
REMARK 500 3 GLN A 32 -34.06 -167.56
REMARK 500 3 TYR A 42 -158.06 -81.50
REMARK 500 3 ALA A 43 82.94 -52.44
REMARK 500 3 THR A 49 47.99 -148.69
REMARK 500 3 HIS A 50 60.83 -167.32
REMARK 500 3 PRO A 59 -164.71 -75.06
REMARK 500 3 LYS A 63 113.39 -160.11
REMARK 500 4 ASN A 9 -69.98 -92.08
REMARK 500 4 CYS A 12 -84.31 -101.74
REMARK 500 4 LYS A 13 -90.05 58.49
REMARK 500 4 TYR A 14 -70.56 -21.77
REMARK 500 4 GLU A 15 66.68 29.02
REMARK 500 4 ASN A 22 38.86 -94.65
REMARK 500 4 GLN A 31 46.92 -92.16
REMARK 500 4 GLN A 32 -39.08 -167.99
REMARK 500 4 ALA A 43 87.60 -52.63
REMARK 500
REMARK 500 THIS ENTRY HAS 194 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 5 VAL A 6 2 -147.76
REMARK 500 CYS A 12 LYS A 13 2 142.22
REMARK 500 GLN A 31 GLN A 32 2 144.99
REMARK 500 GLU A 15 CYS A 16 3 -149.21
REMARK 500 TYR A 33 GLY A 34 3 147.52
REMARK 500 PHE A 44 ALA A 45 3 124.04
REMARK 500 LYS A 13 TYR A 14 4 -148.63
REMARK 500 THR A 49 HIS A 50 4 149.29
REMARK 500 LYS A 13 TYR A 14 5 -130.98
REMARK 500 ALA A 45 CYS A 46 5 -149.57
REMARK 500 PRO A 61 ASN A 62 5 -141.57
REMARK 500 GLN A 31 GLN A 32 6 149.36
REMARK 500 CYS A 16 LEU A 17 8 -143.81
REMARK 500 TYR A 33 GLY A 34 8 145.54
REMARK 500 LEU A 60 PRO A 61 9 -147.56
REMARK 500 GLN A 31 GLN A 32 11 146.49
REMARK 500 GLN A 54 ALA A 55 15 146.44
REMARK 500 ALA A 55 ILE A 56 15 143.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 64 0.08 SIDE CHAIN
REMARK 500 2 ARG A 27 0.08 SIDE CHAIN
REMARK 500 3 ARG A 27 0.10 SIDE CHAIN
REMARK 500 4 ARG A 27 0.09 SIDE CHAIN
REMARK 500 6 ARG A 64 0.08 SIDE CHAIN
REMARK 500 8 ARG A 27 0.11 SIDE CHAIN
REMARK 500 10 ARG A 27 0.16 SIDE CHAIN
REMARK 500 14 ARG A 64 0.10 SIDE CHAIN
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 67
DBREF 1CN2 A 1 66 UNP P01495 SCX2_CENNO 17 82
SEQRES 1 A 67 LYS GLU GLY TYR LEU VAL ASP LYS ASN THR GLY CYS LYS
SEQRES 2 A 67 TYR GLU CYS LEU LYS LEU GLY ASP ASN ASP TYR CYS LEU
SEQRES 3 A 67 ARG GLU CYS LYS GLN GLN TYR GLY LYS GLY ALA GLY GLY
SEQRES 4 A 67 TYR CYS TYR ALA PHE ALA CYS TRP CYS THR HIS LEU TYR
SEQRES 5 A 67 GLU GLN ALA ILE VAL TRP PRO LEU PRO ASN LYS ARG CYS
SEQRES 6 A 67 SER NH2
HET NH2 A 67 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 TYR A 24 LYS A 30 1 7
SHEET 1 A 1 GLY A 3 TYR A 4 0
SHEET 1 B 2 GLY A 39 TYR A 42 0
SHEET 2 B 2 ALA A 45 CYS A 48 -1 N TRP A 47 O TYR A 40
SSBOND 1 CYS A 12 CYS A 65 1555 1555 2.01
SSBOND 2 CYS A 16 CYS A 41 1555 1555 2.09
SSBOND 3 CYS A 25 CYS A 46 1555 1555 1.97
SSBOND 4 CYS A 29 CYS A 48 1555 1555 2.02
LINK C SER A 66 N NH2 A 67 1555 1555 1.33
CISPEP 1 TRP A 58 PRO A 59 1 -16.20
CISPEP 2 TRP A 58 PRO A 59 2 -23.32
CISPEP 3 TRP A 58 PRO A 59 3 -23.33
CISPEP 4 TRP A 58 PRO A 59 4 -29.44
CISPEP 5 TRP A 58 PRO A 59 5 -14.77
CISPEP 6 TRP A 58 PRO A 59 6 -14.64
CISPEP 7 TRP A 58 PRO A 59 7 -16.08
CISPEP 8 TRP A 58 PRO A 59 8 -13.06
CISPEP 9 TRP A 58 PRO A 59 9 -15.43
CISPEP 10 TRP A 58 PRO A 59 10 -14.54
CISPEP 11 TRP A 58 PRO A 59 11 -16.78
CISPEP 12 TRP A 58 PRO A 59 12 -18.75
CISPEP 13 TRP A 58 PRO A 59 13 -12.95
CISPEP 14 TRP A 58 PRO A 59 14 -16.97
CISPEP 15 TRP A 58 PRO A 59 15 -18.50
SITE 1 AC1 2 CYS A 65 SER A 66
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 16 2 Bytes