Header list of 1ktx.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN(POTASSIUM CHANNEL INHIBITOR) 02-JUN-94 1KTX
TITLE KALIOTOXIN (1-37) SHOWS STRUCTURAL DIFFERENCES WITH RELATED POTASSIUM
TITLE 2 CHANNEL BLOCKERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KALIOTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANDROCTONUS MAURETANICUS MAURETANICUS;
SOURCE 3 ORGANISM_TAXID: 6860;
SOURCE 4 STRAIN: MAURETANICUS
KEYWDS NEUROTOXIN(POTASSIUM CHANNEL INHIBITOR)
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR I.FERNANDEZ,R.ROMI,S.SZENDEFI,M.-F.MARTIN-EAUCLAIRE,H.ROCHAT,J.VAN
AUTHOR 2 RIETSCHTOTEN,M.PONS,E.GIRALT
REVDAT 3 29-NOV-17 1KTX 1 REMARK HELIX
REVDAT 2 24-FEB-09 1KTX 1 VERSN
REVDAT 1 26-JAN-95 1KTX 0
JRNL AUTH I.FERNANDEZ,R.ROMI,S.SZENDEFFY,M.F.MARTIN-EAUCLAIRE,
JRNL AUTH 2 H.ROCHAT,J.VAN RIETSCHOTEN,M.PONS,E.GIRALT
JRNL TITL KALIOTOXIN (1-37) SHOWS STRUCTURAL DIFFERENCES WITH RELATED
JRNL TITL 2 POTASSIUM CHANNEL BLOCKERS.
JRNL REF BIOCHEMISTRY V. 33 14256 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7524673
JRNL DOI 10.1021/BI00251A038
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.CREST,G.JACQUET,M.GOLA,H.ZERROUK,A.BENSLIMANE,H.ROCHAT,
REMARK 1 AUTH 2 P.MANSUELLE,M.-F.MARTIN-EAUCLAIRE
REMARK 1 TITL KALIOTOXIN, A NOVEL PEPTIDYL INHIBITOR OF NEURONAL BK-TYPE
REMARK 1 TITL 2 CA(2+)-ACTIVATED K+ CHANNELS CHARACTERIZED FROM ANDROCTONUS
REMARK 1 TITL 3 MAURETANICUS MAURETANICUS VENOM
REMARK 1 REF J.BIOL.CHEM. V. 267 1640 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KTX 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_1000174494.
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 : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 2 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 3 GLU A 3 CD GLU A 3 OE2 0.118
REMARK 500 3 HIS A 34 CG HIS A 34 CD2 0.054
REMARK 500 4 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 5 GLU A 3 CD GLU A 3 OE2 0.118
REMARK 500 6 GLU A 3 CD GLU A 3 OE2 0.120
REMARK 500 7 GLU A 3 CD GLU A 3 OE2 0.118
REMARK 500 8 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 9 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 10 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500 11 GLU A 3 CD GLU A 3 OE2 0.119
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 CYS A 14 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 1 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ASN A 30 N - CA - CB ANGL. DEV. = 12.4 DEGREES
REMARK 500 1 LYS A 32 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 1 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 HIS A 34 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 2 CYS A 14 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 2 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 ASN A 30 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 2 ASN A 30 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 2 LYS A 32 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 2 LYS A 32 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 2 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 HIS A 34 N - CA - C ANGL. DEV. = -18.8 DEGREES
REMARK 500 3 PRO A 12 CA - N - CD ANGL. DEV. = -10.5 DEGREES
REMARK 500 3 CYS A 14 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 3 LYS A 16 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 3 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 ASN A 30 N - CA - CB ANGL. DEV. = 13.3 DEGREES
REMARK 500 3 ASN A 30 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 3 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 3 HIS A 34 N - CA - C ANGL. DEV. = -22.5 DEGREES
REMARK 500 4 CYS A 14 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 ASN A 30 N - CA - CB ANGL. DEV. = 13.2 DEGREES
REMARK 500 4 LYS A 32 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 4 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 4 HIS A 34 N - CA - C ANGL. DEV. = -20.4 DEGREES
REMARK 500 4 CYS A 35 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 5 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 ASN A 30 N - CA - CB ANGL. DEV. = 13.7 DEGREES
REMARK 500 5 ASN A 30 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 5 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 5 HIS A 34 N - CA - C ANGL. DEV. = -21.6 DEGREES
REMARK 500 5 CYS A 35 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 6 CYS A 14 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500 6 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 6 ASN A 30 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 6 LYS A 32 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 6 HIS A 34 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 6 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 6 HIS A 34 N - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 7 CYS A 14 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 7 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 ASN A 30 N - CA - CB ANGL. DEV. = 14.7 DEGREES
REMARK 500 7 HIS A 34 N - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 8 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 8 ASN A 30 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 8 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 8 HIS A 34 N - CA - C ANGL. DEV. = -21.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS.
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 LYS A 7 79.73 166.46
REMARK 500 1 CYS A 8 92.20 -161.61
REMARK 500 1 SER A 9 67.73 -100.58
REMARK 500 1 SER A 11 -88.90 -40.21
REMARK 500 1 PRO A 12 88.34 -64.95
REMARK 500 1 GLN A 13 -49.66 168.12
REMARK 500 1 CYS A 14 -60.19 -100.33
REMARK 500 1 CYS A 18 50.95 -100.38
REMARK 500 1 ALA A 21 -91.31 -121.75
REMARK 500 1 PHE A 25 -35.27 -178.90
REMARK 500 1 LYS A 27 157.20 45.10
REMARK 500 1 MET A 29 124.79 85.30
REMARK 500 1 ASN A 30 -67.01 96.69
REMARK 500 1 CYS A 33 155.75 -32.41
REMARK 500 2 LYS A 7 106.89 71.29
REMARK 500 2 CYS A 8 83.85 -151.17
REMARK 500 2 SER A 9 70.86 -100.28
REMARK 500 2 SER A 11 -93.38 -40.71
REMARK 500 2 PRO A 12 90.48 -60.94
REMARK 500 2 GLN A 13 -51.14 165.84
REMARK 500 2 CYS A 18 50.72 -101.07
REMARK 500 2 ASP A 20 -35.71 -139.39
REMARK 500 2 ALA A 21 -87.52 -109.31
REMARK 500 2 MET A 23 -70.85 -150.58
REMARK 500 2 PHE A 25 -37.86 -173.73
REMARK 500 2 LYS A 27 159.29 51.90
REMARK 500 2 MET A 29 125.87 77.78
REMARK 500 2 ASN A 30 -72.26 103.65
REMARK 500 2 CYS A 33 154.67 -33.68
REMARK 500 3 LYS A 7 113.43 62.44
REMARK 500 3 CYS A 8 89.45 -152.87
REMARK 500 3 SER A 9 61.70 -100.57
REMARK 500 3 SER A 11 -93.18 -52.13
REMARK 500 3 PRO A 12 89.11 -61.87
REMARK 500 3 GLN A 13 -59.53 174.86
REMARK 500 3 ALA A 21 -87.41 -137.01
REMARK 500 3 MET A 23 -71.14 -145.60
REMARK 500 3 PHE A 25 -20.70 161.75
REMARK 500 3 LYS A 27 160.80 65.11
REMARK 500 3 MET A 29 134.43 87.57
REMARK 500 3 ASN A 30 -72.23 99.85
REMARK 500 3 CYS A 33 150.84 -37.09
REMARK 500 4 LYS A 7 88.39 162.38
REMARK 500 4 CYS A 8 97.46 -163.19
REMARK 500 4 SER A 11 -85.64 -53.57
REMARK 500 4 PRO A 12 88.16 -63.40
REMARK 500 4 GLN A 13 -60.04 173.89
REMARK 500 4 CYS A 18 44.85 -100.16
REMARK 500 4 ALA A 21 -95.71 -112.03
REMARK 500 4 MET A 23 -64.60 -150.26
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
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 3 HIS A 34 0.09 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 38
DBREF 1KTX A 1 37 UNP P24662 SCK1_ANDMA 1 37
SEQRES 1 A 38 GLY VAL GLU ILE ASN VAL LYS CYS SER GLY SER PRO GLN
SEQRES 2 A 38 CYS LEU LYS PRO CYS LYS ASP ALA GLY MET ARG PHE GLY
SEQRES 3 A 38 LYS CYS MET ASN ARG LYS CYS HIS CYS THR PRO NH2
HET NH2 A 38 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 A PRO A 12 PRO A 17 1BENT HELIX 6
HELIX 2 A1 CYS A 18 ASP A 20 5 3
SHEET 1 A 2 PHE A 25 GLY A 26 0
SHEET 2 A 2 HIS A 34 CYS A 35 -1 N HIS A 34 O GLY A 26
SSBOND 1 CYS A 8 CYS A 28 1555 1555 2.01
SSBOND 2 CYS A 14 CYS A 33 1555 1555 2.00
SSBOND 3 CYS A 18 CYS A 35 1555 1555 2.01
LINK C PRO A 37 N NH2 A 38 1555 1555 1.32
SITE 1 AC1 1 PRO A 37
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 - 29 20 Bytes