Header list of 1qky.pdb file
Complete list - 15 20 Bytes
HEADER NEUROTOXIN 17-AUG-99 1QKY
TITLE SOLUTION STRUCTURE OF PI7, A NON TOXIC PEPTIDE ISOLATED FROM THE
TITLE 2 SCORPION PANDINUS IMPERATOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOXIN 7 FROM PANDINUS IMPERATOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PI7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PANDINUS IMPERATOR;
SOURCE 3 ORGANISM_COMMON: SCORPION;
SOURCE 4 ORGANISM_TAXID: 55084;
SOURCE 5 SECRETION: VENOM
KEYWDS NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR M.DELEPIERRE,A.PROCHNICKA-CHALUFOUR,J.BOISBOUVIER,L.D.POSSANI
REVDAT 3 15-JAN-20 1QKY 1 JRNL
REVDAT 2 24-FEB-09 1QKY 1 VERSN
REVDAT 1 03-FEB-00 1QKY 0
JRNL AUTH M.DELEPIERRE,A.PROCHNICKA-CHALUFOUR,J.BOISBOUVIER,
JRNL AUTH 2 L.D.POSSANI
JRNL TITL PI7, AN ORPHAN PEPTIDE FROM THE SCORPION PANDINUS IMPERATOR:
JRNL TITL 2 A 1H-NMR ANALYSIS USING A NANO-NMR PROBE.
JRNL REF BIOCHEMISTRY V. 38 16756 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10606507
JRNL DOI 10.1021/BI991685M
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.OLAMENDI-PORTUGAL,F.GOMEZ-LAGUNAS,G.B.GURROLA,L.D.POSSANI
REMARK 1 TITL TWO SIMILAR PEPTIDES FROM THE VENOM OF THE SCORPION PANDINUS
REMARK 1 TITL 2 IMPERATOR, ONE HIGHLY EFFECTIVE BLOCKER AND THE OTHER
REMARK 1 TITL 3 INACTIVE ON K+ CHANNELS
REMARK 1 REF TOXICON V. 36 759 1998
REMARK 1 REFN ISSN 0041-0101
REMARK 1 PMID 9655636
REMARK 1 DOI 10.1016/S0041-0101(97)00163-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS CALCULATED USING THE
REMARK 3 PROGRAM DYANA. TWENTY FIVE BEST DYANA CONFORMERS WERE SUBMITTED
REMARK 3 TO RESTRAINED ENERGY MINIMIZATION IN A SHELL OF 584 WATER
REMARK 3 MOLECULES USING THE PROGRAM OPAL. COORDINATES FOR THE WATER ARE
REMARK 3 NOT CONTAINED IN THIS ENTRY. FOR FURTHER DETAILS ON THE
REMARK 3 REFINEMENT SEE THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1QKY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1290002937.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 3.5
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, OPAL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION,
REMARK 210 STRUCTURE QUALITY ACCORDING TO
REMARK 210 PROCHECK
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE OF THE NATURAL TOXIN EXTRACTED FROM THE
REMARK 210 SCORPION VENOM WAS DETERMINED BY HOMONUCLEAR NMR AT 500 MHZ FROM
REMARK 210 NANOMOLE AMOUNT OF COMPOUND.
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: 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 5 TYR A 13 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 CYS A 6 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
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 ALA A 3 -160.97 49.44
REMARK 500 1 ILE A 19 -74.92 -91.39
REMARK 500 1 ASN A 24 101.15 -48.76
REMARK 500 1 LYS A 30 4.61 55.30
REMARK 500 2 GLU A 2 -147.90 -142.12
REMARK 500 2 ILE A 19 -76.38 -76.31
REMARK 500 2 ASN A 24 82.75 -68.27
REMARK 500 2 ASN A 29 51.07 36.54
REMARK 500 2 LYS A 30 -2.95 70.33
REMARK 500 3 GLU A 2 62.74 -113.63
REMARK 500 3 ALA A 3 -108.85 42.54
REMARK 500 3 ASN A 24 105.48 -53.59
REMARK 500 3 LYS A 30 -7.25 58.29
REMARK 500 4 GLU A 2 -165.35 -73.29
REMARK 500 4 ALA A 3 98.89 65.59
REMARK 500 4 ILE A 14 -70.11 -58.71
REMARK 500 4 PHE A 23 -146.05 -91.60
REMARK 500 4 ASN A 29 -78.52 59.41
REMARK 500 5 THR A 7 -60.18 -122.46
REMARK 500 5 LYS A 30 1.33 55.03
REMARK 500 6 ALA A 3 146.40 -175.92
REMARK 500 6 ASP A 11 -74.95 -68.92
REMARK 500 6 PHE A 23 -151.92 -91.16
REMARK 500 6 LYS A 30 -12.16 58.62
REMARK 500 6 TYR A 35 -105.97 -129.66
REMARK 500 7 ILE A 19 -76.44 -92.00
REMARK 500 7 LYS A 30 -4.13 60.49
REMARK 500 8 ILE A 19 -75.48 -91.08
REMARK 500 8 LYS A 30 9.02 59.70
REMARK 500 8 TYR A 35 43.81 -146.88
REMARK 500 9 CYS A 12 7.25 -67.49
REMARK 500 9 ASN A 24 67.84 125.00
REMARK 500 9 ASN A 29 59.53 34.53
REMARK 500 9 LYS A 30 -5.07 62.23
REMARK 500 10 GLU A 2 4.66 -164.01
REMARK 500 10 ASN A 24 98.80 -66.16
REMARK 500 10 LYS A 30 6.78 56.22
REMARK 500 11 ALA A 3 -132.57 48.32
REMARK 500 11 ILE A 14 -76.70 -71.25
REMARK 500 11 PHE A 23 16.24 -66.75
REMARK 500 11 ASN A 29 58.63 39.21
REMARK 500 11 LYS A 30 5.21 58.14
REMARK 500 11 CYS A 37 -10.08 -142.70
REMARK 500 12 ILE A 14 -77.72 -83.28
REMARK 500 12 LYS A 30 1.28 56.24
REMARK 500 13 GLU A 2 45.29 -151.95
REMARK 500 13 ASN A 24 85.53 -151.96
REMARK 500 13 LYS A 30 3.79 59.25
REMARK 500 14 PHE A 23 28.93 -72.28
REMARK 500 14 ASN A 29 -73.03 53.19
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 1 ARG A 5 0.10 SIDE CHAIN
REMARK 500 2 ARG A 17 0.09 SIDE CHAIN
REMARK 500 9 TYR A 13 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4427 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PEPTIDE STUDIED HERE IS RELATED IN SEQUENCE TO THE
REMARK 999 POTASSIUM CHANNEL BLOCKING TOXINS, HOWEVER THE ALIGNMENT
REMARK 999 IS ONLY 60 PERCENT FOR THE PEPTIDES:
REMARK 999 SCKA_PANIM P55927 (47 AA)
REMARK 999 SCKB_PANIM P55928 (35 AA)
REMARK 999 SCKG_PANIM Q10726 (35 AA)
REMARK 999
REMARK 999 1QKY DEAIRCTGTKDCYIPCRYITGCFNSRCINKSCKCYGCT
REMARK 999 SCKA_PANIM: RGSVDYKDDDDKTISCTNPKQCYPHCKKETGYPNAKCMNRKCKCFGR
REMARK 999 SCKB_PANIM: TISCTNEKQCYPHCKKETGYPNAKCMNRKCKCFGR
REMARK 999 SCKG_PANIM LVKCRGTSDCGRPCQQQTGCPNSKCINRMCKCYGC
REMARK 999 * * * * * *
DBREF 1QKY A 1 38 PDB 1QKY 1QKY 1 38
SEQRES 1 A 38 ASP GLU ALA ILE ARG CYS THR GLY THR LYS ASP CYS TYR
SEQRES 2 A 38 ILE PRO CYS ARG TYR ILE THR GLY CYS PHE ASN SER ARG
SEQRES 3 A 38 CYS ILE ASN LYS SER CYS LYS CYS TYR GLY CYS THR
HELIX 1 1 GLY A 8 THR A 20 1 13
SHEET 1 A 2 SER A 25 ILE A 28 0
SHEET 2 A 2 SER A 31 CYS A 34 -1 N LYS A 33 O ARG A 26
SSBOND 1 CYS A 6 CYS A 27 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 32 1555 1555 2.04
SSBOND 3 CYS A 16 CYS A 34 1555 1555 2.03
SSBOND 4 CYS A 22 CYS A 37 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 - 15 20 Bytes