Header list of 1hp2.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 12-DEC-00 1HP2
TITLE SOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS
TITLE 2 (TSTX-K ALPHA) DETERMINED BY NMR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TITYUSTOXIN K ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TSTX-K ALPHA, TSK4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TITYUS SERRULATUS;
SOURCE 3 ORGANISM_COMMON: BRAZILIAN SCORPION;
SOURCE 4 ORGANISM_TAXID: 6887;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS K+ CHANNEL, SCORPION TOXIN, ALPHA-K TOXIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR K.C.ELLIS,T.C.TENENHOLZ,W.F.GILLY,M.P.BLAUSTEIN,D.J.WEBER
REVDAT 3 23-FEB-22 1HP2 1 REMARK
REVDAT 2 24-FEB-09 1HP2 1 VERSN
REVDAT 1 13-JUN-01 1HP2 0
JRNL AUTH K.C.ELLIS,T.C.TENENHOLZ,H.JERNG,M.HAYHURST,C.S.DUDLAK,
JRNL AUTH 2 W.F.GILLY,M.P.BLAUSTEIN,D.J.WEBER
JRNL TITL INTERACTION OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS
JRNL TITL 2 WITH A CLONED K+ CHANNEL FROM SQUID (SQKV1A).
JRNL REF BIOCHEMISTRY V. 40 5942 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11352729
JRNL DOI 10.1021/BI010173G
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.P.BLAUSTEIN,R.S.ROGOWSKI,M.J.SCHNEIDER,B.K.KRUEGER
REMARK 1 TITL POLYPEPTIDE TOXINS FROM THE VENOMS OF OLD WORLD AND NEW
REMARK 1 TITL 2 WORLD SCORPIONS PREFERENTIALLY BLOCK DIFFERENT POTASSIUM
REMARK 1 TITL 3 CHANNELS
REMARK 1 REF MOL.PHARMACOL. V. 40 932 1991
REMARK 1 REFN ISSN 0026-895X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THESE STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 569 NOE DISTANCE CONTRAINTS, 13 DIHEDRAL ANGLE RESTRAINTS,
REMARK 3 AND 16 PHI ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1HP2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012493.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 305; 300; 295; 290
REMARK 210 PH : 3.50; 3.50; 3.50; 3.50; 3.50
REMARK 210 IONIC STRENGTH : 1.44; 1.44; 1.44; 1.44; 1.44
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM; 1
REMARK 210 ATM
REMARK 210 SAMPLE CONTENTS : 4.53 MM TSTX-KA 2.2 MM D11-TRIS
REMARK 210 0.1 MM EDTA 0.35 MM NAN3; 4.53
REMARK 210 MM TSTX-KA 2.2 MM D11-TRIS 0.1
REMARK 210 MM EDTA 0.35 MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY;
REMARK 210 ROESY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851, XWINNMR, NMRPIPE
REMARK 210 1.7, FELIX
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 25
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 ALA A 5 104.64 -44.25
REMARK 500 1 LYS A 6 88.71 -55.02
REMARK 500 2 LYS A 6 80.02 -58.65
REMARK 500 2 ALA A 24 77.79 -65.53
REMARK 500 2 ASN A 30 23.81 48.77
REMARK 500 3 ALA A 5 94.79 -43.00
REMARK 500 3 LYS A 6 91.04 -47.57
REMARK 500 3 LYS A 23 -156.20 -126.97
REMARK 500 3 ALA A 24 44.47 -160.88
REMARK 500 3 ASN A 30 14.06 57.61
REMARK 500 4 ASN A 4 68.83 -118.91
REMARK 500 4 ALA A 24 62.28 -69.69
REMARK 500 5 ALA A 5 104.52 -41.97
REMARK 500 5 LYS A 6 99.90 -57.40
REMARK 500 5 CYS A 7 -164.59 -70.26
REMARK 500 5 SER A 10 -55.50 170.32
REMARK 500 5 ALA A 25 50.85 -145.23
REMARK 500 6 ALA A 20 -65.55 -91.10
REMARK 500 6 LYS A 27 -162.09 -107.90
REMARK 500 6 ASN A 30 17.87 53.86
REMARK 500 7 LYS A 6 62.63 33.18
REMARK 500 8 ASN A 4 59.31 -113.71
REMARK 500 8 CYS A 7 170.07 -44.14
REMARK 500 8 LYS A 23 -147.50 -123.53
REMARK 500 8 ALA A 24 48.36 -167.56
REMARK 500 8 LYS A 27 -165.00 -127.90
REMARK 500 9 LYS A 6 69.23 -64.35
REMARK 500 9 CYS A 7 156.87 -48.93
REMARK 500 9 SER A 10 -55.83 169.67
REMARK 500 9 ALA A 24 65.01 -65.65
REMARK 500 10 LYS A 6 94.42 -59.85
REMARK 500 11 ASN A 4 30.20 -86.33
REMARK 500 11 LYS A 6 92.56 -39.56
REMARK 500 11 ALA A 20 -65.65 -103.41
REMARK 500 12 LYS A 6 48.80 36.40
REMARK 500 13 CYS A 7 -162.54 -55.54
REMARK 500 13 ARG A 8 -33.87 -141.45
REMARK 500 13 SER A 10 -53.75 168.11
REMARK 500 13 ALA A 24 91.21 -67.30
REMARK 500 14 ASN A 4 46.78 -90.81
REMARK 500 14 ALA A 25 68.19 -150.35
REMARK 500 15 ALA A 5 171.03 -46.88
REMARK 500 15 LYS A 6 69.30 -116.32
REMARK 500 15 CYS A 7 175.24 -49.12
REMARK 500 15 SER A 10 -58.79 175.88
REMARK 500 16 ASN A 4 82.38 -63.87
REMARK 500 16 LYS A 6 92.02 -36.01
REMARK 500 16 ILE A 21 -37.40 -148.52
REMARK 500 17 ASN A 4 48.09 -79.34
REMARK 500 17 LYS A 6 91.08 -45.76
REMARK 500
REMARK 500 THIS ENTRY HAS 86 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 8 0.23 SIDE CHAIN
REMARK 500 2 ARG A 8 0.31 SIDE CHAIN
REMARK 500 3 ARG A 8 0.30 SIDE CHAIN
REMARK 500 4 ARG A 8 0.29 SIDE CHAIN
REMARK 500 5 ARG A 8 0.31 SIDE CHAIN
REMARK 500 6 ARG A 8 0.31 SIDE CHAIN
REMARK 500 7 ARG A 8 0.16 SIDE CHAIN
REMARK 500 8 ARG A 8 0.31 SIDE CHAIN
REMARK 500 9 ARG A 8 0.20 SIDE CHAIN
REMARK 500 10 ARG A 8 0.18 SIDE CHAIN
REMARK 500 11 ARG A 8 0.14 SIDE CHAIN
REMARK 500 12 ARG A 8 0.32 SIDE CHAIN
REMARK 500 13 ARG A 8 0.29 SIDE CHAIN
REMARK 500 14 ARG A 8 0.32 SIDE CHAIN
REMARK 500 15 ARG A 8 0.12 SIDE CHAIN
REMARK 500 16 ARG A 8 0.26 SIDE CHAIN
REMARK 500 17 ARG A 8 0.17 SIDE CHAIN
REMARK 500 18 ARG A 8 0.16 SIDE CHAIN
REMARK 500 19 ARG A 8 0.32 SIDE CHAIN
REMARK 500 20 ARG A 8 0.12 SIDE CHAIN
REMARK 500 21 ARG A 8 0.31 SIDE CHAIN
REMARK 500 22 ARG A 8 0.29 SIDE CHAIN
REMARK 500 23 ARG A 8 0.19 SIDE CHAIN
REMARK 500 24 ARG A 8 0.28 SIDE CHAIN
REMARK 500 25 ARG A 8 0.18 SIDE CHAIN
REMARK 500 26 ARG A 8 0.32 SIDE CHAIN
REMARK 500 27 ARG A 8 0.20 SIDE CHAIN
REMARK 500 28 ARG A 8 0.15 SIDE CHAIN
REMARK 500 29 ARG A 8 0.27 SIDE CHAIN
REMARK 500 30 ARG A 8 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HP2 A 1 37 UNP P46114 SCKA_TITSE 1 37
SEQRES 1 A 37 VAL PHE ILE ASN ALA LYS CYS ARG GLY SER PRO GLU CYS
SEQRES 2 A 37 LEU PRO LYS CYS LYS GLU ALA ILE GLY LYS ALA ALA GLY
SEQRES 3 A 37 LYS CYS MET ASN GLY LYS CYS LYS CYS TYR PRO
HELIX 1 1 GLY A 9 ILE A 21 1 13
SHEET 1 A 3 PHE A 2 ILE A 3 0
SHEET 2 A 3 LYS A 32 CYS A 35 -1 N CYS A 33 O ILE A 3
SHEET 3 A 3 GLY A 26 MET A 29 -1 O LYS A 27 N LYS A 34
SSBOND 1 CYS A 7 CYS A 28 1555 1555 2.02
SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 35 1555 1555 2.02
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