Header list of 1c49.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 17-AUG-99 1C49
TITLE STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCORPION
TITLE 2 PANDINUS IMPERATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOXIN K-BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COMPLETE PEPTIDE;
COMPND 5 SYNONYM: PITX-KB, ALPHA-KTX5.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PANDINUS IMPERATOR;
SOURCE 3 ORGANISM_COMMON: EMPEROR SCORPION;
SOURCE 4 ORGANISM_TAXID: 55084;
SOURCE 5 TISSUE: VENOM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSR9
KEYWDS SCORPION TOXIN, POTASSIUM CHANNELS BLOCKERS, ALPHA-K TOXIN FAMILY,
KEYWDS 2 NEUROTOXIN, NMR SOLUTION STRUCTURE, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR K.C.KLENK,T.C.TENENHOLZ,D.R.MATTESON,R.S.ROGOWSKI,M.P.BLAUSTEIN,
AUTHOR 2 D.J.WEBER
REVDAT 3 16-FEB-22 1C49 1 REMARK
REVDAT 2 24-FEB-09 1C49 1 VERSN
REVDAT 1 22-MAR-00 1C49 0
JRNL AUTH K.C.KLENK,T.C.TENENHOLZ,D.R.MATTESON,R.S.ROGOWSKI,
JRNL AUTH 2 M.P.BLAUSTEIN,D.J.WEBER
JRNL TITL STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE
JRNL TITL 2 SCORPION PANDINUS IMPERATOR.
JRNL REF PROTEINS V. 38 441 2000
JRNL REFN ISSN 0887-3585
JRNL PMID 10707030
JRNL DOI 10.1002/(SICI)1097-0134(20000301)38:4<441::AID-PROT9>3.3.CO;
JRNL DOI 2 2-C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.S.ROGOWSKI,J.H.COLLINS,T.J.O'NEILL,T.A.GUSTAFSON,
REMARK 1 AUTH 2 T.R.WERKMAN,M.A.ROGAWSKI,T.C.TENENHOLZ,D.J.WEBER,
REMARK 1 AUTH 3 M.P.BLAUSTEIN
REMARK 1 TITL THREE NEW TOXINS FROM THE SCORPION PANDINUS IMPERATOR
REMARK 1 TITL 2 SELECTIVELY BLOCK CERTAIN VOLTAGE-GATED K+ CHANNELS
REMARK 1 REF MOL.PHARMACOL. V. 50 1167 1996
REMARK 1 REFN ISSN 0026-895X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 425 NOE DISTANCE CONSTRAINTS, 22 H-BOND CONSTRAINTS, 11 CHI ANGLE
REMARK 3 CONSTRAINTS,
REMARK 3 26 PHI ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1C49 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000001286.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310.00
REMARK 210 PH : 3.50
REMARK 210 IONIC STRENGTH : 1.44 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O AND 100%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; ROESY;
REMARK 210 P.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 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL NMR ON AN
REMARK 210 UNLABELED SAMPLE
REMARK 210 OF RECOMBINANT PITX-KB (M).
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 SG CYS A 13 SG CYS A 33 2.02
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 ILE A 5 -163.67 -55.95
REMARK 500 1 THR A 8 -59.40 -131.49
REMARK 500 2 THR A 21 -45.26 -136.01
REMARK 500 2 ASN A 25 107.97 -41.46
REMARK 500 2 MET A 29 -165.15 -115.09
REMARK 500 2 ASN A 30 90.68 -52.21
REMARK 500 2 PHE A 36 46.33 -155.71
REMARK 500 3 ASN A 25 103.25 -54.37
REMARK 500 4 THR A 8 -37.81 -130.36
REMARK 500 5 THR A 8 -39.92 -138.66
REMARK 500 5 THR A 21 -40.17 -146.07
REMARK 500 5 ASN A 25 109.28 -45.48
REMARK 500 5 CYS A 33 152.58 -43.48
REMARK 500 6 ILE A 5 -163.00 -58.19
REMARK 500 6 ASN A 25 91.42 -52.21
REMARK 500 6 ASN A 30 70.93 45.89
REMARK 500 6 ARG A 31 40.17 38.98
REMARK 500 6 PHE A 36 -36.77 -156.04
REMARK 500 7 THR A 21 -36.34 -139.53
REMARK 500 7 ASN A 30 93.90 -50.22
REMARK 500 8 ILE A 5 -154.27 -64.87
REMARK 500 8 SER A 6 98.86 -169.12
REMARK 500 8 THR A 8 -50.59 -133.12
REMARK 500 8 ASN A 25 94.03 -39.65
REMARK 500 8 ASN A 30 98.10 -59.92
REMARK 500 8 PHE A 36 -81.30 -149.24
REMARK 500 9 PHE A 36 57.83 -151.72
REMARK 500 10 ILE A 5 -168.82 -67.00
REMARK 500 10 THR A 8 -47.47 -140.24
REMARK 500 10 ASN A 30 56.24 38.24
REMARK 500 11 ILE A 5 -169.01 -62.69
REMARK 500 11 THR A 21 -51.66 -150.07
REMARK 500 11 ASN A 25 91.00 -61.41
REMARK 500 11 ARG A 31 29.77 43.60
REMARK 500 11 PHE A 36 -70.31 -81.06
REMARK 500 12 SER A 6 44.37 -106.04
REMARK 500 12 THR A 8 14.43 -140.36
REMARK 500 12 THR A 21 -60.85 -143.60
REMARK 500 13 ILE A 5 -154.01 -72.28
REMARK 500 13 SER A 6 106.64 177.90
REMARK 500 13 PRO A 24 42.56 -80.58
REMARK 500 14 THR A 8 12.83 -140.93
REMARK 500 14 ASN A 25 90.25 -62.41
REMARK 500 15 ILE A 5 -174.98 -69.36
REMARK 500 15 THR A 21 -59.21 -148.40
REMARK 500 16 THR A 21 -70.70 -148.04
REMARK 500 16 MET A 29 -165.41 -100.50
REMARK 500 16 ASN A 30 88.97 -50.41
REMARK 500 17 ILE A 5 -156.93 -61.08
REMARK 500 17 THR A 8 -50.60 -138.96
REMARK 500
REMARK 500 THIS ENTRY HAS 56 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 31 0.12 SIDE CHAIN
REMARK 500 1 ARG A 38 0.26 SIDE CHAIN
REMARK 500 2 ARG A 31 0.26 SIDE CHAIN
REMARK 500 2 ARG A 38 0.27 SIDE CHAIN
REMARK 500 3 ARG A 31 0.26 SIDE CHAIN
REMARK 500 3 ARG A 38 0.30 SIDE CHAIN
REMARK 500 4 ARG A 31 0.17 SIDE CHAIN
REMARK 500 4 ARG A 38 0.21 SIDE CHAIN
REMARK 500 5 ARG A 31 0.31 SIDE CHAIN
REMARK 500 5 ARG A 38 0.23 SIDE CHAIN
REMARK 500 6 ARG A 31 0.24 SIDE CHAIN
REMARK 500 6 ARG A 38 0.32 SIDE CHAIN
REMARK 500 7 ARG A 31 0.18 SIDE CHAIN
REMARK 500 7 ARG A 38 0.32 SIDE CHAIN
REMARK 500 8 ARG A 31 0.24 SIDE CHAIN
REMARK 500 8 ARG A 38 0.31 SIDE CHAIN
REMARK 500 9 ARG A 31 0.28 SIDE CHAIN
REMARK 500 9 ARG A 38 0.10 SIDE CHAIN
REMARK 500 10 ARG A 31 0.21 SIDE CHAIN
REMARK 500 10 ARG A 38 0.20 SIDE CHAIN
REMARK 500 11 ARG A 31 0.32 SIDE CHAIN
REMARK 500 11 ARG A 38 0.21 SIDE CHAIN
REMARK 500 12 ARG A 31 0.27 SIDE CHAIN
REMARK 500 12 ARG A 38 0.23 SIDE CHAIN
REMARK 500 13 ARG A 31 0.24 SIDE CHAIN
REMARK 500 13 ARG A 38 0.24 SIDE CHAIN
REMARK 500 14 ARG A 31 0.28 SIDE CHAIN
REMARK 500 14 ARG A 38 0.17 SIDE CHAIN
REMARK 500 15 ARG A 31 0.32 SIDE CHAIN
REMARK 500 15 ARG A 38 0.09 SIDE CHAIN
REMARK 500 16 ARG A 31 0.22 SIDE CHAIN
REMARK 500 17 ARG A 31 0.20 SIDE CHAIN
REMARK 500 17 ARG A 38 0.32 SIDE CHAIN
REMARK 500 18 ARG A 31 0.29 SIDE CHAIN
REMARK 500 18 ARG A 38 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C49 A 4 38 UNP P55928 SCKB_PANIM 1 35
SEQRES 1 A 35 THR ILE SER CYS THR ASN GLU LYS GLN CYS TYR PRO HIS
SEQRES 2 A 35 CYS LYS LYS GLU THR GLY TYR PRO ASN ALA LYS CYS MET
SEQRES 3 A 35 ASN ARG LYS CYS LYS CYS PHE GLY ARG
HELIX 1 1 ASN A 9 GLN A 12 5 4
HELIX 2 2 CYS A 13 THR A 21 1 9
SHEET 1 A 2 ALA A 26 MET A 29 0
SHEET 2 A 2 LYS A 32 CYS A 35 -1 O LYS A 32 N MET A 29
SSBOND 1 CYS A 7 CYS A 28 1555 1555 2.02
SSBOND 2 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 - 16 20 Bytes