Header list of 1ie6.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 07-APR-01 1IE6 TITLE SOLUTION STRUCTURE OF IMPERATOXIN A COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMPERATOXIN A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PEPTIDE NEUROTOXIN, RYANODINE RECEPTOR ACTIVATOR; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE SOURCE 4 OCCURS NATURALLY IN THE VENOM OF SCORPION PANDINUS IMPERATOR. KEYWDS TRIPLE STRANDED ANTIPARELLEL BETA-SHEET, INHIBITORY CYSTINE KNOT, KEYWDS 2 TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.W.LEE,K.TAKEUCHI,H.TAKAHASHI,K.SATO,I.SHIMADA,D.H.KIM,J.I.KIM REVDAT 4 23-FEB-22 1IE6 1 REMARK REVDAT 3 24-FEB-09 1IE6 1 VERSN REVDAT 2 02-MAR-04 1IE6 1 JRNL REVDAT 1 10-JUN-03 1IE6 0 JRNL AUTH C.W.LEE,E.H.LEE,K.TAKEUCHI,H.TAKAHASHI,I.SHIMADA,K.SATO, JRNL AUTH 2 S.Y.SHIN,D.H.KIM,J.I.KIM JRNL TITL MOLECULAR BASIS OF THE HIGH-AFFINITY ACTIVATION OF TYPE 1 JRNL TITL 2 RYANODINE RECEPTORS BY IMPERATOXIN A. JRNL REF BIOCHEM.J. V. 377 385 2004 JRNL REFN ISSN 0264-6021 JRNL PMID 14535845 JRNL DOI 10.1042/BJ20031192 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR 3.851 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 519 RESTRAINTS, 473 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 25 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 12 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS, AND 9 DISTANCE RESTRAINTS FORM DISULFIDE BONDS. REMARK 4 REMARK 4 1IE6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013198. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 3.4 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5MM IMPERATOXIN A; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.0, X-PLOR 3.851 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THOSE WITH THE LOWEST ENERGY REMARK 210 AND THE LEAST RESTRAINT REMARK 210 VIOLATIONS. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11 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 H LEU A 4 O ASP A 15 1.49 REMARK 500 O LYS A 22 H LYS A 30 1.49 REMARK 500 O CYS A 21 HH21 ARG A 23 1.55 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 LEU A 7 13.85 -161.67 REMARK 500 1 ASN A 14 45.39 -90.75 REMARK 500 1 ARG A 24 52.83 -98.22 REMARK 500 1 ASN A 27 119.25 57.06 REMARK 500 1 ALA A 28 -64.29 -159.32 REMARK 500 1 GLU A 29 59.82 159.77 REMARK 500 1 LYS A 30 -73.85 -96.22 REMARK 500 2 HIS A 6 37.15 -90.63 REMARK 500 2 LEU A 7 18.00 -161.84 REMARK 500 2 ARG A 24 49.76 -161.07 REMARK 500 2 THR A 26 51.61 38.39 REMARK 500 2 ASN A 27 -150.82 40.75 REMARK 500 2 ALA A 28 -123.08 78.36 REMARK 500 2 CYS A 32 93.27 -58.59 REMARK 500 3 ASP A 2 60.81 64.93 REMARK 500 3 HIS A 6 34.65 -85.57 REMARK 500 3 LEU A 7 48.77 -155.24 REMARK 500 3 ASN A 14 54.01 -90.90 REMARK 500 3 ARG A 24 53.27 -154.19 REMARK 500 3 THR A 26 37.74 39.40 REMARK 500 3 ASN A 27 100.45 26.90 REMARK 500 3 ALA A 28 -39.76 -143.49 REMARK 500 3 GLU A 29 96.88 -179.19 REMARK 500 3 LYS A 30 -87.89 -117.37 REMARK 500 4 HIS A 6 33.23 -89.36 REMARK 500 4 LEU A 7 16.60 -162.41 REMARK 500 4 ARG A 24 49.70 -91.53 REMARK 500 4 ASN A 27 139.34 51.38 REMARK 500 4 ALA A 28 -54.94 167.83 REMARK 500 4 GLU A 29 54.20 -179.46 REMARK 500 4 LYS A 30 -86.15 -108.19 REMARK 500 5 ASP A 2 56.81 -102.28 REMARK 500 5 HIS A 6 38.84 -87.77 REMARK 500 5 LEU A 7 28.87 -156.35 REMARK 500 5 THR A 26 59.60 -145.34 REMARK 500 5 ASN A 27 140.02 58.21 REMARK 500 5 ALA A 28 -49.19 169.85 REMARK 500 5 GLU A 29 74.20 171.56 REMARK 500 5 LYS A 30 -87.05 -126.60 REMARK 500 6 ASP A 2 115.84 174.04 REMARK 500 6 HIS A 6 35.02 -88.65 REMARK 500 6 LEU A 7 15.03 -161.11 REMARK 500 6 LYS A 19 18.86 56.27 REMARK 500 6 THR A 26 58.25 -179.63 REMARK 500 6 ASN A 27 118.74 56.58 REMARK 500 6 ALA A 28 -33.92 -178.31 REMARK 500 6 GLU A 29 70.64 165.97 REMARK 500 6 LYS A 30 -87.23 -133.88 REMARK 500 7 CYS A 3 -150.08 -155.84 REMARK 500 7 HIS A 6 32.68 -90.47 REMARK 500 REMARK 500 THIS ENTRY HAS 166 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 24 0.31 SIDE CHAIN REMARK 500 1 ARG A 31 0.31 SIDE CHAIN REMARK 500 1 ARG A 33 0.27 SIDE CHAIN REMARK 500 2 ARG A 9 0.31 SIDE CHAIN REMARK 500 2 ARG A 23 0.24 SIDE CHAIN REMARK 500 2 ARG A 24 0.12 SIDE CHAIN REMARK 500 2 ARG A 31 0.14 SIDE CHAIN REMARK 500 2 ARG A 33 0.24 SIDE CHAIN REMARK 500 3 ARG A 9 0.31 SIDE CHAIN REMARK 500 3 ARG A 23 0.20 SIDE CHAIN REMARK 500 3 ARG A 24 0.24 SIDE CHAIN REMARK 500 3 ARG A 31 0.11 SIDE CHAIN REMARK 500 3 ARG A 33 0.19 SIDE CHAIN REMARK 500 4 ARG A 9 0.13 SIDE CHAIN REMARK 500 4 ARG A 23 0.31 SIDE CHAIN REMARK 500 4 ARG A 24 0.28 SIDE CHAIN REMARK 500 4 ARG A 31 0.12 SIDE CHAIN REMARK 500 4 ARG A 33 0.27 SIDE CHAIN REMARK 500 5 ARG A 9 0.18 SIDE CHAIN REMARK 500 5 ARG A 24 0.31 SIDE CHAIN REMARK 500 5 ARG A 31 0.30 SIDE CHAIN REMARK 500 5 ARG A 33 0.13 SIDE CHAIN REMARK 500 6 ARG A 9 0.21 SIDE CHAIN REMARK 500 6 ARG A 23 0.30 SIDE CHAIN REMARK 500 6 ARG A 24 0.25 SIDE CHAIN REMARK 500 6 ARG A 31 0.24 SIDE CHAIN REMARK 500 6 ARG A 33 0.23 SIDE CHAIN REMARK 500 7 ARG A 9 0.29 SIDE CHAIN REMARK 500 7 ARG A 23 0.10 SIDE CHAIN REMARK 500 7 ARG A 24 0.32 SIDE CHAIN REMARK 500 7 ARG A 31 0.31 SIDE CHAIN REMARK 500 7 ARG A 33 0.28 SIDE CHAIN REMARK 500 8 ARG A 9 0.24 SIDE CHAIN REMARK 500 8 ARG A 23 0.23 SIDE CHAIN REMARK 500 8 ARG A 24 0.29 SIDE CHAIN REMARK 500 8 ARG A 31 0.29 SIDE CHAIN REMARK 500 8 ARG A 33 0.23 SIDE CHAIN REMARK 500 9 ARG A 9 0.32 SIDE CHAIN REMARK 500 9 ARG A 23 0.08 SIDE CHAIN REMARK 500 9 ARG A 24 0.12 SIDE CHAIN REMARK 500 9 ARG A 31 0.27 SIDE CHAIN REMARK 500 9 ARG A 33 0.28 SIDE CHAIN REMARK 500 10 ARG A 9 0.20 SIDE CHAIN REMARK 500 10 ARG A 23 0.23 SIDE CHAIN REMARK 500 10 ARG A 24 0.32 SIDE CHAIN REMARK 500 10 ARG A 31 0.12 SIDE CHAIN REMARK 500 10 ARG A 33 0.27 SIDE CHAIN REMARK 500 11 ARG A 9 0.31 SIDE CHAIN REMARK 500 11 ARG A 23 0.32 SIDE CHAIN REMARK 500 11 ARG A 24 0.23 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 94 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS PUBLISHED IN A JOURNAL REMARK 999 (ZAMUDIO, F. Z., ET AL. 1997, FEBS LETT. 405, 385-389). DBREF 1IE6 A 1 33 UNP P59868 IPTXA_PANIM 1 33 SEQRES 1 A 33 GLY ASP CYS LEU PRO HIS LEU LYS ARG CYS LYS ALA ASP SEQRES 2 A 33 ASN ASP CYS CYS GLY LYS LYS CYS LYS ARG ARG GLY THR SEQRES 3 A 33 ASN ALA GLU LYS ARG CYS ARG HELIX 1 1 ALA A 12 ASP A 15 5 4 SSBOND 1 CYS A 3 CYS A 17 1555 1555 2.02 SSBOND 2 CYS A 10 CYS A 21 1555 1555 2.02 SSBOND 3 CYS A 16 CYS A 32 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 - 23 20 Bytes