Header list of 1eyo.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 07-MAY-00 1EYO TITLE SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONOTOXIN TVIIA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SOURCE 4 SEQUENCE OCCURS NATURALLY IN CONUS TULIPA (TULIP CONE) KEYWDS CYSTINE KNOT MOTIF, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.HILL,P.F.ALEWOOD,D.J.CRAIK REVDAT 3 16-FEB-22 1EYO 1 REMARK LINK REVDAT 2 24-FEB-09 1EYO 1 VERSN REVDAT 1 06-SEP-00 1EYO 0 JRNL AUTH J.M.HILL,P.F.ALEWOOD,D.J.CRAIK JRNL TITL CONOTOXIN TVIIA, A NOVEL PEPTIDE FROM THE VENOM OF CONUS JRNL TITL 2 TULIPA 2. THREE-DIMENSIONAL SOLUTION STRUCTURE. JRNL REF EUR.J.BIOCHEM. V. 267 4649 2000 JRNL REFN ISSN 0014-2956 JRNL PMID 10903497 JRNL DOI 10.1046/J.1432-1327.2000.01507.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.M.HILL,A.R.ATKINS,M.L.LOUGHNAN,A.JONES,D.A.ADAMS,R.MARTIN, REMARK 1 AUTH 2 R.J.LEWIS,D.J.CRAIK,P.F.ALEWOOD REMARK 1 TITL CONOTOXIN TVIIA, A NOVEL PEPTIDE FROM THE VENOM OF CONUS REMARK 1 TITL 2 TULIPA 1. ISOLATION, CHARACTERISATION AND CHEMICAL SYNTHESIS REMARK 1 REF EUR.J.BIOCHEM. V. 267 4642 2000 REMARK 1 REFN ISSN 0014-2956 REMARK 1 DOI 10.1046/J.1432-1327.2000.01508.X REMARK 1 REFERENCE 2 REMARK 1 AUTH J.M.HILL,P.F.ALEWOOD,D.J.CRAIK REMARK 1 TITL SOLUTION STRUCTURE OF THE SODIUM CHANNEL ANTAGONIST REMARK 1 TITL 2 CONOTOXIN GS: A NEW MOLECULAR CALIPER FOR PROBING SODIUM REMARK 1 TITL 3 CHANNEL GEOMETRY REMARK 1 REF STRUCTURE V. 5 571 1997 REMARK 1 REFN ISSN 0969-2126 REMARK 1 DOI 10.1016/S0969-2126(97)00212-8 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: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 562 INTERPROTON DISTANCE RESTRAINTS, AND 18 BACKBONE AND 9 SIDE REMARK 3 CHAIN DIHEDRAL ANGLE RESTRAINTS DERIVED FROM SPIN-SPIN COUPLING REMARK 3 CONSTANTS. REMARK 4 REMARK 4 1EYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00. REMARK 100 THE DEPOSITION ID IS D_1000011033. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 3.0 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM CONOTOXIN TVIIA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY; REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : ARX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 5 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 6 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 11 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 13 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 19 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 19 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.0 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 ARG A 5 125.63 -39.79 REMARK 500 1 ASP A 6 -0.26 79.41 REMARK 500 1 HYP A 11 50.51 -95.00 REMARK 500 1 MET A 18 -140.24 -130.21 REMARK 500 2 ARG A 5 125.73 -39.97 REMARK 500 2 HYP A 11 51.75 -95.29 REMARK 500 2 MET A 18 -132.76 -131.00 REMARK 500 3 ARG A 5 122.01 -39.77 REMARK 500 3 ASP A 6 0.72 81.18 REMARK 500 3 HYP A 11 51.23 -94.72 REMARK 500 3 MET A 18 -133.69 -133.90 REMARK 500 4 CYS A 2 162.95 54.84 REMARK 500 4 ASP A 6 -1.39 82.75 REMARK 500 4 HYP A 11 49.00 -95.07 REMARK 500 4 MET A 18 -131.33 -130.00 REMARK 500 5 ARG A 5 128.11 -39.86 REMARK 500 5 ASP A 6 -5.54 79.24 REMARK 500 5 HYP A 11 47.75 -94.63 REMARK 500 5 CYS A 13 154.49 -49.13 REMARK 500 5 MET A 18 -144.62 -130.10 REMARK 500 5 ARG A 21 -3.70 76.67 REMARK 500 6 ASP A 6 -2.52 86.18 REMARK 500 6 HYP A 11 51.04 -95.53 REMARK 500 6 MET A 18 -128.13 -132.13 REMARK 500 7 ARG A 5 124.61 -39.53 REMARK 500 7 HYP A 11 51.14 -94.88 REMARK 500 7 MET A 18 -132.35 -133.49 REMARK 500 8 ARG A 5 121.93 -39.98 REMARK 500 8 ASP A 6 0.67 81.55 REMARK 500 8 HYP A 11 50.13 -95.01 REMARK 500 8 MET A 18 -136.37 -132.62 REMARK 500 9 ARG A 5 125.63 -39.79 REMARK 500 9 ASP A 6 -0.26 79.41 REMARK 500 9 HYP A 11 50.51 -95.00 REMARK 500 9 MET A 18 -140.24 -130.21 REMARK 500 10 ASP A 6 -9.22 89.57 REMARK 500 10 HYP A 11 49.62 -94.71 REMARK 500 10 MET A 18 -134.69 -128.77 REMARK 500 10 ARG A 21 -1.69 76.98 REMARK 500 11 ASP A 6 -7.71 89.95 REMARK 500 11 HYP A 11 50.96 -95.18 REMARK 500 11 MET A 18 -131.24 -130.25 REMARK 500 11 ARG A 21 -5.75 77.92 REMARK 500 12 ARG A 5 122.88 -39.63 REMARK 500 12 ASP A 6 0.82 80.36 REMARK 500 12 HYP A 11 50.98 -95.28 REMARK 500 12 MET A 18 -133.82 -129.24 REMARK 500 12 ARG A 21 -8.69 79.38 REMARK 500 13 ASP A 6 0.89 81.90 REMARK 500 13 HYP A 11 51.33 -95.47 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1EYO A 1 30 UNP P58923 CX7A_CONTU 1 30 SEQRES 1 A 30 SER CYS SER GLY ARG ASP SER ARG CYS HYP HYP VAL CYS SEQRES 2 A 30 CYS MET GLY LEU MET CYS SER ARG GLY LYS CYS VAL SER SEQRES 3 A 30 ILE TYR GLY GLU MODRES 1EYO HYP A 10 PRO 4-HYDROXYPROLINE MODRES 1EYO HYP A 11 PRO 4-HYDROXYPROLINE HET HYP A 10 15 HET HYP A 11 15 HETNAM HYP 4-HYDROXYPROLINE HETSYN HYP HYDROXYPROLINE FORMUL 1 HYP 2(C5 H9 N O3) SSBOND 1 CYS A 2 CYS A 14 1555 1555 2.02 SSBOND 2 CYS A 9 CYS A 19 1555 1555 2.02 SSBOND 3 CYS A 13 CYS A 24 1555 1555 2.02 LINK C CYS A 9 N HYP A 10 1555 1555 1.32 LINK C HYP A 10 N HYP A 11 1555 1555 1.32 LINK C HYP A 11 N VAL A 12 1555 1555 1.30 CISPEP 1 CYS A 9 HYP A 10 1 -8.16 CISPEP 2 HYP A 10 HYP A 11 1 -3.14 CISPEP 3 CYS A 9 HYP A 10 2 -7.52 CISPEP 4 HYP A 10 HYP A 11 2 -3.15 CISPEP 5 CYS A 9 HYP A 10 3 -7.65 CISPEP 6 HYP A 10 HYP A 11 3 -3.35 CISPEP 7 CYS A 9 HYP A 10 4 -8.57 CISPEP 8 HYP A 10 HYP A 11 4 -3.44 CISPEP 9 CYS A 9 HYP A 10 5 -8.59 CISPEP 10 HYP A 10 HYP A 11 5 -3.47 CISPEP 11 CYS A 9 HYP A 10 6 -7.35 CISPEP 12 HYP A 10 HYP A 11 6 -3.18 CISPEP 13 CYS A 9 HYP A 10 7 -7.54 CISPEP 14 HYP A 10 HYP A 11 7 -3.18 CISPEP 15 CYS A 9 HYP A 10 8 -7.84 CISPEP 16 HYP A 10 HYP A 11 8 -3.18 CISPEP 17 CYS A 9 HYP A 10 9 -8.16 CISPEP 18 HYP A 10 HYP A 11 9 -3.14 CISPEP 19 CYS A 9 HYP A 10 10 -8.20 CISPEP 20 HYP A 10 HYP A 11 10 -3.23 CISPEP 21 CYS A 9 HYP A 10 11 -7.94 CISPEP 22 HYP A 10 HYP A 11 11 -3.21 CISPEP 23 CYS A 9 HYP A 10 12 -8.14 CISPEP 24 HYP A 10 HYP A 11 12 -3.18 CISPEP 25 CYS A 9 HYP A 10 13 -8.20 CISPEP 26 HYP A 10 HYP A 11 13 -3.30 CISPEP 27 CYS A 9 HYP A 10 14 -7.89 CISPEP 28 HYP A 10 HYP A 11 14 -3.22 CISPEP 29 CYS A 9 HYP A 10 15 -7.74 CISPEP 30 HYP A 10 HYP A 11 15 -3.13 CISPEP 31 CYS A 9 HYP A 10 16 -7.88 CISPEP 32 HYP A 10 HYP A 11 16 -3.25 CISPEP 33 CYS A 9 HYP A 10 17 -8.14 CISPEP 34 HYP A 10 HYP A 11 17 -3.45 CISPEP 35 CYS A 9 HYP A 10 18 -7.54 CISPEP 36 HYP A 10 HYP A 11 18 -3.17 CISPEP 37 CYS A 9 HYP A 10 19 -7.86 CISPEP 38 HYP A 10 HYP A 11 19 -3.29 CISPEP 39 CYS A 9 HYP A 10 20 -7.90 CISPEP 40 HYP A 10 HYP A 11 20 -3.36 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