Header list of 1e74.pdb file
Complete list - 9 20 Bytes
HEADER PEPTIDE TOXIN 24-AUG-00 1E74 TITLE NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT TITLE 2 R11E COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-CONOTOXIN IM1(R11E); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: CONUS IMPERIALIS; SOURCE 4 ORGANISM_TAXID: 35631; SOURCE 5 OTHER_DETAILS: SYNTHESIZED USING STANDARD FMOC CHEMISTRY. IM1 SOURCE 6 SEQUENCE FOUND NATURALLY IN CONUS IMPERIALIS VENOM KEYWDS PEPTIDE TOXIN, NEUROTOXIN, NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR KEYWDS 2 ANTAGONIST, ALPHA-CONOTOXIN, NMR SOLUTION STRUCTURE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.P.ROGERS,P.LUGINBUHL,K.PEMBERTON,P.HARTY,D.E.WEMMER,R.C.STEVENS REVDAT 5 14-JUN-23 1E74 1 REMARK REVDAT 4 15-JAN-20 1E74 1 LINK REVDAT 3 14-JUN-17 1E74 1 REMARK REVDAT 2 24-FEB-09 1E74 1 VERSN REVDAT 1 27-DEC-00 1E74 0 JRNL AUTH J.P.ROGERS,P.LUGINBUHL,K.PEMBERTON,P.HARTY,D.E.WEMMER, JRNL AUTH 2 R.C.STEVENS JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS IN A PEPTIDIC ALPHA7 JRNL TITL 2 NICOTINIC ACETYLCHOLINE RECEPTOR ANTAGONIST JRNL REF J.MOL.BIOL. V. 304 911 2000 JRNL REFN ISSN 0022-2836 JRNL PMID 11124036 JRNL DOI 10.1006/JMBI.2000.4247 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.P.ROGERS,P.LUGINBUHL,G.S.SHEN,R.T.MCCABE,R.C.STEVENS, REMARK 1 AUTH 2 D.E.WEMMER REMARK 1 TITL NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IMI AND COMPARISON REMARK 1 TITL 2 TO OTHER CONOTOXINS SPECIFIC FOR NEURONAL NICOTINIC REMARK 1 TITL 3 ACETYLCHOLINE RECEPTORS REMARK 1 REF BIOCHEMISTRY V. 38 3874 1999 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 10194298 REMARK 1 DOI 10.1021/BI9826254 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.S.JOHNSON,J.MARTINEZ,A.B.ELGOYHEN,S.F.HEINEMANN, REMARK 1 AUTH 2 J.M.MCINTOSH REMARK 1 TITL ALPHA-CONOTOXIN IMI EXHIBITS SUBTYPE-SPECIFIC NICOTINIC REMARK 1 TITL 2 ACETYLCHOLINE RECEPTOR BLOCKADE: PREFERENTIAL INHIBITION OF REMARK 1 TITL 3 HOMOMERIC ALPHA7 AND ALPHA9 RECEPTORS REMARK 1 REF MOL.PHARMACOL. V. 48 194 1995 REMARK 1 REFN ISSN 0026-895X REMARK 1 PMID 7651351 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.M.MCINTOSH,D.YOSHIKAMI,E.MAHE,D.B.NIELSEN,J.E.RIVIER, REMARK 1 AUTH 2 W.R.GRAY,B.M.OLIVERA REMARK 1 TITL A NICOTINIC ACETYLCHOLINE RECEPTOR LIGAND OF UNIQUE REMARK 1 TITL 2 SPECIFICITY, ALPHA-CONOTOXIN IMI REMARK 1 REF J.BIOL.CHEM. V. 269 16733 1994 REMARK 1 REFN ISSN 0021-9258 REMARK 1 PMID 8206995 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: FOR THE PRESENT STRUCTURES THE NMR REMARK 3 DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN REMARK 3 UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF REMARK 3 KT/2. THE CONSTRAINTS ON DIHEDRAL ANGLES RESULTING FROM REMARK 3 MEASUREMENTS OF VICINAL COUPLING CONSTANTS WERE WEIGHTED SUCH REMARK 3 THAT A VIOLATION OF 2.5 DEGREES CORRESPONDS TO AN ENERGY OF KT/2. REMARK 4 REMARK 4 1E74 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-00. REMARK 100 THE DEPOSITION ID IS D_1290005307. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.1 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; ROESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA, OPAL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINED ENERGY MINIMISATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6 REMARK 210 REMARK 210 REMARK: DATA CONSIST OF 61 UPPER LIMITS ON DISTANCES OBTAINED FROM REMARK 210 NOE MEASUREMENTS AND 26 ANGLE CONSTRAINTS OBTAINED FROM NOE REMARK 210 MEASUREMENTS AND COUPLING CONSTANT MEASUREMENTS. THESE INPUT REMARK 210 DATA ARE ALSO AVAILABLE FROM THE PROTEIN DATA BANK. ONE REMARK 210 STEREOSPECIFIC RESONANCE ASSIGNMENT HAS BEEN MADE. TORSION ANGLE REMARK 210 DYNAMICS CALCULATIONS WERE PERFORMED WITH THE PROGRAM DYANA (P. REMARK 210 GUNTERT, C. MUMENTHALER, K. WUTHRICH, J. MOL. BIOL. (1997) VOL. REMARK 210 273, 283-298). FOR THE RESTRAINED ENERGY MINIMIZATION THE REMARK 210 PROGRAM OPAL (P. LUGINBUHL, P. GUNTERT, M. BILLETER, K. WUTHRICH, REMARK 210 J. BIOMOL. NMR (1996) VOL. 8, 136-146) WAS USED. DEPOSITED REMARK 210 COORDINATES ARE THOSE OF CONFORMERS 1-20 IN THE PAPER CITED ON * REMARK 210 JRNL* RECORDS ABOVE. NO VIOLATIONS OF DISTANCE CONSTRAINTS FROM REMARK 210 NOES EXCEED 0.10 ANGSTROMS, AND NO VIOLATIONS OF ANGLE REMARK 210 CONSTRAINTS EXCEED 2.0 DEGREES. REPRESENTATIVE CONFORMER HAS THE REMARK 210 SMALLEST RMSD TO THE MEAN STRUCTURE UPON SUPERPOSITION OF THE REMARK 210 BACKBONE ATOMS N, CA, AND C' OF RESIDUES 2-11. 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 2 CYS A 12 CB - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 2 CYS A 12 CA - CB - SG ANGL. DEV. = 9.0 DEGREES REMARK 500 3 CYS A 12 CB - CA - C ANGL. DEV. = 7.5 DEGREES REMARK 500 3 CYS A 12 CA - CB - SG ANGL. DEV. = 9.6 DEGREES REMARK 500 4 CYS A 12 CA - CB - SG ANGL. DEV. = 8.4 DEGREES REMARK 500 8 CYS A 12 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 9 CYS A 12 CB - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 9 CYS A 12 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 10 CYS A 12 CB - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 11 CYS A 12 CB - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 11 CYS A 12 CA - CB - SG ANGL. DEV. = 11.2 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 2 ALA A 9 12.74 -60.99 REMARK 500 2 GLU A 11 -3.84 -141.91 REMARK 500 3 CYS A 2 18.48 45.62 REMARK 500 3 ALA A 9 0.27 -62.58 REMARK 500 4 CYS A 2 -18.73 65.49 REMARK 500 4 ALA A 9 2.69 -62.00 REMARK 500 6 ALA A 9 -5.55 -57.68 REMARK 500 7 CYS A 2 -44.93 -153.74 REMARK 500 8 GLU A 11 -18.58 -140.43 REMARK 500 9 ALA A 9 -4.33 -58.23 REMARK 500 10 CYS A 2 -27.08 63.93 REMARK 500 10 ALA A 9 -6.03 -59.50 REMARK 500 11 CYS A 2 -37.36 69.70 REMARK 500 12 CYS A 2 -4.42 82.00 REMARK 500 12 ALA A 9 23.03 -67.37 REMARK 500 12 GLU A 11 -32.25 -146.09 REMARK 500 14 ALA A 9 20.79 -67.48 REMARK 500 14 TRP A 10 -93.86 -66.74 REMARK 500 15 CYS A 2 -42.02 68.48 REMARK 500 16 CYS A 2 -39.14 69.80 REMARK 500 16 ALA A 9 7.89 -66.58 REMARK 500 16 TRP A 10 -72.95 -56.76 REMARK 500 17 CYS A 2 -5.25 58.58 REMARK 500 18 CYS A 2 -45.60 -153.79 REMARK 500 18 ALA A 9 49.08 -72.08 REMARK 500 19 CYS A 3 2.39 -63.03 REMARK 500 19 ALA A 9 4.74 -63.86 REMARK 500 19 GLU A 11 -8.43 -144.43 REMARK 500 20 CYS A 2 22.87 -69.58 REMARK 500 20 CYS A 8 -92.15 -126.10 REMARK 500 20 ALA A 9 35.49 38.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E75 RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION REMARK 900 VARIANT R7L (20 STRUCTURES) REMARK 900 RELATED ID: 1E76 RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION REMARK 900 VARIANT D5N (20 STRUCTURES) REMARK 900 RELATED ID: 1IM1 RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, (20 STRUCTURES) REMARK 900 RELATED ID: 1IMI RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 REMARK 900 RELATED ID: 1CNL RELATED DB: PDB REMARK 900 ALPHA-CONOTOXIN IMI (10 STRUCTURES) REMARK 900 RELATED ID: 4845 RELATED DB: BMRB DBREF 1E74 A 1 12 UNP P50983 CXA1_CONIM 1 12 SEQADV 1E74 GLU A 11 UNP P50983 ARG 11 ENGINEERED MUTATION SEQRES 1 A 13 GLY CYS CYS SER ASP PRO ARG CYS ALA TRP GLU CYS NH2 HET NH2 A 13 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 GLY A 1 ALA A 9 5 9 SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.04 SSBOND 2 CYS A 3 CYS A 12 1555 1555 2.04 LINK C CYS A 12 N NH2 A 13 1555 1555 1.32 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 - 9 20 Bytes