Header list of 1tt3.pdb file
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HEADER TOXIN 21-JUN-04 1TT3 TITLE NMR SOULUTION STRUCTURE OF OMEGA-CONOTOXIN [K10]MVIIA COMPND MOL_ID: 1; COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: OMEGA-CONOTOXIN [K10]MVIIA; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE CONTAINS A [R10K] MUTATION OF THE SOURCE 4 NATURALLY OCCURING MVIIA FROM CONUS MAGUS KEYWDS CYSTEINE KNOT, FOUR LOOP FRAME WORK, TOXIN EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR D.J.ADAMS,A.B.SMITH,C.I.SCHROEDER,T.YASUDA,R.J.LEWIS REVDAT 3 10-NOV-21 1TT3 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1TT3 1 VERSN REVDAT 1 06-JUL-04 1TT3 0 JRNL AUTH D.J.ADAMS,A.B.SMITH,C.I.SCHROEDER,T.YASUDA,R.J.LEWIS JRNL TITL OMEGA-CONOTOXIN CVID INHIBITS A PHARMACOLOGICALLY DISTINCT JRNL TITL 2 VOLTAGE-SENSITIVE CALCIUM CHANNEL ASSOCIATED WITH JRNL TITL 3 TRANSMITTER RELEASE FROM PREGANGLIONIC NERVE TERMINALS JRNL REF J.BIOL.CHEM. V. 278 4057 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12441339 JRNL DOI 10.1074/JBC.M209969200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.MOULD,T.YASUDA,C.I.SCHROEDER,A.M.BEEDLE,C.J.DOERING, REMARK 1 AUTH 2 G.W.ZAMPONI,D.J.ADAMS,R.J.LEWIS REMARK 1 TITL THE ALFA2DELTA AUXILIARY SUBUNIT REDUCES THE AFFINITY OF REMARK 1 TITL 2 OMEGA-CONOTOXINS FOR RECOMBINANT N-TYPE CALCIUM CHANNELS REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 479 DISTANCE RESTRAINTS REMARK 3 (INCLUDING H-BONDS) AND 30 DIHEDRAL ANGLE RESTRAINTS (INCLUDING REMARK 3 21 PHI, 9 CHI) WERE USED TO CALCULATE THE STRUCTURES. REMARK 4 REMARK 4 1TT3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000022880. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293; 280 REMARK 210 PH : 3.5; 3.5 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM [K10]MVIIA, 95% H2O, 5% D2O, REMARK 210 DSS; 2MM [K10]MVIIA, 100% D2O, REMARK 210 DSS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; E REMARK 210 -COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING REMARK 210 TORSION ANGLE DYNAMICS/SIMULATED REMARK 210 ANNEALING PROTOCOL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7 REMARK 210 REMARK 210 REMARK: NULL 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 O ALA A 6 H CYS A 25 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 LYS A 7 147.87 -38.26 REMARK 500 1 CYS A 8 -168.52 -121.31 REMARK 500 1 MET A 12 -33.15 -143.87 REMARK 500 2 MET A 12 84.92 -168.53 REMARK 500 2 TYR A 13 86.54 -57.78 REMARK 500 2 ASP A 14 46.73 -92.77 REMARK 500 3 MET A 12 -36.61 -170.14 REMARK 500 3 THR A 17 41.44 -93.43 REMARK 500 3 SER A 19 -162.78 -115.18 REMARK 500 3 ARG A 21 88.36 -150.03 REMARK 500 4 ALA A 6 -166.45 -73.32 REMARK 500 4 MET A 12 -41.34 -164.36 REMARK 500 4 SER A 19 -157.63 -125.54 REMARK 500 5 LEU A 11 40.30 -105.19 REMARK 500 5 MET A 12 -40.62 -168.67 REMARK 500 6 ALA A 6 -166.19 -71.57 REMARK 500 6 LEU A 11 40.47 -103.72 REMARK 500 6 MET A 12 -41.80 -169.96 REMARK 500 6 SER A 19 -164.54 -126.99 REMARK 500 7 LYS A 7 147.09 -36.17 REMARK 500 7 LEU A 11 44.07 -108.67 REMARK 500 7 MET A 12 -37.86 -169.45 REMARK 500 7 ARG A 21 88.95 -150.31 REMARK 500 8 LYS A 7 148.35 -36.99 REMARK 500 8 LEU A 11 -22.08 169.54 REMARK 500 8 ARG A 21 87.42 -150.01 REMARK 500 9 LYS A 7 143.36 -34.76 REMARK 500 9 MET A 12 -40.28 -170.08 REMARK 500 9 ASP A 14 55.73 -90.67 REMARK 500 9 ARG A 21 88.01 -150.08 REMARK 500 10 MET A 12 -33.68 -170.08 REMARK 500 11 MET A 12 -39.81 -166.97 REMARK 500 11 SER A 19 -158.40 -136.21 REMARK 500 11 ARG A 21 87.99 -150.19 REMARK 500 12 LYS A 10 60.27 -69.92 REMARK 500 12 LEU A 11 -25.39 169.73 REMARK 500 12 ARG A 21 89.23 -150.20 REMARK 500 13 LYS A 7 143.98 -34.86 REMARK 500 13 MET A 12 75.41 -170.11 REMARK 500 13 TYR A 13 87.10 -52.93 REMARK 500 13 ASP A 14 52.16 -91.47 REMARK 500 13 THR A 17 52.03 -118.06 REMARK 500 14 LYS A 10 65.54 -67.50 REMARK 500 14 LEU A 11 -16.73 159.42 REMARK 500 14 ARG A 21 89.59 -150.33 REMARK 500 15 ALA A 6 -167.37 -77.11 REMARK 500 15 CYS A 8 -168.58 -118.51 REMARK 500 15 MET A 12 -32.95 -166.43 REMARK 500 15 ARG A 21 88.18 -150.28 REMARK 500 16 LEU A 11 -31.99 169.58 REMARK 500 REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 26 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OMG RELATED DB: PDB REMARK 900 NMR STUDY OF OMEGA-CONOTOXIN MVIIA REMARK 900 RELATED ID: 1MVJ RELATED DB: PDB REMARK 900 N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA NMR, 15 REMARK 900 STRUCTURES REMARK 900 RELATED ID: 1DW4 RELATED DB: PDB REMARK 900 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: CONSTRAINTS ON DISULPHIDE REMARK 900 BRIDGES REMARK 900 RELATED ID: 1TTK RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF OMEGA-CONOTOXIN MVIIA, A N-TYPE CALCIUM REMARK 900 CHANNEL BLOCKER DBREF 1TT3 A 1 25 UNP P05484 CXO7A_CONMA 46 70 SEQADV 1TT3 LYS A 10 UNP P05484 ARG 55 ENGINEERED MUTATION SEQRES 1 A 26 CYS LYS GLY LYS GLY ALA LYS CYS SER LYS LEU MET TYR SEQRES 2 A 26 ASP CYS CYS THR GLY SER CYS ARG SER GLY LYS CYS NH2 HET NH2 A 26 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.02 SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.02 SSBOND 3 CYS A 15 CYS A 25 1555 1555 2.02 LINK C CYS A 25 N NH2 A 26 1555 1555 1.31 SITE 1 AC1 2 SER A 19 CYS A 25 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
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