Header list of 1tvj.pdb file
Complete list - r 2 2 Bytes
HEADER ACTIN-BINDING PROTEIN 29-JUN-04 1TVJ TITLE SOLUTION STRUCTURE OF CHICK COFILIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: COFILIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COFILIN, ADF, ACTIN BINDING PROTEIN, ACTIN DEPOLYMERIZING FACTOR, KEYWDS 2 ACTIN-BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR V.Y.GORBATYUK,N.J.NOSWORTHY,S.A.ROBSON,M.W.MACIEJEWSKI,C.G.DOS AUTHOR 2 REMEDIOS,G.F.KING REVDAT 3 02-MAR-22 1TVJ 1 REMARK REVDAT 2 24-FEB-09 1TVJ 1 VERSN REVDAT 1 20-SEP-05 1TVJ 0 JRNL AUTH V.Y.GORBATYUK,N.J.NOSWORTHY,S.A.ROBSON,M.W.MACIEJEWSKI, JRNL AUTH 2 C.G.DOS REMEDIOS,G.F.KING JRNL TITL NMR STUDY OF THE MOLECULAR BASIS FOR PHOSPHOINOSITIDE JRNL TITL 2 REGULATION OF THE COFILIN-ACTIN INTERACTIONS. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH N.P.S.BAINS,V.Y.GORBATYUK,N.J.NOSWORTHY,S.A.ROBSON, REMARK 1 AUTH 2 M.W.MACIEJEWSKI,C.G.DOS REMEDIOS,G.F.KING REMARK 1 TITL LETTER TO THE EDITOR: BACKBONE AND SIDE-CHAIN 1H, 15N, AND REMARK 1 TITL 2 13C ASSIGNMENTS FOR CHICK COFILIN REMARK 1 REF J.BIOMOL.NMR V. 22 193 2002 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 11885570 REMARK 1 DOI 10.1023/A:1014227808686 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 1.0, X-PLOR 3.1 REMARK 3 AUTHORS : FRANK DELAGLIO AND AD BAX (NMRPIPE), AXEL BRUNGER REMARK 3 (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TVJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000022943. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 0.06 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C COFILIN; 50 MM REMARK 210 KCL; 10 MM PIPES; 0.02% NAN3; PH REMARK 210 6.8 93% H2O, 7% D2O; 1 MM U-15N, REMARK 210 13C COFILIN; 50 MM KCL; 10 MM REMARK 210 PIPES; 0.02% NAN3; PH 6.8 100% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 3D REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D HC(CO) REMARK 210 NH-TOCSY; 3D C(CO)NH-TOCSY; 3D REMARK 210 HCCH-TOCSY; 3D HCCH-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.2, DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED REMARK 210 BY SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY, REMARK 210 BEST COVALENT GEOMETRY, AND REMARK 210 LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 H CYS A 39 O ILE A 48 1.60 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 SER A 24 -63.01 -120.80 REMARK 500 1 PHE A 128 39.67 -96.40 REMARK 500 2 PHE A 128 40.53 -95.46 REMARK 500 2 GLU A 162 29.49 46.78 REMARK 500 3 SER A 3 -47.57 -167.66 REMARK 500 3 SER A 24 -72.24 -103.92 REMARK 500 3 PRO A 26 -37.38 -39.11 REMARK 500 3 PHE A 128 40.17 -95.10 REMARK 500 4 ASP A 62 -60.20 -103.98 REMARK 500 4 PHE A 128 42.26 -95.07 REMARK 500 5 PHE A 128 40.59 -97.66 REMARK 500 6 SER A 3 -65.81 -148.79 REMARK 500 6 ASP A 62 -61.03 -95.69 REMARK 500 6 PHE A 128 40.01 -97.16 REMARK 500 7 SER A 3 107.95 59.01 REMARK 500 7 LYS A 53 74.23 -118.58 REMARK 500 7 ASP A 62 -60.96 -94.11 REMARK 500 7 PHE A 128 41.44 -94.62 REMARK 500 8 SER A 24 -65.20 -128.40 REMARK 500 8 PHE A 128 40.76 -96.83 REMARK 500 9 SER A 24 -67.39 -106.14 REMARK 500 9 PHE A 128 42.99 -95.80 REMARK 500 10 SER A 3 74.14 -174.84 REMARK 500 10 ASP A 62 -61.10 -91.33 REMARK 500 10 PHE A 128 41.89 -96.12 REMARK 500 11 ASP A 62 -60.55 -96.24 REMARK 500 11 PHE A 128 39.98 -96.26 REMARK 500 12 SER A 3 -178.26 -61.98 REMARK 500 12 LYS A 53 77.10 -119.63 REMARK 500 12 PHE A 128 44.02 -94.81 REMARK 500 13 SER A 3 169.64 60.00 REMARK 500 13 ASP A 62 -61.13 -94.04 REMARK 500 13 PHE A 128 40.77 -96.11 REMARK 500 14 SER A 24 -66.97 -109.42 REMARK 500 14 ASP A 62 -61.07 -91.93 REMARK 500 14 PHE A 128 39.48 -97.30 REMARK 500 15 SER A 24 -67.76 -109.32 REMARK 500 15 ASP A 62 -61.13 -91.75 REMARK 500 15 PHE A 128 39.31 -96.39 REMARK 500 16 SER A 3 79.21 59.39 REMARK 500 16 PHE A 128 44.22 -93.99 REMARK 500 17 SER A 24 -67.76 -109.32 REMARK 500 17 ASP A 62 -61.13 -91.75 REMARK 500 17 PHE A 128 39.31 -96.39 REMARK 500 18 SER A 24 -66.97 -109.42 REMARK 500 18 ASP A 62 -61.07 -91.93 REMARK 500 18 PHE A 128 39.48 -97.30 REMARK 500 19 SER A 3 175.71 62.09 REMARK 500 19 PHE A 128 41.09 -96.52 REMARK 500 20 SER A 3 -62.32 -162.31 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 SHEET DETERMINATION METHOD: AUTHOR DETERMINED DBREF 1TVJ A 1 166 UNP P21566 COF2_CHICK 1 166 SEQRES 1 A 166 MET ALA SER GLY VAL THR VAL ASN ASP GLU VAL ILE LYS SEQRES 2 A 166 VAL PHE ASN ASP MET LYS VAL ARG LYS SER SER THR PRO SEQRES 3 A 166 GLU GLU ILE LYS LYS ARG LYS LYS ALA VAL LEU PHE CYS SEQRES 4 A 166 LEU SER ASP ASP LYS LYS GLN ILE ILE VAL GLU GLU ALA SEQRES 5 A 166 LYS GLN ILE LEU VAL GLY ASP ILE GLY ASP THR VAL GLU SEQRES 6 A 166 ASP PRO TYR THR ALA PHE VAL LYS LEU LEU PRO LEU ASN SEQRES 7 A 166 ASP CYS ARG TYR ALA LEU TYR ASP ALA THR TYR GLU THR SEQRES 8 A 166 LYS GLU SER LYS LYS GLU ASP LEU VAL PHE ILE PHE TRP SEQRES 9 A 166 ALA PRO GLU SER ALA PRO LEU LYS SER LYS MET ILE TYR SEQRES 10 A 166 ALA SER SER LYS ASP ALA ILE LYS LYS LYS PHE THR GLY SEQRES 11 A 166 ILE LYS HIS GLU TRP GLN VAL ASN GLY LEU ASP ASP ILE SEQRES 12 A 166 LYS ASP ARG SER THR LEU GLY GLU LYS LEU GLY GLY ASN SEQRES 13 A 166 VAL VAL VAL SER LEU GLU GLY LYS PRO LEU HELIX 1 1 ASN A 8 VAL A 20 1 13 HELIX 2 2 THR A 25 LYS A 30 1 6 HELIX 3 3 ASP A 66 LEU A 75 1 10 HELIX 4 4 PRO A 110 LYS A 127 1 18 HELIX 5 5 GLY A 139 ILE A 143 5 5 HELIX 6 6 ASP A 145 GLY A 154 1 10 SHEET 1 A 9 THR A 6 VAL A 7 0 SHEET 2 A 9 GLN A 46 GLU A 50 1 SHEET 3 A 9 LYS A 53 LEU A 56 1 SHEET 4 A 9 LYS A 33 LEU A 40 -1 SHEET 5 A 9 ARG A 81 THR A 91 -1 SHEET 6 A 9 LYS A 95 TRP A 104 -1 SHEET 7 A 9 GLU A 134 VAL A 137 1 SHEET 8 A 9 VAL A 158 LEU A 161 -1 SHEET 9 A 9 LYS A 164 PRO A 165 -1 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 - r 2 2 Bytes