Header list of 1qqv.pdb file
Complete list - 2 20 Bytes
HEADER STRUCTURAL PROTEIN 08-JUN-99 1QQV TITLE SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: VILLIN HEADPIECE DOMAIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: HP67 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031 KEYWDS F-ACTIN BINDING DOMAIN, SALT-BRIDGE, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR D.VARDAR,D.A.BUCKLEY,B.S.FRANK,C.J.MCKNIGHT REVDAT 4 02-MAR-22 1QQV 1 REMARK REVDAT 3 24-FEB-09 1QQV 1 VERSN REVDAT 2 09-FEB-00 1QQV 1 HEADER REMARK REVDAT 1 29-DEC-99 1QQV 0 JRNL AUTH D.VARDAR,D.A.BUCKLEY,B.S.FRANK,C.J.MCKNIGHT JRNL TITL NMR STRUCTURE OF AN F-ACTIN-BINDING "HEADPIECE" MOTIF FROM JRNL TITL 2 VILLIN. JRNL REF J.MOL.BIOL. V. 294 1299 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10600386 JRNL DOI 10.1006/JMBI.1999.3321 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THIS MINIMIZED AVERAGE STRUCTURE BASED ON A TOTAL OF 1219 DISTANCE REMARK 3 RESTRAINTS, REMARK 3 1201 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 18 ARE FROM HYDROGEN REMARK 3 BONDS. THERE REMARK 3 ARE 61 DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1QQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-99. REMARK 100 THE DEPOSITION ID IS D_1000009159. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293; 293; 293; 293 REMARK 210 PH : 7.0; 7.0; 7.0; 7.0 REMARK 210 IONIC STRENGTH : LOW; LOW; LOW; LOW REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM HP67, 10 MM PHOSPHATE REMARK 210 BUFFER, PH 7.0; 1 MM HP67 U-15N , REMARK 210 10 MM PHOSPHATE BUFFER, PH 7.0; REMARK 210 1 MM HP67 U-15N,10% 13C, 10 MM REMARK 210 PHOSPHATE BUFFER, PH 7.0; 1 MM REMARK 210 HP67 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; E-COSY; REMARK 210 HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 31 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATION > 0.3, NO ANGLE REMARK 210 VIOLATIONS GREATER THAN 5 DEGREES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10 REMARK 210 REMARK 210 REMARK: THE COORDINATES ARE THE AVERAGE OF THE 10 LOWEST ENERGY REMARK 210 STRUCTURES OF THE 31 CALCULATED. 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: 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 THR A 11 178.05 64.93 REMARK 500 LYS A 12 136.23 74.21 REMARK 500 LEU A 21 -78.69 -87.90 REMARK 500 ASN A 23 -46.43 172.64 REMARK 500 THR A 24 -133.62 -143.97 REMARK 500 ALA A 25 -158.11 -104.78 REMARK 500 SER A 43 171.09 -52.60 REMARK 500 PRO A 62 -80.46 -77.23 REMARK 500 LEU A 63 -36.43 168.51 REMARK 500 LEU A 75 -45.96 -136.65 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 ARG A 31 0.31 SIDE CHAIN REMARK 500 ARG A 37 0.32 SIDE CHAIN REMARK 500 ARG A 55 0.28 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1QQV A 10 76 UNP P02640 VILI_CHICK 760 826 SEQRES 1 A 67 PRO THR LYS LEU GLU THR PHE PRO LEU ASP VAL LEU VAL SEQRES 2 A 67 ASN THR ALA ALA GLU ASP LEU PRO ARG GLY VAL ASP PRO SEQRES 3 A 67 SER ARG LYS GLU ASN HIS LEU SER ASP GLU ASP PHE LYS SEQRES 4 A 67 ALA VAL PHE GLY MET THR ARG SER ALA PHE ALA ASN LEU SEQRES 5 A 67 PRO LEU TRP LYS GLN GLN ASN LEU LYS LYS GLU LYS GLY SEQRES 6 A 67 LEU PHE HELIX 1 1 PRO A 17 VAL A 22 1 6 HELIX 2 2 LYS A 38 HIS A 41 5 4 HELIX 3 3 SER A 43 PHE A 51 1 9 HELIX 4 4 THR A 54 ASN A 60 1 7 HELIX 5 5 LEU A 63 GLY A 74 1 12 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
Complete list - 2 20 Bytes