Header list of 2aav.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 14-JUL-05 2AAV TITLE SOLUTION NMR STRUCTURE OF FILAMIN A DOMAIN 17 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FILAMIN A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FILAMIN A DOMAIN 17; COMPND 5 SYNONYM: ALPHA-FILAMIN, FILAMIN 1, ENDOTHELIAL ACTIN-BINDING PROTEIN, COMPND 6 ACTIN-BINDING PROTEIN 280, ABP-280, NONMUSCLE FILAMIN; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS FILAMIN A DOMAIN 17, BETA-SANDWICH, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.NAKAMURA,R.PUDAS,O.HEIKKINEN,P.PERMI,I.KILPELAINEN,A.D.MUNDAY, AUTHOR 2 J.H.HARTWIG,T.P.STOSSEL,J.YLANNE REVDAT 3 09-MAR-22 2AAV 1 REMARK SEQADV REVDAT 2 24-FEB-09 2AAV 1 VERSN REVDAT 1 02-MAY-06 2AAV 0 JRNL AUTH F.NAKAMURA,R.PUDAS,O.HEIKKINEN,P.PERMI,I.KILPELAINEN, JRNL AUTH 2 A.D.MUNDAY,J.H.HARTWIG,T.P.STOSSEL,J.YLANNE JRNL TITL THE STRUCTURE OF THE GPIB-FILAMIN A COMPLEX JRNL REF BLOOD V. 107 1925 2006 JRNL REFN ISSN 0006-4971 JRNL PMID 16293600 JRNL DOI 10.1182/BLOOD-2005-10-3964 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1, AMBER 8.0 REMARK 3 AUTHORS : VARIAN INC. (VNMR), REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2AAV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033692. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 50MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : GAMV(1863-1956FLNA), U-13C, U REMARK 210 -15N, NMR SAMPLE 0.3MM; 50MM REMARK 210 SODIUM PHOSPHATE, 10MM REMARK 210 DITHIOTHREITOL; 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : UNITY INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.106, CYANA 2.0 REMARK 210 METHOD USED : THE STRUCTURE CALCULATIONS WERE REMARK 210 MADE WITH THE PROGRAM CYANA 2.0 REMARK 210 USING THE AUTOMATED NOE REMARK 210 ASSIGNMENT AND STRUCTURE REMARK 210 CALCULATION ALGORITHM. THE REMARK 210 STRUCTURE REFINEMENT OF THE 20 REMARK 210 FINAL CYANA STRUCTURES WAS MADE REMARK 210 WITH AMBER 8.0 PROGRAM USING THE REMARK 210 GENERALIZED BORN CONTINUUM REMARK 210 SOLVENT MODEL. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE NUMBERING OF RESIDUES IN CONSTRAINT AND CHEMICAL SHIFT REMARK 210 FILES CORRESPONDS TO THE NUMBERING OF NMR CONSTRUCT (RESIDUES 1- REMARK 210 98). 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 3 VAL A1888 CA - CB - CG1 ANGL. DEV. = 15.3 DEGREES REMARK 500 4 VAL A1943 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES REMARK 500 11 VAL A1943 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES REMARK 500 11 ARG A1951 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 12 VAL A1943 CA - CB - CG1 ANGL. DEV. = 10.3 DEGREES REMARK 500 17 ARG A1951 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 20 ARG A1951 NE - CZ - NH1 ANGL. DEV. = 3.1 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 THR A1890 34.72 -79.29 REMARK 500 1 LYS A1891 -39.35 -37.97 REMARK 500 1 ILE A1910 72.21 25.29 REMARK 500 1 ASN A1915 -165.65 49.89 REMARK 500 1 SER A1921 115.06 -33.91 REMARK 500 1 ASN A1939 71.89 44.77 REMARK 500 1 GLU A1940 -9.12 68.15 REMARK 500 2 ALA A -3 -32.09 -130.19 REMARK 500 2 ASN A1864 -27.08 63.94 REMARK 500 2 LYS A1891 -68.22 58.17 REMARK 500 2 ALA A1893 71.90 -67.81 REMARK 500 2 ASN A1939 73.07 52.20 REMARK 500 2 GLU A1940 -16.72 69.86 REMARK 500 2 PRO A1944 108.67 -57.91 REMARK 500 2 VAL A1952 109.77 -59.00 REMARK 500 3 ALA A -3 -177.68 -67.68 REMARK 500 3 ASP A1892 -8.59 60.84 REMARK 500 3 SER A1921 58.00 22.63 REMARK 500 3 GLU A1940 -8.18 63.02 REMARK 500 4 CYS A1865 109.32 -56.23 REMARK 500 4 LYS A1891 -85.96 -91.66 REMARK 500 4 LEU A1935 66.54 -106.74 REMARK 500 4 ASN A1939 78.40 52.51 REMARK 500 4 GLU A1940 -15.11 70.78 REMARK 500 4 PRO A1944 97.19 -61.67 REMARK 500 4 ASP A1955 -31.89 -139.79 REMARK 500 5 VAL A1888 42.04 -150.14 REMARK 500 5 ASN A1889 104.97 -48.32 REMARK 500 5 ASP A1914 88.43 -67.93 REMARK 500 5 SER A1921 90.75 15.97 REMARK 500 5 LEU A1935 78.36 -115.33 REMARK 500 5 ASN A1939 73.13 54.83 REMARK 500 5 GLU A1940 -6.14 65.58 REMARK 500 5 VAL A1952 93.47 -65.10 REMARK 500 5 ASP A1955 -43.38 -137.64 REMARK 500 6 SER A1921 108.20 -22.19 REMARK 500 6 ASN A1939 79.76 53.53 REMARK 500 6 GLU A1940 -4.77 64.10 REMARK 500 6 ASP A1955 -71.99 -134.18 REMARK 500 7 VAL A -1 -0.45 64.35 REMARK 500 7 ASN A1881 18.05 54.58 REMARK 500 7 THR A1890 74.19 -104.69 REMARK 500 7 LYS A1891 -72.25 -107.49 REMARK 500 7 GLU A1895 19.29 49.14 REMARK 500 7 SER A1921 86.20 13.63 REMARK 500 7 LEU A1925 85.08 -152.45 REMARK 500 7 GLU A1940 -3.66 66.51 REMARK 500 7 PRO A1944 109.46 -58.63 REMARK 500 7 VAL A1952 104.07 -8.43 REMARK 500 7 ASP A1955 -46.30 -144.27 REMARK 500 REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS. 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 18 TYR A1938 0.07 SIDE CHAIN REMARK 500 20 TYR A1932 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2BP3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FILAMIN A DOMAIN 17 AND GPIB ALPHA CYTOPLASMIC REMARK 900 DOMAIN COMPLEX DBREF 2AAV A 1863 1956 UNP P21333 FLNA_HUMAN 1862 1955 SEQADV 2AAV GLY A -4 UNP P21333 CLONING ARTIFACT SEQADV 2AAV ALA A -3 UNP P21333 CLONING ARTIFACT SEQADV 2AAV MET A -2 UNP P21333 CLONING ARTIFACT SEQADV 2AAV VAL A -1 UNP P21333 CLONING ARTIFACT SEQRES 1 A 98 GLY ALA MET VAL VAL ASN CYS GLY HIS VAL THR ALA TYR SEQRES 2 A 98 GLY PRO GLY LEU THR HIS GLY VAL VAL ASN LYS PRO ALA SEQRES 3 A 98 THR PHE THR VAL ASN THR LYS ASP ALA GLY GLU GLY GLY SEQRES 4 A 98 LEU SER LEU ALA ILE GLU GLY PRO SER LYS ALA GLU ILE SEQRES 5 A 98 SER CYS THR ASP ASN GLN ASP GLY THR CYS SER VAL SER SEQRES 6 A 98 TYR LEU PRO VAL LEU PRO GLY ASP TYR SER ILE LEU VAL SEQRES 7 A 98 LYS TYR ASN GLU GLN HIS VAL PRO GLY SER PRO PHE THR SEQRES 8 A 98 ALA ARG VAL THR GLY ASP ASP HELIX 1 1 GLY A 1872 LEU A 1875 5 4 SHEET 1 A 4 HIS A1877 GLY A1878 0 SHEET 2 A 4 PHE A1948 VAL A1952 1 O ARG A1951 N GLY A1878 SHEET 3 A 4 GLY A1930 TYR A1938 -1 N TYR A1932 O ALA A1950 SHEET 4 A 4 LEU A1898 GLU A1903 -1 N SER A1899 O LYS A1937 SHEET 1 B 4 HIS A1877 GLY A1878 0 SHEET 2 B 4 PHE A1948 VAL A1952 1 O ARG A1951 N GLY A1878 SHEET 3 B 4 GLY A1930 TYR A1938 -1 N TYR A1932 O ALA A1950 SHEET 4 B 4 GLN A1941 HIS A1942 -1 O GLN A1941 N TYR A1938 SHEET 1 C 3 ALA A1884 PHE A1886 0 SHEET 2 C 3 VAL A1922 TYR A1924 -1 O TYR A1924 N ALA A1884 SHEET 3 C 3 SER A1911 CYS A1912 -1 N SER A1911 O SER A1923 CISPEP 1 SER A 1946 PRO A 1947 1 -11.96 CISPEP 2 SER A 1946 PRO A 1947 2 -10.92 CISPEP 3 SER A 1946 PRO A 1947 3 -4.30 CISPEP 4 SER A 1946 PRO A 1947 4 -2.81 CISPEP 5 SER A 1946 PRO A 1947 5 -1.97 CISPEP 6 SER A 1946 PRO A 1947 6 -3.31 CISPEP 7 SER A 1946 PRO A 1947 7 -10.89 CISPEP 8 SER A 1946 PRO A 1947 8 -7.58 CISPEP 9 SER A 1946 PRO A 1947 9 -2.62 CISPEP 10 SER A 1946 PRO A 1947 10 -6.07 CISPEP 11 SER A 1946 PRO A 1947 11 -3.89 CISPEP 12 SER A 1946 PRO A 1947 12 -2.82 CISPEP 13 SER A 1946 PRO A 1947 13 -8.44 CISPEP 14 SER A 1946 PRO A 1947 14 -5.55 CISPEP 15 SER A 1946 PRO A 1947 15 -3.26 CISPEP 16 SER A 1946 PRO A 1947 16 -15.51 CISPEP 17 SER A 1946 PRO A 1947 17 -14.41 CISPEP 18 SER A 1946 PRO A 1947 18 -5.94 CISPEP 19 SER A 1946 PRO A 1947 19 -9.95 CISPEP 20 SER A 1946 PRO A 1947 20 -10.71 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 9 2 Bytes