Header list of 2fjl.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 03-JAN-06 2FJL TITLE SOLUTION STRUCTURE OF THE SPLIT PH DOMAIN IN PHOSPHOLIPASE C-GAMMA1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE COMPND 3 GAMMA 1; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: THE SPLIT PH2 DOMAIN, RESIDUSE 1-35 AND 112-148; COMPND 6 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C, PLC-GAMMA-1, PHOSPHOLIPASE COMPND 7 C-GAMMA-1, PLC-II, PLC-148; COMPND 8 EC: 3.1.4.11; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS BETA-BARREL, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR W.WEN,M.ZHANG REVDAT 4 09-MAR-22 2FJL 1 REMARK SEQADV REVDAT 3 24-FEB-09 2FJL 1 VERSN REVDAT 2 09-MAY-06 2FJL 1 JRNL REVDAT 1 14-MAR-06 2FJL 0 JRNL AUTH W.WEN,J.YAN,M.ZHANG JRNL TITL STRUCTURAL CHARACTERIZATION OF THE SPLIT PLECKSTRIN HOMOLOGY JRNL TITL 2 DOMAIN IN PHOSPHOLIPASE C-{GAMMA}1 AND ITS INTERACTION WITH JRNL TITL 3 TRPC3 JRNL REF J.BIOL.CHEM. V. 281 12060 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16500902 JRNL DOI 10.1074/JBC.M600336200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2145 RESTRAINTS, 2023 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 60 DIHEDRAL ANGLE RESTRAINTS,62 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 2FJL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-06. REMARK 100 THE DEPOSITION ID IS D_1000035953. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0MM OF THE PHN-PHC TANDEM U REMARK 210 -15N; 50MM POTASSIUM PHOSPHATE; REMARK 210 90% H2O, 10% D2O; 1.0MM OF THE REMARK 210 PHN-PHC TANDEM U-15N,13C; 50MM REMARK 210 POTASSIUM PHOSPHATE; 90% H2O, 10% REMARK 210 D2O; 1.0MM OF THE PHN-PHC REMARK 210 TANDEM U-15N,13C; 50MM POTASSIUM REMARK 210 PHOSPHATE; 100% D2O; 1.0MM OF REMARK 210 THE PHN-PHC TANDEM; 50MM REMARK 210 POTASSIUM PHOSPHATE; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNCACB, REMARK 210 CBCA(CO)NH; 3D_13C-SEPARATED_ REMARK 210 NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 1 LEU A 9 134.38 -171.86 REMARK 500 1 GLU A 10 90.54 -65.31 REMARK 500 1 SER A 26 -32.45 -39.94 REMARK 500 1 SER A 27 48.27 -152.09 REMARK 500 1 GLU A 34 96.77 68.49 REMARK 500 1 SER A 36 39.92 -98.20 REMARK 500 1 ASP A 38 80.51 -161.28 REMARK 500 1 ASP A 43 85.80 -154.12 REMARK 500 1 PRO A 47 63.16 -69.96 REMARK 500 1 LYS A 48 137.91 63.54 REMARK 500 1 SER A 53 32.67 -98.68 REMARK 500 1 HIS A 57 90.24 -176.07 REMARK 500 1 LEU A 60 -10.58 80.67 REMARK 500 1 GLN A 65 26.47 -151.43 REMARK 500 1 PRO A 67 84.22 -62.61 REMARK 500 1 ASN A 68 80.49 59.56 REMARK 500 1 ALA A 70 30.18 -96.50 REMARK 500 1 GLU A 73 66.86 -150.31 REMARK 500 1 PRO A 74 59.56 -68.69 REMARK 500 1 ASP A 80 72.33 -68.91 REMARK 500 1 LEU A 85 -44.04 -164.57 REMARK 500 1 ASP A 87 -44.81 -165.77 REMARK 500 1 LEU A 88 89.17 56.12 REMARK 500 1 PRO A 96 49.77 -85.51 REMARK 500 1 ALA A 97 38.13 -179.43 REMARK 500 1 PRO A 104 22.85 -77.69 REMARK 500 1 GLU A 105 64.86 -173.38 REMARK 500 1 LYS A 107 156.04 179.85 REMARK 500 1 SER A 117 128.66 -173.29 REMARK 500 1 PRO A 119 48.15 -84.37 REMARK 500 1 SER A 120 39.25 177.80 REMARK 500 1 VAL A 121 -49.61 -131.72 REMARK 500 1 ALA A 122 40.16 165.30 REMARK 500 2 GLU A 10 -169.80 46.50 REMARK 500 2 TYR A 31 102.70 -162.04 REMARK 500 2 SER A 32 85.40 178.29 REMARK 500 2 GLU A 33 177.93 62.71 REMARK 500 2 SER A 36 37.45 -163.69 REMARK 500 2 SER A 37 171.43 60.65 REMARK 500 2 GLU A 45 84.46 -151.82 REMARK 500 2 LYS A 48 51.40 -111.65 REMARK 500 2 GLU A 49 177.45 61.34 REMARK 500 2 SER A 51 -72.48 -148.76 REMARK 500 2 LEU A 60 -45.85 -147.45 REMARK 500 2 GLN A 65 33.50 177.04 REMARK 500 2 ASN A 68 105.69 62.91 REMARK 500 2 GLU A 73 83.73 -156.24 REMARK 500 2 PRO A 74 57.24 -68.87 REMARK 500 2 GLU A 75 -76.89 -92.21 REMARK 500 2 GLU A 77 80.32 -160.63 REMARK 500 REMARK 500 THIS ENTRY HAS 399 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2FJL A 1 59 UNP P10686 PLCG1_RAT 489 547 DBREF 2FJL A 68 150 UNP P10686 PLCG1_RAT 851 933 SEQADV 2FJL LEU A 60 UNP P10686 LINKER SEQADV 2FJL GLU A 61 UNP P10686 LINKER SEQADV 2FJL VAL A 62 UNP P10686 LINKER SEQADV 2FJL LEU A 63 UNP P10686 LINKER SEQADV 2FJL PHE A 64 UNP P10686 LINKER SEQADV 2FJL GLN A 65 UNP P10686 LINKER SEQADV 2FJL GLY A 66 UNP P10686 LINKER SEQADV 2FJL PRO A 67 UNP P10686 LINKER SEQRES 1 A 150 SER ILE LYS ASN GLY ILE LEU TYR LEU GLU ASP PRO VAL SEQRES 2 A 150 ASN HIS GLU TRP TYR PRO HIS TYR PHE VAL LEU THR SER SEQRES 3 A 150 SER LYS ILE TYR TYR SER GLU GLU THR SER SER ASP GLN SEQRES 4 A 150 GLY ASN GLU ASP GLU GLU GLU PRO LYS GLU ALA SER GLY SEQRES 5 A 150 SER THR GLU LEU HIS SER SER LEU GLU VAL LEU PHE GLN SEQRES 6 A 150 GLY PRO ASN PRO ALA ILE LEU GLU PRO GLU ARG GLU HIS SEQRES 7 A 150 LEU ASP GLU ASN SER PRO LEU GLY ASP LEU LEU ARG GLY SEQRES 8 A 150 VAL LEU ASP VAL PRO ALA CYS GLN ILE ALA ILE ARG PRO SEQRES 9 A 150 GLU GLY LYS ASN ASN ARG LEU PHE VAL PHE SER ILE SER SEQRES 10 A 150 MET PRO SER VAL ALA GLN TRP SER LEU ASP VAL ALA ALA SEQRES 11 A 150 ASP SER GLN GLU GLU LEU GLN ASP TRP VAL LYS LYS ILE SEQRES 12 A 150 ARG GLU VAL ALA GLN THR ALA HELIX 1 1 VAL A 62 GLY A 66 5 5 HELIX 2 2 SER A 132 GLN A 148 1 17 SHEET 1 A 4 LYS A 3 ASP A 11 0 SHEET 2 A 4 GLU A 16 THR A 25 -1 O LEU A 24 N LYS A 3 SHEET 3 A 4 LYS A 28 TYR A 31 -1 O LYS A 28 N THR A 25 SHEET 4 A 4 GLY A 91 LEU A 93 -1 O LEU A 93 N ILE A 29 SHEET 1 B 3 GLN A 99 ARG A 103 0 SHEET 2 B 3 VAL A 113 SER A 117 -1 O SER A 115 N ALA A 101 SHEET 3 B 3 LEU A 126 VAL A 128 -1 O LEU A 126 N ILE A 116 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