Header list of 1tuz.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 25-JUN-04 1TUZ TITLE NMR STRUCTURE OF THE DIACYLGLYCEROL KINASE ALPHA, NESGC TARGET HR532 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIACYLGLYCEROL KINASE ALPHA; COMPND 3 CHAIN: A; COMPND 4 EC: 2.7.1.107; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: DAGK1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14 KEYWDS KINASE, TRANSFERASE, HR532, NESGC, STRUCTURAL GENOMICS, PSI, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.LIU,Y.SHAO,R.XIAO,T.ACTON,G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 3 02-MAR-22 1TUZ 1 REMARK REVDAT 2 24-FEB-09 1TUZ 1 VERSN REVDAT 1 04-JAN-05 1TUZ 0 JRNL AUTH G.LIU,Y.SHAO,R.XIAO,T.ACTON,G.T.MONTELIONE,T.SZYPERSKI JRNL TITL NMR STRUCTURE OF DIACYLGLYCEROL KINASE ALPHA, NESGC TARGET JRNL TITL 2 HR532 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GUENTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2205 RESTRAINTS, 2039 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 166 DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1TUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1000022924. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : N.A. REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM, U-15N,13C HR532, 5% D2O, REMARK 210 0.02% NAN3, 10MM DTT, 5MM CACL2, REMARK 210 100MM NACL, 20MM MES, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; RD REMARK 210 HABCABCONHN; RD HCCH COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, XWINNMR N.A, VNMR REMARK 210 N.A, XEASY 1.3.13 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE AND RD REMARK 210 NMR 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: 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 14 H LYS A 18 1.51 REMARK 500 O LEU A 96 H SER A 100 1.57 REMARK 500 O PHE A 56 H TYR A 60 1.57 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 ALA A 2 73.43 -111.44 REMARK 500 1 LYS A 3 -130.11 -103.92 REMARK 500 1 GLU A 4 149.05 79.37 REMARK 500 1 ARG A 5 35.54 -176.02 REMARK 500 1 SER A 9 179.73 -50.15 REMARK 500 1 GLU A 62 24.96 47.43 REMARK 500 1 ASN A 65 116.87 -175.36 REMARK 500 1 THR A 80 134.35 167.96 REMARK 500 1 CYS A 83 138.37 -170.03 REMARK 500 1 LEU A 84 42.61 -90.06 REMARK 500 1 ASN A 85 45.34 -177.72 REMARK 500 1 THR A 87 47.40 -107.26 REMARK 500 1 LYS A 91 80.07 36.40 REMARK 500 1 GLU A 112 -34.60 175.64 REMARK 500 1 ASP A 113 115.24 177.05 REMARK 500 1 TRP A 117 71.45 -106.53 REMARK 500 2 LYS A 3 -130.13 -144.17 REMARK 500 2 GLU A 4 144.97 68.27 REMARK 500 2 SER A 9 179.45 -49.67 REMARK 500 2 SER A 23 90.72 44.70 REMARK 500 2 TYR A 60 -73.37 -40.38 REMARK 500 2 GLU A 62 10.82 82.28 REMARK 500 2 ASN A 65 117.46 -175.20 REMARK 500 2 SER A 77 -77.98 -55.57 REMARK 500 2 GLU A 79 41.66 -177.97 REMARK 500 2 THR A 80 105.85 52.13 REMARK 500 2 ASN A 85 108.35 64.20 REMARK 500 2 GLU A 86 133.82 179.70 REMARK 500 2 ASN A 88 54.97 -145.94 REMARK 500 2 VAL A 89 74.93 -109.09 REMARK 500 2 ASP A 113 113.12 177.87 REMARK 500 2 LEU A 115 177.14 -50.23 REMARK 500 2 TRP A 117 73.22 -108.29 REMARK 500 3 LYS A 3 -121.31 -174.54 REMARK 500 3 GLU A 4 148.05 171.29 REMARK 500 3 ARG A 5 46.13 -86.52 REMARK 500 3 SER A 9 171.30 53.38 REMARK 500 3 THR A 24 18.01 -146.48 REMARK 500 3 TYR A 60 -72.55 -39.73 REMARK 500 3 ASN A 65 116.70 -173.86 REMARK 500 3 LEU A 84 102.37 67.19 REMARK 500 3 ASN A 85 101.17 64.02 REMARK 500 3 GLU A 86 133.32 -178.65 REMARK 500 3 ASP A 113 110.79 175.62 REMARK 500 3 TRP A 117 72.69 -106.94 REMARK 500 4 ALA A 2 47.11 -87.43 REMARK 500 4 LYS A 3 -124.61 -76.97 REMARK 500 4 GLU A 4 142.35 68.32 REMARK 500 4 ARG A 5 48.63 -144.85 REMARK 500 4 SER A 9 172.51 61.70 REMARK 500 REMARK 500 THIS ENTRY HAS 305 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6208 RELATED DB: BMRB REMARK 900 NMR CHEMICAL SHIFT REMARK 900 RELATED ID: HR532 RELATED DB: TARGETDB DBREF 1TUZ A 1 118 GB 3551834 AAC34806 1 118 SEQRES 1 A 118 MET ALA LYS GLU ARG GLY LEU ILE SER PRO SER ASP PHE SEQRES 2 A 118 ALA GLN LEU GLN LYS TYR MET GLU TYR SER THR LYS LYS SEQRES 3 A 118 VAL SER ASP VAL LEU LYS LEU PHE GLU ASP GLY GLU MET SEQRES 4 A 118 ALA LYS TYR VAL GLN GLY ASP ALA ILE GLY TYR GLU GLY SEQRES 5 A 118 PHE GLN GLN PHE LEU LYS ILE TYR LEU GLU VAL ASP ASN SEQRES 6 A 118 VAL PRO ARG HIS LEU SER LEU ALA LEU PHE GLN SER PHE SEQRES 7 A 118 GLU THR GLY HIS CYS LEU ASN GLU THR ASN VAL THR LYS SEQRES 8 A 118 ASP VAL VAL CYS LEU ASN ASP VAL SER CYS TYR PHE SER SEQRES 9 A 118 LEU LEU GLU GLY GLY ARG PRO GLU ASP LYS LEU GLU TRP SEQRES 10 A 118 SER HELIX 1 1 SER A 9 SER A 23 1 15 HELIX 2 2 LYS A 26 ASP A 36 1 11 HELIX 3 3 GLY A 37 LYS A 41 5 5 HELIX 4 4 GLY A 49 LEU A 61 1 13 HELIX 5 5 PRO A 67 PHE A 78 1 12 HELIX 6 6 LEU A 96 GLY A 108 1 13 SHEET 1 A 3 VAL A 43 GLN A 44 0 SHEET 2 A 3 ALA A 47 ILE A 48 -1 O ALA A 47 N GLN A 44 SHEET 3 A 3 VAL A 94 CYS A 95 -1 O VAL A 94 N ILE A 48 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