Header list of 1dp3.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 23-DEC-99 1DP3 TITLE SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE TRAM PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRAM PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TRAMM26; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET28A(+) KEYWDS HELIX-LOOP-HELIX, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.STOCKNER,C.PLUGARIU,G.KORAIMANN,G.HOEGENAUER,W.BERMEL,S.PRYTULLA, AUTHOR 2 H.STERK REVDAT 4 16-FEB-22 1DP3 1 REMARK REVDAT 3 24-FEB-09 1DP3 1 VERSN REVDAT 2 01-APR-03 1DP3 1 JRNL REVDAT 1 04-APR-01 1DP3 0 JRNL AUTH T.STOCKNER,C.PLUGARIU,G.KORAIMANN,G.HOGENAUER,W.BERMEL, JRNL AUTH 2 S.PRYTULLA,H.STERK JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF TRAM. JRNL REF BIOCHEMISTRY V. 40 3370 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11258958 JRNL DOI 10.1021/BI002031C REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851 REMARK 3 AUTHORS : BRUKER ANALYTICAL GMBH (XWINNMR), BRUNGER, A.T. (X REMARK 3 -PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURES ARE BASED ON 438 NOE REMARK 3 RESTRAINTS DERIVED FROM 15N LABELED NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS, 115 DISTANCE RESTRAINTS FROM 2D HOMONUCLEAR NOESY REMARK 3 EXPERIMENTS AND 40 DIHEDRAL ANGLE RESTRAINTS. THE DIHEDRAL REMARK 3 RESTRAINTS WITH RANDOM COIL VALUES FOR THE FLEXIBLE TERMINAL REMARK 3 PART EXTRACTED FROM THE HNHA SPECTRA WERE NOT USED IN THE REMARK 3 STRUCTURE CALCULATIONS. REMARK 4 REMARK 4 1DP3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-00. REMARK 100 THE DEPOSITION ID IS D_1000010259. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300; 300 REMARK 210 PH : 4.0; 4.0 REMARK 210 IONIC STRENGTH : 50 MM POSPHATE BUFFER; 50 MM REMARK 210 PHOSPATE BUFFER REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : UNLABELED TRAMM26, UNIFORM REMARK 210 LABELED TRAMM26 WITH 15N; 50MM REMARK 210 PHOSPHATE BUFFER NA; 95% H2O 5% REMARK 210 D2O; UNIFORM LABELED TRAMM26 REMARK 210 WITH 15N; 50MM PHOSPHATE BUFFER REMARK 210 NA; 95% H2O 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D-15N-NOESY-HSQC; REMARK 210 HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; UNITY INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG 3.3, MOLMOL 2.6, REMARK 210 VNMR 5.2 REMARK 210 METHOD USED : DISTANCE GEOMETRY; SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13 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 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 GLN A 5 -162.44 48.01 REMARK 500 1 ALA A 6 124.21 61.01 REMARK 500 1 SER A 9 -169.23 -123.35 REMARK 500 1 ASP A 10 78.69 -59.90 REMARK 500 1 ALA A 28 173.17 -50.54 REMARK 500 1 SER A 30 146.64 62.63 REMARK 500 1 THR A 31 32.42 -89.20 REMARK 500 1 LEU A 47 22.69 47.37 REMARK 500 1 ARG A 48 -120.74 -74.68 REMARK 500 1 GLU A 55 -170.65 45.22 REMARK 500 2 VAL A 4 123.47 60.53 REMARK 500 2 ALA A 6 90.13 -166.93 REMARK 500 2 TYR A 7 56.05 -143.07 REMARK 500 2 ASP A 10 78.07 -60.02 REMARK 500 2 ARG A 23 -71.23 -53.71 REMARK 500 2 LYS A 29 -32.00 -179.46 REMARK 500 2 SER A 34 151.51 177.13 REMARK 500 2 LEU A 47 -3.22 73.24 REMARK 500 2 VAL A 49 -113.05 -56.21 REMARK 500 2 GLU A 55 -160.70 38.80 REMARK 500 3 LYS A 3 -172.08 -170.53 REMARK 500 3 GLN A 5 157.11 58.98 REMARK 500 3 ALA A 6 89.22 54.37 REMARK 500 3 TYR A 7 50.94 -160.62 REMARK 500 3 VAL A 8 130.62 -176.81 REMARK 500 3 ASP A 10 71.31 -63.24 REMARK 500 3 ALA A 28 40.22 -97.01 REMARK 500 3 LYS A 29 32.03 177.37 REMARK 500 3 SER A 30 -170.56 52.36 REMARK 500 3 SER A 34 148.05 179.09 REMARK 500 3 LEU A 47 14.73 50.69 REMARK 500 3 ARG A 48 -73.27 -75.81 REMARK 500 3 GLU A 55 -165.60 -79.44 REMARK 500 4 LYS A 3 73.25 56.65 REMARK 500 4 GLN A 5 164.65 54.86 REMARK 500 4 ALA A 6 48.01 175.47 REMARK 500 4 TYR A 7 73.88 47.84 REMARK 500 4 ASP A 10 77.49 -60.49 REMARK 500 4 ALA A 28 144.54 -36.05 REMARK 500 4 LYS A 29 -67.14 179.74 REMARK 500 4 VAL A 33 173.71 -45.80 REMARK 500 4 LEU A 47 -18.99 77.17 REMARK 500 4 VAL A 49 -71.47 -53.28 REMARK 500 5 GLN A 5 -163.37 -66.62 REMARK 500 5 TYR A 7 -175.72 -66.05 REMARK 500 5 SER A 9 -152.32 43.24 REMARK 500 5 ASP A 10 90.09 -31.95 REMARK 500 5 LYS A 29 -35.19 -173.89 REMARK 500 5 SER A 30 155.31 -43.44 REMARK 500 5 THR A 31 39.61 -86.54 REMARK 500 REMARK 500 THIS ENTRY HAS 214 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 1 ARG A 22 0.23 SIDE CHAIN REMARK 500 1 ARG A 23 0.26 SIDE CHAIN REMARK 500 1 ARG A 24 0.27 SIDE CHAIN REMARK 500 1 ARG A 48 0.19 SIDE CHAIN REMARK 500 1 ARG A 56 0.29 SIDE CHAIN REMARK 500 2 ARG A 22 0.28 SIDE CHAIN REMARK 500 2 ARG A 23 0.32 SIDE CHAIN REMARK 500 2 ARG A 24 0.24 SIDE CHAIN REMARK 500 2 ARG A 48 0.31 SIDE CHAIN REMARK 500 2 ARG A 56 0.09 SIDE CHAIN REMARK 500 3 ARG A 22 0.31 SIDE CHAIN REMARK 500 3 ARG A 23 0.21 SIDE CHAIN REMARK 500 3 ARG A 24 0.31 SIDE CHAIN REMARK 500 3 ARG A 48 0.30 SIDE CHAIN REMARK 500 3 ARG A 56 0.27 SIDE CHAIN REMARK 500 4 ARG A 22 0.24 SIDE CHAIN REMARK 500 4 ARG A 23 0.29 SIDE CHAIN REMARK 500 4 ARG A 24 0.31 SIDE CHAIN REMARK 500 4 ARG A 48 0.26 SIDE CHAIN REMARK 500 4 ARG A 56 0.31 SIDE CHAIN REMARK 500 5 ARG A 22 0.31 SIDE CHAIN REMARK 500 5 ARG A 23 0.29 SIDE CHAIN REMARK 500 5 ARG A 24 0.25 SIDE CHAIN REMARK 500 5 ARG A 48 0.24 SIDE CHAIN REMARK 500 5 ARG A 56 0.31 SIDE CHAIN REMARK 500 6 ARG A 22 0.30 SIDE CHAIN REMARK 500 6 ARG A 23 0.20 SIDE CHAIN REMARK 500 6 ARG A 24 0.32 SIDE CHAIN REMARK 500 6 ARG A 48 0.31 SIDE CHAIN REMARK 500 6 ARG A 56 0.29 SIDE CHAIN REMARK 500 7 ARG A 22 0.26 SIDE CHAIN REMARK 500 7 ARG A 23 0.30 SIDE CHAIN REMARK 500 7 ARG A 24 0.23 SIDE CHAIN REMARK 500 7 ARG A 48 0.32 SIDE CHAIN REMARK 500 7 ARG A 56 0.32 SIDE CHAIN REMARK 500 8 ARG A 22 0.25 SIDE CHAIN REMARK 500 8 ARG A 23 0.20 SIDE CHAIN REMARK 500 8 ARG A 24 0.28 SIDE CHAIN REMARK 500 8 ARG A 48 0.19 SIDE CHAIN REMARK 500 8 ARG A 56 0.26 SIDE CHAIN REMARK 500 9 ARG A 23 0.31 SIDE CHAIN REMARK 500 9 ARG A 24 0.23 SIDE CHAIN REMARK 500 9 ARG A 48 0.21 SIDE CHAIN REMARK 500 9 ARG A 56 0.28 SIDE CHAIN REMARK 500 10 ARG A 22 0.31 SIDE CHAIN REMARK 500 10 ARG A 23 0.31 SIDE CHAIN REMARK 500 10 ARG A 24 0.31 SIDE CHAIN REMARK 500 10 ARG A 48 0.13 SIDE CHAIN REMARK 500 11 ARG A 22 0.25 SIDE CHAIN REMARK 500 11 ARG A 23 0.25 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 96 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1DP3 A 2 56 UNP P07294 TRAM2_ECOLI 2 56 SEQRES 1 A 55 ALA LYS VAL GLN ALA TYR VAL SER ASP GLU ILE VAL TYR SEQRES 2 A 55 LYS ILE ASN LYS ILE VAL GLU ARG ARG ARG ALA GLU GLY SEQRES 3 A 55 ALA LYS SER THR ASP VAL SER PHE SER SER ILE SER THR SEQRES 4 A 55 MET LEU LEU GLU LEU GLY LEU ARG VAL TYR GLU ALA GLN SEQRES 5 A 55 MET GLU ARG HELIX 1 1 ASP A 10 GLY A 27 1 18 HELIX 2 2 SER A 34 GLY A 46 1 13 HELIX 3 3 LEU A 47 GLN A 53 1 7 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 - b 16 2 Bytes