Header list of 1h1j.pdb file
Complete list - n 24 2 Bytes
HEADER DNA BINDING 16-JUL-02 1H1J TITLE THE SAP DOMAIN IS A DNA-BINDING DOMAIN CAPABLE OF BINDING S/MAR DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: THO1 PROTEIN; COMPND 3 CHAIN: S; COMPND 4 FRAGMENT: SAP DOMAIN, RESIDUES 2-50; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKERS YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGRO KEYWDS SAP DOMAIN, DNA BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.O.B.JACOBSEN,S.M.V.FREUND,M.BYCROFT REVDAT 3 24-JAN-18 1H1J 1 SOURCE REVDAT 2 24-FEB-09 1H1J 1 VERSN REVDAT 1 08-AUG-02 1H1J 0 JRNL AUTH J.O.B.JACOBSEN,S.M.V.FREUND,M.BYCROFT JRNL TITL THE SAP DOMAIN IS A DNA-BINDING DOMAIN CAPABLE OF BINDING JRNL TITL 2 S/MAR DNA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.ARAVIND,E.V.KOONIN REMARK 1 TITL SAP - A PUTATIVE DNA-BINDING MOTIF INVOLVED IN CHROMOSOMAL REMARK 1 TITL 2 ORGANIZATION REMARK 1 REF TRENDS BIOCHEM.SCI. V. 25 112 2000 REMARK 1 REFN ISSN 0968-0004 REMARK 1 PMID 10694879 REMARK 1 DOI 10.1016/S0968-0004(99)01537-6 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.I.PIRUAT,A.AGUILERA REMARK 1 TITL A NOVEL YEAST GENE, THO2, IS INVOLVED IN RNA POL II REMARK 1 TITL 2 TRANSCRIPTION AND PROVIDES NEW EVIDENCE FOR TRANSCRIPTIONAL REMARK 1 TITL 3 ELONGATION-ASSOCIATED RECOMBINATION. REMARK 1 REF EMBO J. V. 17 4859 1998 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 9707445 REMARK 1 DOI 10.1093/EMBOJ/17.16.4859 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. RESIDUES 45-51 ARE DISORDERED WITH NO REMARK 3 DEFINED STRUCTURE AND NOT INCLUDED IN THE COORDINATES. REMARK 4 REMARK 4 1H1J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-02. REMARK 100 THE DEPOSITION ID IS D_1290011077. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 150 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C-FILTERED NOESY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, SPARKY, XPLOR 3.8 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST NOE ENERGIES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURE DETERMINED USING STANDARD TRIPLE-RESONANCE AND REMARK 210 3D 1H,13C- NOESY/TOCSY EXPERIMENTS ON 13C, 15N-LABELED PROTEIN. 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: S 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLU S 45 REMARK 465 SER S 46 REMARK 465 GLU S 47 REMARK 465 VAL S 48 REMARK 465 SER S 49 REMARK 465 PRO S 50 REMARK 465 GLN S 51 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 SER S 2 -52.25 -151.48 REMARK 500 1 ALA S 3 -178.19 49.26 REMARK 500 1 ASP S 4 -95.69 -121.11 REMARK 500 1 SER S 6 -64.38 -3.11 REMARK 500 1 SER S 7 48.15 -153.19 REMARK 500 1 LYS S 43 105.45 -178.74 REMARK 500 2 ASP S 4 -95.46 -128.84 REMARK 500 2 SER S 6 -70.08 1.99 REMARK 500 2 SER S 7 56.84 -151.92 REMARK 500 2 GLU S 41 73.97 42.69 REMARK 500 3 SER S 2 179.71 64.95 REMARK 500 3 ASP S 4 -95.38 -128.35 REMARK 500 3 SER S 6 -60.58 -6.55 REMARK 500 3 SER S 7 49.67 -152.96 REMARK 500 3 GLU S 41 96.68 65.31 REMARK 500 4 ALA S 3 95.17 57.39 REMARK 500 4 ASP S 4 -94.87 -124.60 REMARK 500 4 SER S 6 -70.92 4.12 REMARK 500 4 SER S 7 55.90 -151.90 REMARK 500 4 SER S 23 -170.99 -53.00 REMARK 500 4 LYS S 43 -69.99 -153.37 REMARK 500 5 SER S 2 -88.29 52.76 REMARK 500 5 ALA S 3 13.23 59.74 REMARK 500 5 ASP S 4 -95.77 -124.28 REMARK 500 5 SER S 6 -74.97 8.07 REMARK 500 5 SER S 7 55.49 -152.32 REMARK 500 5 SER S 23 151.67 -39.20 REMARK 500 6 SER S 2 -58.46 -167.96 REMARK 500 6 ALA S 3 159.82 172.46 REMARK 500 6 ASP S 4 -94.97 -118.02 REMARK 500 6 SER S 6 -62.23 -5.17 REMARK 500 6 SER S 7 50.72 -152.64 REMARK 500 6 SER S 23 -172.43 -50.07 REMARK 500 6 SER S 42 -177.27 55.91 REMARK 500 6 LYS S 43 164.00 61.44 REMARK 500 7 ASP S 4 -95.48 -117.69 REMARK 500 7 SER S 6 -69.10 1.28 REMARK 500 7 SER S 7 53.91 -151.36 REMARK 500 7 LYS S 43 137.01 61.33 REMARK 500 8 ALA S 3 91.18 -162.60 REMARK 500 8 ASP S 4 -95.13 -123.69 REMARK 500 8 SER S 6 -55.27 -11.22 REMARK 500 8 SER S 7 48.80 -154.43 REMARK 500 8 SER S 23 -167.66 -72.12 REMARK 500 8 SER S 42 77.67 -176.75 REMARK 500 9 ASP S 4 -95.12 -120.79 REMARK 500 9 SER S 6 -64.18 -3.81 REMARK 500 9 SER S 7 56.17 -153.17 REMARK 500 9 SER S 23 -170.77 -52.53 REMARK 500 9 GLU S 41 -152.38 42.11 REMARK 500 REMARK 500 THIS ENTRY HAS 114 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 S 20 0.19 SIDE CHAIN REMARK 500 1 ARG S 34 0.27 SIDE CHAIN REMARK 500 2 ARG S 20 0.32 SIDE CHAIN REMARK 500 2 ARG S 34 0.23 SIDE CHAIN REMARK 500 3 ARG S 20 0.27 SIDE CHAIN REMARK 500 3 ARG S 34 0.22 SIDE CHAIN REMARK 500 4 ARG S 20 0.22 SIDE CHAIN REMARK 500 4 ARG S 34 0.30 SIDE CHAIN REMARK 500 5 ARG S 20 0.28 SIDE CHAIN REMARK 500 5 ARG S 34 0.21 SIDE CHAIN REMARK 500 6 ARG S 20 0.29 SIDE CHAIN REMARK 500 6 ARG S 34 0.20 SIDE CHAIN REMARK 500 7 ARG S 20 0.28 SIDE CHAIN REMARK 500 7 ARG S 34 0.15 SIDE CHAIN REMARK 500 8 ARG S 20 0.29 SIDE CHAIN REMARK 500 8 ARG S 34 0.29 SIDE CHAIN REMARK 500 9 ARG S 20 0.27 SIDE CHAIN REMARK 500 10 ARG S 20 0.31 SIDE CHAIN REMARK 500 10 ARG S 34 0.21 SIDE CHAIN REMARK 500 11 ARG S 20 0.31 SIDE CHAIN REMARK 500 11 ARG S 34 0.23 SIDE CHAIN REMARK 500 12 ARG S 20 0.20 SIDE CHAIN REMARK 500 12 ARG S 34 0.24 SIDE CHAIN REMARK 500 13 ARG S 20 0.26 SIDE CHAIN REMARK 500 13 ARG S 34 0.32 SIDE CHAIN REMARK 500 14 ARG S 20 0.31 SIDE CHAIN REMARK 500 14 ARG S 34 0.32 SIDE CHAIN REMARK 500 15 ARG S 20 0.18 SIDE CHAIN REMARK 500 15 ARG S 34 0.32 SIDE CHAIN REMARK 500 16 ARG S 20 0.23 SIDE CHAIN REMARK 500 16 ARG S 34 0.29 SIDE CHAIN REMARK 500 17 ARG S 20 0.30 SIDE CHAIN REMARK 500 17 ARG S 34 0.30 SIDE CHAIN REMARK 500 18 ARG S 20 0.32 SIDE CHAIN REMARK 500 18 ARG S 34 0.32 SIDE CHAIN REMARK 500 19 ARG S 20 0.31 SIDE CHAIN REMARK 500 19 ARG S 34 0.32 SIDE CHAIN REMARK 500 20 ARG S 20 0.31 SIDE CHAIN REMARK 500 20 ARG S 34 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 GLY 1, THROMBIN CLEAVAGE SITE INSERTION REMARK 999 SER 2, THROMBIN CLEAVAGE SITE INSERTION DBREF 1H1J S 1 2 PDB 1H1J 1H1J 1 2 DBREF 1H1J S 3 51 UNP P40040 THO1_YEAST 2 50 SEQRES 1 S 51 GLY SER ALA ASP TYR SER SER LEU THR VAL VAL GLN LEU SEQRES 2 S 51 LYS ASP LEU LEU THR LYS ARG ASN LEU SER VAL GLY GLY SEQRES 3 S 51 LEU LYS ASN GLU LEU VAL GLN ARG LEU ILE LYS ASP ASP SEQRES 4 S 51 GLU GLU SER LYS GLY GLU SER GLU VAL SER PRO GLN HELIX 1 1 ASP S 4 LEU S 8 5 5 HELIX 2 2 VAL S 10 ARG S 20 1 11 HELIX 3 3 LEU S 27 GLU S 40 1 14 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 - n 24 2 Bytes