Header list of 1jr5.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 10-AUG-01 1JR5 TITLE SOLUTION STRUCTURE OF THE ANTI-SIGMA FACTOR ASIA HOMODIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: 10 KDA ANTI-SIGMA FACTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: AUDREY STEVENS' INHIBITOR; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 10665; SOURCE 4 GENE: ASIA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24B KEYWDS ALL-ALPHA, HELIX-TURN-HELIX, COILED-COIL, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR J.L.URBAUER,M.F.SIMEONOV,R.J.BIEBER URBAUER,K.ADELMAN,J.M.GILMORE, AUTHOR 2 E.N.BRODY REVDAT 5 23-FEB-22 1JR5 1 REMARK REVDAT 4 24-FEB-09 1JR5 1 VERSN REVDAT 3 01-APR-03 1JR5 1 JRNL REVDAT 2 27-FEB-02 1JR5 1 JRNL REMARK REVDAT 1 20-FEB-02 1JR5 0 JRNL AUTH J.L.URBAUER,M.F.SIMEONOV,R.J.URBAUER,K.ADELMAN,J.M.GILMORE, JRNL AUTH 2 E.N.BRODY JRNL TITL SOLUTION STRUCTURE AND STABILITY OF THE ANTI-SIGMA FACTOR JRNL TITL 2 ASIA: IMPLICATIONS FOR NOVEL FUNCTIONS. JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 1831 2002 JRNL REFN ISSN 0027-8424 JRNL PMID 11830637 JRNL DOI 10.1073/PNAS.032464699 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.L.URBAUER,K.ADELMAN,R.J.BIEBER URBAUER,M.F.SIMEONOV, REMARK 1 AUTH 2 J.M.GILMORE,M.ZOLKIEWSKI,E.N.BRODY REMARK 1 TITL CONSERVED REGIONS 4.1 AND 4.2 OF SIGMA(70) CONSTITUTE THE REMARK 1 TITL 2 RECOGNITION SITES FOR THE ANTI-SIGMA FACTOR ASIA, AND ASIA REMARK 1 TITL 3 IS A DIMER FREE IN SOLUTION REMARK 1 REF J.BIOL.CHEM. V. 276 41128 2001 REMARK 1 REFN ISSN 0021-9258 REMARK 1 DOI 10.1074/JBC.M106400200 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.L.URBAUER,K.ADELMAN,E.N.BRODY REMARK 1 TITL MAIN-CHAIN NMR ASSIGNMENTS FOR ASIA REMARK 1 REF J.BIOMOL.NMR V. 10 205 1997 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1018343223888 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.0 REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER ET AL (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 2061 TOTAL NOE-BASED DISTANCE REMARK 3 RESTRAINTS INCLUDING 34 HYDROGEN BOND RESTRAINTS AND 36 REMARK 3 INTERMOLECULAR RESTRAINTS, 153 DIHEDRAL ANGLE RESTRAINTS REMARK 4 REMARK 4 1JR5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-01. REMARK 100 THE DEPOSITION ID IS D_1000014093. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298 REMARK 210 PH : 6.3; 6.3; 6.3 REMARK 210 IONIC STRENGTH : 50 MM D4-ACETATE, 50 MM KCL; 50 REMARK 210 MM D4-ACETATE, 50 MM KCL; 50 MM REMARK 210 D4-ACETATE, 50 MM KCL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5 MM ASIA U-13C, 15N; 50 MM D4 REMARK 210 -ACETATE, 50 MM KCL; 90% H2O, 10% REMARK 210 D2O; 1.5 MM ASIA U-15N; 50 MM REMARK 210 D4-ACETATE, 50 MM KCL; 90% H2O, REMARK 210 10% D2O; 1.0 MM U-13C, 15N AND REMARK 210 1.0 MM UNLABELED; 50 MM D4- REMARK 210 ACETATE, 50 MM KCL; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C_F1-FILTERED_F3-EDITED_NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS, TORSION ANGLE AND REMARK 210 CARTESIAN DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 GLU A 45 42.49 172.92 REMARK 500 1 LYS A 48 -152.09 -62.53 REMARK 500 1 GLN A 51 -32.36 168.97 REMARK 500 1 SER A 53 -70.58 -41.23 REMARK 500 1 PHE A 73 57.76 -95.22 REMARK 500 1 ASN A 74 -87.37 -41.27 REMARK 500 1 GLU B 45 42.45 172.86 REMARK 500 1 LYS B 48 -152.16 -62.52 REMARK 500 1 GLN B 51 -32.33 169.00 REMARK 500 1 SER B 53 -70.51 -41.25 REMARK 500 1 PHE B 73 57.66 -95.27 REMARK 500 1 ASN B 74 -87.29 -41.32 REMARK 500 2 ILE A 5 -32.34 -39.50 REMARK 500 2 GLU A 45 42.92 171.25 REMARK 500 2 LYS A 48 -146.48 -62.72 REMARK 500 2 GLN A 51 -30.09 177.27 REMARK 500 2 PHE A 73 50.14 -99.75 REMARK 500 2 ASN A 74 -90.67 -39.91 REMARK 500 2 ILE B 5 -32.40 -39.46 REMARK 500 2 GLU B 45 42.80 171.21 REMARK 500 2 LYS B 48 -146.41 -62.67 REMARK 500 2 GLN B 51 -30.14 177.34 REMARK 500 2 PHE B 73 50.15 -99.78 REMARK 500 2 ASN B 74 -90.66 -39.92 REMARK 500 3 ILE A 5 -32.46 -39.42 REMARK 500 3 GLU A 45 42.78 171.22 REMARK 500 3 LYS A 48 -146.54 -62.73 REMARK 500 3 GLN A 51 -30.15 177.33 REMARK 500 3 PHE A 73 50.08 -99.76 REMARK 500 3 ASN A 74 -90.70 -39.87 REMARK 500 3 ILE B 5 -32.39 -39.45 REMARK 500 3 GLU B 45 42.83 171.23 REMARK 500 3 LYS B 48 -146.47 -62.70 REMARK 500 3 GLN B 51 -30.11 177.34 REMARK 500 3 PHE B 73 50.10 -99.69 REMARK 500 3 ASN B 74 -90.81 -39.88 REMARK 500 4 GLU A 45 43.85 168.24 REMARK 500 4 LYS A 48 -141.84 -64.81 REMARK 500 4 GLN A 51 -26.55 173.17 REMARK 500 4 ASN A 74 -86.93 -47.40 REMARK 500 4 THR A 88 87.58 -150.01 REMARK 500 4 GLU B 45 43.85 168.24 REMARK 500 4 LYS B 48 -141.80 -64.80 REMARK 500 4 GLN B 51 -26.48 173.07 REMARK 500 4 ASN B 74 -86.97 -47.33 REMARK 500 4 THR B 88 87.52 -150.00 REMARK 500 5 GLU A 45 42.21 171.07 REMARK 500 5 LYS A 48 -140.29 -64.63 REMARK 500 5 GLN A 51 -30.34 170.85 REMARK 500 5 PHE A 73 55.84 -96.04 REMARK 500 REMARK 500 THIS ENTRY HAS 307 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4040 RELATED DB: BMRB REMARK 900 4040 IS THE CHEMICAL SHIFT DATA FOR THIS STRUCTURE. DBREF 1JR5 A 1 90 UNP P32267 ASIA_BPT4 1 90 DBREF 1JR5 B 1 90 UNP P32267 ASIA_BPT4 1 90 SEQRES 1 A 90 MET ASN LYS ASN ILE ASP THR VAL ARG GLU ILE ILE THR SEQRES 2 A 90 VAL ALA SER ILE LEU ILE LYS PHE SER ARG GLU ASP ILE SEQRES 3 A 90 VAL GLU ASN ARG ALA ASN PHE ILE ALA PHE LEU ASN GLU SEQRES 4 A 90 ILE GLY VAL THR HIS GLU GLY ARG LYS LEU ASN GLN ASN SEQRES 5 A 90 SER PHE ARG LYS ILE VAL SER GLU LEU THR GLN GLU ASP SEQRES 6 A 90 LYS LYS THR LEU ILE ASP GLU PHE ASN GLU GLY PHE GLU SEQRES 7 A 90 GLY VAL TYR ARG TYR LEU GLU MET TYR THR ASN LYS SEQRES 1 B 90 MET ASN LYS ASN ILE ASP THR VAL ARG GLU ILE ILE THR SEQRES 2 B 90 VAL ALA SER ILE LEU ILE LYS PHE SER ARG GLU ASP ILE SEQRES 3 B 90 VAL GLU ASN ARG ALA ASN PHE ILE ALA PHE LEU ASN GLU SEQRES 4 B 90 ILE GLY VAL THR HIS GLU GLY ARG LYS LEU ASN GLN ASN SEQRES 5 B 90 SER PHE ARG LYS ILE VAL SER GLU LEU THR GLN GLU ASP SEQRES 6 B 90 LYS LYS THR LEU ILE ASP GLU PHE ASN GLU GLY PHE GLU SEQRES 7 B 90 GLY VAL TYR ARG TYR LEU GLU MET TYR THR ASN LYS HELIX 1 1 LYS A 3 PHE A 21 1 19 HELIX 2 2 ARG A 23 GLU A 28 1 6 HELIX 3 3 ASN A 29 GLY A 41 1 13 HELIX 4 4 GLN A 51 GLU A 60 1 10 HELIX 5 5 THR A 62 ASP A 71 1 10 HELIX 6 6 ARG A 82 THR A 88 1 7 HELIX 7 7 LYS B 3 PHE B 21 1 19 HELIX 8 8 ARG B 23 GLU B 28 1 6 HELIX 9 9 ASN B 29 GLY B 41 1 13 HELIX 10 10 GLN B 51 GLU B 60 1 10 HELIX 11 11 THR B 62 ASP B 71 1 10 HELIX 12 12 ARG B 82 THR B 88 1 7 CRYST1 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 23 2 Bytes