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HEADER APOPTOSIS 28-OCT-02 1N3K TITLE SOLUTION STRUCTURE OF PHOSPHOPROTEIN ENRICHED IN ASTROCYTES TITLE 2 15 KDA (PEA-15) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ASTROCYTIC PHOSPHOPROTEIN PEA-15; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PHOSPHOPROTEIN ENRICHED IN ASTROCYTES 15 KDA; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS; SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER; SOURCE 4 GENE: PEA15; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE-9 KEYWDS DEATH EFFECTOR DOMAIN, SIX HELIX BUNDLE EXPDTA NMR, 20 STRUCTURES AUTHOR J.M.HILL,H.VAIDYANATHAN,J.W.RAMOS,M.H.GINSBERG,M.H.WERNER REVDAT 1 14-JAN-03 1N3K 0 JRNL AUTH J.M.HILL,H.VAIDYANATHAN,J.W.RAMOS,M.H.GINSBERG, JRNL AUTH 2 M.H.WERNER JRNL TITL RECOGNITION OF ERK MAP KINASE BY PEA-15 REVEALS A JRNL TITL 2 COMMON DOCKING SITE WITHIN THE DEATH DOMAIN AND JRNL TITL 3 DEATH EFFECTOR DOMAIN JRNL REF EMBO J. V. 21 6494 2002 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL REMARK 3 OF 2937 NMR-DERIVED RESTRAINTS, INCLUDING 2522 NOES, 308 REMARK 3 DIHEDRAL ANGLE RESTRAINTS (121 PHI, 95 PSI, 84 CHI1 AND 8 REMARK 3 CHI2) AND 107 3J(NH-HA) COUPLING CONSTANTS REMARK 4 REMARK 4 1N3K COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB017474. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE BUFFER REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS DOUBLE AND TRIPLE REMARK 210 RESONANCE EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ, 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.843 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 : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, REMARK 210 STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 ILE A 15 CB ILE A 15 CG1 -0.033 DBREF 1N3K A 1 130 UNP Q9Z297 PEA15_CRIGR 1 130 SEQRES 1 A 130 MET ALA GLU TYR GLY THR LEU LEU GLN ASP LEU THR ASN SEQRES 2 A 130 ASN ILE THR LEU GLU ASP LEU GLU GLN LEU LYS SER ALA SEQRES 3 A 130 CYS LYS GLU ASP ILE PRO SER GLU LYS SER GLU GLU ILE SEQRES 4 A 130 THR THR GLY SER ALA TRP PHE SER PHE LEU GLU SER HIS SEQRES 5 A 130 ASN LYS LEU ASP LYS ASP ASN LEU SER TYR ILE GLU HIS SEQRES 6 A 130 ILE PHE GLU ILE SER ARG ARG PRO ASP LEU LEU THR MET SEQRES 7 A 130 VAL VAL ASP TYR ARG THR ARG VAL LEU LYS ILE SER GLU SEQRES 8 A 130 GLU ASP GLU LEU ASP THR LYS LEU THR ARG ILE PRO SER SEQRES 9 A 130 ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN PRO SER GLU SEQRES 10 A 130 GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO LYS LYS ALA HELIX 1 1 MET A 1 ILE A 15 1 15 HELIX 2 2 THR A 16 LYS A 28 1 13 HELIX 3 3 PRO A 32 GLU A 37 1 6 HELIX 4 4 THR A 41 HIS A 52 1 12 HELIX 5 5 LEU A 60 SER A 70 1 11 HELIX 6 6 ARG A 72 SER A 90 1 19 HELIX 7 7 GLU A 119 ALA A 124 5 6 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