HEADER TRANSFERASE 05-JAN-05 1YGO TITLE SOLUTION STRUCTURE OF THE PELLE DEATH DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROBABLE SERINE/THREONINE-PROTEIN KINASE PELLE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PELLE KINASE DEATH DOMAIN RESIDUES 26-131; COMPND 5 EC: 2.7.1.37; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 GENE: PLL; 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: PET28A KEYWDS ANTI-PARALLEL 6 HELIX BUNDLE EXPDTA NMR, 20 STRUCTURES AUTHOR M.C.MONCRIEFFE,K.M.STOTT,N.J.GAY REVDAT 1 26-JUL-05 1YGO 0 JRNL AUTH M.C.MONCRIEFFE,K.M.STOTT,N.J.GAY JRNL TITL SOLUTION STRUCTURE OF THE ISOLATED PELLE DEATH JRNL TITL 2 DOMAIN. JRNL REF FEBS LETT. V. 579 3920 2005 JRNL REFN ASTM FEBLAL NE ISSN 0014-5793 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER, A REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YGO 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 RCSB031492. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1MM PELLE DEATH DOMAIN, U- REMARK 210 15N, 13C; 20MM PHOSPHATE, REMARK 210 100MM NACL, PH 7.6; 10% D20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY, 3D_ REMARK 210 15N-SEPARATED_NOESY, HNHA 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 : ANSIG 1.03 FOR OPENGL, AZARA REMARK 210 2.5, ARIA 1.2 REMARK 210 METHOD USED : SIMULATED ANEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: 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 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 2 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 3 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 4 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 4 TYR A 107 CE1 TYR A 107 CZ 0.013 REMARK 500 5 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 5 LEU A 18 C PRO A 19 N 0.014 REMARK 500 6 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 6 LEU A 18 C PRO A 19 N 0.015 REMARK 500 7 GLY A 1 N GLY A 1 CA 0.037 REMARK 500 7 LEU A 18 C PRO A 19 N 0.014 REMARK 500 8 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 8 LEU A 18 C PRO A 19 N 0.014 REMARK 500 9 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 9 LEU A 18 C PRO A 19 N 0.014 REMARK 500 9 PHE A 65 CZ PHE A 65 CE2 -0.014 REMARK 500 9 TYR A 107 CE1 TYR A 107 CZ 0.020 REMARK 500 9 TYR A 107 CZ TYR A 107 CE2 -0.018 REMARK 500 10 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 10 LEU A 18 C PRO A 19 N 0.014 REMARK 500 10 PHE A 84 CE1 PHE A 84 CZ 0.015 REMARK 500 10 PHE A 84 CZ PHE A 84 CE2 -0.018 REMARK 500 11 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 11 LEU A 18 C PRO A 19 N 0.014 REMARK 500 12 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 12 LEU A 18 C PRO A 19 N 0.014 REMARK 500 13 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 13 PHE A 65 CE1 PHE A 65 CZ 0.016 REMARK 500 13 PHE A 65 CZ PHE A 65 CE2 -0.017 REMARK 500 14 GLY A 1 N GLY A 1 CA 0.039 REMARK 500 14 PHE A 84 CZ PHE A 84 CE2 -0.014 REMARK 500 15 GLY A 1 N GLY A 1 CA 0.037 REMARK 500 15 LEU A 18 C PRO A 19 N 0.014 REMARK 500 15 TYR A 107 CE1 TYR A 107 CZ 0.015 REMARK 500 16 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 16 LEU A 18 C PRO A 19 N 0.014 REMARK 500 17 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 18 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 19 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 19 TYR A 99 CE1 TYR A 99 CZ 0.014 REMARK 500 20 GLY A 1 N GLY A 1 CA 0.038 REMARK 500 20 HIS A 75 CA HIS A 75 C 0.014 REMARK 500 20 THR A 76 N THR A 76 CA 0.015 REMARK 500 20 PHE A 84 CE1 PHE A 84 CZ 0.058 REMARK 500 20 PHE A 84 CZ PHE A 84 CE2 -0.060 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 5 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 6 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 7 LEU A 18 CA - C - N ANGL. DEV. = 1.8 DEGREES REMARK 500 8 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 9 ILE A 13 CB - CA - C ANGL. DEV. = 1.9 DEGREES REMARK 500 12 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 14 LEU A 18 CA - C - N ANGL. DEV. = 1.9 DEGREES REMARK 500 15 LEU A 18 CA - C - N ANGL. DEV. = 2.0 DEGREES REMARK 500 16 LEU A 18 CA - C - N ANGL. DEV. = 1.8 DEGREES REMARK 500 16 HIS A 105 CB - CA - C ANGL. DEV. = 2.6 DEGREES REMARK 500 18 LEU A 104 N - CA - C ANGL. DEV. = 2.9 DEGREES REMARK 500 19 VAL A 100 CB - CA - C ANGL. DEV. = 2.3 DEGREES REMARK 500 19 VAL A 100 CA - CB - CG1 ANGL. DEV. = 3.1 DEGREES REMARK 500 20 TRP A 34 N - CA - C ANGL. DEV. = -1.8 DEGREES REMARK 500 20 THR A 76 N - CA - CB ANGL. DEV. = 2.5 DEGREES REMARK 500 20 THR A 76 C - N - CA ANGL. DEV. = 2.4 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 1 ASN A 74 145.64 65.44 REMARK 500 3 SER A 2 123.89 64.82 REMARK 500 5 ASN A 74 143.12 65.43 REMARK 500 6 LEU A 7 -94.47 57.50 REMARK 500 6 ASN A 74 120.92 63.50 REMARK 500 11 ASN A 9 160.68 65.17 REMARK 500 12 SER A 2 132.26 65.96 REMARK 500 15 LYS A 97 -51.77 72.80 REMARK 500 16 LYS A 97 -69.76 67.88 REMARK 500 17 LYS A 97 -74.05 65.72 REMARK 500 19 HIS A 3 -90.28 58.27 REMARK 500 19 ASN A 9 -101.53 57.18 REMARK 500 20 THR A 76 151.66 80.36 DBREF 1YGO A 5 110 UNP Q05652 KPEL_DROME 26 131 SEQADV 1YGO GLY A 1 UNP Q05652 CLONING ARTIFACT SEQADV 1YGO SER A 2 UNP Q05652 CLONING ARTIFACT SEQADV 1YGO HIS A 3 UNP Q05652 CLONING ARTIFACT SEQADV 1YGO MET A 4 UNP Q05652 CLONING ARTIFACT SEQRES 1 A 110 GLY SER HIS MET SER HIS LEU ASP ASN THR MET ALA ILE SEQRES 2 A 110 ARG LEU LEU PRO LEU PRO VAL ARG ALA GLN LEU CYS ALA SEQRES 3 A 110 HIS LEU ASP ALA LEU ASP VAL TRP GLN GLN LEU ALA THR SEQRES 4 A 110 ALA VAL LYS LEU TYR PRO ASP GLN VAL GLU GLN ILE SER SEQRES 5 A 110 SER GLN LYS GLN ARG GLY ARG SER ALA SER ASN GLU PHE SEQRES 6 A 110 LEU ASN ILE TRP GLY GLY GLN TYR ASN HIS THR VAL GLN SEQRES 7 A 110 THR LEU PHE ALA LEU PHE LYS LYS LEU LYS LEU HIS ASN SEQRES 8 A 110 ALA MET ARG LEU ILE LYS ASP TYR VAL SER GLU ASP LEU SEQRES 9 A 110 HIS LYS TYR ILE PRO ARG HELIX 1 1 PRO A 17 ASP A 32 1 16 HELIX 2 2 TRP A 34 THR A 39 1 6 HELIX 3 3 ALA A 40 LYS A 42 5 3 HELIX 4 4 TYR A 44 ARG A 57 1 14 HELIX 5 5 SER A 60 GLY A 70 1 11 HELIX 6 6 THR A 76 LYS A 85 1 10 HELIX 7 7 LEU A 89 ILE A 96 1 8 HELIX 8 8 SER A 101 HIS A 105 5 5 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