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HEADER APOPTOSIS 12-JUN-03 1PN5 TITLE NMR STRUCTURE OF THE NALP1 PYRIN DOMAIN (PYD) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NACHT-, LRR- AND PYD-CONTAINING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PYRIN DOMAIN (PYD); COMPND 5 SYNONYM: DEATH EFFECTOR FILAMENT-FORMING CED-4-LIKE COMPND 6 APOPTOSIS PROTEIN, NUCLEOTIDE-BINDING DOMAIN AND CASPASE COMPND 7 RECRUITMENT DOMAIN, CASPASE RECRUITMENT DOMAIN PROTEIN 7; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: RESIDUES 1-56 CORRESPOND TO THE FUSED COMPND 10 IMMUNOGLOBULIN G BINDING PROTEIN G (SWS P06654, RESIDUES COMPND 11 228-282) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: NALP1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B+ KEYWDS 5 ALPHA-HELIX BUNDLE EXPDTA NMR, 20 STRUCTURES AUTHOR S.HILLER,A.KOHL,F.FIORITO,T.HERRMANN,G.WIDER,J.TSCHOPP, AUTHOR 2 M.G.GRUTTER,K.WUTHRICH REVDAT 1 07-OCT-03 1PN5 0 JRNL AUTH S.HILLER,A.KOHL,F.FIORITO,T.HERRMANN,G.WIDER, JRNL AUTH 2 J.TSCHOPP,M.G.GRUTTER,K.WUTHRICH JRNL TITL NMR STRUCTURE OF THE APOPTOSIS- AND JRNL TITL 2 INFLAMMATION-RELATED NALP1 PYRIN DOMAIN JRNL REF STRUCTURE V. 11 1199 2003 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ATNOS REMARK 3 AUTHORS : HERRMANN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PN5 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 RCSB019442. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1ATM REMARK 210 SAMPLE CONTENTS : 1MM NALP1 PYD U-15N,13C; 50MM REMARK 210 NA / PO4 - BUFFER; 50MM NACL; REMARK 210 1MM CHAPS; 20MM DTT (D10); REMARK 210 0.02% NAN3; 0.1MM EDTA; REMARK 210 PROTEASE INHIBITOR COCKTAIL REMARK 210 (COMPLETE, ROCHE); 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_ REMARK 210 13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ, 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, DYANA, CANDID, REMARK 210 ATNOS, CARA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17 REMARK 210 REMARK 210 REMARK: PROTEIN WAS EXPRESSED AS A FUSION PROTEIN WITH G B1 TO REMARK 210 ENHANCE SOLUBILITY (ZHOU ET AL., J. BIOMOL. NMR 20, 11-14) 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: 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 2 THR A 99 142.06 66.76 REMARK 500 3 ALA A 148 -84.58 65.50 REMARK 500 4 ALA A 101 152.41 66.80 REMARK 500 5 HIS A 150 161.89 65.31 REMARK 500 6 HIS A 91 -126.65 27.75 REMARK 500 8 HIS A 91 165.05 63.82 REMARK 500 8 ARG A 93 127.28 56.83 REMARK 500 11 THR A 99 167.41 55.30 REMARK 500 13 THR A 99 162.12 71.00 REMARK 500 14 SER A 92 144.48 56.19 REMARK 500 14 THR A 99 146.04 59.80 REMARK 500 15 THR A 99 141.95 59.05 REMARK 500 16 HIS A 91 155.01 69.98 REMARK 500 17 HIS A 91 -172.10 95.79 REMARK 500 18 SER A 95 161.36 63.66 REMARK 500 19 ARG A 93 -55.31 61.04 REMARK 500 19 THR A 99 166.45 70.35 REMARK 500 19 HIS A 150 -76.11 60.85 REMARK 500 20 SER A 95 -45.27 66.64 REMARK 500 20 SER A 96 -86.20 57.00 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 95 SER A 96 11 149.95 REMARK 500 LYS A 89 ALA A 90 12 -149.61 REMARK 500 ARG A 93 SER A 94 12 -136.87 REMARK 500 SER A 96 GLY A 97 12 144.60 REMARK 500 ALA A 101 GLN A 102 12 -148.13 REMARK 500 ALA A 90 HIS A 91 16 -139.53 REMARK 500 GLN A 118 TYR A 119 16 -149.84 REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES 1-58 ARE MISSING FROM THE COORDINATES REMARK 999 BECAUSE THEY WERE NOT INCLUDED IN THE MODEL. REMARK 999 RESIDUES 57 AND 58 ARE INDEPENDENT LINKING RESIDUES, REMARK 999 WHICH HAVE BEEN INSERTED TO PROVIDE DISTANCE AND REMARK 999 FLEXIBILTIY IN THIS TWO-DOMAIN FUSION PROTEIN. DBREF 1PN5 A 2 56 UNP P06654 SPG1_STRSG 228 282 DBREF 1PN5 A 59 151 UNP Q9C000 NAL1_HUMAN 1 93 SEQADV 1PN5 MET A 1 UNP P06654 INITIATING MET SEQADV 1PN5 GLN A 2 UNP P06654 THR 228 ENGINEERED SEQADV 1PN5 GLY A 57 UNP P06654 SEE REMARK 999 SEQADV 1PN5 SER A 58 UNP P06654 SEE REMARK 999 SEQADV 1PN5 LEU A 152 UNP Q9C000 HIS TAG SEQADV 1PN5 GLU A 153 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 154 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 155 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 156 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 157 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 158 UNP Q9C000 HIS TAG SEQADV 1PN5 HIS A 159 UNP Q9C000 HIS TAG SEQRES 1 A 159 MET GLN TYR LYS LEU ILE LEU ASN GLY LYS THR LEU LYS SEQRES 2 A 159 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA SEQRES 3 A 159 GLU LYS VAL PHE LYS GLN TYR ALA ASN ASP ASN GLY VAL SEQRES 4 A 159 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE SEQRES 5 A 159 THR VAL THR GLU GLY SER MET ALA GLY GLY ALA TRP GLY SEQRES 6 A 159 ARG LEU ALA CYS TYR LEU GLU PHE LEU LYS LYS GLU GLU SEQRES 7 A 159 LEU LYS GLU PHE GLN LEU LEU LEU ALA ASN LYS ALA HIS SEQRES 8 A 159 SER ARG SER SER SER GLY GLU THR PRO ALA GLN PRO GLU SEQRES 9 A 159 LYS THR SER GLY MET GLU VAL ALA SER TYR LEU VAL ALA SEQRES 10 A 159 GLN TYR GLY GLU GLN ARG ALA TRP ASP LEU ALA LEU HIS SEQRES 11 A 159 THR TRP GLU GLN MET GLY LEU ARG SER LEU CYS ALA GLN SEQRES 12 A 159 ALA GLN GLU GLY ALA GLY HIS SER LEU GLU HIS HIS HIS SEQRES 13 A 159 HIS HIS HIS HELIX 1 1 ARG A 66 LEU A 71 1 6 HELIX 2 2 LYS A 76 ASN A 88 1 13 HELIX 3 3 MET A 109 ALA A 117 1 9 HELIX 4 4 GLU A 121 GLN A 134 1 14 HELIX 5 5 ARG A 138 GLN A 143 1 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