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HEADER EXOCYTOSIS 05-MAR-03 1HK6 TITLE RAL BINDING DOMAIN FROM SEC5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: EXOCYST COMPLEX COMPONENT SEC5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: IPT DOMAIN,RESIDUES 5-97; COMPND 5 SYNONYM: SEC5L1; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: HIS-MET AT N-TERMINUS FROM CLONING SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 6 EXPRESSION_SYSTEM_VARIANT: DE3; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET16B KEYWDS IPT RAL SEC5 EXOCYST,EXOCYTOSIS,PROTEIN TRANSPORT, KEYWDS 2 IMMUNOGLOBULIN FOLD EXPDTA NMR, 25 STRUCTURES AUTHOR H.R.MOTT,D.NIETLISPACH,L.J.HOPKINS,G.MIREY,J.H.CAMONIS, AUTHOR 2 D.OWEN REVDAT 2 08-MAY-03 1HK6 1 JRNL REVDAT 1 13-MAR-03 1HK6 0 JRNL AUTH H.R.MOTT,D.NIETLISPACH,L.J.HOPKINS,G.MIREY, JRNL AUTH 2 J.H.CAMONIS,D.OWEN JRNL TITL STRUCTURE OF THE GTPASE-BINDING DOMAIN OF SEC5 AND JRNL TITL 2 ELUCIDATION OF ITS RAL BINDING SITE. JRNL REF J.BIOL.CHEM. V. 278 17053 2003 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER NUMBER OF NON-HYDROGEN ATOMS USED IN REMARK 3 REFINEMENT. PROTEIN ATOMS : 706 NUCLEIC ACID REMARK 3 ATOMS : 0 HETEROGEN ATOMS : 0 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL ABOVE REMARK 4 REMARK 4 1HK6 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 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI. REMARK 100 THE EBI ID CODE IS EBI-12285. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 200 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 DRX800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS/ARIA1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING 15N-LEBELLED AND 13C,15N REMARK 210 -LABELLED SEC5 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 2 PRO A 15 CG PRO A 15 CD 0.013 REMARK 500 4 PRO A 15 CG PRO A 15 CD 0.014 REMARK 500 4 SER A 14 C PRO A 15 N 0.013 REMARK 500 5 PRO A 15 N PRO A 15 CA -0.013 REMARK 500 5 SER A 14 C PRO A 15 N 0.013 REMARK 500 6 SER A 14 C PRO A 15 N 0.013 REMARK 500 6 LYS A 71 CB LYS A 71 CG -0.012 REMARK 500 7 PRO A 15 N PRO A 15 CA -0.013 REMARK 500 7 PRO A 15 CG PRO A 15 CD 0.013 REMARK 500 7 VAL A 64 CA VAL A 64 C 0.015 REMARK 500 8 SER A 14 C PRO A 15 N 0.013 REMARK 500 9 SER A 14 C PRO A 15 N 0.013 REMARK 500 10 PRO A 15 N PRO A 15 CA -0.015 REMARK 500 10 PRO A 15 CG PRO A 15 CD 0.014 REMARK 500 11 PRO A 15 N PRO A 15 CA -0.013 REMARK 500 11 PRO A 15 CG PRO A 15 CD 0.013 REMARK 500 12 PRO A 15 N PRO A 15 CA -0.012 REMARK 500 13 VAL A 64 C GLY A 65 N -0.015 REMARK 500 15 SER A 14 C PRO A 15 N 0.013 REMARK 500 16 PRO A 15 N PRO A 15 CA -0.015 REMARK 500 16 VAL A 64 C GLY A 65 N -0.014 REMARK 500 18 PRO A 15 N PRO A 15 CA -0.015 REMARK 500 23 PRO A 15 N PRO A 15 CA -0.014 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 5 PRO A 20 N - CA - C ANGL. DEV. = 2.3 DEGREES REMARK 500 7 VAL A 64 CB - CA - C ANGL. DEV. = 3.4 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 6 ASP A 70 -40.77 73.87 REMARK 500 6 LYS A 71 124.28 64.34 REMARK 500 8 CYS A 44 -66.42 69.26 REMARK 500 10 CYS A 44 -38.30 73.78 REMARK 500 12 CYS A 44 -37.80 73.91 REMARK 500 12 ASP A 70 -62.55 74.87 REMARK 500 13 ARG A 5 134.92 63.49 REMARK 500 15 ARG A 5 130.67 65.31 REMARK 500 16 CYS A 44 -35.20 72.82 REMARK 500 17 CYS A 44 -72.74 65.47 REMARK 500 20 CYS A 44 -38.01 74.91 REMARK 500 20 LYS A 71 -71.72 62.59 REMARK 500 22 CYS A 44 -30.46 70.68 REMARK 500 23 CYS A 44 -35.79 74.04 REMARK 500 24 MET A 4 -41.08 73.56 REMARK 500 24 CYS A 44 -38.56 73.36 DBREF 1HK6 A 3 4 UNP Q9D4H1 EXOC2_MOUSE 3 4 DBREF 1HK6 A 5 97 UNP Q9D4H1 SEC5_MOUSE 5 97 SEQRES 1 A 95 HIS MET ARG GLN PRO PRO LEU VAL THR GLY ILE SER PRO SEQRES 2 A 95 ASN GLU GLY ILE PRO TRP THR LYS VAL THR ILE ARG GLY SEQRES 3 A 95 GLU ASN LEU GLY THR GLY PRO THR ASP LEU ILE GLY LEU SEQRES 4 A 95 THR ILE CYS GLY HIS ASN CYS LEU LEU THR ALA GLU TRP SEQRES 5 A 95 MET SER ALA SER LYS ILE VAL CYS ARG VAL GLY GLN ALA SEQRES 6 A 95 LYS ASN ASP LYS GLY ASP ILE ILE VAL THR THR LYS SER SEQRES 7 A 95 GLY GLY LYS GLY THR SER THR VAL SER PHE LYS LEU LEU SEQRES 8 A 95 LYS PRO GLU LYS SHEET 1 AA 5 GLU A 53 TRP A 54 0 SHEET 2 AA 5 ILE A 60 ARG A 63 -1 O VAL A 61 N GLU A 53 SHEET 3 AA 5 LYS A 23 GLU A 29 -1 O VAL A 24 N CYS A 62 SHEET 4 AA 5 LEU A 9 ILE A 13 -1 O LEU A 9 N GLU A 29 SHEET 5 AA 5 THR A 85 SER A 86 1 O THR A 85 N VAL A 10 SHEET 1 AB 3 HIS A 46 ASN A 47 0 SHEET 2 AB 3 LEU A 41 ILE A 43 -1 O ILE A 43 N HIS A 46 SHEET 3 AB 3 ILE A 74 VAL A 76 -1 O ILE A 75 N THR A 42 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