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HEADER PROTEIN BINDING/TRANSFERASE 05-JUL-05 2A78 TITLE CRYSTAL STRUCTURE OF THE C3BOT-RALA COMPLEX REVEALS A NOVEL TITLE 2 TYPE OF ACTION OF A BACTERIAL EXOENZYME COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAL-A; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MONO-ADP-RIBOSYLTRANSFERASE C3; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: EXOENZYME C3; COMPND 9 EC: 2.4.2.-; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: RALA, RAL; 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: PGEX-2T; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM D BACTERIOPHAGE; SOURCE 12 GENE: C3; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PGEX-2T KEYWDS EXOENZYME C3, BACTERIAL ADP-RIBOSYLTRANSFERASE, RAL, RHO, KEYWDS 2 GDP-BINDING EXPDTA X-RAY DIFFRACTION AUTHOR A.PAUTSCH,M.VOGELSGESANG,J.TRANKLE,C.HERRMANN,K.AKTORIES REVDAT 2 01-NOV-05 2A78 1 JRNL REVDAT 1 11-OCT-05 2A78 0 JRNL AUTH A.PAUTSCH,M.VOGELSGESANG,J.TRANKLE,C.HERRMANN, JRNL AUTH 2 K.AKTORIES JRNL TITL CRYSTAL STRUCTURE OF THE C3BOT-RALA COMPLEX JRNL TITL 2 REVEALS A NOVEL TYPE OF ACTION OF A BACTERIAL JRNL TITL 3 EXOENZYME. JRNL REF EMBO J. V. 24 3670 2005 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.P.HOLBOURN,J.M.SUTTON,H.R.EVANS,C.C.SHONE, REMARK 1 AUTH 2 K.R.ACHARYA REMARK 1 TITL MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING REMARK 1 TITL 2 CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE. REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 5357 2005 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. 1.81 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.57 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 34024 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1791 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.81 REMARK 3 BIN RESOLUTION RANGE LOW : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1509 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3130 REMARK 3 BIN FREE R VALUE SET COUNT : 79 REMARK 3 BIN FREE R VALUE : 0.4350 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 3354 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.56000 REMARK 3 B22 (A**2) : 0.09000 REMARK 3 B33 (A**2) : 0.70000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.46000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.134 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.338 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3074 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4138 ; 1.048 ; 1.972 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 375 ; 5.769 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;38.533 ;24.966 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 572 ;13.995 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;15.084 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 451 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2295 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1693 ; 0.193 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2131 ; 0.305 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 363 ; 0.123 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.016 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 53 ; 0.207 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.106 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1922 ; 0.499 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3004 ; 0.886 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1306 ; 1.398 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1134 ; 2.257 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 13 A 180 REMARK 3 ORIGIN FOR THE GROUP (A): 12.9142 0.2229 7.6387 REMARK 3 T TENSOR REMARK 3 T11: -0.0515 T22: -0.0309 REMARK 3 T33: -0.0315 T12: 0.0025 REMARK 3 T13: -0.0030 T23: -0.0090 REMARK 3 L TENSOR REMARK 3 L11: 0.9027 L22: 1.2677 REMARK 3 L33: 0.7516 L12: -0.1757 REMARK 3 L13: -0.0373 L23: -0.1361 REMARK 3 S TENSOR REMARK 3 S11: 0.0168 S12: 0.0400 S13: -0.0860 REMARK 3 S21: -0.0334 S22: -0.0284 S23: 0.0158 REMARK 3 S31: -0.0027 S32: -0.0070 S33: 0.0116 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 45 B 251 REMARK 3 ORIGIN FOR THE GROUP (A): 5.6654 25.0536 28.3452 REMARK 3 T TENSOR REMARK 3 T11: -0.0506 T22: -0.0304 REMARK 3 T33: -0.0222 T12: -0.0045 REMARK 3 T13: -0.0014 T23: -0.0009 REMARK 3 L TENSOR REMARK 3 L11: 0.4038 L22: 0.5992 REMARK 3 L33: 1.1039 L12: -0.0821 REMARK 3 L13: -0.0170 L23: 0.3128 REMARK 3 S TENSOR REMARK 3 S11: 0.0141 S12: -0.0495 S13: 0.0228 REMARK 3 S21: -0.0102 S22: -0.0381 S23: 0.0539 REMARK 3 S31: -0.0140 S32: 0.0131 S33: 0.0240 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A78 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB033574. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUL-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : OSMIC MIRRORS REMARK 200 OPTICS : OSMIC BLUE REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35816 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05900 REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91 REMARK 200 COMPLETENESS FOR SHELL (%) : 62.9 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.34500 REMARK 200 FOR SHELL : 2.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1G24, 1UAD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M BIS- REMARK 280 TRIS, 25% W/V POLYETHYLENE GLYCOL 3350, PH 5.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 56.41500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 PRO A -1 REMARK 465 GLY A 0 REMARK 465 ILE A 1 REMARK 465 SER A 2 REMARK 465 GLY A 3 REMARK 465 GLY A 4 REMARK 465 GLY A 5 REMARK 465 GLY A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 GLN A 9 REMARK 465 ASN A 10 REMARK 465 SER A 11 REMARK 465 LEU A 12 REMARK 465 SER A 183 REMARK 465 GLY B 29 REMARK 465 SER B 30 REMARK 465 PRO B 31 REMARK 465 GLY B 32 REMARK 465 ILE B 33 REMARK 465 SER B 34 REMARK 465 GLY B 35 REMARK 465 GLY B 36 REMARK 465 GLY B 37 REMARK 465 GLY B 38 REMARK 465 GLY B 39 REMARK 465 SER B 40 REMARK 465 ALA B 41 REMARK 465 TYR B 42 REMARK 465 SER B 43 REMARK 465 ASN B 44 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 LEU B 111 CA - CB - CG ANGL. DEV. = 7.2 DEGREES REMARK 500 PHE B 162 N - CA - C ANGL. DEV. = 6.3 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 309 DISTANCE = 5.04 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1U8Y RELATED DB: PDB REMARK 900 RALA-GDP REMARK 900 RELATED ID: 1U8Z RELATED DB: PDB REMARK 900 RALA-GDP REMARK 900 RELATED ID: 1U90 RELATED DB: PDB REMARK 900 RALA-GTP REMARK 900 RELATED ID: 1UAD RELATED DB: PDB REMARK 900 RALA-GPPNHP-SEC5 COMPLEX REMARK 900 RELATED ID: 2BOV RELATED DB: PDB REMARK 900 RALA-C3BOT COMPLEX REMARK 900 RELATED ID: 1G24 RELATED DB: PDB REMARK 900 EXOENZYME C3, CLOSTRIDIUM BOTULINUM DBREF 2A78 A 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 2A78 B 41 251 UNP P15879 ARC3_CBDP 41 251 SEQADV 2A78 GLY A -3 UNP P11233 CLONING ARTIFACT SEQADV 2A78 SER A -2 UNP P11233 CLONING ARTIFACT SEQADV 2A78 PRO A -1 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 0 UNP P11233 CLONING ARTIFACT SEQADV 2A78 ILE A 1 UNP P11233 CLONING ARTIFACT SEQADV 2A78 SER A 2 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 3 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 4 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 5 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 6 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY A 7 UNP P11233 CLONING ARTIFACT SEQADV 2A78 SER A 8 UNP P11233 CLONING ARTIFACT SEQADV 2A78 GLY B 29 UNP P15879 CLONING ARTIFACT SEQADV 2A78 SER B 30 UNP P15879 CLONING ARTIFACT SEQADV 2A78 PRO B 31 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 32 UNP P15879 CLONING ARTIFACT SEQADV 2A78 ILE B 33 UNP P15879 CLONING ARTIFACT SEQADV 2A78 SER B 34 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 35 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 36 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 37 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 38 UNP P15879 CLONING ARTIFACT SEQADV 2A78 GLY B 39 UNP P15879 CLONING ARTIFACT SEQADV 2A78 SER B 40 UNP P15879 CLONING ARTIFACT SEQRES 1 A 187 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY SER GLN SEQRES 2 A 187 ASN SER LEU ALA LEU HIS LYS VAL ILE MET VAL GLY SER SEQRES 3 A 187 GLY GLY VAL GLY LYS SER ALA LEU THR LEU GLN PHE MET SEQRES 4 A 187 TYR ASP GLU PHE VAL GLU ASP TYR GLU PRO THR LYS ALA SEQRES 5 A 187 ASP SER TYR ARG LYS LYS VAL VAL LEU ASP GLY GLU GLU SEQRES 6 A 187 VAL GLN ILE ASP ILE LEU ASP THR ALA GLY GLN GLU ASP SEQRES 7 A 187 TYR ALA ALA ILE ARG ASP ASN TYR PHE ARG SER GLY GLU SEQRES 8 A 187 GLY PHE LEU CYS VAL PHE SER ILE THR GLU MET GLU SER SEQRES 9 A 187 PHE ALA ALA THR ALA ASP PHE ARG GLU GLN ILE LEU ARG SEQRES 10 A 187 VAL LYS GLU ASP GLU ASN VAL PRO PHE LEU LEU VAL GLY SEQRES 11 A 187 ASN LYS SER ASP LEU GLU ASP LYS ARG GLN VAL SER VAL SEQRES 12 A 187 GLU GLU ALA LYS ASN ARG ALA GLU GLN TRP ASN VAL ASN SEQRES 13 A 187 TYR VAL GLU THR SER ALA LYS THR ARG ALA ASN VAL ASP SEQRES 14 A 187 LYS VAL PHE PHE ASP LEU MET ARG GLU ILE ARG ALA ARG SEQRES 15 A 187 LYS MET GLU ASP SER SEQRES 1 B 223 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY SER ALA SEQRES 2 B 223 TYR SER ASN THR TYR GLN GLU PHE THR ASN ILE ASP GLN SEQRES 3 B 223 ALA LYS ALA TRP GLY ASN ALA GLN TYR LYS LYS TYR GLY SEQRES 4 B 223 LEU SER LYS SER GLU LYS GLU ALA ILE VAL SER TYR THR SEQRES 5 B 223 LYS SER ALA SER GLU ILE ASN GLY LYS LEU ARG GLN ASN SEQRES 6 B 223 LYS GLY VAL ILE ASN GLY PHE PRO SER ASN LEU ILE LYS SEQRES 7 B 223 GLN VAL GLU LEU LEU ASP LYS SER PHE ASN LYS MET LYS SEQRES 8 B 223 THR PRO GLU ASN ILE MET LEU PHE ARG GLY ASP ASP PRO SEQRES 9 B 223 ALA TYR LEU GLY THR GLU PHE GLN ASN THR LEU LEU ASN SEQRES 10 B 223 SER ASN GLY THR ILE ASN LYS THR ALA PHE GLU LYS ALA SEQRES 11 B 223 LYS ALA LYS PHE LEU ASN LYS ASP ARG LEU GLU TYR GLY SEQRES 12 B 223 TYR ILE SER THR SER LEU MET ASN VAL SER GLN PHE ALA SEQRES 13 B 223 GLY ARG PRO ILE ILE THR LYS PHE LYS VAL ALA LYS GLY SEQRES 14 B 223 SER LYS ALA GLY TYR ILE ASP PRO ILE SER ALA PHE ALA SEQRES 15 B 223 GLY GLN LEU GLU MET LEU LEU PRO ARG HIS SER THR TYR SEQRES 16 B 223 HIS ILE ASP ASP MET ARG LEU SER SER ASP GLY LYS GLN SEQRES 17 B 223 ILE ILE ILE THR ALA THR MET MET GLY THR ALA ILE ASN SEQRES 18 B 223 PRO LYS HET MG 400 1 HET GDP 500 28 HETNAM MG MAGNESIUM ION HETNAM GDP GUANOSINE-5'-DIPHOSPHATE FORMUL 3 MG MG 2+ FORMUL 4 GDP C10 H15 N5 O11 P2 FORMUL 5 HOH *330(H2 O) HELIX 1 1 GLY A 26 ASP A 37 1 12 HELIX 2 2 TYR A 75 GLY A 86 1 12 HELIX 3 3 GLU A 97 GLU A 116 1 20 HELIX 4 4 LYS A 128 ARG A 135 5 8 HELIX 5 5 SER A 138 TRP A 149 1 12 HELIX 6 6 ASN A 163 MET A 180 1 18 HELIX 7 7 ASN B 51 LYS B 64 1 14 HELIX 8 8 SER B 69 ASN B 93 1 25 HELIX 9 9 PRO B 101 PHE B 115 1 15 HELIX 10 10 ASP B 131 GLN B 140 5 10 HELIX 11 11 ASN B 151 LEU B 163 1 13 HELIX 12 12 VAL B 180 GLY B 185 1 6 HELIX 13 13 ASP B 204 SER B 207 5 4 SHEET 1 A 6 ASP A 49 LEU A 57 0 SHEET 2 A 6 GLU A 60 ASP A 68 -1 O VAL A 62 N VAL A 55 SHEET 3 A 6 LEU A 14 VAL A 20 1 N VAL A 17 O ASP A 65 SHEET 4 A 6 GLY A 88 SER A 94 1 O VAL A 92 N VAL A 20 SHEET 5 A 6 PHE A 122 ASN A 127 1 O VAL A 125 N CYS A 91 SHEET 6 A 6 ASN A 152 GLU A 155 1 O ASN A 152 N LEU A 124 SHEET 1 B 5 ILE B 124 ASP B 130 0 SHEET 2 B 5 ILE B 188 VAL B 194 -1 O PHE B 192 N LEU B 126 SHEET 3 B 5 ILE B 237 THR B 246 1 O ILE B 239 N ILE B 189 SHEET 4 B 5 SER B 221 LEU B 230 -1 N ARG B 229 O ILE B 238 SHEET 5 B 5 ASP B 166 GLU B 169 -1 N ARG B 167 O TYR B 223 SHEET 1 C 3 ILE B 173 SER B 176 0 SHEET 2 C 3 GLU B 214 LEU B 217 -1 O LEU B 217 N ILE B 173 SHEET 3 C 3 GLY B 201 TYR B 202 -1 N GLY B 201 O LEU B 216 CISPEP 1 GLU A 181 ASP A 182 0 9.93 CRYST1 34.940 112.830 56.350 90.00 105.10 90.00 P 1 21 1 2 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 0.028620 0.000000 0.007722 0.00000 SCALE2 0.000000 0.008863 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018381 0.00000