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HEADER PROTEIN BINDING/TRANSFERASE 12-JUL-05 2A9K TITLE CRYSTAL STRUCTURE OF THE C3BOT-NAD-RALA COMPLEX REVEALS A TITLE 2 NOVEL 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 2A9K 1 JRNL REVDAT 1 11-OCT-05 2A9K 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. 1.73 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) : 1.73 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 38073 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) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.73 REMARK 3 BIN RESOLUTION RANGE LOW : 1.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1652 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.2870 REMARK 3 BIN FREE R VALUE SET COUNT : 87 REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 3278 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.79000 REMARK 3 B22 (A**2) : -0.42000 REMARK 3 B33 (A**2) : 1.45000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.42000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.119 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.808 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3122 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4211 ; 1.110 ; 1.990 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 375 ; 5.202 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;38.090 ;24.966 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 572 ;13.677 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.503 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 459 ; 0.077 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2316 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1430 ; 0.191 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2142 ; 0.301 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 229 ; 0.186 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.235 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.105 ; 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): 1935 ; 0.485 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3004 ; 0.816 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1358 ; 1.291 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1207 ; 2.080 ; 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): 12.4513 0.1970 7.2727 REMARK 3 T TENSOR REMARK 3 T11: -0.0369 T22: -0.0114 REMARK 3 T33: -0.0592 T12: 0.0053 REMARK 3 T13: -0.0086 T23: -0.0015 REMARK 3 L TENSOR REMARK 3 L11: 0.8820 L22: 1.2407 REMARK 3 L33: 0.6421 L12: -0.1070 REMARK 3 L13: -0.0151 L23: -0.0860 REMARK 3 S TENSOR REMARK 3 S11: -0.0039 S12: 0.0656 S13: -0.0862 REMARK 3 S21: -0.0198 S22: -0.0243 S23: 0.0138 REMARK 3 S31: -0.0260 S32: -0.0009 S33: 0.0282 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): 5.1117 25.2547 27.9962 REMARK 3 T TENSOR REMARK 3 T11: -0.0310 T22: -0.0221 REMARK 3 T33: -0.0400 T12: -0.0043 REMARK 3 T13: -0.0081 T23: -0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.4198 L22: 0.5600 REMARK 3 L33: 0.7983 L12: 0.0034 REMARK 3 L13: -0.0585 L23: 0.1415 REMARK 3 S TENSOR REMARK 3 S11: 0.0180 S12: -0.0439 S13: 0.0304 REMARK 3 S21: -0.0168 S22: -0.0356 S23: 0.0336 REMARK 3 S31: -0.0134 S32: 0.0159 S33: 0.0176 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 2A9K 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 RCSB033656. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-SEP-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 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 : 40078 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730 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 (%) : 90.2 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04900 REMARK 200 FOR THE DATA SET : 13.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 62.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.23900 REMARK 200 FOR SHELL : 3.600 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 CITRATE PH 7.0, 25% REMARK 280 PEG 3350, VAPOR 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 56.92500 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 TYR A 82 CA - CB - CG ANGL. DEV. = 7.2 DEGREES REMARK 500 LEU B 111 CA - CB - CG ANGL. DEV. = 6.7 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A78 RELATED DB: PDB REMARK 900 RALA-GDP-C3BOT COMPLEX 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 REMARK 900 RELATED ID: 2BOV RELATED DB: PDB REMARK 900 RALA-GDP-C3BOT COMPLEX REMARK 900 RELATED ID: 1G24 RELATED DB: PDB REMARK 900 EXOENZYME C3, CLOSTRIDIUM BOTULINUM DBREF 2A9K A 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 2A9K B 41 251 UNP P15879 ARC3_CBDP 41 251 SEQADV 2A9K GLY A -3 UNP P11233 CLONING ARTIFACT SEQADV 2A9K SER A -2 UNP P11233 CLONING ARTIFACT SEQADV 2A9K PRO A -1 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 0 UNP P11233 CLONING ARTIFACT SEQADV 2A9K ILE A 1 UNP P11233 CLONING ARTIFACT SEQADV 2A9K SER A 2 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 3 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 4 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 5 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 6 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY A 7 UNP P11233 CLONING ARTIFACT SEQADV 2A9K SER A 8 UNP P11233 CLONING ARTIFACT SEQADV 2A9K GLY B 29 UNP P15879 CLONING ARTIFACT SEQADV 2A9K SER B 30 UNP P15879 CLONING ARTIFACT SEQADV 2A9K PRO B 31 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 32 UNP P15879 CLONING ARTIFACT SEQADV 2A9K ILE B 33 UNP P15879 CLONING ARTIFACT SEQADV 2A9K SER B 34 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 35 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 36 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 37 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 38 UNP P15879 CLONING ARTIFACT SEQADV 2A9K GLY B 39 UNP P15879 CLONING ARTIFACT SEQADV 2A9K 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 300 1 HET GDP 500 28 HET NAD 400 44 HETNAM MG MAGNESIUM ION HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE FORMUL 3 MG MG 2+ FORMUL 4 GDP C10 H15 N5 O11 P2 FORMUL 5 NAD C21 H27 N7 O14 P2 FORMUL 6 HOH *210(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 GLU A 181 1 19 HELIX 7 7 ASN B 51 GLY B 67 1 17 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 SER B 181 ARG B 186 5 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 GLU A 60 N LEU A 57 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 ASN A 127 N PHE A 93 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 THR B 190 N ARG B 128 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 MET B 215 N THR B 175 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 6.07 CRYST1 35.260 113.850 56.310 90.00 106.40 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 0.028361 0.000000 0.008347 0.00000 SCALE2 0.000000 0.008783 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018512 0.00000