HEADER HYDROLASE 01-DEC-01 1KHZ
TITLE STRUCTURE OF THE ADPR-ASE IN COMPLEX WITH AMPCPR AND MG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSE PYROPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADP-RIBOSE DIPHOSPHATASE, ADENOSINE
COMPND 5 DIPHOSPHORIBOSE PYROPHOSPHATASE, ADPR-PPASE, ADP-RIBOSE
COMPND 6 PHOSPHOHYDROLASE;
COMPND 7 EC: 3.6.1.13;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ORF209;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NUDIX, ADP-RIBOSE PYROPHOSPHATASE, AMPCPR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.B.GABELLI,M.A.BIANCHET,M.J.BESSMAN,L.M.AMZEL
REVDAT 2 24-FEB-09 1KHZ 1 VERSN
REVDAT 1 09-OCT-02 1KHZ 0
JRNL AUTH S.B.GABELLI,M.A.BIANCHET,Y.OHNISHI,Y.ICHIKAWA,
JRNL AUTH 2 M.J.BESSMAN,L.M.AMZEL
JRNL TITL MECHANISM OF THE ESCHERICHIA COLI ADP-RIBOSE
JRNL TITL 2 PYROPHOSPHATASE, A NUDIX HYDROLASE.
JRNL REF BIOCHEMISTRY V. 41 9279 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12135348
JRNL DOI 10.1021/BI0259296
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 271730.100
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 27097
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2682
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3347
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 364
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.73000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : 0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.07
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.330 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.600 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 60.40
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : INHIBITOR.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : INHIBITOR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KHZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB014983.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27097
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 26.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 18K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 33.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
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 155
REMARK 465 ILE A 156
REMARK 465 HIS A 157
REMARK 465 GLY A 158
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 ASP B 5
REMARK 465 ASN B 6
REMARK 465 LEU B 7
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 186 NH2 ARG B 140 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 101 129.96 -34.40
REMARK 500 LYS A 122 -108.43 -102.68
REMARK 500 VAL A 127 -68.86 -102.80
REMARK 500 SER A 133 75.65 -166.69
REMARK 500 ASP A 161 -72.38 -49.21
REMARK 500 GLU A 162 46.69 -80.63
REMARK 500 LYS B 122 -113.95 -96.03
REMARK 500 VAL B 127 -80.85 -113.08
REMARK 500 SER B 133 77.62 -164.76
REMARK 500 PRO B 134 -17.29 -46.76
REMARK 500 ASN B 163 52.89 70.13
REMARK 500 ASP B 186 25.30 -141.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 403 O
REMARK 620 2 GLU B 116 OE2 99.0
REMARK 620 3 GLU B 164 OE2 87.3 85.7
REMARK 620 4 ADV B 402 O1A 176.5 84.4 93.6
REMARK 620 5 GLU B 112 OE1 80.8 79.0 158.8 99.4
REMARK 620 6 HOH B 407 O 89.0 170.5 99.9 87.5 97.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADV B 402 O2A
REMARK 620 2 HOH B 405 O 88.4
REMARK 620 3 GLU B 112 OE2 94.2 164.8
REMARK 620 4 HOH B 404 O 166.2 88.7 92.1
REMARK 620 5 HOH B 406 O 95.2 85.8 79.1 98.0
REMARK 620 6 HOH B 407 O 84.2 96.9 98.2 82.9 177.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 310 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 116 OE2
REMARK 620 2 ADV B 402 O2B 163.6
REMARK 620 3 ADV B 402 O1A 78.9 89.6
REMARK 620 4 HOH B 409 O 86.4 104.5 86.1
REMARK 620 5 HOH B 410 O 91.1 101.0 169.4 89.8
REMARK 620 6 ALA B 96 O 83.1 84.5 86.1 168.0 96.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 304
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 310
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADV B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G0S RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE E.COLI ADP-RIBOSE
REMARK 900 PYROPHOSPHATASE
REMARK 900 RELATED ID: 1G9Q RELATED DB: PDB
REMARK 900 COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-
REMARK 900 RIBOSE
REMARK 900 RELATED ID: 1GA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ADP-RIBOSE PYROPHOSPHATASE IN
REMARK 900 COMPLEX WITH GD+3
DBREF 1KHZ A 1 209 UNP Q93K97 ADPP_ECOLI 1 209
DBREF 1KHZ B 1 209 UNP Q93K97 ADPP_ECOLI 1 209
SEQRES 1 A 209 MET LEU LYS PRO ASP ASN LEU PRO VAL THR PHE GLY LYS
SEQRES 2 A 209 ASN ASP VAL GLU ILE ILE ALA ARG GLU THR LEU TYR ARG
SEQRES 3 A 209 GLY PHE PHE SER LEU ASP LEU TYR ARG PHE ARG HIS ARG
SEQRES 4 A 209 LEU PHE ASN GLY GLN MET SER HIS GLU VAL ARG ARG GLU
SEQRES 5 A 209 ILE PHE GLU ARG GLY HIS ALA ALA VAL LEU LEU PRO PHE
SEQRES 6 A 209 ASP PRO VAL ARG ASP GLU VAL VAL LEU ILE GLU GLN ILE
SEQRES 7 A 209 ARG ILE ALA ALA TYR ASP THR SER GLU THR PRO TRP LEU
SEQRES 8 A 209 LEU GLU MET VAL ALA GLY MET ILE GLU GLU GLY GLU SER
SEQRES 9 A 209 VAL GLU ASP VAL ALA ARG ARG GLU ALA ILE GLU GLU ALA
SEQRES 10 A 209 GLY LEU ILE VAL LYS ARG THR LYS PRO VAL LEU SER PHE
SEQRES 11 A 209 LEU ALA SER PRO GLY GLY THR SER GLU ARG SER SER ILE
SEQRES 12 A 209 MET VAL GLY GLU VAL ASP ALA THR THR ALA SER GLY ILE
SEQRES 13 A 209 HIS GLY LEU ALA ASP GLU ASN GLU ASP ILE ARG VAL HIS
SEQRES 14 A 209 VAL VAL SER ARG GLU GLN ALA TYR GLN TRP VAL GLU GLU
SEQRES 15 A 209 GLY LYS ILE ASP ASN ALA ALA SER VAL ILE ALA LEU GLN
SEQRES 16 A 209 TRP LEU GLN LEU HIS HIS GLN ALA LEU LYS ASN GLU TRP
SEQRES 17 A 209 ALA
SEQRES 1 B 209 MET LEU LYS PRO ASP ASN LEU PRO VAL THR PHE GLY LYS
SEQRES 2 B 209 ASN ASP VAL GLU ILE ILE ALA ARG GLU THR LEU TYR ARG
SEQRES 3 B 209 GLY PHE PHE SER LEU ASP LEU TYR ARG PHE ARG HIS ARG
SEQRES 4 B 209 LEU PHE ASN GLY GLN MET SER HIS GLU VAL ARG ARG GLU
SEQRES 5 B 209 ILE PHE GLU ARG GLY HIS ALA ALA VAL LEU LEU PRO PHE
SEQRES 6 B 209 ASP PRO VAL ARG ASP GLU VAL VAL LEU ILE GLU GLN ILE
SEQRES 7 B 209 ARG ILE ALA ALA TYR ASP THR SER GLU THR PRO TRP LEU
SEQRES 8 B 209 LEU GLU MET VAL ALA GLY MET ILE GLU GLU GLY GLU SER
SEQRES 9 B 209 VAL GLU ASP VAL ALA ARG ARG GLU ALA ILE GLU GLU ALA
SEQRES 10 B 209 GLY LEU ILE VAL LYS ARG THR LYS PRO VAL LEU SER PHE
SEQRES 11 B 209 LEU ALA SER PRO GLY GLY THR SER GLU ARG SER SER ILE
SEQRES 12 B 209 MET VAL GLY GLU VAL ASP ALA THR THR ALA SER GLY ILE
SEQRES 13 B 209 HIS GLY LEU ALA ASP GLU ASN GLU ASP ILE ARG VAL HIS
SEQRES 14 B 209 VAL VAL SER ARG GLU GLN ALA TYR GLN TRP VAL GLU GLU
SEQRES 15 B 209 GLY LYS ILE ASP ASN ALA ALA SER VAL ILE ALA LEU GLN
SEQRES 16 B 209 TRP LEU GLN LEU HIS HIS GLN ALA LEU LYS ASN GLU TRP
SEQRES 17 B 209 ALA
HET CL A 401 1
HET MG B 301 1
HET MG B 304 1
HET MG B 310 1
HET ADV B 402 36
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM ADV ALPHA-BETA METHYLENE ADP-RIBOSE
HETSYN ADV AMPCPR; {[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-
HETSYN 2 ADV TETRAHYDRO-FURAN-2-YLMETHOXY]-HYDROXY-
HETSYN 3 ADV PHOSPHORYLMETHYL}-PHOSPHONIC ACID MONO-(3,4,5-
HETSYN 4 ADV TRIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL) ESTER
FORMUL 3 CL CL 1-
FORMUL 4 MG 3(MG 2+)
FORMUL 7 ADV C16 H25 N5 O13 P2
FORMUL 8 HOH *223(H2 O)
HELIX 1 1 GLY A 12 ASN A 14 5 3
HELIX 2 2 ILE A 80 SER A 86 5 7
HELIX 3 3 SER A 104 GLY A 118 1 15
HELIX 4 4 ASP A 149 ALA A 153 5 5
HELIX 5 5 ARG A 173 GLU A 182 1 10
HELIX 6 6 ASN A 187 TRP A 208 1 22
HELIX 7 7 GLY B 12 ASN B 14 5 3
HELIX 8 8 ILE B 80 SER B 86 5 7
HELIX 9 9 SER B 104 GLY B 118 1 15
HELIX 10 10 ASP B 149 ALA B 153 5 5
HELIX 11 11 ARG B 173 GLU B 182 1 10
HELIX 12 12 ASN B 187 ALA B 209 1 23
SHEET 1 A 3 VAL A 16 TYR A 25 0
SHEET 2 A 3 SER A 30 HIS A 38 -1 N LEU A 31 O TYR A 25
SHEET 3 A 3 VAL A 49 GLU A 55 -1 N VAL A 49 O PHE A 36
SHEET 1 B 9 THR A 124 LEU A 131 0
SHEET 2 B 9 ARG A 140 GLU A 147 -1 N SER A 141 O PHE A 130
SHEET 3 B 9 HIS A 58 ASP A 66 1 N ALA A 59 O ARG A 140
SHEET 4 B 9 VAL A 95 MET A 98 -1 O VAL A 95 N LEU A 62
SHEET 5 B 9 HIS A 58 ASP A 66 -1 N ALA A 60 O GLY A 97
SHEET 6 B 9 GLU A 71 ILE A 78 -1 O GLU A 71 N ASP A 66
SHEET 7 B 9 TRP A 90 GLU A 93 -1 N LEU A 91 O GLN A 77
SHEET 8 B 9 GLU A 71 ILE A 78 -1 O ILE A 75 N GLU A 93
SHEET 9 B 9 ARG A 167 SER A 172 -1 O ARG A 167 N GLU A 76
SHEET 1 C 3 VAL B 16 ARG B 26 0
SHEET 2 C 3 SER B 30 HIS B 38 -1 O LEU B 31 N LEU B 24
SHEET 3 C 3 VAL B 49 GLU B 55 -1 N VAL B 49 O PHE B 36
SHEET 1 D10 THR B 124 LEU B 131 0
SHEET 2 D10 ARG B 140 GLU B 147 -1 N SER B 141 O PHE B 130
SHEET 3 D10 ALA B 59 ASP B 66 1 O ALA B 59 N SER B 142
SHEET 4 D10 VAL B 95 MET B 98 -1 O VAL B 95 N LEU B 62
SHEET 5 D10 ALA B 59 ASP B 66 -1 N ALA B 60 O GLY B 97
SHEET 6 D10 GLU B 71 ILE B 78 -1 O GLU B 71 N ASP B 66
SHEET 7 D10 TRP B 90 GLU B 93 -1 N LEU B 91 O GLN B 77
SHEET 8 D10 GLU B 71 ILE B 78 -1 O ILE B 75 N GLU B 93
SHEET 9 D10 ILE B 166 SER B 172 -1 O ARG B 167 N GLU B 76
SHEET 10 D10 ILE B 156 HIS B 157 -1 N HIS B 157 O ILE B 166
LINK MG MG B 301 O HOH B 403 1555 1555 2.12
LINK MG MG B 301 OE2 GLU B 116 1555 1555 2.13
LINK MG MG B 301 OE2 GLU B 164 1555 1555 2.19
LINK MG MG B 301 O1A ADV B 402 1555 1555 2.14
LINK MG MG B 301 OE1 GLU B 112 1555 1555 2.20
LINK MG MG B 301 O HOH B 407 1555 1555 2.04
LINK MG MG B 304 O2A ADV B 402 1555 1555 2.21
LINK MG MG B 304 O HOH B 405 1555 1555 1.84
LINK MG MG B 304 OE2 GLU B 112 1555 1555 2.24
LINK MG MG B 304 O HOH B 404 1555 1555 2.16
LINK MG MG B 304 O HOH B 406 1555 1555 2.32
LINK MG MG B 304 O HOH B 407 1555 1555 1.98
LINK MG MG B 310 OE2 GLU B 116 1555 1555 2.25
LINK MG MG B 310 O2B ADV B 402 1555 1555 2.13
LINK MG MG B 310 O1A ADV B 402 1555 1555 2.27
LINK MG MG B 310 O HOH B 409 1555 1555 2.25
LINK MG MG B 310 O HOH B 410 1555 1555 2.00
LINK MG MG B 310 O ALA B 96 1555 1555 2.24
SITE 1 AC1 2 ARG B 50 GLU B 207
SITE 1 AC2 8 GLU B 112 GLU B 116 GLU B 164 MG B 304
SITE 2 AC2 8 MG B 310 ADV B 402 HOH B 403 HOH B 407
SITE 1 AC3 8 GLU B 112 GLU B 162 MG B 301 ADV B 402
SITE 2 AC3 8 HOH B 404 HOH B 405 HOH B 406 HOH B 407
SITE 1 AC4 6 ALA B 96 GLU B 116 MG B 301 ADV B 402
SITE 2 AC4 6 HOH B 409 HOH B 410
SITE 1 AC5 27 ARG A 51 GLU A 52 SER A 133 PRO A 134
SITE 2 AC5 27 GLY A 135 PHE B 28 PHE B 29 ARG B 56
SITE 3 AC5 27 ARG B 79 ALA B 96 GLY B 97 MET B 98
SITE 4 AC5 27 GLU B 112 GLU B 116 GLU B 139 GLU B 162
SITE 5 AC5 27 GLU B 164 MG B 301 MG B 304 MG B 310
SITE 6 AC5 27 HOH B 405 HOH B 407 HOH B 408 HOH B 409
SITE 7 AC5 27 HOH B 436 HOH B 489 HOH B 501
CRYST1 67.100 67.400 96.500 90.00 90.00 90.00 P 21 21 21 8
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 0.014903 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010363 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
