HEADER HYDROLASE 02-APR-04 1SZ3
TITLE CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEXED WITH GNP AND
TITLE 2 MG+2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUTT/NUDIX FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.6.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DR1025;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 TUNER;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS NUDIX FOLD, ALPHA-BETA-ALPHA SANDWICH, STRUCTURAL GENOMICS, BSGC
KEYWDS 2 STRUCTURE FUNDED BY NIH, PROTEIN STRUCTURE INITIATIVE, PSI, BERKELEY
KEYWDS 3 STRUCTURAL GENOMICS CENTER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.RANATUNGA,E.E.HILL,J.L.MOOSTER,E.L.HOLBROOK,U.SCHULZE-GAHMEN,W.XU,
AUTHOR 2 M.J.BESSMAN,S.E.BRENNER,S.R.HOLBROOK,BERKELEY STRUCTURAL GENOMICS
AUTHOR 3 CENTER (BSGC)
REVDAT 5 14-FEB-24 1SZ3 1 REMARK LINK
REVDAT 4 24-FEB-09 1SZ3 1 VERSN
REVDAT 3 25-JAN-05 1SZ3 1 AUTHOR KEYWDS REMARK
REVDAT 2 24-AUG-04 1SZ3 1 KEYWDS
REVDAT 1 11-MAY-04 1SZ3 0
JRNL AUTH W.RANATUNGA,E.E.HILL,J.L.MOOSTER,E.L.HOLBROOK,
JRNL AUTH 2 U.SCHULZE-GAHMEN,W.XU,M.J.BESSMAN,S.E.BRENNER,S.R.HOLBROOK
JRNL TITL STRUCTURAL STUDIES OF THE NUDIX HYDROLASE DR1025 FROM
JRNL TITL 2 DEINOCOCCUS RADIODURANS AND ITS LIGAND COMPLEXES.
JRNL REF J.MOL.BIOL. V. 339 103 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15123424
JRNL DOI 10.1016/J.JMB.2004.01.065
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1734.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 43122
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) : 0.213
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4346
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3943
REMARK 3 BIN R VALUE (WORKING SET) : 0.2451
REMARK 3 BIN FREE R VALUE : 0.2783
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 390
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2426
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.47400
REMARK 3 B22 (A**2) : -1.47400
REMARK 3 B33 (A**2) : 2.94700
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.09
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.762
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.31
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.135
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) : 1.455 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.359 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.739 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.112 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : GNP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44122
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 47.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
REMARK 200 R SYM FOR SHELL (I) : 0.47350
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.780
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, SODIUM FORMATE, PH
REMARK 280 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.09850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.54925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 91.64775
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 300 REMARK: ASYMMETRIC UNIT OF THE CRYSTAL STRUCTURE IS A DIMER AND THE
REMARK 300 BIOLOGICAL UNIT IS A DIMER.
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: 5170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 PRO A 36
REMARK 465 GLY A 37
REMARK 465 HIS A 38
REMARK 465 VAL A 159
REMARK 465 PRO B 36
REMARK 465 GLY B 37
REMARK 465 HIS B 38
REMARK 465 VAL B 159
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 39 CA - N - CD ANGL. DEV. = -18.7 DEGREES
REMARK 500 PRO B 39 CA - N - CD ANGL. DEV. = -20.9 DEGREES
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 2 -155.22 -103.67
REMARK 500 GLU A 118 -177.90 178.23
REMARK 500 GLU B 2 72.97 -108.80
REMARK 500 HIS B 3 -20.60 46.83
REMARK 500 GLU B 40 -58.23 47.44
REMARK 500 ALA B 42 91.04 54.84
REMARK 500 GLU B 118 -179.15 178.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 124 0.14 SIDE CHAIN
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 A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 65 OE2
REMARK 620 2 HOH A 765 O 88.0
REMARK 620 3 HOH A 846 O 75.3 97.9
REMARK 620 4 HOH A 853 O 76.9 69.0 149.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 65 OE2
REMARK 620 2 HOH B 817 O 98.6
REMARK 620 3 HOH B 844 O 82.4 170.0
REMARK 620 4 HOH B 878 O 62.7 95.2 76.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 3030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 2030
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BSGCAIR30561 RELATED DB: TARGETDB
DBREF 1SZ3 A 1 159 UNP Q9RVK2 Q9RVK2_DEIRA 1 159
DBREF 1SZ3 B 1 159 UNP Q9RVK2 Q9RVK2_DEIRA 1 159
SEQRES 1 A 159 MET GLU HIS ASP GLU ARG THR HIS VAL PRO VAL GLU LEU
SEQRES 2 A 159 ARG ALA ALA GLY VAL VAL LEU LEU ASN GLU ARG GLY ASP
SEQRES 3 A 159 ILE LEU LEU VAL GLN GLU LYS GLY ILE PRO GLY HIS PRO
SEQRES 4 A 159 GLU LYS ALA GLY LEU TRP HIS ILE PRO SER GLY ALA VAL
SEQRES 5 A 159 GLU ASP GLY GLU ASN PRO GLN ASP ALA ALA VAL ARG GLU
SEQRES 6 A 159 ALA CYS GLU GLU THR GLY LEU ARG VAL ARG PRO VAL LYS
SEQRES 7 A 159 PHE LEU GLY ALA TYR LEU GLY ARG PHE PRO ASP GLY VAL
SEQRES 8 A 159 LEU ILE LEU ARG HIS VAL TRP LEU ALA GLU PRO GLU PRO
SEQRES 9 A 159 GLY GLN THR LEU ALA PRO ALA PHE THR ASP GLU ILE ALA
SEQRES 10 A 159 GLU ALA SER PHE VAL SER ARG GLU ASP PHE ALA GLN LEU
SEQRES 11 A 159 TYR ALA ALA GLY GLN ILE ARG MET TYR GLN THR LYS LEU
SEQRES 12 A 159 PHE TYR ALA ASP ALA LEU ARG GLU LYS GLY PHE PRO ALA
SEQRES 13 A 159 LEU PRO VAL
SEQRES 1 B 159 MET GLU HIS ASP GLU ARG THR HIS VAL PRO VAL GLU LEU
SEQRES 2 B 159 ARG ALA ALA GLY VAL VAL LEU LEU ASN GLU ARG GLY ASP
SEQRES 3 B 159 ILE LEU LEU VAL GLN GLU LYS GLY ILE PRO GLY HIS PRO
SEQRES 4 B 159 GLU LYS ALA GLY LEU TRP HIS ILE PRO SER GLY ALA VAL
SEQRES 5 B 159 GLU ASP GLY GLU ASN PRO GLN ASP ALA ALA VAL ARG GLU
SEQRES 6 B 159 ALA CYS GLU GLU THR GLY LEU ARG VAL ARG PRO VAL LYS
SEQRES 7 B 159 PHE LEU GLY ALA TYR LEU GLY ARG PHE PRO ASP GLY VAL
SEQRES 8 B 159 LEU ILE LEU ARG HIS VAL TRP LEU ALA GLU PRO GLU PRO
SEQRES 9 B 159 GLY GLN THR LEU ALA PRO ALA PHE THR ASP GLU ILE ALA
SEQRES 10 B 159 GLU ALA SER PHE VAL SER ARG GLU ASP PHE ALA GLN LEU
SEQRES 11 B 159 TYR ALA ALA GLY GLN ILE ARG MET TYR GLN THR LYS LEU
SEQRES 12 B 159 PHE TYR ALA ASP ALA LEU ARG GLU LYS GLY PHE PRO ALA
SEQRES 13 B 159 LEU PRO VAL
HET MG A 201 1
HET GNP A3030 32
HET GNP A2030 32
HET MG B 202 1
HETNAM MG MAGNESIUM ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL 3 MG 2(MG 2+)
FORMUL 4 GNP 2(C10 H17 N6 O13 P3)
FORMUL 7 HOH *223(H2 O)
HELIX 1 1 ASN A 57 GLY A 71 1 15
HELIX 2 2 SER A 123 ALA A 133 1 11
HELIX 3 3 TYR A 139 GLY A 153 1 15
HELIX 4 4 ASN B 57 GLY B 71 1 15
HELIX 5 5 SER B 123 ALA B 133 1 11
HELIX 6 6 TYR B 139 GLY B 153 1 15
SHEET 1 A 5 THR A 7 HIS A 8 0
SHEET 2 A 5 VAL B 74 ARG B 86 -1 O ARG B 86 N THR A 7
SHEET 3 A 5 LEU B 92 PRO B 102 -1 O LEU B 99 N LYS B 78
SHEET 4 A 5 LEU B 13 LEU B 20 1 N VAL B 19 O TRP B 98
SHEET 5 A 5 SER B 49 ALA B 51 -1 O GLY B 50 N ALA B 16
SHEET 1 B 5 SER A 49 ALA A 51 0
SHEET 2 B 5 LEU A 13 LEU A 20 -1 N ALA A 16 O GLY A 50
SHEET 3 B 5 LEU A 92 PRO A 102 1 O TRP A 98 N VAL A 19
SHEET 4 B 5 VAL A 74 ARG A 86 -1 N LYS A 78 O LEU A 99
SHEET 5 B 5 THR B 7 HIS B 8 -1 O THR B 7 N ARG A 86
SHEET 1 C 3 TRP A 45 HIS A 46 0
SHEET 2 C 3 ILE A 27 GLN A 31 -1 N VAL A 30 O HIS A 46
SHEET 3 C 3 GLU A 118 VAL A 122 -1 O SER A 120 N LEU A 29
SHEET 1 D 3 TRP B 45 HIS B 46 0
SHEET 2 D 3 ILE B 27 GLU B 32 -1 N VAL B 30 O HIS B 46
SHEET 3 D 3 ILE B 116 VAL B 122 -1 O GLU B 118 N GLN B 31
LINK OE2 GLU A 65 MG MG A 201 1555 1555 2.74
LINK MG MG A 201 O HOH A 765 1555 1555 2.66
LINK MG MG A 201 O HOH A 846 1555 1555 2.73
LINK MG MG A 201 O HOH A 853 1555 1555 3.07
LINK OE2 GLU B 65 MG MG B 202 1555 1555 2.66
LINK MG MG B 202 O HOH B 817 1555 1555 2.64
LINK MG MG B 202 O HOH B 844 1555 1555 2.73
LINK MG MG B 202 O HOH B 878 1555 1555 2.70
SITE 1 AC1 4 GLU A 65 HOH A 765 HOH A 846 HOH A 853
SITE 1 AC2 4 GLU B 65 HOH B 817 HOH B 844 HOH B 878
SITE 1 AC3 17 LEU A 13 ALA A 15 HIS A 46 SER A 49
SITE 2 AC3 17 GLY A 50 ALA A 51 GLU A 69 PHE A 87
SITE 3 AC3 17 ASP A 89 ILE A 93 ARG A 95 HOH A 810
SITE 4 AC3 17 HOH A 845 MET B 1 GLU B 2 ASP B 4
SITE 5 AC3 17 ARG B 6
SITE 1 AC4 19 MET A 1 GLU A 2 ASP A 4 HOH A 793
SITE 2 AC4 19 HOH A 804 HOH A 862 LEU B 13 ALA B 15
SITE 3 AC4 19 SER B 49 GLY B 50 ALA B 51 PHE B 87
SITE 4 AC4 19 PRO B 88 ASP B 89 VAL B 91 ILE B 93
SITE 5 AC4 19 ARG B 95 HOH B 817 HOH B 867
CRYST1 53.072 53.072 122.197 90.00 90.00 90.00 P 41 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 0.018847 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018847 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
