HEADER LYASE 08-OCT-08 3ETH
TITLE CRYSTAL STRUCTURE OF E. COLI PURK IN COMPLEX WITH MGATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AIR CARBOXYLASE, AIRC;
COMPND 5 EC: 4.1.1.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B0522, JW0511, PURK, PURK_ECOLI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET31
KEYWDS ATP-GRASP, PURINE BIOSYNTHESIS, ANTIMICROBIAL, ATP-BINDING,
KEYWDS 2 DECARBOXYLASE, LYASE, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.HOLDEN,J.B.THODEN
REVDAT 5 25-OCT-17 3ETH 1 REMARK
REVDAT 4 09-JUN-09 3ETH 1 REVDAT
REVDAT 3 24-FEB-09 3ETH 1 VERSN
REVDAT 2 30-DEC-08 3ETH 1 JRNL
REVDAT 1 21-OCT-08 3ETH 0
JRNL AUTH J.B.THODEN,H.M.HOLDEN,S.M.FIRESTINE
JRNL TITL STRUCTURAL ANALYSIS OF THE ACTIVE SITE GEOMETRY OF
JRNL TITL 2 N(5)-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE FROM
JRNL TITL 3 ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 47 13346 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 19053251
JRNL DOI 10.1021/BI801734Z
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 87820
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDON
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8777
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1780
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 87820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 690
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH & HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ETH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049746.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : D*TREK, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : 0.03300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
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 (%) : 81.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.09800
REMARK 200 R SYM FOR SHELL (I) : 0.09800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1B6S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% MONOMETHYLETHER POLY(ETHYLENE
REMARK 280 GLYCOL) 5000, 10 MM MGATP, 10 MM AMINOPYRAZOLE RIBONUCLEOTIDE,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: 5060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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 O HOH A 615 O HOH A 616 2.19
REMARK 500 O HIS A 65 NH2 ARG A 71 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 1 CG - SD - CE ANGL. DEV. = 9.6 DEGREES
REMARK 500 LYS A 2 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLU A 153 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 LEU A 271 CB - CG - CD2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 LEU B 92 CB - CG - CD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500 ARG B 112 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU B 134 CB - CG - CD1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG B 168 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 168 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 205 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 LEU B 210 CB - CG - CD1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASP B 306 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG B 313 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG B 313 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU B 320 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU B 320 CB - CG - CD2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG B 327 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 327 NE - CZ - NH2 ANGL. DEV. = -6.5 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 LYS A 2 149.06 -27.92
REMARK 500 ALA A 67 50.44 -96.29
REMARK 500 ASP A 127 28.35 46.43
REMARK 500 ARG A 242 -178.50 172.81
REMARK 500 ARG B 64 14.30 58.22
REMARK 500 ARG B 242 177.83 177.62
REMARK 500 GLU B 342 -9.01 -58.00
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 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 226 OE1
REMARK 620 2 GLU A 226 OE2 58.7
REMARK 620 3 GLU A 238 OE1 101.8 99.0
REMARK 620 4 ATP A 400 O1G 147.0 89.2 90.1
REMARK 620 5 ATP A 400 O2A 100.4 159.1 83.0 111.7
REMARK 620 6 HOH A 738 O 91.3 88.3 166.9 79.1 94.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 238 OE1
REMARK 620 2 GLU A 238 OE2 60.4
REMARK 620 3 ATP A 400 O2G 101.9 162.0
REMARK 620 4 ATP A 400 O2B 95.7 91.0 93.9
REMARK 620 5 HOH A 736 O 86.1 85.3 90.8 174.5
REMARK 620 6 HOH A 734 O 154.0 94.0 103.3 89.1 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 226 OE1
REMARK 620 2 GLU B 226 OE2 56.4
REMARK 620 3 GLU B 238 OE2 90.6 91.1
REMARK 620 4 ATP B 400 O1G 86.2 142.4 93.6
REMARK 620 5 ATP B 400 O2A 154.2 97.9 87.7 119.6
REMARK 620 6 HOH B 651 O 88.8 88.0 179.1 87.1 92.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 238 OE1
REMARK 620 2 GLU B 238 OE2 58.2
REMARK 620 3 ATP B 400 O2G 161.1 103.4
REMARK 620 4 ATP B 400 O2B 87.1 91.6 89.7
REMARK 620 5 HOH B 652 O 99.8 156.7 99.0 94.7
REMARK 620 6 HOH B 653 O 88.5 84.5 93.9 175.2 87.8
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 ATP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ETJ RELATED DB: PDB
DBREF 3ETH A 1 355 UNP P09029 PURK_ECOLI 1 355
DBREF 3ETH B 1 355 UNP P09029 PURK_ECOLI 1 355
SEQADV 3ETH GLN A 61 UNP P09029 GLU 61 ENGINEERED
SEQADV 3ETH ARG A 205 UNP P09029 GLN 205 ENGINEERED
SEQADV 3ETH GLN B 61 UNP P09029 GLU 61 ENGINEERED
SEQADV 3ETH ARG B 205 UNP P09029 GLN 205 ENGINEERED
SEQRES 1 A 355 MET LYS GLN VAL CYS VAL LEU GLY ASN GLY GLN LEU GLY
SEQRES 2 A 355 ARG MET LEU ARG GLN ALA GLY GLU PRO LEU GLY ILE ALA
SEQRES 3 A 355 VAL TRP PRO VAL GLY LEU ASP ALA GLU PRO ALA ALA VAL
SEQRES 4 A 355 PRO PHE GLN GLN SER VAL ILE THR ALA GLU ILE GLU ARG
SEQRES 5 A 355 TRP PRO GLU THR ALA LEU THR ARG GLN LEU ALA ARG HIS
SEQRES 6 A 355 PRO ALA PHE VAL ASN ARG ASP VAL PHE PRO ILE ILE ALA
SEQRES 7 A 355 ASP ARG LEU THR GLN LYS GLN LEU PHE ASP LYS LEU HIS
SEQRES 8 A 355 LEU PRO THR ALA PRO TRP GLN LEU LEU ALA GLU ARG SER
SEQRES 9 A 355 GLU TRP PRO ALA VAL PHE ASP ARG LEU GLY GLU LEU ALA
SEQRES 10 A 355 ILE VAL LYS ARG ARG THR GLY GLY TYR ASP GLY ARG GLY
SEQRES 11 A 355 GLN TRP ARG LEU ARG ALA ASN GLU THR GLU GLN LEU PRO
SEQRES 12 A 355 ALA GLU CYS TYR GLY GLU CYS ILE VAL GLU GLN GLY ILE
SEQRES 13 A 355 ASN PHE SER GLY GLU VAL SER LEU VAL GLY ALA ARG GLY
SEQRES 14 A 355 PHE ASP GLY SER THR VAL PHE TYR PRO LEU THR HIS ASN
SEQRES 15 A 355 LEU HIS GLN ASP GLY ILE LEU ARG THR SER VAL ALA PHE
SEQRES 16 A 355 PRO GLN ALA ASN ALA GLN GLN GLN ALA ARG ALA GLU GLU
SEQRES 17 A 355 MET LEU SER ALA ILE MET GLN GLU LEU GLY TYR VAL GLY
SEQRES 18 A 355 VAL MET ALA MET GLU CYS PHE VAL THR PRO GLN GLY LEU
SEQRES 19 A 355 LEU ILE ASN GLU LEU ALA PRO ARG VAL HIS ASN SER GLY
SEQRES 20 A 355 HIS TRP THR GLN ASN GLY ALA SER ILE SER GLN PHE GLU
SEQRES 21 A 355 LEU HIS LEU ARG ALA ILE THR ASP LEU PRO LEU PRO GLN
SEQRES 22 A 355 PRO VAL VAL ASN ASN PRO SER VAL MET ILE ASN LEU ILE
SEQRES 23 A 355 GLY SER ASP VAL ASN TYR ASP TRP LEU LYS LEU PRO LEU
SEQRES 24 A 355 VAL HIS LEU HIS TRP TYR ASP LYS GLU VAL ARG PRO GLY
SEQRES 25 A 355 ARG LYS VAL GLY HIS LEU ASN LEU THR ASP SER ASP THR
SEQRES 26 A 355 SER ARG LEU THR ALA THR LEU GLU ALA LEU ILE PRO LEU
SEQRES 27 A 355 LEU PRO PRO GLU TYR ALA SER GLY VAL ILE TRP ALA GLN
SEQRES 28 A 355 SER LYS PHE GLY
SEQRES 1 B 355 MET LYS GLN VAL CYS VAL LEU GLY ASN GLY GLN LEU GLY
SEQRES 2 B 355 ARG MET LEU ARG GLN ALA GLY GLU PRO LEU GLY ILE ALA
SEQRES 3 B 355 VAL TRP PRO VAL GLY LEU ASP ALA GLU PRO ALA ALA VAL
SEQRES 4 B 355 PRO PHE GLN GLN SER VAL ILE THR ALA GLU ILE GLU ARG
SEQRES 5 B 355 TRP PRO GLU THR ALA LEU THR ARG GLN LEU ALA ARG HIS
SEQRES 6 B 355 PRO ALA PHE VAL ASN ARG ASP VAL PHE PRO ILE ILE ALA
SEQRES 7 B 355 ASP ARG LEU THR GLN LYS GLN LEU PHE ASP LYS LEU HIS
SEQRES 8 B 355 LEU PRO THR ALA PRO TRP GLN LEU LEU ALA GLU ARG SER
SEQRES 9 B 355 GLU TRP PRO ALA VAL PHE ASP ARG LEU GLY GLU LEU ALA
SEQRES 10 B 355 ILE VAL LYS ARG ARG THR GLY GLY TYR ASP GLY ARG GLY
SEQRES 11 B 355 GLN TRP ARG LEU ARG ALA ASN GLU THR GLU GLN LEU PRO
SEQRES 12 B 355 ALA GLU CYS TYR GLY GLU CYS ILE VAL GLU GLN GLY ILE
SEQRES 13 B 355 ASN PHE SER GLY GLU VAL SER LEU VAL GLY ALA ARG GLY
SEQRES 14 B 355 PHE ASP GLY SER THR VAL PHE TYR PRO LEU THR HIS ASN
SEQRES 15 B 355 LEU HIS GLN ASP GLY ILE LEU ARG THR SER VAL ALA PHE
SEQRES 16 B 355 PRO GLN ALA ASN ALA GLN GLN GLN ALA ARG ALA GLU GLU
SEQRES 17 B 355 MET LEU SER ALA ILE MET GLN GLU LEU GLY TYR VAL GLY
SEQRES 18 B 355 VAL MET ALA MET GLU CYS PHE VAL THR PRO GLN GLY LEU
SEQRES 19 B 355 LEU ILE ASN GLU LEU ALA PRO ARG VAL HIS ASN SER GLY
SEQRES 20 B 355 HIS TRP THR GLN ASN GLY ALA SER ILE SER GLN PHE GLU
SEQRES 21 B 355 LEU HIS LEU ARG ALA ILE THR ASP LEU PRO LEU PRO GLN
SEQRES 22 B 355 PRO VAL VAL ASN ASN PRO SER VAL MET ILE ASN LEU ILE
SEQRES 23 B 355 GLY SER ASP VAL ASN TYR ASP TRP LEU LYS LEU PRO LEU
SEQRES 24 B 355 VAL HIS LEU HIS TRP TYR ASP LYS GLU VAL ARG PRO GLY
SEQRES 25 B 355 ARG LYS VAL GLY HIS LEU ASN LEU THR ASP SER ASP THR
SEQRES 26 B 355 SER ARG LEU THR ALA THR LEU GLU ALA LEU ILE PRO LEU
SEQRES 27 B 355 LEU PRO PRO GLU TYR ALA SER GLY VAL ILE TRP ALA GLN
SEQRES 28 B 355 SER LYS PHE GLY
HET ATP A 400 31
HET MG A 401 1
HET MG A 402 1
HET ATP B 400 31
HET MG B 401 1
HET MG B 402 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 4 MG 4(MG 2+)
FORMUL 9 HOH *690(H2 O)
HELIX 1 1 GLY A 10 GLU A 21 1 12
HELIX 2 2 PRO A 22 GLY A 24 5 3
HELIX 3 3 GLU A 35 VAL A 39 5 5
HELIX 4 4 THR A 56 ARG A 64 1 9
HELIX 5 5 ASP A 72 ASP A 79 1 8
HELIX 6 6 ASP A 79 LEU A 90 1 12
HELIX 7 7 GLU A 102 SER A 104 5 3
HELIX 8 8 GLU A 105 GLY A 114 1 10
HELIX 9 9 GLU A 138 LEU A 142 5 5
HELIX 10 10 PRO A 143 TYR A 147 5 5
HELIX 11 11 ASN A 199 GLY A 218 1 20
HELIX 12 12 HIS A 244 HIS A 248 5 5
HELIX 13 13 TRP A 249 ALA A 254 1 6
HELIX 14 14 SER A 257 THR A 267 1 11
HELIX 15 15 ASN A 291 LEU A 297 5 7
HELIX 16 16 ASP A 324 ILE A 336 1 13
HELIX 17 17 PRO A 337 LEU A 339 5 3
HELIX 18 18 PRO A 340 GLU A 342 5 3
HELIX 19 19 TYR A 343 PHE A 354 1 12
HELIX 20 20 GLY B 10 GLU B 21 1 12
HELIX 21 21 PRO B 22 GLY B 24 5 3
HELIX 22 22 GLU B 35 VAL B 39 5 5
HELIX 23 23 THR B 56 ALA B 63 1 8
HELIX 24 24 VAL B 73 ASP B 79 1 7
HELIX 25 25 ASP B 79 LEU B 90 1 12
HELIX 26 26 GLU B 102 SER B 104 5 3
HELIX 27 27 GLU B 105 GLY B 114 1 10
HELIX 28 28 GLU B 138 LEU B 142 5 5
HELIX 29 29 PRO B 143 TYR B 147 5 5
HELIX 30 30 ASN B 199 GLY B 218 1 20
HELIX 31 31 HIS B 244 HIS B 248 5 5
HELIX 32 32 TRP B 249 ALA B 254 1 6
HELIX 33 33 SER B 257 THR B 267 1 11
HELIX 34 34 ASN B 291 LEU B 297 5 7
HELIX 35 35 ASP B 324 ILE B 336 1 13
HELIX 36 36 PRO B 337 LEU B 339 5 3
HELIX 37 37 PRO B 340 GLU B 342 5 3
HELIX 38 38 TYR B 343 PHE B 354 1 12
SHEET 1 A 3 ALA A 26 VAL A 30 0
SHEET 2 A 3 GLN A 3 LEU A 7 1 N VAL A 6 O VAL A 30
SHEET 3 A 3 VAL A 45 ALA A 48 1 O THR A 47 N LEU A 7
SHEET 1 B 4 TRP A 97 LEU A 100 0
SHEET 2 B 4 CYS A 150 GLN A 154 -1 O CYS A 150 N LEU A 100
SHEET 3 B 4 LEU A 116 ARG A 121 -1 N ILE A 118 O GLU A 153
SHEET 4 B 4 GLN A 131 ARG A 135 -1 O LEU A 134 N ALA A 117
SHEET 1 C 4 THR A 174 PHE A 176 0
SHEET 2 C 4 GLY A 160 ARG A 168 -1 N ALA A 167 O VAL A 175
SHEET 3 C 4 GLY A 221 THR A 230 -1 O MET A 225 N LEU A 164
SHEET 4 C 4 GLY A 233 ALA A 240 -1 O ASN A 237 N GLU A 226
SHEET 1 D 7 THR A 174 PHE A 176 0
SHEET 2 D 7 GLY A 160 ARG A 168 -1 N ALA A 167 O VAL A 175
SHEET 3 D 7 THR A 180 GLN A 185 -1 O THR A 180 N SER A 163
SHEET 4 D 7 ILE A 188 ALA A 194 -1 O ARG A 190 N LEU A 183
SHEET 5 D 7 SER A 280 ILE A 286 -1 O SER A 280 N ALA A 194
SHEET 6 D 7 LYS A 314 THR A 321 -1 O GLY A 316 N LEU A 285
SHEET 7 D 7 HIS A 301 TRP A 304 -1 N HIS A 301 O ASN A 319
SHEET 1 E 3 ALA B 26 VAL B 30 0
SHEET 2 E 3 GLN B 3 LEU B 7 1 N VAL B 4 O ALA B 26
SHEET 3 E 3 VAL B 45 ALA B 48 1 O THR B 47 N LEU B 7
SHEET 1 F 4 TRP B 97 LEU B 100 0
SHEET 2 F 4 CYS B 150 GLN B 154 -1 O VAL B 152 N GLN B 98
SHEET 3 F 4 ALA B 117 ARG B 121 -1 N ILE B 118 O GLU B 153
SHEET 4 F 4 GLN B 131 LEU B 134 -1 O TRP B 132 N VAL B 119
SHEET 1 G 4 THR B 174 PHE B 176 0
SHEET 2 G 4 GLY B 160 ARG B 168 -1 N ALA B 167 O VAL B 175
SHEET 3 G 4 GLY B 221 THR B 230 -1 O CYS B 227 N VAL B 162
SHEET 4 G 4 GLY B 233 ALA B 240 -1 O LEU B 235 N PHE B 228
SHEET 1 H 7 THR B 174 PHE B 176 0
SHEET 2 H 7 GLY B 160 ARG B 168 -1 N ALA B 167 O VAL B 175
SHEET 3 H 7 THR B 180 GLN B 185 -1 O THR B 180 N SER B 163
SHEET 4 H 7 ILE B 188 ALA B 194 -1 O ARG B 190 N LEU B 183
SHEET 5 H 7 SER B 280 ILE B 286 -1 O ASN B 284 N ARG B 190
SHEET 6 H 7 LYS B 314 THR B 321 -1 O GLY B 316 N LEU B 285
SHEET 7 H 7 HIS B 301 TRP B 304 -1 N HIS B 301 O ASN B 319
LINK OE1 GLU A 226 MG MG A 401 1555 1555 2.12
LINK OE2 GLU A 226 MG MG A 401 1555 1555 2.30
LINK OE1 GLU A 238 MG MG A 402 1555 1555 2.11
LINK OE1 GLU A 238 MG MG A 401 1555 1555 1.97
LINK OE2 GLU A 238 MG MG A 402 1555 1555 2.21
LINK OE1 GLU B 226 MG MG B 401 1555 1555 2.46
LINK OE2 GLU B 226 MG MG B 401 1555 1555 2.12
LINK OE1 GLU B 238 MG MG B 402 1555 1555 2.20
LINK OE2 GLU B 238 MG MG B 402 1555 1555 2.28
LINK OE2 GLU B 238 MG MG B 401 1555 1555 2.11
LINK O1G ATP A 400 MG MG A 401 1555 1555 2.03
LINK O2G ATP A 400 MG MG A 402 1555 1555 1.85
LINK O2B ATP A 400 MG MG A 402 1555 1555 1.86
LINK O2A ATP A 400 MG MG A 401 1555 1555 2.04
LINK MG MG A 401 O HOH A 738 1555 1555 2.10
LINK MG MG A 402 O HOH A 736 1555 1555 2.14
LINK MG MG A 402 O HOH A 734 1555 1555 2.12
LINK O1G ATP B 400 MG MG B 401 1555 1555 2.02
LINK O2G ATP B 400 MG MG B 402 1555 1555 2.01
LINK O2B ATP B 400 MG MG B 402 1555 1555 1.94
LINK O2A ATP B 400 MG MG B 401 1555 1555 1.94
LINK MG MG B 401 O HOH B 651 1555 1555 2.05
LINK MG MG B 402 O HOH B 652 1555 1555 1.98
LINK MG MG B 402 O HOH B 653 1555 1555 2.02
SITE 1 AC1 29 ARG A 80 ILE A 118 LYS A 120 GLY A 125
SITE 2 AC1 29 TYR A 126 ASP A 127 GLY A 128 GLN A 131
SITE 3 AC1 29 GLU A 153 GLN A 154 ILE A 156 PHE A 158
SITE 4 AC1 29 GLU A 161 HIS A 184 GLU A 226 PHE A 228
SITE 5 AC1 29 ASN A 237 GLU A 238 MG A 401 MG A 402
SITE 6 AC1 29 HOH A 664 HOH A 733 HOH A 734 HOH A 735
SITE 7 AC1 29 HOH A 736 HOH A 737 HOH A 738 HOH A 739
SITE 8 AC1 29 HOH A 740
SITE 1 AC2 5 GLU A 226 GLU A 238 ATP A 400 MG A 402
SITE 2 AC2 5 HOH A 738
SITE 1 AC3 5 GLU A 238 ATP A 400 MG A 401 HOH A 734
SITE 2 AC3 5 HOH A 736
SITE 1 AC4 30 ARG B 80 ILE B 118 LYS B 120 GLY B 125
SITE 2 AC4 30 TYR B 126 ASP B 127 GLY B 128 GLN B 131
SITE 3 AC4 30 GLU B 153 GLN B 154 GLY B 155 ILE B 156
SITE 4 AC4 30 PHE B 158 GLU B 161 HIS B 184 GLU B 226
SITE 5 AC4 30 PHE B 228 ASN B 237 GLU B 238 MG B 401
SITE 6 AC4 30 MG B 402 HOH B 524 HOH B 525 HOH B 528
SITE 7 AC4 30 HOH B 649 HOH B 651 HOH B 652 HOH B 653
SITE 8 AC4 30 HOH B 658 HOH B 685
SITE 1 AC5 4 GLU B 226 GLU B 238 ATP B 400 HOH B 651
SITE 1 AC6 4 GLU B 238 ATP B 400 HOH B 652 HOH B 653
CRYST1 57.101 57.109 59.215 77.46 82.39 77.26 P 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 0.017513 -0.003958 -0.001602 0.00000
SCALE2 0.000000 0.017952 -0.003556 0.00000
SCALE3 0.000000 0.000000 0.017369 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
