HEADER OXIDOREDUCTASE 09-DEC-97 1A05
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF 3-ISOPROPYLMALATE DEHYDROGENASE
TITLE 2 FROM THIOBACILLUS FERROOXIDANS WITH 3-ISOPROPYLMALATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IPMDH, IMDH;
COMPND 5 EC: 1.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDITHIOBACILLUS FERROOXIDANS;
SOURCE 3 ORGANISM_TAXID: 920;
SOURCE 4 STRAIN: AP19-3;
SOURCE 5 GENE: LEUB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JA221;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKKLEUB1
KEYWDS OXIDOREDUCTASE, DECARBOXYLATING DEHYDROGENASE, LEUCINE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.IMADA,K.INAGAKI,H.MATSUNAMI,H.KAWAGUCHI,H.TANAKA,N.TANAKA,K.NAMBA
REVDAT 3 02-AUG-23 1A05 1 REMARK LINK
REVDAT 2 24-FEB-09 1A05 1 VERSN
REVDAT 1 17-JUN-98 1A05 0
JRNL AUTH K.IMADA,K.INAGAKI,H.MATSUNAMI,H.KAWAGUCHI,H.TANAKA,N.TANAKA,
JRNL AUTH 2 K.NAMBA
JRNL TITL STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE IN COMPLEX WITH
JRNL TITL 2 3-ISOPROPYLMALATE AT 2.0 A RESOLUTION: THE ROLE OF GLU88 IN
JRNL TITL 3 THE UNIQUE SUBSTRATE-RECOGNITION MECHANISM.
JRNL REF STRUCTURE V. 6 971 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9739088
JRNL DOI 10.1016/S0969-2126(98)00099-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.MATSUNAMI,H.KAWAGUCHI,K.INAGAKI,T.EGUCHI,K.KAKINUMA,
REMARK 1 AUTH 2 H.TANAKA
REMARK 1 TITL OVERPRODUCTION AND SUBSTRATE SPECIFICITY OF
REMARK 1 TITL 2 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS
REMARK 1 TITL 3 FERROOXIDANS
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 62 372 1998
REMARK 1 REFN ISSN 0916-8451
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.KAWAGUCHI,K.INAGAKI,Y.KUWATA,H.TANAKA,T.TANO
REMARK 1 TITL 3-ISOPROPYLMALATE DEHYDROGENASE FROM CHEMOLITHOAUTOTROPH
REMARK 1 TITL 2 THIOBACILLUS FERROOXIDANS: DNA SEQUENCE, ENZYME
REMARK 1 TITL 3 PURIFICATION, AND CHARACTERIZATION
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 114 370 1993
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.INAGAKI,H.KAWAGUCHI,Y.KUWATA,T.SUGIO,H.TANAKA,T.TANO
REMARK 1 TITL CLONING AND EXPRESSION OF THE THIOBACILLUS FERROOXIDANS
REMARK 1 TITL 2 3-ISOPROPYLMALATE DEHYDROGENASE GENE IN ESCHERICHIA COLI
REMARK 1 REF J.FERMENT.BIOENG. V. 70 71 1990
REMARK 1 REFN ISSN 0922-338X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 550.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.7
REMARK 3 NUMBER OF REFLECTIONS : 43200
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) : 0.198
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4320
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.55
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2918
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 342
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5384
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.37
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.220
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) : 2.271 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.331 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.026 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.798 ; NULL
REMARK 3
REMARK 3 NCS MODEL : UNRESTRAINED
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.ION
REMARK 3 PARAMETER FILE 3 : PARAM19.SOL
REMARK 3 PARAMETER FILE 4 : IPM.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.ION
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : IPM.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
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 FR-C
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : PROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44212
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.14200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1IPD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 28.27000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.27000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.12000
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: 6480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 ASP A 358
REMARK 465 ASP B 358
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 LEU A 54 77.66 -159.94
REMARK 500 ASP A 138 -167.82 71.75
REMARK 500 ARG A 181 -116.80 -127.45
REMARK 500 LYS A 190 46.82 -144.39
REMARK 500 VAL A 193 -50.63 -133.51
REMARK 500 ALA A 231 70.07 -155.22
REMARK 500 ASP A 236 -83.96 -119.19
REMARK 500 ALA A 272 145.63 -173.77
REMARK 500 ALA A 281 69.24 24.66
REMARK 500 PRO B 121 -41.24 -29.46
REMARK 500 ARG B 125 -38.47 -39.53
REMARK 500 ASP B 138 -172.00 67.19
REMARK 500 ARG B 181 -131.26 -115.60
REMARK 500 LYS B 190 49.51 -146.87
REMARK 500 VAL B 193 -40.88 -134.20
REMARK 500 ALA B 231 71.96 -154.84
REMARK 500 ASP B 236 -83.85 -114.88
REMARK 500 ALA B 281 64.26 29.76
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 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 222 OD2
REMARK 620 2 HOH A 532 O 80.7
REMARK 620 3 ASP B 246 OD1 95.8 176.3
REMARK 620 4 IPM B 402 O2 150.9 88.5 94.0
REMARK 620 5 IPM B 402 O1 82.6 80.0 98.4 68.8
REMARK 620 6 HOH B 419 O 118.6 91.4 91.4 88.4 155.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 246 OD1
REMARK 620 2 IPM A 401 O3 76.7
REMARK 620 3 IPM A 401 O1 94.1 72.3
REMARK 620 4 HOH A 562 O 172.5 105.6 93.4
REMARK 620 5 HOH A 602 O 73.2 85.2 156.4 99.7
REMARK 620 6 ASP B 222 OD2 90.7 147.8 79.3 90.8 119.8
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 MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPM B 402
DBREF 1A05 A 1 358 UNP Q56268 LEU3_THIFE 1 358
DBREF 1A05 B 1 358 UNP Q56268 LEU3_THIFE 1 358
SEQRES 1 A 358 MET LYS LYS ILE ALA ILE PHE ALA GLY ASP GLY ILE GLY
SEQRES 2 A 358 PRO GLU ILE VAL ALA ALA ALA ARG GLN VAL LEU ASP ALA
SEQRES 3 A 358 VAL ASP GLN ALA ALA HIS LEU GLY LEU ARG CYS THR GLU
SEQRES 4 A 358 GLY LEU VAL GLY GLY ALA ALA LEU ASP ALA SER ASP ASP
SEQRES 5 A 358 PRO LEU PRO ALA ALA SER LEU GLN LEU ALA MET ALA ALA
SEQRES 6 A 358 ASP ALA VAL ILE LEU GLY ALA VAL GLY GLY PRO ARG TRP
SEQRES 7 A 358 ASP ALA TYR PRO PRO ALA LYS ARG PRO GLU GLN GLY LEU
SEQRES 8 A 358 LEU ARG LEU ARG LYS GLY LEU ASP LEU TYR ALA ASN LEU
SEQRES 9 A 358 ARG PRO ALA GLN ILE PHE PRO GLN LEU LEU ASP ALA SER
SEQRES 10 A 358 PRO LEU ARG PRO GLU LEU VAL ARG ASP VAL ASP ILE LEU
SEQRES 11 A 358 VAL VAL ARG GLU LEU THR GLY ASP ILE TYR PHE GLY GLN
SEQRES 12 A 358 PRO ARG GLY LEU GLU VAL ILE ASP GLY LYS ARG ARG GLY
SEQRES 13 A 358 PHE ASN THR MET VAL TYR ASP GLU ASP GLU ILE ARG ARG
SEQRES 14 A 358 ILE ALA HIS VAL ALA PHE ARG ALA ALA GLN GLY ARG ARG
SEQRES 15 A 358 LYS GLN LEU CYS SER VAL ASP LYS ALA ASN VAL LEU GLU
SEQRES 16 A 358 THR THR ARG LEU TRP ARG GLU VAL VAL THR GLU VAL ALA
SEQRES 17 A 358 ARG ASP TYR PRO ASP VAL ARG LEU SER HIS MET TYR VAL
SEQRES 18 A 358 ASP ASN ALA ALA MET GLN LEU ILE ARG ALA PRO ALA GLN
SEQRES 19 A 358 PHE ASP VAL LEU LEU THR GLY ASN MET PHE GLY ASP ILE
SEQRES 20 A 358 LEU SER ASP GLU ALA SER GLN LEU THR GLY SER ILE GLY
SEQRES 21 A 358 MET LEU PRO SER ALA SER LEU GLY GLU GLY ARG ALA MET
SEQRES 22 A 358 TYR GLU PRO ILE HIS GLY SER ALA PRO ASP ILE ALA GLY
SEQRES 23 A 358 GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU SER VAL
SEQRES 24 A 358 ALA MET MET LEU ARG HIS SER LEU ASN ALA GLU PRO TRP
SEQRES 25 A 358 ALA GLN ARG VAL GLU ALA ALA VAL GLN ARG VAL LEU ASP
SEQRES 26 A 358 GLN GLY LEU ARG THR ALA ASP ILE ALA ALA PRO GLY THR
SEQRES 27 A 358 PRO VAL ILE GLY THR LYS ALA MET GLY ALA ALA VAL VAL
SEQRES 28 A 358 ASN ALA LEU ASN LEU LYS ASP
SEQRES 1 B 358 MET LYS LYS ILE ALA ILE PHE ALA GLY ASP GLY ILE GLY
SEQRES 2 B 358 PRO GLU ILE VAL ALA ALA ALA ARG GLN VAL LEU ASP ALA
SEQRES 3 B 358 VAL ASP GLN ALA ALA HIS LEU GLY LEU ARG CYS THR GLU
SEQRES 4 B 358 GLY LEU VAL GLY GLY ALA ALA LEU ASP ALA SER ASP ASP
SEQRES 5 B 358 PRO LEU PRO ALA ALA SER LEU GLN LEU ALA MET ALA ALA
SEQRES 6 B 358 ASP ALA VAL ILE LEU GLY ALA VAL GLY GLY PRO ARG TRP
SEQRES 7 B 358 ASP ALA TYR PRO PRO ALA LYS ARG PRO GLU GLN GLY LEU
SEQRES 8 B 358 LEU ARG LEU ARG LYS GLY LEU ASP LEU TYR ALA ASN LEU
SEQRES 9 B 358 ARG PRO ALA GLN ILE PHE PRO GLN LEU LEU ASP ALA SER
SEQRES 10 B 358 PRO LEU ARG PRO GLU LEU VAL ARG ASP VAL ASP ILE LEU
SEQRES 11 B 358 VAL VAL ARG GLU LEU THR GLY ASP ILE TYR PHE GLY GLN
SEQRES 12 B 358 PRO ARG GLY LEU GLU VAL ILE ASP GLY LYS ARG ARG GLY
SEQRES 13 B 358 PHE ASN THR MET VAL TYR ASP GLU ASP GLU ILE ARG ARG
SEQRES 14 B 358 ILE ALA HIS VAL ALA PHE ARG ALA ALA GLN GLY ARG ARG
SEQRES 15 B 358 LYS GLN LEU CYS SER VAL ASP LYS ALA ASN VAL LEU GLU
SEQRES 16 B 358 THR THR ARG LEU TRP ARG GLU VAL VAL THR GLU VAL ALA
SEQRES 17 B 358 ARG ASP TYR PRO ASP VAL ARG LEU SER HIS MET TYR VAL
SEQRES 18 B 358 ASP ASN ALA ALA MET GLN LEU ILE ARG ALA PRO ALA GLN
SEQRES 19 B 358 PHE ASP VAL LEU LEU THR GLY ASN MET PHE GLY ASP ILE
SEQRES 20 B 358 LEU SER ASP GLU ALA SER GLN LEU THR GLY SER ILE GLY
SEQRES 21 B 358 MET LEU PRO SER ALA SER LEU GLY GLU GLY ARG ALA MET
SEQRES 22 B 358 TYR GLU PRO ILE HIS GLY SER ALA PRO ASP ILE ALA GLY
SEQRES 23 B 358 GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU SER VAL
SEQRES 24 B 358 ALA MET MET LEU ARG HIS SER LEU ASN ALA GLU PRO TRP
SEQRES 25 B 358 ALA GLN ARG VAL GLU ALA ALA VAL GLN ARG VAL LEU ASP
SEQRES 26 B 358 GLN GLY LEU ARG THR ALA ASP ILE ALA ALA PRO GLY THR
SEQRES 27 B 358 PRO VAL ILE GLY THR LYS ALA MET GLY ALA ALA VAL VAL
SEQRES 28 B 358 ASN ALA LEU ASN LEU LYS ASP
HET MG A 501 1
HET MG A 502 1
HET IPM A 401 12
HET IPM B 402 12
HETNAM MG MAGNESIUM ION
HETNAM IPM 3-ISOPROPYLMALIC ACID
FORMUL 3 MG 2(MG 2+)
FORMUL 5 IPM 2(C7 H12 O5)
FORMUL 7 HOH *504(H2 O)
HELIX 1 1 GLY A 13 ALA A 31 1 19
HELIX 2 2 GLY A 43 SER A 50 1 8
HELIX 3 3 PRO A 55 ALA A 64 1 10
HELIX 4 4 PRO A 87 GLY A 97 1 11
HELIX 5 5 GLU A 164 GLN A 179 1 16
HELIX 6 6 GLU A 195 ASP A 210 1 16
HELIX 7 7 VAL A 221 ARG A 230 1 10
HELIX 8 8 ASN A 242 THR A 256 1 15
HELIX 9 9 PRO A 292 HIS A 305 1 14
HELIX 10 10 GLU A 310 GLN A 326 1 17
HELIX 11 11 THR A 343 LEU A 354 1 12
HELIX 12 12 GLY B 13 ALA B 31 1 19
HELIX 13 13 GLY B 43 SER B 50 1 8
HELIX 14 14 PRO B 55 ALA B 64 1 10
HELIX 15 15 PRO B 87 GLY B 97 1 11
HELIX 16 16 GLU B 164 GLN B 179 1 16
HELIX 17 17 GLU B 195 ASP B 210 1 16
HELIX 18 18 VAL B 221 ARG B 230 1 10
HELIX 19 19 ASN B 242 THR B 256 1 15
HELIX 20 20 PRO B 292 HIS B 305 1 14
HELIX 21 21 GLU B 310 GLN B 326 1 17
HELIX 22 22 THR B 343 LEU B 354 1 12
SHEET 1 A10 ARG A 36 GLU A 39 0
SHEET 2 A10 LYS A 3 PHE A 7 1 N ILE A 4 O ARG A 36
SHEET 3 A10 ALA A 67 ALA A 72 1 N ALA A 67 O LYS A 3
SHEET 4 A10 ALA A 272 PRO A 276 1 N TYR A 274 O VAL A 68
SHEET 5 A10 PRO A 263 LEU A 267 -1 N SER A 266 O MET A 273
SHEET 6 A10 ALA A 102 GLN A 108 -1 N LEU A 104 O ALA A 265
SHEET 7 A10 ASP A 128 GLU A 134 -1 N ARG A 133 O ASN A 103
SHEET 8 A10 VAL A 237 THR A 240 1 N THR A 240 O VAL A 132
SHEET 9 A10 GLN A 184 ASP A 189 1 N VAL A 188 O LEU A 239
SHEET 10 A10 ARG A 215 TYR A 220 1 N MET A 219 O SER A 187
SHEET 1 B 4 ARG A 145 ILE A 150 0
SHEET 2 B 4 LYS A 153 ASP A 163 -1 N ARG A 155 O GLU A 148
SHEET 3 B 4 LYS B 153 ASP B 163 -1 N TYR B 162 O GLY A 156
SHEET 4 B 4 ARG B 145 ILE B 150 -1 N GLY B 146 O PHE B 157
SHEET 1 C10 ARG B 36 GLU B 39 0
SHEET 2 C10 LYS B 3 PHE B 7 1 N ILE B 4 O ARG B 36
SHEET 3 C10 ALA B 67 ALA B 72 1 N ALA B 67 O LYS B 3
SHEET 4 C10 ALA B 272 PRO B 276 1 N TYR B 274 O VAL B 68
SHEET 5 C10 PRO B 263 LEU B 267 -1 N SER B 266 O MET B 273
SHEET 6 C10 ALA B 102 GLN B 108 -1 N LEU B 104 O ALA B 265
SHEET 7 C10 ASP B 128 GLU B 134 -1 N ARG B 133 O ASN B 103
SHEET 8 C10 VAL B 237 THR B 240 1 N THR B 240 O VAL B 132
SHEET 9 C10 GLN B 184 ASP B 189 1 N VAL B 188 O LEU B 239
SHEET 10 C10 ARG B 215 TYR B 220 1 N MET B 219 O SER B 187
LINK OD2 ASP A 222 MG MG A 502 1555 1555 2.45
LINK OD1 ASP A 246 MG MG A 501 1555 1555 2.38
LINK O3 IPM A 401 MG MG A 501 1555 1555 2.32
LINK O1 IPM A 401 MG MG A 501 1555 1555 2.45
LINK MG MG A 501 O HOH A 562 1555 1555 2.31
LINK MG MG A 501 O HOH A 602 1555 1555 2.35
LINK MG MG A 501 OD2 ASP B 222 1555 1555 2.44
LINK MG MG A 502 O HOH A 532 1555 1555 2.44
LINK MG MG A 502 OD1 ASP B 246 1555 1555 2.36
LINK MG MG A 502 O2 IPM B 402 1555 1555 2.37
LINK MG MG A 502 O1 IPM B 402 1555 1555 2.55
LINK MG MG A 502 O HOH B 419 1555 1555 2.42
CISPEP 1 GLN A 143 PRO A 144 0 -0.20
CISPEP 2 GLN B 143 PRO B 144 0 0.19
SITE 1 AC1 5 ASP A 246 IPM A 401 HOH A 562 HOH A 602
SITE 2 AC1 5 ASP B 222
SITE 1 AC2 5 ASP A 222 HOH A 532 ASP B 246 IPM B 402
SITE 2 AC2 5 HOH B 419
SITE 1 AC3 12 GLU A 88 ARG A 95 ARG A 105 ARG A 133
SITE 2 AC3 12 TYR A 140 ASP A 246 MG A 501 HOH A 553
SITE 3 AC3 12 HOH A 693 LYS B 190 VAL B 193 ASP B 222
SITE 1 AC4 11 LYS A 190 VAL A 193 ASP A 222 MG A 502
SITE 2 AC4 11 ARG B 95 ARG B 105 ARG B 133 TYR B 140
SITE 3 AC4 11 ASP B 246 HOH B 428 HOH B 441
CRYST1 56.540 114.240 130.890 90.00 90.00 90.00 P 21 21 2 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 0.017687 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008754 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007640 0.00000
MTRIX1 1 -1.000000 0.002110 0.000440 8.62482 1
MTRIX2 1 0.002110 1.000000 -0.000030 0.00510 1
MTRIX3 1 -0.000440 -0.000030 -1.000000 65.46259 1
(ATOM LINES ARE NOT SHOWN.)
END
