HEADER OXIDOREDUCTASE 06-NOV-00 1G6K
TITLE CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE MUTANT E96A COMPLEXED WITH
TITLE 2 NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE 1-DEHYDROGENASE;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 EC: 1.1.1.47;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 STRAIN: IWG3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KP3998;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKP1500
KEYWDS SHORT-CHAIN DEHYDROGENASE/REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.YAMAMOTO,G.KURISU,M.KUSUNOKI,S.TABATA,I.URABE,S.OSAKI
REVDAT 5 25-OCT-23 1G6K 1 REMARK
REVDAT 4 10-NOV-21 1G6K 1 REMARK SEQADV
REVDAT 3 13-JUL-11 1G6K 1 VERSN
REVDAT 2 24-FEB-09 1G6K 1 VERSN
REVDAT 1 12-AUG-03 1G6K 0
JRNL AUTH K.YAMAMOTO,G.KURISU,M.KUSUNOKI,S.TABATA,I.URABE,S.OSAKI
JRNL TITL STRUCTURAL ANALYSIS OF STABILITY-INCREASING MUTANTS OF
JRNL TITL 2 GLUCOSE DEHYDROGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.YAMAMOTO,G.KURISU,M.KUSUNOKI,S.TABATA,I.URABE,S.OSAKI
REMARK 1 TITL CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE FROM BACILLUS
REMARK 1 TITL 2 MEGATERIUM IWG3 AT 1.7 A RESOLUTION
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 129 303 2001
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.YAMAOTO,M.KUSUNOKI,I.URABE,S.TABATA,S.OSAKI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF GLUCOSE
REMARK 1 TITL 2 DEHYDROGENASE FROM BACILLUS MEGATERIUM IWG3
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1443 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S090744490000994X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 61350
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) : 0.219
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3059
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.63000
REMARK 3 B22 (A**2) : 5.62000
REMARK 3 B33 (A**2) : -7.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.82000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.42
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.180
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 294512
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 4.780
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GCO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000, SODIUM PHOSPHATE, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 60.97750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.32000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.97750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.32000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: THE BIOLOGICAL ACTIVE FORM IS TETRAMER.
REMARK 300 FOR TETRAMER1, APPLY (-X, Y, -Z)+A TO CHAINS A AND B.
REMARK 300 FOR TETRAMER2, APPLY (-X, Y, -Z)+C TO CHAINS E AND F.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 121.95500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 21450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -7.20429
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 119.84866
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 SER A 40 -67.06 -131.14
REMARK 500 SER A 144 -136.98 -105.45
REMARK 500 LEU A 154 -13.85 82.07
REMARK 500 TYR A 253 74.77 58.17
REMARK 500 SER B 40 -71.16 -91.83
REMARK 500 ASP B 43 -57.03 -160.06
REMARK 500 SER B 144 -136.35 -105.22
REMARK 500 LEU B 154 -14.41 81.77
REMARK 500 TYR B 253 74.95 57.70
REMARK 500 SER E 144 -136.58 -104.35
REMARK 500 LEU E 154 -15.22 81.61
REMARK 500 TYR E 253 76.74 57.23
REMARK 500 SER F 40 -82.70 -109.08
REMARK 500 SER F 144 -135.26 -104.28
REMARK 500 LEU F 154 -14.67 81.59
REMARK 500 TYR F 253 75.25 58.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 2262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 3262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 4262
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GCO RELATED DB: PDB
REMARK 900 1GCO CONTAINS WILD TYPE GLUCOSE DEHYDROGENASE
REMARK 900 RELATED ID: 1GEE RELATED DB: PDB
REMARK 900 1GEE CONTAINS GLUCOSE 1-DEHYDROGENASE (Q252L).
DBREF 1G6K A 1 261 UNP P40288 DHG_BACME 1 261
DBREF 1G6K B 1 261 UNP P40288 DHG_BACME 1 261
DBREF 1G6K E 1 261 UNP P40288 DHG_BACME 1 261
DBREF 1G6K F 1 261 UNP P40288 DHG_BACME 1 261
SEQADV 1G6K ALA A 96 UNP P40288 GLU 96 ENGINEERED MUTATION
SEQADV 1G6K ALA B 96 UNP P40288 GLU 96 ENGINEERED MUTATION
SEQADV 1G6K ALA E 96 UNP P40288 GLU 96 ENGINEERED MUTATION
SEQADV 1G6K ALA F 96 UNP P40288 GLU 96 ENGINEERED MUTATION
SEQRES 1 A 261 MET TYR LYS ASP LEU GLU GLY LYS VAL VAL VAL ILE THR
SEQRES 2 A 261 GLY SER SER THR GLY LEU GLY LYS SER MET ALA ILE ARG
SEQRES 3 A 261 PHE ALA THR GLU LYS ALA LYS VAL VAL VAL ASN TYR ARG
SEQRES 4 A 261 SER LYS GLU ASP GLU ALA ASN SER VAL LEU GLU GLU ILE
SEQRES 5 A 261 LYS LYS VAL GLY GLY GLU ALA ILE ALA VAL LYS GLY ASP
SEQRES 6 A 261 VAL THR VAL GLU SER ASP VAL ILE ASN LEU VAL GLN SER
SEQRES 7 A 261 ALA ILE LYS GLU PHE GLY LYS LEU ASP VAL MET ILE ASN
SEQRES 8 A 261 ASN ALA GLY LEU ALA ASN PRO VAL SER SER HIS GLU MET
SEQRES 9 A 261 SER LEU SER ASP TRP ASN LYS VAL ILE ASP THR ASN LEU
SEQRES 10 A 261 THR GLY ALA PHE LEU GLY SER ARG GLU ALA ILE LYS TYR
SEQRES 11 A 261 PHE VAL GLU ASN ASP ILE LYS GLY THR VAL ILE ASN MET
SEQRES 12 A 261 SER SER VAL HIS GLU LYS ILE PRO TRP PRO LEU PHE VAL
SEQRES 13 A 261 HIS TYR ALA ALA SER LYS GLY GLY MET LYS LEU MET THR
SEQRES 14 A 261 GLU THR LEU ALA LEU GLU TYR ALA PRO LYS GLY ILE ARG
SEQRES 15 A 261 VAL ASN ASN ILE GLY PRO GLY ALA ILE ASN THR PRO ILE
SEQRES 16 A 261 ASN ALA GLU LYS PHE ALA ASP PRO GLU GLN ARG ALA ASP
SEQRES 17 A 261 VAL GLU SER MET ILE PRO MET GLY TYR ILE GLY GLU PRO
SEQRES 18 A 261 GLU GLU ILE ALA ALA VAL ALA ALA TRP LEU ALA SER SER
SEQRES 19 A 261 GLU ALA SER TYR VAL THR GLY ILE THR LEU PHE ALA ASP
SEQRES 20 A 261 GLY GLY MET THR GLN TYR PRO SER PHE GLN ALA GLY ARG
SEQRES 21 A 261 GLY
SEQRES 1 B 261 MET TYR LYS ASP LEU GLU GLY LYS VAL VAL VAL ILE THR
SEQRES 2 B 261 GLY SER SER THR GLY LEU GLY LYS SER MET ALA ILE ARG
SEQRES 3 B 261 PHE ALA THR GLU LYS ALA LYS VAL VAL VAL ASN TYR ARG
SEQRES 4 B 261 SER LYS GLU ASP GLU ALA ASN SER VAL LEU GLU GLU ILE
SEQRES 5 B 261 LYS LYS VAL GLY GLY GLU ALA ILE ALA VAL LYS GLY ASP
SEQRES 6 B 261 VAL THR VAL GLU SER ASP VAL ILE ASN LEU VAL GLN SER
SEQRES 7 B 261 ALA ILE LYS GLU PHE GLY LYS LEU ASP VAL MET ILE ASN
SEQRES 8 B 261 ASN ALA GLY LEU ALA ASN PRO VAL SER SER HIS GLU MET
SEQRES 9 B 261 SER LEU SER ASP TRP ASN LYS VAL ILE ASP THR ASN LEU
SEQRES 10 B 261 THR GLY ALA PHE LEU GLY SER ARG GLU ALA ILE LYS TYR
SEQRES 11 B 261 PHE VAL GLU ASN ASP ILE LYS GLY THR VAL ILE ASN MET
SEQRES 12 B 261 SER SER VAL HIS GLU LYS ILE PRO TRP PRO LEU PHE VAL
SEQRES 13 B 261 HIS TYR ALA ALA SER LYS GLY GLY MET LYS LEU MET THR
SEQRES 14 B 261 GLU THR LEU ALA LEU GLU TYR ALA PRO LYS GLY ILE ARG
SEQRES 15 B 261 VAL ASN ASN ILE GLY PRO GLY ALA ILE ASN THR PRO ILE
SEQRES 16 B 261 ASN ALA GLU LYS PHE ALA ASP PRO GLU GLN ARG ALA ASP
SEQRES 17 B 261 VAL GLU SER MET ILE PRO MET GLY TYR ILE GLY GLU PRO
SEQRES 18 B 261 GLU GLU ILE ALA ALA VAL ALA ALA TRP LEU ALA SER SER
SEQRES 19 B 261 GLU ALA SER TYR VAL THR GLY ILE THR LEU PHE ALA ASP
SEQRES 20 B 261 GLY GLY MET THR GLN TYR PRO SER PHE GLN ALA GLY ARG
SEQRES 21 B 261 GLY
SEQRES 1 E 261 MET TYR LYS ASP LEU GLU GLY LYS VAL VAL VAL ILE THR
SEQRES 2 E 261 GLY SER SER THR GLY LEU GLY LYS SER MET ALA ILE ARG
SEQRES 3 E 261 PHE ALA THR GLU LYS ALA LYS VAL VAL VAL ASN TYR ARG
SEQRES 4 E 261 SER LYS GLU ASP GLU ALA ASN SER VAL LEU GLU GLU ILE
SEQRES 5 E 261 LYS LYS VAL GLY GLY GLU ALA ILE ALA VAL LYS GLY ASP
SEQRES 6 E 261 VAL THR VAL GLU SER ASP VAL ILE ASN LEU VAL GLN SER
SEQRES 7 E 261 ALA ILE LYS GLU PHE GLY LYS LEU ASP VAL MET ILE ASN
SEQRES 8 E 261 ASN ALA GLY LEU ALA ASN PRO VAL SER SER HIS GLU MET
SEQRES 9 E 261 SER LEU SER ASP TRP ASN LYS VAL ILE ASP THR ASN LEU
SEQRES 10 E 261 THR GLY ALA PHE LEU GLY SER ARG GLU ALA ILE LYS TYR
SEQRES 11 E 261 PHE VAL GLU ASN ASP ILE LYS GLY THR VAL ILE ASN MET
SEQRES 12 E 261 SER SER VAL HIS GLU LYS ILE PRO TRP PRO LEU PHE VAL
SEQRES 13 E 261 HIS TYR ALA ALA SER LYS GLY GLY MET LYS LEU MET THR
SEQRES 14 E 261 GLU THR LEU ALA LEU GLU TYR ALA PRO LYS GLY ILE ARG
SEQRES 15 E 261 VAL ASN ASN ILE GLY PRO GLY ALA ILE ASN THR PRO ILE
SEQRES 16 E 261 ASN ALA GLU LYS PHE ALA ASP PRO GLU GLN ARG ALA ASP
SEQRES 17 E 261 VAL GLU SER MET ILE PRO MET GLY TYR ILE GLY GLU PRO
SEQRES 18 E 261 GLU GLU ILE ALA ALA VAL ALA ALA TRP LEU ALA SER SER
SEQRES 19 E 261 GLU ALA SER TYR VAL THR GLY ILE THR LEU PHE ALA ASP
SEQRES 20 E 261 GLY GLY MET THR GLN TYR PRO SER PHE GLN ALA GLY ARG
SEQRES 21 E 261 GLY
SEQRES 1 F 261 MET TYR LYS ASP LEU GLU GLY LYS VAL VAL VAL ILE THR
SEQRES 2 F 261 GLY SER SER THR GLY LEU GLY LYS SER MET ALA ILE ARG
SEQRES 3 F 261 PHE ALA THR GLU LYS ALA LYS VAL VAL VAL ASN TYR ARG
SEQRES 4 F 261 SER LYS GLU ASP GLU ALA ASN SER VAL LEU GLU GLU ILE
SEQRES 5 F 261 LYS LYS VAL GLY GLY GLU ALA ILE ALA VAL LYS GLY ASP
SEQRES 6 F 261 VAL THR VAL GLU SER ASP VAL ILE ASN LEU VAL GLN SER
SEQRES 7 F 261 ALA ILE LYS GLU PHE GLY LYS LEU ASP VAL MET ILE ASN
SEQRES 8 F 261 ASN ALA GLY LEU ALA ASN PRO VAL SER SER HIS GLU MET
SEQRES 9 F 261 SER LEU SER ASP TRP ASN LYS VAL ILE ASP THR ASN LEU
SEQRES 10 F 261 THR GLY ALA PHE LEU GLY SER ARG GLU ALA ILE LYS TYR
SEQRES 11 F 261 PHE VAL GLU ASN ASP ILE LYS GLY THR VAL ILE ASN MET
SEQRES 12 F 261 SER SER VAL HIS GLU LYS ILE PRO TRP PRO LEU PHE VAL
SEQRES 13 F 261 HIS TYR ALA ALA SER LYS GLY GLY MET LYS LEU MET THR
SEQRES 14 F 261 GLU THR LEU ALA LEU GLU TYR ALA PRO LYS GLY ILE ARG
SEQRES 15 F 261 VAL ASN ASN ILE GLY PRO GLY ALA ILE ASN THR PRO ILE
SEQRES 16 F 261 ASN ALA GLU LYS PHE ALA ASP PRO GLU GLN ARG ALA ASP
SEQRES 17 F 261 VAL GLU SER MET ILE PRO MET GLY TYR ILE GLY GLU PRO
SEQRES 18 F 261 GLU GLU ILE ALA ALA VAL ALA ALA TRP LEU ALA SER SER
SEQRES 19 F 261 GLU ALA SER TYR VAL THR GLY ILE THR LEU PHE ALA ASP
SEQRES 20 F 261 GLY GLY MET THR GLN TYR PRO SER PHE GLN ALA GLY ARG
SEQRES 21 F 261 GLY
HET NAD A1262 44
HET NAD B2262 44
HET NAD E3262 44
HET NAD F4262 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 9 HOH *311(H2 O)
HELIX 1 1 TYR A 2 GLU A 6 5 5
HELIX 2 2 THR A 17 GLU A 30 1 14
HELIX 3 3 LYS A 41 VAL A 55 1 15
HELIX 4 4 VAL A 68 GLY A 84 1 17
HELIX 5 5 SER A 100 MET A 104 5 5
HELIX 6 6 SER A 105 LEU A 117 1 13
HELIX 7 7 LEU A 117 ASN A 134 1 18
HELIX 8 8 SER A 145 LYS A 149 5 5
HELIX 9 9 PHE A 155 ALA A 177 1 23
HELIX 10 10 PRO A 178 GLY A 180 5 3
HELIX 11 11 THR A 193 ALA A 197 5 5
HELIX 12 12 ASP A 202 SER A 211 1 10
HELIX 13 13 GLU A 220 SER A 233 1 14
HELIX 14 14 SER A 234 SER A 237 5 4
HELIX 15 15 GLY A 249 TYR A 253 5 5
HELIX 16 16 TYR A 253 GLN A 257 5 5
HELIX 17 17 PHE A 256 ARG A 260 5 5
HELIX 18 18 TYR B 2 GLU B 6 5 5
HELIX 19 19 THR B 17 GLU B 30 1 14
HELIX 20 20 ASP B 43 VAL B 55 1 13
HELIX 21 21 VAL B 68 GLY B 84 1 17
HELIX 22 22 SER B 100 MET B 104 5 5
HELIX 23 23 SER B 105 LEU B 117 1 13
HELIX 24 24 LEU B 117 ASN B 134 1 18
HELIX 25 25 SER B 145 LYS B 149 5 5
HELIX 26 26 PHE B 155 ALA B 177 1 23
HELIX 27 27 PRO B 178 GLY B 180 5 3
HELIX 28 28 THR B 193 ALA B 197 5 5
HELIX 29 29 ASP B 202 SER B 211 1 10
HELIX 30 30 GLU B 220 SER B 233 1 14
HELIX 31 31 SER B 234 SER B 237 5 4
HELIX 32 32 GLY B 249 TYR B 253 5 5
HELIX 33 33 TYR B 253 GLN B 257 5 5
HELIX 34 34 PHE B 256 ARG B 260 5 5
HELIX 35 35 TYR E 2 GLU E 6 5 5
HELIX 36 36 THR E 17 GLU E 30 1 14
HELIX 37 37 LYS E 41 GLU E 44 5 4
HELIX 38 38 ALA E 45 VAL E 55 1 11
HELIX 39 39 VAL E 68 GLY E 84 1 17
HELIX 40 40 SER E 100 MET E 104 5 5
HELIX 41 41 SER E 105 LEU E 117 1 13
HELIX 42 42 LEU E 117 ASN E 134 1 18
HELIX 43 43 SER E 145 LYS E 149 5 5
HELIX 44 44 PHE E 155 ALA E 177 1 23
HELIX 45 45 PRO E 178 GLY E 180 5 3
HELIX 46 46 THR E 193 ALA E 197 5 5
HELIX 47 47 ASP E 202 SER E 211 1 10
HELIX 48 48 GLU E 220 SER E 233 1 14
HELIX 49 49 SER E 234 SER E 237 5 4
HELIX 50 50 GLY E 249 TYR E 253 5 5
HELIX 51 51 TYR E 253 GLN E 257 5 5
HELIX 52 52 PHE E 256 ARG E 260 5 5
HELIX 53 53 TYR F 2 GLU F 6 5 5
HELIX 54 54 THR F 17 GLU F 30 1 14
HELIX 55 55 LYS F 41 GLU F 44 5 4
HELIX 56 56 ALA F 45 VAL F 55 1 11
HELIX 57 57 VAL F 68 GLY F 84 1 17
HELIX 58 58 SER F 100 MET F 104 5 5
HELIX 59 59 SER F 105 LEU F 117 1 13
HELIX 60 60 LEU F 117 ASN F 134 1 18
HELIX 61 61 SER F 145 LYS F 149 5 5
HELIX 62 62 PHE F 155 ALA F 177 1 23
HELIX 63 63 PRO F 178 GLY F 180 5 3
HELIX 64 64 THR F 193 ALA F 197 5 5
HELIX 65 65 ASP F 202 SER F 211 1 10
HELIX 66 66 GLU F 220 SER F 233 1 14
HELIX 67 67 SER F 234 SER F 237 5 4
HELIX 68 68 GLY F 249 TYR F 253 5 5
HELIX 69 69 TYR F 253 GLN F 257 5 5
HELIX 70 70 PHE F 256 ARG F 260 5 5
SHEET 1 A 7 GLU A 58 LYS A 63 0
SHEET 2 A 7 LYS A 33 TYR A 38 1 N VAL A 34 O GLU A 58
SHEET 3 A 7 VAL A 9 ILE A 12 1 N VAL A 10 O LYS A 33
SHEET 4 A 7 VAL A 88 ASN A 91 1 O VAL A 88 N VAL A 11
SHEET 5 A 7 THR A 139 MET A 143 1 O THR A 139 N MET A 89
SHEET 6 A 7 ARG A 182 PRO A 188 1 O ARG A 182 N VAL A 140
SHEET 7 A 7 THR A 243 ALA A 246 1 O LEU A 244 N GLY A 187
SHEET 1 B 7 GLU B 58 LYS B 63 0
SHEET 2 B 7 LYS B 33 TYR B 38 1 N VAL B 34 O GLU B 58
SHEET 3 B 7 VAL B 9 ILE B 12 1 N VAL B 10 O LYS B 33
SHEET 4 B 7 VAL B 88 ASN B 91 1 O VAL B 88 N VAL B 11
SHEET 5 B 7 THR B 139 MET B 143 1 O THR B 139 N MET B 89
SHEET 6 B 7 ARG B 182 PRO B 188 1 O ARG B 182 N VAL B 140
SHEET 7 B 7 THR B 243 ALA B 246 1 N LEU B 244 O ASN B 185
SHEET 1 C 7 GLU E 58 LYS E 63 0
SHEET 2 C 7 LYS E 33 TYR E 38 1 N VAL E 34 O GLU E 58
SHEET 3 C 7 VAL E 9 ILE E 12 1 N VAL E 10 O LYS E 33
SHEET 4 C 7 VAL E 88 ASN E 91 1 O VAL E 88 N VAL E 11
SHEET 5 C 7 THR E 139 MET E 143 1 O THR E 139 N MET E 89
SHEET 6 C 7 ARG E 182 PRO E 188 1 O ARG E 182 N VAL E 140
SHEET 7 C 7 THR E 243 ALA E 246 1 N LEU E 244 O ASN E 185
SHEET 1 D 7 GLU F 58 LYS F 63 0
SHEET 2 D 7 LYS F 33 TYR F 38 1 N VAL F 34 O GLU F 58
SHEET 3 D 7 VAL F 9 ILE F 12 1 N VAL F 10 O LYS F 33
SHEET 4 D 7 VAL F 88 ASN F 91 1 O VAL F 88 N VAL F 11
SHEET 5 D 7 THR F 139 MET F 143 1 O THR F 139 N MET F 89
SHEET 6 D 7 ARG F 182 PRO F 188 1 O ARG F 182 N VAL F 140
SHEET 7 D 7 THR F 243 ALA F 246 1 O LEU F 244 N GLY F 187
SITE 1 AC1 27 GLY A 14 THR A 17 GLY A 18 LEU A 19
SITE 2 AC1 27 ARG A 39 GLY A 64 ASP A 65 VAL A 66
SITE 3 AC1 27 ASN A 92 ALA A 93 GLY A 94 THR A 115
SITE 4 AC1 27 MET A 143 SER A 144 SER A 145 TYR A 158
SITE 5 AC1 27 LYS A 162 PRO A 188 GLY A 189 ILE A 191
SITE 6 AC1 27 THR A 193 ILE A 195 ASN A 196 HOH A1273
SITE 7 AC1 27 HOH A1291 HOH A1299 HOH A1300
SITE 1 AC2 25 GLY B 14 THR B 17 GLY B 18 LEU B 19
SITE 2 AC2 25 GLY B 64 ASP B 65 VAL B 66 ASN B 92
SITE 3 AC2 25 ALA B 93 GLY B 94 THR B 115 MET B 143
SITE 4 AC2 25 SER B 144 SER B 145 TYR B 158 LYS B 162
SITE 5 AC2 25 PRO B 188 GLY B 189 ILE B 191 THR B 193
SITE 6 AC2 25 ILE B 195 ASN B 196 HOH B2265 HOH B2293
SITE 7 AC2 25 HOH B2331
SITE 1 AC3 25 GLY E 14 THR E 17 GLY E 18 LEU E 19
SITE 2 AC3 25 ARG E 39 GLY E 64 ASP E 65 VAL E 66
SITE 3 AC3 25 ASN E 92 ALA E 93 GLY E 94 THR E 115
SITE 4 AC3 25 MET E 143 SER E 144 SER E 145 TYR E 158
SITE 5 AC3 25 LYS E 162 PRO E 188 GLY E 189 ILE E 191
SITE 6 AC3 25 THR E 193 ILE E 195 ASN E 196 HOH E3279
SITE 7 AC3 25 HOH E3284
SITE 1 AC4 24 GLY F 14 THR F 17 GLY F 18 LEU F 19
SITE 2 AC4 24 GLY F 64 ASP F 65 VAL F 66 ASN F 92
SITE 3 AC4 24 ALA F 93 GLY F 94 THR F 115 MET F 143
SITE 4 AC4 24 SER F 144 SER F 145 TYR F 158 LYS F 162
SITE 5 AC4 24 PRO F 188 GLY F 189 ILE F 191 THR F 193
SITE 6 AC4 24 ILE F 195 ASN F 196 HOH F4272 HOH F4304
CRYST1 121.955 66.640 120.065 90.00 93.44 90.00 C 1 2 1 16
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 0.008200 0.000000 0.000494 0.00000
SCALE2 0.000000 0.015006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008344 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
