HEADER OXIDOREDUCTASE 25-NOV-98 1B14
TITLE ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS BINARY COMPLEX WITH
TITLE 2 NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.1;
COMPND 5 OTHER_DETAILS: NAD+
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCAPTODROSOPHILA LEBANONENSIS;
SOURCE 3 ORGANISM_TAXID: 7225
KEYWDS DETOXIFICATION, METABOLISM, ALCOHOL DEHYDROGENASE, DROSOPHILA
KEYWDS 2 LEBANONENSIS, SHORT-CHAIN DEHYDROGENASES/REDUCTASES, BINARY COMPLEX,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BENACH,S.ATRIAN,R.GONZALEZ-DUARTE,R.LADENSTEIN
REVDAT 4 09-AUG-23 1B14 1 REMARK
REVDAT 3 13-JUL-11 1B14 1 VERSN
REVDAT 2 24-FEB-09 1B14 1 VERSN
REVDAT 1 26-NOV-99 1B14 0
JRNL AUTH J.BENACH,S.ATRIAN,R.GONZALEZ-DUARTE,R.LADENSTEIN
JRNL TITL THE CATALYTIC REACTION AND INHIBITION MECHANISM OF
JRNL TITL 2 DROSOPHILA ALCOHOL DEHYDROGENASE: OBSERVATION OF AN
JRNL TITL 3 ENZYME-BOUND NAD-KETONE ADDUCT AT 1.4 A RESOLUTION BY X-RAY
JRNL TITL 4 CRYSTALLOGRAPHY.
JRNL REF J.MOL.BIOL. V. 289 335 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10366509
JRNL DOI 10.1006/JMBI.1999.2765
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16724
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.40
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-97
REMARK 200 TEMPERATURE (KELVIN) : 290
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18139
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
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, X-PLOR, CCP4, MAIN, RAVE
REMARK 200 STARTING MODEL: 1A4U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 28% PEG
REMARK 280 2000, 0.2 M CACL2, 0.1 M TRIS-HCL, PH=7.0, 277 K., PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 27.70000
REMARK 290 SMTRY3 2 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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: 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 ALA A 12 49.44 70.90
REMARK 500 LYS A 83 -54.37 74.38
REMARK 500 ASP A 96 90.85 -178.91
REMARK 500 GLN A 99 78.64 -110.16
REMARK 500 CYS A 137 -108.77 -101.97
REMARK 500 SER A 138 142.84 167.42
REMARK 500 GLU A 199 89.29 -153.77
REMARK 500 PRO A 210 118.94 -39.14
REMARK 500 LYS B 31 -72.62 -61.04
REMARK 500 LYS B 83 -58.91 78.46
REMARK 500 ASP B 96 96.46 -178.73
REMARK 500 CYS B 137 -109.49 -101.65
REMARK 500 SER B 138 144.38 169.38
REMARK 500 ASP B 197 46.74 34.65
REMARK 500 PRO B 210 120.85 -38.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 144 ILE A 145 141.56
REMARK 500 ALA B 144 ILE B 145 141.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: NA1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD BINDING MOTIF IN DADHS G(A)XGXXG
REMARK 800
REMARK 800 SITE_IDENTIFIER: NA2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD BINDING MOTIF IN SDRS GXXXGXG
REMARK 800
REMARK 800 SITE_IDENTIFIER: NA3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD/NADP SELECTIVITY AMINO ACID
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA2+ BINDING RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: NB1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD BINDING MOTIF IN DADHS G(A)XGXXG
REMARK 800
REMARK 800 SITE_IDENTIFIER: NB2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD BINDING MOTIF IN SDRS GXXXGXG
REMARK 800
REMARK 800 SITE_IDENTIFIER: NB3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NAD/NADP SELECTIVITY AMINO ACID
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA2+ BINDING RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 256
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B15 RELATED DB: PDB
REMARK 900 ALCOHOL DEHYDROGENASE, NAD-ACETONE ADDUCT
REMARK 900 RELATED ID: 1B2L RELATED DB: PDB
REMARK 900 ALCOHOL DEHYDROGENASE, NAD-CYCLOHEXANONE ADDUCT
DBREF 1B14 A 1 254 UNP P10807 ADH_DROLE 1 254
DBREF 1B14 B 1 254 UNP P10807 ADH_DROLE 1 254
SEQRES 1 A 254 MET ASP LEU THR ASN LYS ASN VAL ILE PHE VAL ALA ALA
SEQRES 2 A 254 LEU GLY GLY ILE GLY LEU ASP THR SER ARG GLU LEU VAL
SEQRES 3 A 254 LYS ARG ASN LEU LYS ASN PHE VAL ILE LEU ASP ARG VAL
SEQRES 4 A 254 GLU ASN PRO THR ALA LEU ALA GLU LEU LYS ALA ILE ASN
SEQRES 5 A 254 PRO LYS VAL ASN ILE THR PHE HIS THR TYR ASP VAL THR
SEQRES 6 A 254 VAL PRO VAL ALA GLU SER LYS LYS LEU LEU LYS LYS ILE
SEQRES 7 A 254 PHE ASP GLN LEU LYS THR VAL ASP ILE LEU ILE ASN GLY
SEQRES 8 A 254 ALA GLY ILE LEU ASP ASP HIS GLN ILE GLU ARG THR ILE
SEQRES 9 A 254 ALA ILE ASN PHE THR GLY LEU VAL ASN THR THR THR ALA
SEQRES 10 A 254 ILE LEU ASP PHE TRP ASP LYS ARG LYS GLY GLY PRO GLY
SEQRES 11 A 254 GLY ILE ILE ALA ASN ILE CYS SER VAL THR GLY PHE ASN
SEQRES 12 A 254 ALA ILE HIS GLN VAL PRO VAL TYR SER ALA SER LYS ALA
SEQRES 13 A 254 ALA VAL VAL SER PHE THR ASN SER LEU ALA LYS LEU ALA
SEQRES 14 A 254 PRO ILE THR GLY VAL THR ALA TYR SER ILE ASN PRO GLY
SEQRES 15 A 254 ILE THR ARG THR PRO LEU VAL HIS THR PHE ASN SER TRP
SEQRES 16 A 254 LEU ASP VAL GLU PRO ARG VAL ALA GLU LEU LEU LEU SER
SEQRES 17 A 254 HIS PRO THR GLN THR SER GLU GLN CYS GLY GLN ASN PHE
SEQRES 18 A 254 VAL LYS ALA ILE GLU ALA ASN LYS ASN GLY ALA ILE TRP
SEQRES 19 A 254 LYS LEU ASP LEU GLY THR LEU GLU ALA ILE GLU TRP THR
SEQRES 20 A 254 LYS HIS TRP ASP SER HIS ILE
SEQRES 1 B 254 MET ASP LEU THR ASN LYS ASN VAL ILE PHE VAL ALA ALA
SEQRES 2 B 254 LEU GLY GLY ILE GLY LEU ASP THR SER ARG GLU LEU VAL
SEQRES 3 B 254 LYS ARG ASN LEU LYS ASN PHE VAL ILE LEU ASP ARG VAL
SEQRES 4 B 254 GLU ASN PRO THR ALA LEU ALA GLU LEU LYS ALA ILE ASN
SEQRES 5 B 254 PRO LYS VAL ASN ILE THR PHE HIS THR TYR ASP VAL THR
SEQRES 6 B 254 VAL PRO VAL ALA GLU SER LYS LYS LEU LEU LYS LYS ILE
SEQRES 7 B 254 PHE ASP GLN LEU LYS THR VAL ASP ILE LEU ILE ASN GLY
SEQRES 8 B 254 ALA GLY ILE LEU ASP ASP HIS GLN ILE GLU ARG THR ILE
SEQRES 9 B 254 ALA ILE ASN PHE THR GLY LEU VAL ASN THR THR THR ALA
SEQRES 10 B 254 ILE LEU ASP PHE TRP ASP LYS ARG LYS GLY GLY PRO GLY
SEQRES 11 B 254 GLY ILE ILE ALA ASN ILE CYS SER VAL THR GLY PHE ASN
SEQRES 12 B 254 ALA ILE HIS GLN VAL PRO VAL TYR SER ALA SER LYS ALA
SEQRES 13 B 254 ALA VAL VAL SER PHE THR ASN SER LEU ALA LYS LEU ALA
SEQRES 14 B 254 PRO ILE THR GLY VAL THR ALA TYR SER ILE ASN PRO GLY
SEQRES 15 B 254 ILE THR ARG THR PRO LEU VAL HIS THR PHE ASN SER TRP
SEQRES 16 B 254 LEU ASP VAL GLU PRO ARG VAL ALA GLU LEU LEU LEU SER
SEQRES 17 B 254 HIS PRO THR GLN THR SER GLU GLN CYS GLY GLN ASN PHE
SEQRES 18 B 254 VAL LYS ALA ILE GLU ALA ASN LYS ASN GLY ALA ILE TRP
SEQRES 19 B 254 LYS LEU ASP LEU GLY THR LEU GLU ALA ILE GLU TRP THR
SEQRES 20 B 254 LYS HIS TRP ASP SER HIS ILE
HET NAD A 255 44
HET NAD B 256 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 5 HOH *52(H2 O)
HELIX 1 1 GLY A 16 ARG A 28 1 13
HELIX 2 2 PRO A 42 ILE A 51 1 10
HELIX 3 3 VAL A 68 LEU A 82 1 15
HELIX 4 4 ILE A 100 ASN A 107 1 8
HELIX 5 5 THR A 109 TRP A 122 1 14
HELIX 6 6 LYS A 124 LYS A 126 5 3
HELIX 7 7 VAL A 139 GLY A 141 5 3
HELIX 8 8 HIS A 146 THR A 172 5 27
HELIX 9 9 PRO A 187 HIS A 190 1 4
HELIX 10 10 TRP A 195 ASP A 197 5 3
HELIX 11 11 VAL A 202 SER A 208 1 7
HELIX 12 12 SER A 214 ALA A 227 1 14
HELIX 13 13 GLY B 16 ARG B 28 1 13
HELIX 14 14 PRO B 42 ILE B 51 1 10
HELIX 15 15 VAL B 68 LEU B 82 1 15
HELIX 16 16 ILE B 100 ASN B 107 1 8
HELIX 17 17 THR B 109 TRP B 122 1 14
HELIX 18 18 LYS B 124 LYS B 126 5 3
HELIX 19 19 VAL B 139 GLY B 141 5 3
HELIX 20 20 HIS B 146 THR B 172 5 27
HELIX 21 21 PRO B 187 HIS B 190 1 4
HELIX 22 22 TRP B 195 ASP B 197 5 3
HELIX 23 23 VAL B 202 SER B 208 1 7
HELIX 24 24 SER B 214 ALA B 227 1 14
SHEET 1 A 7 ILE A 233 LEU A 236 0
SHEET 2 A 7 VAL A 174 PRO A 181 1 N SER A 178 O TRP A 234
SHEET 3 A 7 GLY A 131 ILE A 136 1 N GLY A 131 O THR A 175
SHEET 4 A 7 ILE A 87 ASN A 90 1 N LEU A 88 O ILE A 132
SHEET 5 A 7 ASN A 7 VAL A 11 1 N ILE A 9 O ILE A 87
SHEET 6 A 7 ASN A 32 ASP A 37 1 N ASN A 32 O VAL A 8
SHEET 7 A 7 ASN A 56 THR A 61 1 N ASN A 56 O PHE A 33
SHEET 1 B 8 THR B 240 ALA B 243 0
SHEET 2 B 8 ILE B 233 ASP B 237 -1 N ASP B 237 O THR B 240
SHEET 3 B 8 VAL B 174 PRO B 181 1 N SER B 178 O TRP B 234
SHEET 4 B 8 GLY B 131 ILE B 136 1 N GLY B 131 O THR B 175
SHEET 5 B 8 ILE B 87 ASN B 90 1 N LEU B 88 O ILE B 132
SHEET 6 B 8 ASN B 7 VAL B 11 1 N ILE B 9 O ILE B 87
SHEET 7 B 8 ASN B 32 ASP B 37 1 N ASN B 32 O VAL B 8
SHEET 8 B 8 ASN B 56 THR B 61 1 N ASN B 56 O PHE B 33
SITE 1 ACA 3 SER A 138 TYR A 151 LYS A 155
SITE 1 NA1 3 ALA A 13 GLY A 15 GLY A 18
SITE 1 NA2 3 ALA A 12 GLY A 16 GLY A 18
SITE 1 NA3 1 ASP A 37
SITE 1 CAA 2 ASP A 2 THR A 4
SITE 1 ACB 3 SER B 138 TYR B 151 LYS B 155
SITE 1 NB1 3 ALA B 13 GLY B 15 GLY B 18
SITE 1 NB2 3 ALA B 12 GLY B 16 GLY B 18
SITE 1 NB3 1 ASP B 37
SITE 1 CAB 2 ASP B 2 THR B 4
SITE 1 AC1 25 ALA A 12 GLY A 15 GLY A 16 ILE A 17
SITE 2 AC1 25 ASP A 37 ARG A 38 TYR A 62 ASP A 63
SITE 3 AC1 25 VAL A 64 GLY A 91 ALA A 92 GLY A 93
SITE 4 AC1 25 ILE A 106 ILE A 136 CYS A 137 SER A 138
SITE 5 AC1 25 TYR A 151 LYS A 155 PRO A 181 GLY A 182
SITE 6 AC1 25 THR A 184 THR A 186 LEU A 188 VAL A 189
SITE 7 AC1 25 HOH A 259
SITE 1 AC2 24 ALA B 12 GLY B 15 GLY B 16 ILE B 17
SITE 2 AC2 24 ASP B 37 ARG B 38 TYR B 62 ASP B 63
SITE 3 AC2 24 VAL B 64 GLY B 91 ALA B 92 GLY B 93
SITE 4 AC2 24 ILE B 106 ILE B 136 CYS B 137 SER B 138
SITE 5 AC2 24 TYR B 151 LYS B 155 PRO B 181 GLY B 182
SITE 6 AC2 24 THR B 184 THR B 186 LEU B 188 VAL B 189
CRYST1 65.600 55.400 70.000 90.00 107.00 90.00 P 1 21 1 4
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 0.015244 0.000000 0.004660 0.00000
SCALE2 0.000000 0.018050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014938 0.00000
MTRIX1 1 -0.977729 -0.193102 0.082209 22.41785 1
MTRIX2 1 -0.196852 0.707960 -0.678264 12.49119 1
MTRIX3 1 0.072774 -0.679341 -0.730205 25.27568 1
(ATOM LINES ARE NOT SHOWN.)
END
