HEADER OXIDOREDUCTASE 27-DEC-04 1YE3
TITLE HORSE LIVER ALCOHOL DEHYDROGENASE APOENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE E CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 OTHER_DETAILS: LIVER
KEYWDS DEHYDROGENASE, ALCOHOL, LIVER, APOENZYME, METHYLPENTANEDIOL,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.V.PLAPP,B.R.SAVARIMUTHU,S.RAMASWAMY
REVDAT 4 23-AUG-23 1YE3 1 REMARK LINK
REVDAT 3 13-JUL-11 1YE3 1 VERSN
REVDAT 2 24-FEB-09 1YE3 1 VERSN
REVDAT 1 11-JAN-05 1YE3 0
JRNL AUTH B.V.PLAPP,B.R.SAVARIMUTHU,S.RAMASWAMY
JRNL TITL HORSE LIVER ALCOHOL DEHYDROGENASE APOENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND,I.OHLSSON,
REMARK 1 AUTH 2 T.BOIWE,B.-O.SODERBERG,O.TAPIA,C.-I.BRANDEN,A.AKESON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 102 27 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.EKLUND,J.-P.SAMAMA,L.WALLEN,C.-I.BRANDEN,A.AKESON,
REMARK 1 AUTH 2 T.A JONES
REMARK 1 TITL STRUCTURE OF A TRICLINIC TERNARY COMPLEX OF HORSE LIVER
REMARK 1 TITL 2 ALCOHOL DEHYDROGENASE AT 2.9 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 146 561 1981
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.RAMASWAMY,D.H.PARK,B.V.PLAPP
REMARK 1 TITL SUBSTITUTIONS IN THE FLEXIBLE LOOP OF HORSE LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASE HINDER THE CONFORMATIONAL CHANGE AND UNMASK
REMARK 1 TITL 3 HYDROGEN TRANSFER
REMARK 1 REF BIOCHEMISTRY V. 38 13951 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.K.RUBACH,S.RAMASWAMY,B.V.PLAPP
REMARK 1 TITL CONTRIBUTIONS OF VALINE-292 IN THE NICOTINAMIDE BINDING SITE
REMARK 1 TITL 2 OF LIVER ALCOHOL DEHYDROGENASE AND DYNAMICS TO CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 40 12686 2001
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH H.EKLUND,B.V.PLAPP,J.-P.SAMAMA,C.-I.BRANDEN
REMARK 1 TITL BINDING OF SUBSTRATE IN A TERNARY COMPLEX OF HORSE LIVER
REMARK 1 TITL 2 ALCOHOL DEHYDROGENASE
REMARK 1 REF J.BIOL.CHEM. V. 257 14349 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 6
REMARK 1 AUTH S.RAMASWAMY,H.EKLUND,B.V.PLAPP
REMARK 1 TITL STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED
REMARK 1 TITL 2 WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS
REMARK 1 REF BIOCHEMISTRY V. 33 5230 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 7
REMARK 1 AUTH J.K.RUBACH,B.V.PLAPP
REMARK 1 TITL MOBILITY OF FLUOROBENZYL ALCOHOLS BOUND TO LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASES AS DETERMINED BY NMR AND X-RAY
REMARK 1 TITL 3 CRYSTALLOGRAPHIC STUDIES
REMARK 1 REF BIOCHEMISTRY V. 41 15770 2002
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 8
REMARK 1 AUTH J.K.RUBACH,B.V.PLAPP
REMARK 1 TITL AMINO ACID RESIDUES IN THE NICOTINAMIDE BINDING SITE
REMARK 1 TITL 2 CONTRIBUTE TO CATALYSIS BY HORSE LIVER ALCOHOL DEHYDROGENASE
REMARK 1 REF BIOCHEMISTRY V. 42 2907 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 9
REMARK 1 AUTH H.EKLUND,J.-P.SAMAMA,T.A.JONES
REMARK 1 TITL CRYSTALLOGRAPHIC INVESTIGATIONS OF NICOTINAMIDE ADENINE
REMARK 1 TITL 2 DINUCLEOTIDE BINDING TO HORSE LIVER ALCOHOL DEHYDROGENASE
REMARK 1 REF BIOCHEMISTRY V. 23 5982 1984
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 10
REMARK 1 AUTH E.CEDERGREN-ZEPPEZAUER,J.-P.SAMAMA,H.EKLUND
REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATIONS OF COENZYME ANALOGUE AND
REMARK 1 TITL 2 SUBSTRATE COMPLEXES OF LIVER ALCOHOL DEHYDROGENASE. BINDING
REMARK 1 TITL 3 OF 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE AND
REMARK 1 TITL 4 TRANS-4-(N,N-DIMETHYLAMINO)CINNAMALDEHYDE TO THE ENZYME
REMARK 1 REF BIOCHEMISTRY V. 21 4895 1982
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 71.9
REMARK 3 NUMBER OF REFLECTIONS : 35539
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 + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1143
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2002
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2785
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.86000
REMARK 3 B22 (A**2) : 1.46000
REMARK 3 B33 (A**2) : -2.32000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.926
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2844 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3846 ; 1.529 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 373 ; 5.908 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;36.304 ;24.330
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 498 ;14.379 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.041 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 448 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2072 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1284 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1971 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 187 ; 0.144 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.011 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 52 ; 0.153 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.100 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1895 ; 1.493 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2996 ; 2.218 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1043 ; 3.249 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 850 ; 4.532 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2931 ; 1.671 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 2 ;17.858 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2785 ; 8.267 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 POSITIONS FOR RESIDUES A269-A270 WERE NOT WELL-DEFINED BY THE
REMARK 3 ELECTRON DENSITY.
REMARK 3 SEVERAL RESIDUES, INCLUDING A306, HAVE ALTERNATIVE CONFORMATIONS,
REMARK 3 BUT THESE WERE
REMARK 3 NOT MODELED.
REMARK 4
REMARK 4 1YE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031421.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36732
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 20.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 71.9
REMARK 200 DATA REDUNDANCY : 5.660
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.74
REMARK 200 R MERGE FOR SHELL (I) : 0.21100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 8ADH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS-HCL, 25% METHYLPENTANEDIOL,
REMARK 280 PH 8.4, MICRODIALYSIS, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 90.62500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.62500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 27.89000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.14500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.89000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.14500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.62500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.89000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.14500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.62500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.89000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 37.14500
REMARK 290 SMTRY3 8 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: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 90.62500
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 HIS A 67 -3.97 -142.31
REMARK 500 ASN A 109 -8.28 -142.81
REMARK 500 THR A 143 -66.06 -121.26
REMARK 500 SER A 144 72.75 56.80
REMARK 500 CYS A 174 -70.68 -162.32
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 ZN A 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 67 NE2 103.5
REMARK 620 3 CYS A 174 SG 129.3 118.9
REMARK 620 4 HOH A 463 O 99.0 101.4 98.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 100 SG 110.8
REMARK 620 3 CYS A 103 SG 115.2 104.2
REMARK 620 4 CYS A 111 SG 104.3 117.5 105.1
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 ZN A 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8ADH RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE APOENZYME AT 2.4 A
DBREF 1YE3 A 1 374 UNP P00327 ADHE_HORSE 1 374
SEQRES 1 A 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES 2 A 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL
SEQRES 3 A 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS
SEQRES 4 A 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL
SEQRES 5 A 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA
SEQRES 6 A 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU
SEQRES 7 A 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO
SEQRES 8 A 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS
SEQRES 9 A 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER
SEQRES 10 A 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE
SEQRES 11 A 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR
SEQRES 12 A 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER
SEQRES 13 A 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL
SEQRES 14 A 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER
SEQRES 15 A 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS
SEQRES 16 A 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE
SEQRES 17 A 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY
SEQRES 18 A 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU
SEQRES 19 A 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS
SEQRES 20 A 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY
SEQRES 21 A 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP
SEQRES 22 A 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR
SEQRES 23 A 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN
SEQRES 24 A 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG
SEQRES 25 A 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS
SEQRES 26 A 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS
SEQRES 27 A 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO
SEQRES 28 A 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER
SEQRES 29 A 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE
HET ZN A 375 1
HET ZN A 376 1
HET MPD A2001 8
HETNAM ZN ZINC ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 MPD C6 H14 O2
FORMUL 5 HOH *200(H2 O)
HELIX 1 1 CYS A 46 SER A 54 1 9
HELIX 2 2 PRO A 165 CYS A 170 1 6
HELIX 3 3 LEU A 171 GLY A 173 5 3
HELIX 4 4 CYS A 174 LYS A 185 1 12
HELIX 5 5 GLY A 201 ALA A 214 1 14
HELIX 6 6 ASN A 225 ASP A 227 5 3
HELIX 7 7 LYS A 228 GLY A 236 1 9
HELIX 8 8 ASN A 242 TYR A 246 5 5
HELIX 9 9 PRO A 249 SER A 258 1 10
HELIX 10 10 ARG A 271 CYS A 282 1 12
HELIX 11 11 PRO A 305 SER A 310 1 6
HELIX 12 12 ILE A 318 PHE A 322 5 5
HELIX 13 13 LYS A 323 ALA A 337 1 15
HELIX 14 14 LEU A 342 ILE A 346 5 5
HELIX 15 15 LYS A 354 SER A 364 1 11
SHEET 1 A 4 ILE A 7 VAL A 13 0
SHEET 2 A 4 SER A 22 VAL A 28 -1 O GLU A 24 N ALA A 11
SHEET 3 A 4 PHE A 130 CYS A 132 -1 O THR A 131 N GLU A 27
SHEET 4 A 4 LYS A 135 ILE A 137 -1 O LYS A 135 N CYS A 132
SHEET 1 B 5 TYR A 149 ASP A 153 0
SHEET 2 B 5 GLU A 35 GLY A 44 -1 N ILE A 38 O THR A 150
SHEET 3 B 5 ALA A 69 ILE A 76 -1 O ILE A 72 N LYS A 39
SHEET 4 B 5 LYS A 88 PRO A 91 -1 O VAL A 89 N GLY A 71
SHEET 5 B 5 VAL A 157 ILE A 160 -1 O ILE A 160 N LYS A 88
SHEET 1 C 4 TYR A 149 ASP A 153 0
SHEET 2 C 4 GLU A 35 GLY A 44 -1 N ILE A 38 O THR A 150
SHEET 3 C 4 THR A 370 THR A 373 -1 O LEU A 372 N THR A 43
SHEET 4 C 4 HIS A 348 PRO A 351 1 N LEU A 350 O ILE A 371
SHEET 1 D 6 GLU A 239 VAL A 241 0
SHEET 2 D 6 ARG A 218 VAL A 222 1 N GLY A 221 O VAL A 241
SHEET 3 D 6 THR A 194 PHE A 198 1 N CYS A 195 O ILE A 220
SHEET 4 D 6 PHE A 264 GLU A 267 1 O PHE A 266 N PHE A 198
SHEET 5 D 6 VAL A 288 ILE A 291 1 O VAL A 290 N SER A 265
SHEET 6 D 6 THR A 313 GLY A 316 1 O LYS A 315 N ILE A 291
LINK SG CYS A 46 ZN ZN A 375 1555 1555 2.42
LINK NE2 HIS A 67 ZN ZN A 375 1555 1555 2.05
LINK SG CYS A 97 ZN ZN A 376 1555 1555 2.30
LINK SG CYS A 100 ZN ZN A 376 1555 1555 2.37
LINK SG CYS A 103 ZN ZN A 376 1555 1555 2.35
LINK SG CYS A 111 ZN ZN A 376 1555 1555 2.33
LINK SG CYS A 174 ZN ZN A 375 1555 1555 2.21
LINK ZN ZN A 375 O HOH A 463 1555 1555 2.11
CISPEP 1 LEU A 61 PRO A 62 0 -0.99
SITE 1 AC1 4 CYS A 46 HIS A 67 CYS A 174 HOH A 463
SITE 1 AC2 4 CYS A 97 CYS A 100 CYS A 103 CYS A 111
SITE 1 AC3 5 LEU A 116 VAL A 294 PRO A 296 MET A 306
SITE 2 AC3 5 HOH A 464
CRYST1 55.780 74.290 181.250 90.00 90.00 90.00 C 2 2 21 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 0.017928 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005517 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
