HEADER OXIDOREDUCTASE 04-JUL-15 5CDT
TITLE I220V HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD AND
TITLE 2 PENTAFLUOROBENZYL ALCOHOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE E CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: I220V SUBSTITUTION IN OTHERWISE WILD-TYPE ENZYME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBPP/EQADH1E
KEYWDS OXIDOREDUCTASE, ALCOHOL, ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR B.V.PLAPP,K.SHANMUGANATHAM
REVDAT 5 27-SEP-23 5CDT 1 LINK
REVDAT 4 25-DEC-19 5CDT 1 REMARK
REVDAT 3 03-JAN-18 5CDT 1 JRNL
REVDAT 2 27-SEP-17 5CDT 1 SOURCE REMARK
REVDAT 1 15-JUL-15 5CDT 0
JRNL AUTH K.K.SHANMUGANATHAM,R.S.WALLACE,A.T.LEE,B.V.PLAPP
JRNL TITL CONTRIBUTION OF BURIED DISTAL AMINO ACID RESIDUES IN HORSE
JRNL TITL 2 LIVER ALCOHOL DEHYDROGENASE TO STRUCTURE AND CATALYSIS.
JRNL REF PROTEIN SCI. 2017
JRNL REFN ESSN 1469-896X
JRNL PMID 29271062
JRNL DOI 10.1002/PRO.3370
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 77459
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5547
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5568
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 835
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : 1.36000
REMARK 3 B33 (A**2) : -1.21000
REMARK 3 B12 (A**2) : -0.27000
REMARK 3 B13 (A**2) : 0.31000
REMARK 3 B23 (A**2) : -0.18000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.664
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5946 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5815 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8072 ; 2.039 ; 2.015
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13511 ; 0.955 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 760 ; 6.568 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;38.453 ;24.686
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1057 ;13.316 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.342 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 946 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6506 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1184 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3015 ; 1.791 ; 2.040
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3014 ; 1.790 ; 2.039
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3771 ; 2.327 ; 3.056
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3772 ; 2.328 ; 3.056
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2931 ; 2.774 ; 2.344
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2932 ; 2.774 ; 2.345
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4296 ; 4.103 ; 3.389
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7498 ; 5.982 ;18.433
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6963 ; 5.553 ;17.336
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5CDT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.80
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77459
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.230
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.15
REMARK 200 R MERGE FOR SHELL (I) : 0.34400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 4DWV
REMARK 200
REMARK 200 REMARK: COLUMNS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM N
REMARK 280 -[TRIS(HYDROXYMETHYL)METHYL]-2-AMINOETHANE SULFONATE, PH 6.7 (AT
REMARK 280 25 C), 0.25 MM EDTA,10 MG/ML PROTEIN, 1 MM NAD+, 10 MM 2,3,4,5,6-
REMARK 280 PENTAFLUOROBENZYL ALCOHOL, 12 TO 25 % 2-METHYL-2,4-PENTANEDIOL,
REMARK 280 PH 7.0, MICRODIALYSIS, TEMPERATURE 278K
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: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 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 ASP A 245 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 312 NE - CZ - NH2 ANGL. DEV. = -3.0 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 HIS A 67 -5.49 -142.84
REMARK 500 CYS A 174 -71.99 -153.67
REMARK 500 ILE A 269 -60.58 -124.08
REMARK 500 ILE A 368 -88.59 -99.52
REMARK 500 HIS B 67 -6.41 -149.07
REMARK 500 THR B 143 -59.63 -120.71
REMARK 500 SER B 144 70.18 48.32
REMARK 500 CYS B 174 -73.27 -152.63
REMARK 500 GLU B 239 146.16 -170.34
REMARK 500 ILE B 269 -59.25 -126.70
REMARK 500 ILE B 368 -92.51 -93.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 954 DISTANCE = 6.28 ANGSTROMS
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 67 NE2 106.9
REMARK 620 3 CYS A 174 SG 121.4 113.6
REMARK 620 4 PFB A 404 O1 104.6 99.2 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 100 SG 108.7
REMARK 620 3 CYS A 103 SG 116.3 106.7
REMARK 620 4 CYS A 111 SG 103.3 120.6 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 46 SG
REMARK 620 2 HIS B 67 NE2 107.0
REMARK 620 3 CYS B 174 SG 122.9 113.3
REMARK 620 4 PFB B 404 O1 105.8 104.3 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 97 SG
REMARK 620 2 CYS B 100 SG 106.9
REMARK 620 3 CYS B 103 SG 117.4 105.0
REMARK 620 4 CYS B 111 SG 103.1 120.2 105.0
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAJ A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PFB A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAJ B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PFB B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DWV RELATED DB: PDB
REMARK 900 4DWV IS FOR WILD-TYPE COMPLEXES
REMARK 900 RELATED ID: 5CDG RELATED DB: PDB
REMARK 900 5CDG IS FOR I220F ENZYME
REMARK 900 RELATED ID: 5CDS RELATED DB: PDB
REMARK 900 5CDS IS FOR I220L ENZYME
REMARK 900 RELATED ID: 5CDU RELATED DB: PDB
DBREF 5CDT A 1 374 UNP P00327 ADH1E_HORSE 2 375
DBREF 5CDT B 1 374 UNP P00327 ADH1E_HORSE 2 375
SEQADV 5CDT VAL A 220 UNP P00327 ILE 221 ENGINEERED MUTATION
SEQADV 5CDT VAL B 220 UNP P00327 ILE 221 ENGINEERED MUTATION
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 VAL 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
SEQRES 1 B 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES 2 B 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL
SEQRES 3 B 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS
SEQRES 4 B 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL
SEQRES 5 B 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA
SEQRES 6 B 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU
SEQRES 7 B 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO
SEQRES 8 B 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS
SEQRES 9 B 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER
SEQRES 10 B 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE
SEQRES 11 B 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR
SEQRES 12 B 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER
SEQRES 13 B 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL
SEQRES 14 B 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER
SEQRES 15 B 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS
SEQRES 16 B 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE
SEQRES 17 B 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE VAL GLY
SEQRES 18 B 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU
SEQRES 19 B 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS
SEQRES 20 B 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY
SEQRES 21 B 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP
SEQRES 22 B 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR
SEQRES 23 B 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN
SEQRES 24 B 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG
SEQRES 25 B 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS
SEQRES 26 B 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS
SEQRES 27 B 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO
SEQRES 28 B 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER
SEQRES 29 B 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE
HET ZN A 401 1
HET ZN A 402 1
HET NAJ A 403 44
HET PFB A 404 13
HET MRD A 405 8
HET MRD A 406 8
HET ZN B 401 1
HET ZN B 402 1
HET NAJ B 403 44
HET PFB B 404 13
HETNAM ZN ZINC ION
HETNAM NAJ NICOTINAMIDE-ADENINE-DINUCLEOTIDE (ACIDIC FORM)
HETNAM PFB 2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 NAJ 2(C21 H27 N7 O14 P2)
FORMUL 6 PFB 2(C7 H3 F5 O)
FORMUL 7 MRD 2(C6 H14 O2)
FORMUL 13 HOH *835(H2 O)
HELIX 1 AA1 CYS A 46 GLY A 55 1 10
HELIX 2 AA2 CYS A 100 HIS A 105 1 6
HELIX 3 AA3 PRO A 165 CYS A 170 1 6
HELIX 4 AA4 LEU A 171 GLY A 173 5 3
HELIX 5 AA5 CYS A 174 LYS A 185 1 12
HELIX 6 AA6 GLY A 201 ALA A 214 1 14
HELIX 7 AA7 ASN A 225 ASP A 227 5 3
HELIX 8 AA8 LYS A 228 GLY A 236 1 9
HELIX 9 AA9 ASN A 242 TYR A 246 5 5
HELIX 10 AB1 PRO A 249 SER A 258 1 10
HELIX 11 AB2 ARG A 271 CYS A 282 1 12
HELIX 12 AB3 PRO A 305 SER A 310 1 6
HELIX 13 AB4 ILE A 318 PHE A 322 5 5
HELIX 14 AB5 LYS A 323 ALA A 337 1 15
HELIX 15 AB6 LEU A 342 PRO A 344 5 3
HELIX 16 AB7 LYS A 354 SER A 364 1 11
HELIX 17 AB8 CYS B 46 GLY B 55 1 10
HELIX 18 AB9 CYS B 100 HIS B 105 1 6
HELIX 19 AC1 PRO B 165 CYS B 170 1 6
HELIX 20 AC2 LEU B 171 GLY B 173 5 3
HELIX 21 AC3 CYS B 174 LYS B 185 1 12
HELIX 22 AC4 GLY B 201 ALA B 214 1 14
HELIX 23 AC5 ASN B 225 ASP B 227 5 3
HELIX 24 AC6 LYS B 228 GLY B 236 1 9
HELIX 25 AC7 ASN B 242 TYR B 246 5 5
HELIX 26 AC8 PRO B 249 SER B 258 1 10
HELIX 27 AC9 ARG B 271 CYS B 282 1 12
HELIX 28 AD1 PRO B 305 SER B 310 1 6
HELIX 29 AD2 ILE B 318 PHE B 322 5 5
HELIX 30 AD3 LYS B 323 ALA B 337 1 15
HELIX 31 AD4 LEU B 342 PRO B 344 5 3
HELIX 32 AD5 LYS B 354 SER B 364 1 11
SHEET 1 AA1 4 ILE A 7 VAL A 13 0
SHEET 2 AA1 4 SER A 22 VAL A 28 -1 O VAL A 28 N ILE A 7
SHEET 3 AA1 4 PHE A 130 CYS A 132 -1 O THR A 131 N GLU A 27
SHEET 4 AA1 4 LYS A 135 ILE A 137 -1 O LYS A 135 N CYS A 132
SHEET 1 AA2 5 TYR A 149 ASP A 153 0
SHEET 2 AA2 5 GLU A 35 GLY A 44 -1 N ILE A 38 O THR A 150
SHEET 3 AA2 5 GLU A 68 ILE A 76 -1 O ILE A 72 N LYS A 39
SHEET 4 AA2 5 LYS A 88 PRO A 91 -1 O VAL A 89 N GLY A 71
SHEET 5 AA2 5 VAL A 157 LYS A 159 -1 O ALA A 158 N ILE A 90
SHEET 1 AA3 4 TYR A 149 ASP A 153 0
SHEET 2 AA3 4 GLU A 35 GLY A 44 -1 N ILE A 38 O THR A 150
SHEET 3 AA3 4 ARG A 369 THR A 373 -1 O LEU A 372 N THR A 43
SHEET 4 AA3 4 ILE A 346 PRO A 351 1 N LEU A 350 O ILE A 371
SHEET 1 AA412 GLU A 239 VAL A 241 0
SHEET 2 AA412 ARG A 218 VAL A 222 1 N GLY A 221 O VAL A 241
SHEET 3 AA412 THR A 194 PHE A 198 1 N CYS A 195 O VAL A 220
SHEET 4 AA412 PHE A 264 GLU A 267 1 O PHE A 266 N PHE A 198
SHEET 5 AA412 VAL A 288 ILE A 291 1 O VAL A 290 N SER A 265
SHEET 6 AA412 THR A 313 GLY A 316 1 O LYS A 315 N ILE A 291
SHEET 7 AA412 THR B 313 GLY B 316 -1 O TRP B 314 N TRP A 314
SHEET 8 AA412 VAL B 288 ILE B 291 1 N ILE B 291 O LYS B 315
SHEET 9 AA412 PHE B 264 GLU B 267 1 N SER B 265 O VAL B 290
SHEET 10 AA412 THR B 194 PHE B 198 1 N PHE B 198 O PHE B 266
SHEET 11 AA412 ARG B 218 VAL B 222 1 O VAL B 220 N CYS B 195
SHEET 12 AA412 GLU B 239 VAL B 241 1 O VAL B 241 N GLY B 221
SHEET 1 AA5 2 LEU A 301 MET A 303 0
SHEET 2 AA5 2 LEU B 301 MET B 303 -1 O MET B 303 N LEU A 301
SHEET 1 AA6 4 ILE B 7 VAL B 13 0
SHEET 2 AA6 4 SER B 22 VAL B 28 -1 O SER B 22 N VAL B 13
SHEET 3 AA6 4 PHE B 130 CYS B 132 -1 O THR B 131 N GLU B 27
SHEET 4 AA6 4 LYS B 135 ILE B 137 -1 O LYS B 135 N CYS B 132
SHEET 1 AA7 5 TYR B 149 ASP B 153 0
SHEET 2 AA7 5 GLU B 35 GLY B 44 -1 N ILE B 38 O THR B 150
SHEET 3 AA7 5 ALA B 69 ILE B 76 -1 O ILE B 72 N LYS B 39
SHEET 4 AA7 5 LYS B 88 PRO B 91 -1 O VAL B 89 N GLY B 71
SHEET 5 AA7 5 VAL B 157 LYS B 159 -1 O ALA B 158 N ILE B 90
SHEET 1 AA8 4 TYR B 149 ASP B 153 0
SHEET 2 AA8 4 GLU B 35 GLY B 44 -1 N ILE B 38 O THR B 150
SHEET 3 AA8 4 ARG B 369 THR B 373 -1 O LEU B 372 N THR B 43
SHEET 4 AA8 4 ILE B 346 PRO B 351 1 N LEU B 350 O THR B 373
LINK SG CYS A 46 ZN ZN A 401 1555 1555 2.30
LINK NE2 HIS A 67 ZN ZN A 401 1555 1555 2.09
LINK SG CYS A 97 ZN ZN A 402 1555 1555 2.32
LINK SG CYS A 100 ZN ZN A 402 1555 1555 2.33
LINK SG CYS A 103 ZN ZN A 402 1555 1555 2.36
LINK SG CYS A 111 ZN ZN A 402 1555 1555 2.34
LINK SG CYS A 174 ZN ZN A 401 1555 1555 2.30
LINK ZN ZN A 401 O1 PFB A 404 1555 1555 1.99
LINK SG CYS B 46 ZN ZN B 401 1555 1555 2.31
LINK NE2 HIS B 67 ZN ZN B 401 1555 1555 2.16
LINK SG CYS B 97 ZN ZN B 402 1555 1555 2.38
LINK SG CYS B 100 ZN ZN B 402 1555 1555 2.36
LINK SG CYS B 103 ZN ZN B 402 1555 1555 2.34
LINK SG CYS B 111 ZN ZN B 402 1555 1555 2.30
LINK SG CYS B 174 ZN ZN B 401 1555 1555 2.29
LINK ZN ZN B 401 O1 PFB B 404 1555 1555 2.00
CISPEP 1 LEU A 61 PRO A 62 0 -1.14
CISPEP 2 LEU B 61 PRO B 62 0 -0.49
SITE 1 AC1 5 CYS A 46 HIS A 67 CYS A 174 NAJ A 403
SITE 2 AC1 5 PFB A 404
SITE 1 AC2 4 CYS A 97 CYS A 100 CYS A 103 CYS A 111
SITE 1 AC3 32 ARG A 47 SER A 48 HIS A 51 CYS A 174
SITE 2 AC3 32 THR A 178 GLY A 199 GLY A 201 GLY A 202
SITE 3 AC3 32 VAL A 203 ASP A 223 ILE A 224 LYS A 228
SITE 4 AC3 32 VAL A 268 ILE A 269 VAL A 292 GLY A 293
SITE 5 AC3 32 VAL A 294 ALA A 317 ILE A 318 PHE A 319
SITE 6 AC3 32 ARG A 369 ZN A 401 PFB A 404 HOH A 543
SITE 7 AC3 32 HOH A 584 HOH A 590 HOH A 597 HOH A 653
SITE 8 AC3 32 HOH A 689 HOH A 765 HOH A 786 HOH A 794
SITE 1 AC4 13 CYS A 46 SER A 48 LEU A 57 HIS A 67
SITE 2 AC4 13 PHE A 93 LEU A 116 PHE A 140 LEU A 141
SITE 3 AC4 13 CYS A 174 VAL A 294 ZN A 401 NAJ A 403
SITE 4 AC4 13 LEU B 309
SITE 1 AC5 8 ASP A 297 GLN A 299 LYS A 338 PHE A 340
SITE 2 AC5 8 HOH A 503 HOH A 556 HOH A 570 HOH A 658
SITE 1 AC6 6 ARG A 218 THR A 238 GLU A 239 HOH A 515
SITE 2 AC6 6 GLU B 239 HOH B 504
SITE 1 AC7 5 CYS B 46 HIS B 67 CYS B 174 NAJ B 403
SITE 2 AC7 5 PFB B 404
SITE 1 AC8 4 CYS B 97 CYS B 100 CYS B 103 CYS B 111
SITE 1 AC9 32 ARG B 47 SER B 48 HIS B 51 CYS B 174
SITE 2 AC9 32 THR B 178 GLY B 199 GLY B 201 GLY B 202
SITE 3 AC9 32 VAL B 203 ASP B 223 ILE B 224 LYS B 228
SITE 4 AC9 32 VAL B 268 ILE B 269 VAL B 292 GLY B 293
SITE 5 AC9 32 VAL B 294 ALA B 317 ILE B 318 PHE B 319
SITE 6 AC9 32 LEU B 362 ARG B 369 ZN B 401 PFB B 404
SITE 7 AC9 32 HOH B 502 HOH B 563 HOH B 589 HOH B 602
SITE 8 AC9 32 HOH B 605 HOH B 734 HOH B 756 HOH B 770
SITE 1 AD1 14 LEU A 309 CYS B 46 SER B 48 LEU B 57
SITE 2 AD1 14 HIS B 67 PHE B 93 LEU B 116 PHE B 140
SITE 3 AD1 14 LEU B 141 CYS B 174 VAL B 294 ILE B 318
SITE 4 AD1 14 ZN B 401 NAJ B 403
CRYST1 44.300 51.500 92.350 91.92 103.09 110.17 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 0.022573 0.008292 0.006308 0.00000
SCALE2 0.000000 0.020686 0.002544 0.00000
SCALE3 0.000000 0.000000 0.011201 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
