HEADER OXIDOREDUCTASE 17-JUN-16 5KJ1
TITLE G173A 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: G173A SUBSTITUTION
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: XL-1BLUE
KEYWDS OXIDOREDUCTASE INHIBITOR COMPLEX ROSSMANN FOLD DYNAMICS,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.V.PLAPP
REVDAT 8 18-OCT-23 5KJ1 1 REMARK
REVDAT 7 12-OCT-22 5KJ1 1 JRNL
REVDAT 6 27-APR-22 5KJ1 1 LINK
REVDAT 5 25-DEC-19 5KJ1 1 REMARK
REVDAT 4 28-FEB-18 5KJ1 1 JRNL
REVDAT 3 03-JAN-18 5KJ1 1 JRNL
REVDAT 2 27-SEP-17 5KJ1 1 REMARK
REVDAT 1 06-JUL-16 5KJ1 0
JRNL AUTH B.V.PLAPP,L.GAKHAR,R.SUBRAMANIAN
JRNL TITL DEPENDENCE OF CRYSTALLOGRAPHIC ATOMIC DISPLACEMENT
JRNL TITL 2 PARAMETERS ON TEMPERATURE (25-150 K) FOR COMPLEXES OF HORSE
JRNL TITL 3 LIVER ALCOHOL DEHYDROGENASE.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 78 1221 2022
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 36189742
JRNL DOI 10.1107/S2059798322008361
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.K.SHANMUGANATHAM,R.S.WALLACE,A.TING-I LEE,B.V.PLAPP
REMARK 1 TITL CONTRIBUTION OF BURIED DISTAL AMINO ACID RESIDUES IN HORSE
REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE TO STRUCTURE AND CATALYSIS.
REMARK 1 REF PROTEIN SCI. V. 27 750 2018
REMARK 1 REFN ESSN 1469-896X
REMARK 1 PMID 29271062
REMARK 1 DOI 10.1002/PRO.3370
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 218364
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) : 0.124
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1099
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15362
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 150
REMARK 3 SOLVENT ATOMS : 1016
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : 0.57000
REMARK 3 B33 (A**2) : -0.88000
REMARK 3 B12 (A**2) : -0.35000
REMARK 3 B13 (A**2) : 0.33000
REMARK 3 B23 (A**2) : 0.11000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.440
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6085 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6020 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8260 ; 1.966 ; 2.020
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13992 ; 1.078 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 772 ; 6.424 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;36.925 ;24.739
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1114 ;11.659 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;13.674 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 976 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6568 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1194 ; 0.003 ; 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): 3034 ; 1.284 ; 1.362
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3033 ; 1.283 ; 1.362
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3799 ; 1.509 ; 2.052
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3800 ; 1.510 ; 2.052
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3051 ; 2.071 ; 1.648
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3052 ; 2.073 ; 1.649
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4452 ; 2.326 ; 2.364
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7897 ; 3.674 ;21.177
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7134 ; 2.815 ;18.430
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 12103 ; 3.327 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 213 ;30.732 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 12801 ; 8.439 ; 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 : 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 5KJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 85
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : ROSENBAUM ROCK VERTICAL FOCUSING
REMARK 200 MIRROR WITH PT, GLASS, PD LANES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
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 (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.950
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.87
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: BLOCK
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM N-[TRIS(HYDROXYMETHYL)
REMARK 280 METHYL]-2-AMINOETHANE SULFONATE, PH 6.7 (AT 25 C), 0.25 MM EDTA,
REMARK 280 10 MG/ML PROTEIN, 1 MM NAD+, 10 MM 2,3,4,5,6-PENTAFLUOROBENZYL
REMARK 280 ALCOHOL, 12 TO 25 % 2-METHYL-2,4-PENTANEDIOL, PH 7.0,
REMARK 280 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: 7750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 164 CA SER A 164 CB 0.118
REMARK 500 SER A 164 CB SER A 164 OG -0.093
REMARK 500 SER B 164 CA SER B 164 CB 0.113
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 369 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP B 161 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 273 CB - CG - OD1 ANGL. DEV. = 5.4 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 CYS A 174 -75.25 -150.96
REMARK 500 ILE A 269 -60.57 -125.01
REMARK 500 ILE A 368 -82.16 -101.78
REMARK 500 HIS B 67 -0.73 -145.53
REMARK 500 THR B 143 -60.92 -122.92
REMARK 500 CYS B 174 -74.50 -153.16
REMARK 500 ILE B 269 -63.43 -126.76
REMARK 500 ILE B 368 -89.48 -98.24
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 468 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 782 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH B 724 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 765 DISTANCE = 6.15 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 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 67 NE2 107.3
REMARK 620 3 CYS A 174 SG 123.4 111.6
REMARK 620 4 PFB A 378 O1 103.3 102.4 106.5
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 108.7
REMARK 620 3 CYS A 103 SG 115.9 105.5
REMARK 620 4 CYS A 111 SG 103.4 119.8 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 46 SG
REMARK 620 2 HIS B 67 NE2 107.1
REMARK 620 3 CYS B 174 SG 123.4 112.3
REMARK 620 4 PFB B 378 O1 104.4 102.9 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 97 SG
REMARK 620 2 CYS B 100 SG 109.1
REMARK 620 3 CYS B 103 SG 115.3 106.1
REMARK 620 4 CYS B 111 SG 103.7 119.6 103.3
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 NAJ A 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PFB A 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAJ B 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PFB B 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD B 379
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DWV RELATED DB: PDB
REMARK 900 WILD-TYPE ENZYME
REMARK 900 RELATED ID: 5KCP RELATED DB: PDB
REMARK 900 RELATED ID: 5KCZ RELATED DB: PDB
REMARK 900 RELATED ID: 5KJ6 RELATED DB: PDB
REMARK 900 RELATED ID: 5KJC RELATED DB: PDB
REMARK 900 RELATED ID: 5KJE RELATED DB: PDB
REMARK 900 RELATED ID: 5KJF RELATED DB: PDB
DBREF 5KJ1 A 1 374 UNP P00327 ADH1E_HORSE 2 375
DBREF 5KJ1 B 1 374 UNP P00327 ADH1E_HORSE 2 375
SEQADV 5KJ1 ALA A 173 UNP P00327 GLY 174 ENGINEERED MUTATION
SEQADV 5KJ1 ALA B 173 UNP P00327 GLY 174 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 ALA 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
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 ALA 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 ILE 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 375 1
HET ZN A 376 1
HET NAJ A 377 44
HET PFB A 378 13
HET MRD A 379 8
HET MRD A 380 8
HET MRD A 381 8
HET ZN B 375 1
HET ZN B 376 1
HET NAJ B 377 44
HET PFB B 378 13
HET MRD B 379 8
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 4(C6 H14 O2)
FORMUL 15 HOH *1016(H2 O)
HELIX 1 AA1 CYS A 46 SER A 54 1 9
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 ALA 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 VAL A 235 1 8
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 SER B 54 1 9
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 ALA 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 VAL B 235 1 8
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 ALA A 69 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 ILE 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 ILE 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 LEU B 301 N MET A 303
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 ACYS A 46 ZN ZN A 375 1555 1555 2.34
LINK NE2 HIS A 67 ZN ZN A 375 1555 1555 2.04
LINK SG CYS A 97 ZN ZN A 376 1555 1555 2.34
LINK SG CYS A 100 ZN ZN A 376 1555 1555 2.34
LINK SG CYS A 103 ZN ZN A 376 1555 1555 2.36
LINK SG CYS A 111 ZN ZN A 376 1555 1555 2.33
LINK SG CYS A 174 ZN ZN A 375 1555 1555 2.29
LINK ZN ZN A 375 O1 PFB A 378 1555 1555 1.91
LINK SG CYS B 46 ZN ZN B 375 1555 1555 2.33
LINK NE2 HIS B 67 ZN ZN B 375 1555 1555 2.03
LINK SG CYS B 97 ZN ZN B 376 1555 1555 2.34
LINK SG CYS B 100 ZN ZN B 376 1555 1555 2.34
LINK SG CYS B 103 ZN ZN B 376 1555 1555 2.36
LINK SG CYS B 111 ZN ZN B 376 1555 1555 2.33
LINK SG CYS B 174 ZN ZN B 375 1555 1555 2.29
LINK ZN ZN B 375 O1 PFB B 378 1555 1555 1.93
CISPEP 1 LEU A 61 PRO A 62 0 -2.39
CISPEP 2 LEU B 61 PRO B 62 0 -2.07
SITE 1 AC1 5 CYS A 46 HIS A 67 CYS A 174 NAJ A 377
SITE 2 AC1 5 PFB A 378
SITE 1 AC2 4 CYS A 97 CYS A 100 CYS A 103 CYS A 111
SITE 1 AC3 33 ARG A 47 SER A 48 HIS A 51 CYS A 174
SITE 2 AC3 33 THR A 178 GLY A 199 GLY A 201 GLY A 202
SITE 3 AC3 33 VAL A 203 ASP A 223 ILE A 224 LYS A 228
SITE 4 AC3 33 VAL A 268 ILE A 269 ARG A 271 VAL A 292
SITE 5 AC3 33 GLY A 293 VAL A 294 ALA A 317 ILE A 318
SITE 6 AC3 33 PHE A 319 ARG A 369 ZN A 375 PFB A 378
SITE 7 AC3 33 HOH A 406 HOH A 430 HOH A 439 HOH A 588
SITE 8 AC3 33 HOH A 647 HOH A 664 HOH A 686 HOH A 711
SITE 9 AC3 33 HOH A 902
SITE 1 AC4 14 CYS A 46 SER A 48 LEU A 57 HIS A 67
SITE 2 AC4 14 PHE A 93 LEU A 116 PHE A 140 LEU A 141
SITE 3 AC4 14 CYS A 174 VAL A 294 ILE A 318 ZN A 375
SITE 4 AC4 14 NAJ A 377 LEU B 309
SITE 1 AC5 9 ASP A 297 GLN A 299 LYS A 338 LYS A 339
SITE 2 AC5 9 PHE A 340 HOH A 735 HOH A 752 HOH A 762
SITE 3 AC5 9 HOH A 814
SITE 1 AC6 5 GLU A 239 HOH A 998 ARG B 218 GLU B 239
SITE 2 AC6 5 HOH B 930
SITE 1 AC7 6 LYS A 168 ASP A 343 ILE A 346 THR A 347
SITE 2 AC7 6 HOH A 840 HOH A 852
SITE 1 AC8 5 CYS B 46 HIS B 67 CYS B 174 NAJ B 377
SITE 2 AC8 5 PFB B 378
SITE 1 AC9 4 CYS B 97 CYS B 100 CYS B 103 CYS B 111
SITE 1 AD1 35 ARG B 47 SER B 48 HIS B 51 CYS B 174
SITE 2 AD1 35 THR B 178 GLY B 199 GLY B 201 GLY B 202
SITE 3 AD1 35 VAL B 203 ASP B 223 ILE B 224 LYS B 228
SITE 4 AD1 35 VAL B 268 ILE B 269 ARG B 271 VAL B 292
SITE 5 AD1 35 GLY B 293 VAL B 294 ALA B 317 ILE B 318
SITE 6 AD1 35 PHE B 319 LEU B 362 ARG B 369 ZN B 375
SITE 7 AD1 35 PFB B 378 HOH B 403 HOH B 443 HOH B 449
SITE 8 AD1 35 HOH B 514 HOH B 574 HOH B 649 HOH B 664
SITE 9 AD1 35 HOH B 689 HOH B 879 HOH B 907
SITE 1 AD2 14 LEU A 309 CYS B 46 SER B 48 LEU B 57
SITE 2 AD2 14 HIS B 67 PHE B 93 LEU B 116 PHE B 140
SITE 3 AD2 14 LEU B 141 CYS B 174 VAL B 294 ILE B 318
SITE 4 AD2 14 ZN B 375 NAJ B 377
SITE 1 AD3 1 LYS B 338
CRYST1 44.310 51.500 92.420 91.82 103.05 110.12 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 0.022568 0.008268 0.006265 0.00000
SCALE2 0.000000 0.020679 0.002492 0.00000
SCALE3 0.000000 0.000000 0.011187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
