HEADER OXIDOREDUCTASE 26-NOV-00 1HEU
TITLE ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING
TITLE 2 CADMIUM AND A HYDROXIDE ADDUCT TO NADH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE E CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALCOHOL DEHYDROGENASE I;
COMPND 5 EC: 1.1.1.1;
COMPND 6 OTHER_DETAILS: ADDUCT BETWEEN NC6 OF NADH AND ZINC BOUND HYDROXIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: DOMESTIC HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 ORGAN: LIVER
KEYWDS OXIDOREDUCTASE, OXIDOREDUCTASE(NAD(A)-CHOH(D))
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MEIJERS,R.J.MORRIS,H.W.ADOLPH,A.MERLI,V.S.LAMZIN,E.S.CEDERGEN-
AUTHOR 2 ZEPPEZAUER
REVDAT 6 13-DEC-23 1HEU 1 REMARK LINK
REVDAT 5 24-JUL-19 1HEU 1 REMARK
REVDAT 4 24-FEB-09 1HEU 1 VERSN
REVDAT 3 11-OCT-06 1HEU 1 REMARK ATOM ANISOU
REVDAT 2 16-AUG-01 1HEU 1 HETATM ANISOU
REVDAT 1 31-MAY-01 1HEU 0
JRNL AUTH R.MEIJERS,R.J.MORRIS,H.W.ADOLPH,A.MERLI,V.S.LAMZIN,
JRNL AUTH 2 E.S.CEDERGEN-ZEPPEZAUER
JRNL TITL ON THE ENZYMATIC ACTIVATION OF NADH
JRNL REF J.BIOL.CHEM. V. 276 9316 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11134046
JRNL DOI 10.1074/JBC.M010870200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.RAMASWAMY,D.H.PARK,B.V.PLAPP
REMARK 1 TITL SUBSTITUTIONS IN A 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 PMID 10529241
REMARK 1 DOI 10.1021/BI991731I
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.W.ADOLPH,M.KIEFER,E.S.CEDERGREN-ZEPPEZAUER
REMARK 1 TITL ELECTROSTATIC EFFECTS IN THE KINETICS OF COENZYME BINDING TO
REMARK 1 TITL 2 ISOZYMES OF ALCOHOL DEHYDROGENASE FROM HORSE LIVER
REMARK 1 REF BIOCHEMISTRY V. 36 8743 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9220961
REMARK 1 DOI 10.1021/BI970398K
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.AL-KARADAGHI,E.S.CEDERGREN-ZEPPEZAUER,K.PETRATOS,
REMARK 1 AUTH 2 S.HOVMOELLER,H.TERRY,Z.DAUTER,K.S.WILSON
REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF LIVER
REMARK 1 TITL 2 DERESOLUTIONHYDROGENASE-NADH COMPLEX AT 1.8 ANGSTROM ALCOHOL
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 793 1994
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 15299346
REMARK 1 DOI 10.1107/S0907444994005263
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.SCHNEIDER,H.EKLUND,E.CEDERGREN-ZEPPEZAUER,M.ZEPPEZAUER
REMARK 1 TITL CRYSTAL STRUCTURES OF THE ACTIVE SITE INSPECIFICALLY
REMARK 1 TITL 2 METAL-DEPLETED AND COBALT-SUBSTITUTED HORSE LIVER ALCOHOL
REMARK 1 TITL 3 DEHYDROGENASE DERIVATIVES
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 80 5289 1983
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 6351056
REMARK 1 DOI 10.1073/PNAS.80.17.5289
REMARK 1 REFERENCE 5
REMARK 1 AUTH E.CEDERGREN-ZEPPEZAUER
REMARK 1 TITL CRYSTAL-STRUCTURE DETERMINATION OF REDUCNICOTINAMIDE ADENINE
REMARK 1 TITL 2 DINUCLEOTIDE COMPLEX WITH HORSE LIVER ALCOHOL DEHYDROGENASE
REMARK 1 TITL 3 MAINTAINED IN ITS APO CONFORMATION BY ZINC-BOUND IMIDAZOLEED
REMARK 1 REF BIOCHEMISTRY V. 22 5761 1983
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 6362718
REMARK 1 DOI 10.1021/BI00294A013
REMARK 2
REMARK 2 RESOLUTION. 1.15 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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 254817
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) : 0.119
REMARK 3 R VALUE (WORKING SET) : 0.118
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.300
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 : 5570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 1297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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): 0.030
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) : 0.016 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.025 ; 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 1HEU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 8.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.927
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH X-RAY RESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 254817
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 2OHX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.20
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 300 REMARK: BIOLOGICAL_UNIT: DIMERIC
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 400
REMARK 400 COMPOUND
REMARK 400 ALCOHOL + NAD(+) = ALDEHYDE OR KETONE + NADH.
REMARK 400 REQUIRES ZINC FOR ITS ACTIVITY.
REMARK 400 DIMER OF IDENTICAL OR NONIDENTICAL CHAINS OF TWO TYPES
REMARK 400 (E AND S) CODED BY 2 SEPARATE GENES AT DIFFERENT LOCI.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 248 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 256 O HOH A 2522 1.87
REMARK 500 OE1 GLU A 256 O HOH A 2525 2.01
REMARK 500 O HOH A 2584 O HOH A 2586 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 116 CA LEU A 116 CB 0.345
REMARK 500 LEU A 116 CA LEU A 116 CB -0.267
REMARK 500 GLU A 256 CA GLU A 256 CB 0.210
REMARK 500 GLU A 256 CG GLU A 256 CD -0.197
REMARK 500 GLU A 256 CD GLU A 256 OE1 0.117
REMARK 500 GLU A 256 CD GLU A 256 OE2 0.103
REMARK 500 LYS B 247 CA LYS B 247 CB 0.151
REMARK 500 GLU B 256 CA GLU B 256 CB 0.272
REMARK 500 GLU B 256 CB GLU B 256 CG -0.214
REMARK 500 GLU B 256 CG GLU B 256 CD 0.306
REMARK 500 GLU B 256 CD GLU B 256 OE1 0.130
REMARK 500 GLU B 256 CD GLU B 256 OE2 0.278
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 101 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU A 116 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 LEU A 116 N - CA - CB ANGL. DEV. = -14.8 DEGREES
REMARK 500 LEU A 116 N - CA - CB ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG A 120 CA - CB - CG ANGL. DEV. = 22.4 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 THR A 131 N - CA - CB ANGL. DEV. = 14.1 DEGREES
REMARK 500 PHE A 146 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 GLU A 256 OE1 - CD - OE2 ANGL. DEV. = -21.8 DEGREES
REMARK 500 LYS A 315 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG A 369 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 MET B 40 CG - SD - CE ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG B 84 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 101 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 120 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 THR B 131 N - CA - CB ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLU B 239 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 LYS B 247 CB - CA - C ANGL. DEV. = -20.5 DEGREES
REMARK 500 LYS B 247 CB - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 GLU B 256 CA - CB - CG ANGL. DEV. = -15.9 DEGREES
REMARK 500 GLU B 256 CB - CG - CD ANGL. DEV. = -18.8 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 -5.15 -146.21
REMARK 500 THR A 143 -58.03 -120.07
REMARK 500 CYS A 174 -77.55 -157.74
REMARK 500 ILE A 269 -63.29 -123.17
REMARK 500 ILE A 368 -84.70 -102.49
REMARK 500 HIS B 67 -5.16 -145.29
REMARK 500 THR B 143 -63.87 -123.59
REMARK 500 SER B 144 72.39 52.17
REMARK 500 CYS B 174 -78.40 -155.66
REMARK 500 ILE B 269 -63.37 -123.76
REMARK 500 ILE B 368 -88.25 -102.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU B 256 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR B 82 13.65
REMARK 500 GLU B 107 -10.15
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 A2016 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A2025 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A2031 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A2047 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A2087 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A2163 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2236 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B2012 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B2027 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B2107 DISTANCE = 6.02 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 CD A 400 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 67 NE2 105.2
REMARK 620 3 CYS A 174 SG 143.1 107.9
REMARK 620 4 HOH A2177 O 107.8 73.8 96.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 401 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 100 SG 109.9
REMARK 620 3 CYS A 103 SG 115.4 105.7
REMARK 620 4 CYS A 111 SG 102.9 120.1 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 400 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 46 SG
REMARK 620 2 HIS B 67 NE2 106.0
REMARK 620 3 CYS B 174 SG 139.9 108.8
REMARK 620 4 HOH B2616 O 110.9 73.3 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 401 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 97 SG
REMARK 620 2 CYS B 100 SG 110.6
REMARK 620 3 CYS B 103 SG 114.1 105.0
REMARK 620 4 CYS B 111 SG 104.9 119.4 103.0
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HET RELATED DB: PDB
REMARK 900 ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A
REMARK 900 HYDROXIDE ADDUCT TO NADH
REMARK 900 RELATED ID: 1A71 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER
REMARK 900 ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND
REMARK 900 TRIFLUOROETHANOL
REMARK 900 RELATED ID: 1A72 RELATED DB: PDB
REMARK 900 AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE
REMARK 900 LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD
REMARK 900 ANALOG CPAD
REMARK 900 RELATED ID: 1AXE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP OF HORSE
REMARK 900 LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD AND INHIBITOR
REMARK 900 TRIFLUOROETHANOL
REMARK 900 RELATED ID: 1AXG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL
REMARK 900 DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR
REMARK 900 TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 1BTO RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND (1S,3R)3-
REMARK 900 BUTYLTHIOLANE 1-OXIDE
REMARK 900 RELATED ID: 1LDE RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL
REMARK 900 PIPERDINE
REMARK 900 RELATED ID: 1LDY RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND CYCLOHEXYL
REMARK 900 FORMAMIDE (CXF)
REMARK 900 RELATED ID: 1QLH RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF
REMARK 900 GLY 293 ALA AND PRO 295 THR
REMARK 900 RELATED ID: 1QLJ RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE APO ENZYME DOUBLE MUTANT OF GLY
REMARK 900 293 ALA AND PRO 295 THR
REMARK 900 RELATED ID: 3BTO RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND (1S,3S)3-
REMARK 900 BUTYLTHIOLANE 1-OXIDE
DBREF 1HEU A 1 374 UNP P00327 ADHE_HORSE 1 374
DBREF 1HEU B 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
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 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 CD A 400 1
HET CD A 401 1
HET NAD A 402 54
HET MRD A 403 8
HET CD B 400 1
HET CD B 401 1
HET NAD B 402 54
HET MRD B 403 8
HETNAM CD CADMIUM ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 3 CD 4(CD 2+)
FORMUL 5 NAD 2(C21 H27 N7 O14 P2)
FORMUL 6 MRD 2(C6 H14 O2)
FORMUL 11 HOH *1297(H2 O)
HELIX 1 H1A CYS A 46 THR A 56 1 11
HELIX 2 H2A PRO A 165 PHE A 176 1 12
HELIX 3 HAA SER A 177 VAL A 189 1 13
HELIX 4 HBA GLY A 201 ALA A 216 1 16
HELIX 5 HCA ASN A 225 ALA A 237 1 13
HELIX 6 HDA PRO A 249 GLY A 260 1 12
HELIX 7 HEA ARG A 271 CYS A 282 1 12
HELIX 8 S5A ASN A 304 GLY A 311 5 8
HELIX 9 H3A LYS A 323 LYS A 338 1 16
HELIX 10 H4A LYS A 354 GLY A 365 1 12
HELIX 11 H1B CYS B 46 THR B 56 1 11
HELIX 12 H2B PRO B 165 PHE B 176 1 12
HELIX 13 HAB SER B 177 VAL B 189 1 13
HELIX 14 HBB GLY B 201 ALA B 216 1 16
HELIX 15 HCB ASN B 225 ALA B 237 1 13
HELIX 16 HDB PRO B 249 GLY B 260 1 12
HELIX 17 HEB ARG B 271 CYS B 282 1 12
HELIX 18 S5B ASN B 304 GLY B 311 5 8
HELIX 19 H3B LYS B 323 LYS B 338 1 16
HELIX 20 H4B LYS B 354 GLY B 365 1 12
SHEET 1 S1A 4 GLU A 68 ALA A 70 0
SHEET 2 S1A 4 VAL A 41 ILE A 45 -1 N ALA A 42 O ALA A 70
SHEET 3 S1A 4 ARG A 369 PHE A 374 -1 N LEU A 372 O THR A 43
SHEET 4 S1A 4 LEU A 345 PHE A 352 1 N LEU A 350 O ILE A 371
SHEET 1 S2A 5 GLN A 148 VAL A 152 0
SHEET 2 S2A 5 GLU A 35 MET A 40 -1 N ILE A 38 O THR A 150
SHEET 3 S2A 5 GLY A 71 GLY A 77 -1 N GLU A 74 O ARG A 37
SHEET 4 S2A 5 GLY A 86 LEU A 92 -1 O ASP A 87 N VAL A 73
SHEET 5 S2A 5 SER A 156 ILE A 160 -1 N ALA A 158 O ILE A 90
SHEET 1 S3A 6 ILE A 7 VAL A 13 0
SHEET 2 S3A 6 SER A 22 ALA A 29 -1 O GLU A 24 N ALA A 11
SHEET 3 S3A 6 ARG A 129 CYS A 132 -1 O THR A 131 N GLU A 27
SHEET 4 S3A 6 LYS A 135 HIS A 138 -1 O LYS A 135 N CYS A 132
SHEET 5 S3A 6 PRO A 62 GLY A 66 1 O PRO A 62 N HIS A 138
SHEET 6 S3A 6 THR A 145 PHE A 146 1 N THR A 145 O GLY A 66
SHEET 1 S4A 6 THR A 238 VAL A 241 0
SHEET 2 S4A 6 GLY A 215 ASP A 223 1 O ILE A 219 N THR A 238
SHEET 3 S4A 6 GLY A 192 GLY A 199 1 O CYS A 195 N ILE A 220
SHEET 4 S4A 6 VAL A 262 VAL A 268 1 O PHE A 264 N ALA A 196
SHEET 5 S4A 6 GLY A 287 GLY A 293 1 O VAL A 290 N GLU A 267
SHEET 6 S4A 6 THR A 313 ALA A 317 1 O THR A 313 N SER A 289
SHEET 1 S1B 4 GLU B 68 ALA B 70 0
SHEET 2 S1B 4 VAL B 41 ILE B 45 -1 N ALA B 42 O ALA B 70
SHEET 3 S1B 4 ARG B 369 PHE B 374 -1 N LEU B 372 O THR B 43
SHEET 4 S1B 4 LEU B 345 PHE B 352 1 N LEU B 350 O ILE B 371
SHEET 1 S2B 5 GLN B 148 VAL B 152 0
SHEET 2 S2B 5 GLU B 35 MET B 40 -1 N ILE B 38 O THR B 150
SHEET 3 S2B 5 GLY B 71 GLY B 77 -1 N GLU B 74 O ARG B 37
SHEET 4 S2B 5 GLY B 86 LEU B 92 -1 O ASP B 87 N VAL B 73
SHEET 5 S2B 5 SER B 156 ILE B 160 -1 N ALA B 158 O ILE B 90
SHEET 1 S3B 6 ILE B 7 VAL B 13 0
SHEET 2 S3B 6 SER B 22 ALA B 29 -1 O GLU B 24 N ALA B 11
SHEET 3 S3B 6 ARG B 129 CYS B 132 -1 O THR B 131 N GLU B 27
SHEET 4 S3B 6 LYS B 135 HIS B 138 -1 O LYS B 135 N CYS B 132
SHEET 5 S3B 6 PRO B 62 GLY B 66 1 O PRO B 62 N HIS B 138
SHEET 6 S3B 6 THR B 145 PHE B 146 1 N THR B 145 O GLY B 66
SHEET 1 S4B 6 THR B 238 VAL B 241 0
SHEET 2 S4B 6 GLY B 215 ASP B 223 1 O ILE B 219 N THR B 238
SHEET 3 S4B 6 GLY B 192 GLY B 199 1 O CYS B 195 N ILE B 220
SHEET 4 S4B 6 VAL B 262 VAL B 268 1 O PHE B 264 N ALA B 196
SHEET 5 S4B 6 GLY B 287 GLY B 293 1 O VAL B 290 N GLU B 267
SHEET 6 S4B 6 THR B 313 ALA B 317 1 O THR B 313 N SER B 289
LINK SG CYS A 46 CD A CD A 400 1555 1555 2.44
LINK NE2 HIS A 67 CD A CD A 400 1555 1555 2.30
LINK SG CYS A 97 CD CD A 401 1555 1555 2.55
LINK SG CYS A 100 CD CD A 401 1555 1555 2.53
LINK SG CYS A 103 CD CD A 401 1555 1555 2.56
LINK SG CYS A 111 CD CD A 401 1555 1555 2.55
LINK SG CYS A 174 CD A CD A 400 1555 1555 2.40
LINK CD A CD A 400 O AHOH A2177 1555 1555 2.73
LINK SG CYS B 46 CD A CD B 400 1555 1555 2.45
LINK NE2 HIS B 67 CD A CD B 400 1555 1555 2.30
LINK SG CYS B 97 CD CD B 401 1555 1555 2.55
LINK SG CYS B 100 CD CD B 401 1555 1555 2.54
LINK SG CYS B 103 CD CD B 401 1555 1555 2.56
LINK SG CYS B 111 CD CD B 401 1555 1555 2.55
LINK SG CYS B 174 CD A CD B 400 1555 1555 2.42
LINK CD A CD B 400 O AHOH B2616 1555 1555 2.82
CISPEP 1 LEU A 61 PRO A 62 0 -6.66
CISPEP 2 LEU B 61 PRO B 62 0 -6.02
SITE 1 AC1 7 CYS A 46 HIS A 67 GLU A 68 CYS A 174
SITE 2 AC1 7 NAD A 402 HOH A2177 HOH A2178
SITE 1 AC2 4 CYS A 97 CYS A 100 CYS A 103 CYS A 111
SITE 1 AC3 6 CYS B 46 HIS B 67 CYS B 174 NAD B 402
SITE 2 AC3 6 HOH B2614 HOH B2616
SITE 1 AC4 4 CYS B 97 CYS B 100 CYS B 103 CYS B 111
SITE 1 AC5 35 ARG A 47 SER A 48 HIS A 51 CYS A 174
SITE 2 AC5 35 THR A 178 GLY A 199 GLY A 201 GLY A 202
SITE 3 AC5 35 VAL A 203 ASP A 223 ILE A 224 LYS A 228
SITE 4 AC5 35 VAL A 268 ILE A 269 ARG A 271 VAL A 292
SITE 5 AC5 35 VAL A 294 ALA A 317 ILE A 318 PHE A 319
SITE 6 AC5 35 ARG A 369 CD A 400 MRD A 403 HOH A2172
SITE 7 AC5 35 HOH A2178 HOH A2479 HOH A2547 HOH A2673
SITE 8 AC5 35 HOH A2674 HOH A2675 HOH A2676 HOH A2677
SITE 9 AC5 35 HOH A2678 HOH A2679 HOH A2680
SITE 1 AC6 33 ARG B 47 SER B 48 HIS B 51 CYS B 174
SITE 2 AC6 33 THR B 178 GLY B 201 GLY B 202 VAL B 203
SITE 3 AC6 33 ASP B 223 ILE B 224 LYS B 228 VAL B 268
SITE 4 AC6 33 ILE B 269 ARG B 271 VAL B 292 VAL B 294
SITE 5 AC6 33 ALA B 317 ILE B 318 PHE B 319 ARG B 369
SITE 6 AC6 33 CD B 400 HOH B2420 HOH B2487 HOH B2605
SITE 7 AC6 33 HOH B2606 HOH B2607 HOH B2608 HOH B2609
SITE 8 AC6 33 HOH B2610 HOH B2611 HOH B2612 HOH B2613
SITE 9 AC6 33 HOH B2614
SITE 1 AC7 7 SER A 48 LEU A 57 LEU A 116 VAL A 294
SITE 2 AC7 7 NAD A 402 HOH A2177 HOH A2681
SITE 1 AC8 5 SER B 48 LEU B 57 VAL B 294 HOH B2615
SITE 2 AC8 5 HOH B2616
CRYST1 51.180 44.570 94.100 104.30 101.07 70.67 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 0.019539 -0.006854 0.002515 0.00000
SCALE2 0.000000 0.023777 0.004805 0.00000
SCALE3 0.000000 0.000000 0.011047 0.00000
MTRIX1 1 0.129250 0.985840 -0.106810 0.39900 1
MTRIX2 1 0.986150 -0.139080 -0.090370 -0.21490 1
MTRIX3 1 -0.103940 -0.093660 -0.990160 0.44230 1
(ATOM LINES ARE NOT SHOWN.)
END
