HEADER OXIDOREDUCTASE 28-JUN-14 4URE
TITLE MOLECULAR GENETIC AND CRYSTAL STRUCTURAL ANALYSIS OF 1-(4-
TITLE 2 HYDROXYPHENYL)-ETHANOL DEHYDROGENASE FROM AROMATOLEUM AROMATICUM EBN1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLOHEXANOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROXYPHENYL-ETHANOL DEHYDROGENASE;
COMPND 5 EC: 1.1.1.311;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AROMATOLEUM AROMATICUM EBN1;
SOURCE 3 ORGANISM_TAXID: 76114;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE, AROMATIC COMPOUNDS,
KEYWDS 2 ANAEROBIC DEGRADATION, ALCOHOL DEHYDROGENASE, MOLECULAR GENETICS,
KEYWDS 3 STEREOCHEMISTRY
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BUESING,H.W.HOEFFKEN,M.BREUER,L.WOEHLBRAND,B.HAUER,R.RABUS
REVDAT 4 10-JAN-24 4URE 1 REMARK HETSYN LINK
REVDAT 3 08-MAY-19 4URE 1 REMARK
REVDAT 2 13-JAN-16 4URE 1 JRNL
REVDAT 1 08-JUL-15 4URE 0
JRNL AUTH I.BUSING,H.W.HOFFKEN,M.BREUER,L.WOHLBRAND,B.HAUER,R.RABUS
JRNL TITL MOLECULAR GENETIC AND CRYSTAL STRUCTURAL ANALYSIS OF
JRNL TITL 2 1-(4-HYDROXYPHENYL)-ETHANOL DEHYDROGENASE FROM 'AROMATOLEUM
JRNL TITL 3 AROMATICUM' EBN1.
JRNL REF J.MOL.MICROBIOL.BIOTECHNOL. V. 25 327 2015
JRNL REFN ISSN 1464-1801
JRNL PMID 26488297
JRNL DOI 10.1159/000439113
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 69759
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) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3672
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3232
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.205
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
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): 3967 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3782 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5414 ; 1.873 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8660 ; 0.941 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.475 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;36.270 ;23.795
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 629 ;13.160 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.892 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 617 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4698 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 928 ; 0.002 ; 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): 2080 ; 3.241 ; 1.763
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2076 ; 3.238 ; 1.764
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2626 ; 3.497 ; 2.652
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1887 ; 4.739 ; 2.124
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 7749 ; 5.153 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 108 ;29.264 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 7941 ;13.080 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4URE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1290061109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73410
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 31.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1IY8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP METHOD IN A BUFFER
REMARK 280 CONTAINING 30% PEG 6000, 0.1 M NA-CACODYLATE (PH 6.5), 0.3 M MG-
REMARK 280 ACETATE, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.75000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.55000
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -196.3 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.11905
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 61.65899
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG A1250 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2053 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2199 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2164 LIES ON A SPECIAL POSITION.
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 O HOH A 2112 O HOH A 2113 1.37
REMARK 500 O HOH A 2059 O HOH A 2063 1.96
REMARK 500 OG SER B 175 O HOH B 2130 2.04
REMARK 500 O HOH B 2083 O HOH B 2084 2.06
REMARK 500 OE1 GLU A 44 O HOH A 2027 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2047 O HOH B 2103 3444 1.50
REMARK 500 OE2 GLU A 199 O HOH A 2148 1545 1.80
REMARK 500 O HOH B 2163 O HOH B 2163 2656 2.01
REMARK 500 O HOH A 2197 O HOH A 2197 2656 2.09
REMARK 500 OG SER A 175 OE2 GLU A 199 1565 2.16
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 GLU A 217 CD GLU A 217 OE1 0.068
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 211 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 78 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 MET B 207 CG - SD - CE ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG B 211 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 211 NE - CZ - NH2 ANGL. DEV. = -6.0 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 ALA A 90 -134.34 -140.61
REMARK 500 SER A 141 -127.70 -90.17
REMARK 500 ALA A 186 -151.21 -87.32
REMARK 500 ALA B 90 -153.49 66.51
REMARK 500 LEU B 115 -65.32 -123.41
REMARK 500 SER B 141 -122.62 -93.98
REMARK 500 GLN B 146 -31.28 -130.10
REMARK 500 ALA B 186 -144.57 -91.96
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 B2171 DISTANCE = 6.10 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 MG A1250 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 248 OXT
REMARK 620 2 ARG A 248 OXT 179.4
REMARK 620 3 HOH A2194 O 94.3 85.7
REMARK 620 4 HOH A2194 O 85.7 94.3 178.6
REMARK 620 5 HOH A2196 O 77.9 101.5 78.5 100.1
REMARK 620 6 HOH A2196 O 101.5 77.9 100.1 78.5 33.6
REMARK 620 7 HOH A2199 O 90.3 90.3 90.7 90.7 163.2 163.2
REMARK 620 8 HOH A2199 O 90.3 90.3 90.7 90.8 163.2 163.2 0.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1251 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 248 OXT
REMARK 620 2 ARG B 248 OXT 172.8
REMARK 620 3 HOH B2160 O 81.1 105.2
REMARK 620 4 HOH B2160 O 83.2 90.0 162.5
REMARK 620 5 HOH B2162 O 95.5 88.6 85.3 104.0
REMARK 620 6 HOH B2162 O 72.6 108.6 105.2 77.2 33.6
REMARK 620 7 HOH B2164 O 81.2 95.3 87.3 82.7 172.3 148.5
REMARK 620 8 HOH B2164 O 81.3 95.3 87.3 82.7 172.3 148.5 0.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PS B 1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1254
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4URF RELATED DB: PDB
REMARK 900 MOLECULAR GENETIC AND CRYSTAL STRUCTURAL ANALYSIS OF 1 -(4-
REMARK 900 HYDROXYPHENYL)-ETHANOL DEHYDROGENASE FROM AROMATOLEUM AROMATICUM
REMARK 900 EBN1
DBREF 4URE A 1 248 UNP Q5P8S7 Q5P8S7_AROAE 1 248
DBREF 4URE B 1 248 UNP Q5P8S7 Q5P8S7_AROAE 1 248
SEQRES 1 A 248 MET LEU LEU GLU GLY LYS THR ALA LEU VAL THR GLY ALA
SEQRES 2 A 248 GLY ASN GLY ILE GLY ARG THR ILE ALA LEU THR TYR ALA
SEQRES 3 A 248 ALA GLU GLY ALA ASN VAL VAL VAL SER ASP ILE SER ASP
SEQRES 4 A 248 GLU TRP GLY ARG GLU THR LEU ALA LEU ILE GLU GLY LYS
SEQRES 5 A 248 GLY GLY LYS ALA VAL PHE GLN HIS ALA ASP THR ALA HIS
SEQRES 6 A 248 PRO GLU ASP HIS ASP GLU LEU ILE ALA ALA ALA LYS ARG
SEQRES 7 A 248 ALA PHE GLY ARG LEU ASP ILE ALA CYS ASN ASN ALA GLY
SEQRES 8 A 248 ILE SER GLY GLU PHE THR PRO THR ALA GLU THR THR ASP
SEQRES 9 A 248 ALA GLN TRP GLN ARG VAL ILE GLY ILE ASN LEU SER GLY
SEQRES 10 A 248 VAL PHE TYR GLY VAL ARG ALA GLN ILE ARG ALA MET LEU
SEQRES 11 A 248 GLU THR GLY GLY GLY ALA ILE VAL ASN ILE SER SER ILE
SEQRES 12 A 248 ALA GLY GLN ILE GLY ILE GLU GLY ILE THR PRO TYR THR
SEQRES 13 A 248 ALA ALA LYS HIS GLY VAL VAL GLY LEU THR LYS THR VAL
SEQRES 14 A 248 ALA TRP GLU TYR GLY SER LYS GLY ILE ARG ILE ASN SER
SEQRES 15 A 248 VAL GLY PRO ALA PHE ILE ASN THR THR LEU VAL GLN ASN
SEQRES 16 A 248 VAL PRO LEU GLU THR ARG ARG GLN LEU GLU GLN MET HIS
SEQRES 17 A 248 ALA LEU ARG ARG LEU GLY GLU THR GLU GLU VAL ALA ASN
SEQRES 18 A 248 LEU VAL ALA TRP LEU SER SER ASP LYS ALA SER PHE VAL
SEQRES 19 A 248 THR GLY SER TYR TYR ALA VAL ASP GLY GLY TYR LEU ALA
SEQRES 20 A 248 ARG
SEQRES 1 B 248 MET LEU LEU GLU GLY LYS THR ALA LEU VAL THR GLY ALA
SEQRES 2 B 248 GLY ASN GLY ILE GLY ARG THR ILE ALA LEU THR TYR ALA
SEQRES 3 B 248 ALA GLU GLY ALA ASN VAL VAL VAL SER ASP ILE SER ASP
SEQRES 4 B 248 GLU TRP GLY ARG GLU THR LEU ALA LEU ILE GLU GLY LYS
SEQRES 5 B 248 GLY GLY LYS ALA VAL PHE GLN HIS ALA ASP THR ALA HIS
SEQRES 6 B 248 PRO GLU ASP HIS ASP GLU LEU ILE ALA ALA ALA LYS ARG
SEQRES 7 B 248 ALA PHE GLY ARG LEU ASP ILE ALA CYS ASN ASN ALA GLY
SEQRES 8 B 248 ILE SER GLY GLU PHE THR PRO THR ALA GLU THR THR ASP
SEQRES 9 B 248 ALA GLN TRP GLN ARG VAL ILE GLY ILE ASN LEU SER GLY
SEQRES 10 B 248 VAL PHE TYR GLY VAL ARG ALA GLN ILE ARG ALA MET LEU
SEQRES 11 B 248 GLU THR GLY GLY GLY ALA ILE VAL ASN ILE SER SER ILE
SEQRES 12 B 248 ALA GLY GLN ILE GLY ILE GLU GLY ILE THR PRO TYR THR
SEQRES 13 B 248 ALA ALA LYS HIS GLY VAL VAL GLY LEU THR LYS THR VAL
SEQRES 14 B 248 ALA TRP GLU TYR GLY SER LYS GLY ILE ARG ILE ASN SER
SEQRES 15 B 248 VAL GLY PRO ALA PHE ILE ASN THR THR LEU VAL GLN ASN
SEQRES 16 B 248 VAL PRO LEU GLU THR ARG ARG GLN LEU GLU GLN MET HIS
SEQRES 17 B 248 ALA LEU ARG ARG LEU GLY GLU THR GLU GLU VAL ALA ASN
SEQRES 18 B 248 LEU VAL ALA TRP LEU SER SER ASP LYS ALA SER PHE VAL
SEQRES 19 B 248 THR GLY SER TYR TYR ALA VAL ASP GLY GLY TYR LEU ALA
SEQRES 20 B 248 ARG
HET SO4 A1249 5
HET MG A1250 1
HET SO4 B1249 5
HET 1PS B1250 13
HET MG B1251 1
HET ACT B1252 4
HET ACT B1253 4
HET ACT B1254 4
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM 1PS 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE
HETNAM ACT ACETATE ION
HETSYN 1PS 1-(3-SULFOPROPYL) PYRIDINIUM; PPS
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 MG 2(MG 2+)
FORMUL 6 1PS C8 H11 N O3 S
FORMUL 8 ACT 3(C2 H3 O2 1-)
FORMUL 11 HOH *375(H2 O)
HELIX 1 1 ASN A 15 GLU A 28 1 14
HELIX 2 2 SER A 38 LYS A 52 1 15
HELIX 3 3 HIS A 65 GLY A 81 1 17
HELIX 4 4 PRO A 98 THR A 102 5 5
HELIX 5 5 THR A 103 LEU A 115 1 13
HELIX 6 6 LEU A 115 THR A 132 1 18
HELIX 7 7 SER A 142 GLN A 146 5 5
HELIX 8 8 ILE A 152 GLY A 174 1 23
HELIX 9 9 THR A 190 ASN A 195 1 6
HELIX 10 10 PRO A 197 GLN A 206 1 10
HELIX 11 11 GLU A 215 SER A 227 1 13
HELIX 12 12 SER A 228 SER A 232 5 5
HELIX 13 13 GLY A 244 ARG A 248 5 5
HELIX 14 14 ASN B 15 GLU B 28 1 14
HELIX 15 15 SER B 38 LYS B 52 1 15
HELIX 16 16 HIS B 65 GLY B 81 1 17
HELIX 17 17 PRO B 98 THR B 102 5 5
HELIX 18 18 THR B 103 LEU B 115 1 13
HELIX 19 19 LEU B 115 THR B 132 1 18
HELIX 20 20 SER B 142 GLN B 146 5 5
HELIX 21 21 ILE B 152 GLY B 174 1 23
HELIX 22 22 THR B 190 ASN B 195 1 6
HELIX 23 23 PRO B 197 GLN B 206 1 10
HELIX 24 24 GLU B 215 SER B 227 1 13
HELIX 25 25 SER B 228 SER B 232 5 5
HELIX 26 26 GLY B 244 ARG B 248 5 5
SHEET 1 AA 7 ALA A 56 PHE A 58 0
SHEET 2 AA 7 ASN A 31 VAL A 34 1 O VAL A 32 N VAL A 57
SHEET 3 AA 7 THR A 7 VAL A 10 1 O ALA A 8 N VAL A 33
SHEET 4 AA 7 ILE A 85 ASN A 88 1 O ILE A 85 N LEU A 9
SHEET 5 AA 7 GLY A 135 ILE A 140 1 O ALA A 136 N ALA A 86
SHEET 6 AA 7 ILE A 178 PRO A 185 1 O ARG A 179 N ILE A 137
SHEET 7 AA 7 TYR A 238 VAL A 241 1 O TYR A 239 N GLY A 184
SHEET 1 BA 7 ALA B 56 HIS B 60 0
SHEET 2 BA 7 ASN B 31 ASP B 36 1 O VAL B 32 N VAL B 57
SHEET 3 BA 7 THR B 7 VAL B 10 1 O ALA B 8 N VAL B 33
SHEET 4 BA 7 ILE B 85 ASN B 88 1 O ILE B 85 N LEU B 9
SHEET 5 BA 7 GLY B 135 ILE B 140 1 O ALA B 136 N ALA B 86
SHEET 6 BA 7 ILE B 178 PRO B 185 1 O ARG B 179 N ILE B 137
SHEET 7 BA 7 TYR B 238 VAL B 241 1 O TYR B 239 N GLY B 184
LINK OXT ARG A 248 MG MG A1250 1555 1555 2.03
LINK OXT ARG A 248 MG MG A1250 2656 1555 2.03
LINK MG MG A1250 O HOH A2194 1555 1555 2.08
LINK MG MG A1250 O HOH A2194 1555 2656 2.08
LINK MG MG A1250 O HOH A2196 1555 1555 2.11
LINK MG MG A1250 O HOH A2196 1555 2656 2.11
LINK MG MG A1250 O HOH A2199 1555 1555 2.06
LINK MG MG A1250 O HOH A2199 1555 2656 2.06
LINK OXT ARG B 248 MG MG B1251 2656 1555 2.32
LINK OXT ARG B 248 MG MG B1251 1555 1555 1.77
LINK MG MG B1251 O HOH B2160 1555 1555 2.00
LINK MG MG B1251 O HOH B2160 1555 2656 2.19
LINK MG MG B1251 O HOH B2162 1555 1555 2.07
LINK MG MG B1251 O HOH B2162 1555 2656 2.22
LINK MG MG B1251 O HOH B2164 1555 1555 2.17
LINK MG MG B1251 O HOH B2164 1555 2656 2.17
SITE 1 AC1 6 SER A 142 TYR A 155 ALA A 186 HOH A2154
SITE 2 AC1 6 HOH A2203 HOH A2204
SITE 1 AC2 5 ILE B 92 THR B 190 LEU B 192 VAL B 193
SITE 2 AC2 5 1PS B1250
SITE 1 AC3 15 ASN B 15 GLY B 16 ILE B 17 GLY B 18
SITE 2 AC3 15 ASN B 89 GLY B 91 SER B 141 TYR B 155
SITE 3 AC3 15 PRO B 185 ALA B 186 THR B 190 SO4 B1249
SITE 4 AC3 15 ACT B1253 HOH B2017 HOH B2087
SITE 1 AC4 4 ARG B 248 HOH B2160 HOH B2162 HOH B2164
SITE 1 AC5 4 ARG A 248 HOH A2194 HOH A2196 HOH A2199
SITE 1 AC6 7 HOH A2064 ARG B 19 THR B 20 LEU B 23
SITE 2 AC6 7 HOH B2022 HOH B2153 HOH B2170
SITE 1 AC7 5 SER B 142 TYR B 155 1PS B1250 HOH B2093
SITE 2 AC7 5 HOH B2168
SITE 1 AC8 4 ASN B 15 GLY B 16 THR B 191 LEU B 192
CRYST1 121.500 55.100 86.300 90.00 134.40 90.00 C 1 2 1 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 0.008230 0.000000 0.008060 0.00000
SCALE2 0.000000 0.018149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016218 0.00000
(ATOM LINES ARE NOT SHOWN.)
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