HEADER ELECTRON TRANSPORT 27-MAY-97 1AKU
TITLE D95A HYDROQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVODOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: HYDROQUINONE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP. VULGARIS STR.
SOURCE 3 HILDENBOROUGH;
SOURCE 4 ORGANISM_TAXID: 882;
SOURCE 5 STRAIN: HILDENBOROUGH;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: TG2
KEYWDS ELECTRON TRANSPORT, ELECTRON TRANSFER, FLAVOPROTEIN, FMN, FLAVODOXIN,
KEYWDS 2 MUTANT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCCARTHY,M.WALSH,T.HIGGINS
REVDAT 5 07-FEB-24 1AKU 1 REMARK
REVDAT 4 03-NOV-21 1AKU 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1AKU 1 VERSN
REVDAT 2 23-DEC-02 1AKU 1 JRNL
REVDAT 1 02-DEC-98 1AKU 0
JRNL AUTH A.A.MCCARTHY,M.A.WALSH,C.S.VERMA,D.P.O'CONNELL,M.REINHOLD,
JRNL AUTH 2 G.N.YALLOWAY,D.D'ARCY,T.M.HIGGINS,G.VOORDOUW,S.G.MAYHEW
JRNL TITL CRYSTALLOGRAPHIC INVESTIGATION OF THE ROLE OF ASPARTATE 95
JRNL TITL 2 IN THE MODULATION OF THE REDOX POTENTIALS OF DESULFOVIBRIO
JRNL TITL 3 VULGARIS FLAVODOXIN.
JRNL REF BIOCHEMISTRY V. 41 10950 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12206666
JRNL DOI 10.1021/BI020225H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MCCARTHY
REMARK 1 TITL X-RAY CRYSTALLOGRAPHIC STUDIES ON THE FLAVIN BINDING SITE OF
REMARK 1 TITL 2 FLAVODOXIN FROM DESULFOVIBRIO VULGARIS
REMARK 1 REF THESIS, NATIONAL UNIVERSITY 1997
REMARK 1 REF 2 OF IRELAND
REMARK 1 PUBL DUBLIN : NATIONAL UNIVERSITY OF IRELAND (THESIS)
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 16098
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 805
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2150
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2120
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 805
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 16098
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1101
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 12.0
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.015 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.047 ; 0.050
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.045 ; 0.040
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) : 0.170 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.180 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.260 ; 0.300
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) : 2.340 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 19.460; 15.000
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 1AKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170941.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-95
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.0
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 : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.937
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16098
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.42000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60-70% AMMONIUM SULFATE, 100MM TRIS
REMARK 280 -HCL, PH=7.0., PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 70.13000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.30000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 105.19500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.30000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.06500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.30000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.30000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 105.19500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.30000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.30000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.06500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.13000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 OE1 GLU A 32 O HOH A 259 2.01
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 249 O HOH A 261 4455 1.87
REMARK 500 O HOH A 220 O HOH A 261 4455 2.16
REMARK 500 O HOH A 253 O HOH A 257 6565 2.19
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 24 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 28 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR A 31 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR A 31 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 GLU A 32 OE1 - CD - OE2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLY A 61 CA - C - O ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP A 62 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 63 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ASP A 63 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 63 CA - C - O ANGL. DEV. = 14.3 DEGREES
REMARK 500 ASP A 63 O - C - N ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLU A 66 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 70 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TYR A 98 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP A 106 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP A 106 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 LYS A 113 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 GLN A 121 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP A 129 CB - CG - OD1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 129 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 134 CG - CD - NE ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG A 134 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 134 NH1 - CZ - NH2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 134 NE - CZ - NH2 ANGL. DEV. = -7.5 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 SER A 64 90.70 -169.32
REMARK 500 TYR A 100 79.32 -108.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FMN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FMN CO-FACTOR.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 150
DBREF 1AKU A 2 148 UNP P00323 FLAV_DESVH 2 148
SEQADV 1AKU ALA A 95 UNP P00323 ASP 95 ENGINEERED MUTATION
SEQRES 1 A 147 PRO LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN
SEQRES 2 A 147 THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA
SEQRES 3 A 147 ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER
SEQRES 4 A 147 VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL
SEQRES 5 A 147 LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU
SEQRES 6 A 147 LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU
SEQRES 7 A 147 GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY
SEQRES 8 A 147 CYS GLY ALA SER SER TYR GLU TYR PHE CYS GLY ALA VAL
SEQRES 9 A 147 ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU
SEQRES 10 A 147 ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG
SEQRES 11 A 147 ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL
SEQRES 12 A 147 ARG GLY ALA ILE
HET SO4 A 1 5
HET SO4 A 149 5
HET FMN A 150 31
HETNAM SO4 SULFATE ION
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 FMN C17 H21 N4 O9 P
FORMUL 5 HOH *155(H2 O)
HELIX 1 1 ASN A 14 ASP A 28 1 15
HELIX 2 2 ALA A 38 SER A 40 5 3
HELIX 3 3 ASP A 69 GLU A 80 1 12
HELIX 4 4 GLY A 103 ASN A 114 1 12
HELIX 5 5 PRO A 130 ALA A 132 5 3
HELIX 6 6 ARG A 134 GLY A 146 1 13
SHEET 1 A 5 GLU A 32 ASP A 37 0
SHEET 2 A 5 LYS A 3 GLY A 9 1 N ALA A 4 O GLU A 32
SHEET 3 A 5 LEU A 52 CYS A 57 1 N LEU A 52 O LEU A 5
SHEET 4 A 5 VAL A 88 GLY A 94 1 N ALA A 89 O VAL A 53
SHEET 5 A 5 LEU A 124 ASP A 127 1 N LEU A 124 O GLY A 92
SITE 1 FMN 1 FMN A 150
SITE 1 AC1 3 GLU A 48 GLY A 49 ARG A 86
SITE 1 AC2 3 TYR A 17 ARG A 131 HOH A 214
SITE 1 AC3 24 SER A 10 THR A 11 THR A 12 GLY A 13
SITE 2 AC3 24 ASN A 14 THR A 15 ASP A 28 SER A 58
SITE 3 AC3 24 THR A 59 TRP A 60 GLY A 61 CYS A 93
SITE 4 AC3 24 GLY A 94 ALA A 95 TYR A 98 TYR A 100
SITE 5 AC3 24 PHE A 101 CYS A 102 HOH A 171 HOH A 173
SITE 6 AC3 24 HOH A 185 HOH A 195 HOH A 225 HOH A 244
CRYST1 52.600 52.600 140.260 90.00 90.00 90.00 P 43 21 2 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 0.019011 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
