HEADER OXIDOREDUCTASE 29-NOV-15 5F12
TITLE WRBA IN COMPLEX WITH FMN UNDER CRYSTALLIZATION CONDITIONS OF WRBA-FMN-
TITLE 2 BQ STRUCTURE (4YQE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD(P)H DEHYDROGENASE (QUINONE);
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FLAVOPROTEIN WRBA,NAD(P)H:QUINONE OXIDOREDUCTASE,NQO;
COMPND 5 EC: 1.6.5.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: WRBA, B1004, JW0989;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FLAVIN MONONUCLEOTIDE, NAD(P)H DEHYDROGENASE (QUINONE), OXIDATION-
KEYWDS 2 REDUCTION, PROTEIN BINDING, REPRESSOR PROTEINS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DEGTJARIK,J.BRYNDA,O.ETTRICHOVA,I.KUTA SMATANOVA,J.CAREY,R.ETTRICH
REVDAT 5 10-JAN-24 5F12 1 REMARK
REVDAT 4 22-JUN-16 5F12 1 JRNL
REVDAT 3 08-JUN-16 5F12 1 JRNL
REVDAT 2 01-JUN-16 5F12 1 JRNL
REVDAT 1 25-MAY-16 5F12 0
JRNL AUTH O.DEGTJARIK,J.BRYNDA,O.ETTRICHOVA,M.KUTY,D.SINHA,
JRNL AUTH 2 I.KUTA SMATANOVA,J.CAREY,R.ETTRICH,D.REHA
JRNL TITL QUANTUM CALCULATIONS INDICATE EFFECTIVE ELECTRON TRANSFER
JRNL TITL 2 BETWEEN FMN AND BENZOQUINONE IN A NEW CRYSTAL STRUCTURE OF
JRNL TITL 3 ESCHERICHIA COLI WRBA.
JRNL REF J.PHYS.CHEM.B V. 120 4867 2016
JRNL REFN ISSN 1089-5647
JRNL PMID 27183467
JRNL DOI 10.1021/ACS.JPCB.5B11958
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 49068
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2628
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3540
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2811
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2980 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2761 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4073 ; 2.004 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6374 ; 1.388 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 395 ; 6.943 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;34.081 ;24.273
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 447 ;11.774 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;11.370 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 453 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3420 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 652 ; 0.006 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 197 B 1 197 10243 0.120 0.050
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5F12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215812.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS XDSAPP
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51696
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 3B6I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOL, 12.5 % PEG 1000,
REMARK 280 12.5% PEG 3350, 12.5% MPD, 0.2M 1,6-HEXANEDIOL, 0.2 M 1-BUTANOL,
REMARK 280 0.2 M (RS)-1,2-PROPANEDIOL, 0.2 M 2-PROPANOL, 0.2 M 1,4-
REMARK 280 BUTANEDIOL, 0.2 M 1,3-PROPANEDIOL, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 84.51000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.37500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.37500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.25500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.37500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.37500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 126.76500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.37500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.37500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.25500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.37500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.37500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 126.76500
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 84.51000
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 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 DIHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = D2).
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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 153
REMARK 465 ARG A 154
REMARK 465 GLY A 155
REMARK 465 GLN B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 PHE B 148
REMARK 465 ASP B 149
REMARK 465 VAL B 150
REMARK 465 SER B 151
REMARK 465 GLN B 152
REMARK 465 VAL B 153
REMARK 465 ARG B 154
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 37 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 37 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ASP B 168 138.88 83.49
REMARK 500 ARG B 171 -148.59 29.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 169 SER B 170 -143.76
REMARK 500 ARG B 171 GLN B 172 -129.39
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 B 405 DISTANCE = 5.93 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YQE RELATED DB: PDB
REMARK 900 COMPLEX WITH FMN AND BQ
REMARK 900 RELATED ID: 1RG1 RELATED DB: PDB
REMARK 900 WRBA APOPROTEIN
REMARK 900 RELATED ID: 3ZHO RELATED DB: PDB
REMARK 900 WRBA IN COMPLEX WITH FMN AT 1.2 A RESOLUTION
DBREF 5F12 A 1 197 UNP P0A8G6 NQOR_ECOLI 2 198
DBREF 5F12 B 1 197 UNP P0A8G6 NQOR_ECOLI 2 198
SEQRES 1 A 197 ALA LYS VAL LEU VAL LEU TYR TYR SER MHO TYR GLY HIS
SEQRES 2 A 197 ILE GLU THR MET ALA ARG ALA VAL ALA GLU GLY ALA SER
SEQRES 3 A 197 LYS VAL ASP GLY ALA GLU VAL VAL VAL LYS ARG VAL PRO
SEQRES 4 A 197 GLU THR MET PRO PRO GLN LEU PHE GLU LYS ALA GLY GLY
SEQRES 5 A 197 LYS THR GLN THR ALA PRO VAL ALA THR PRO GLN GLU LEU
SEQRES 6 A 197 ALA ASP TYR ASP ALA ILE ILE PHE GLY THR PRO THR ARG
SEQRES 7 A 197 PHE GLY ASN MET SER GLY GLN MET ARG THR PHE LEU ASP
SEQRES 8 A 197 GLN THR GLY GLY LEU TRP ALA SER GLY ALA LEU TYR GLY
SEQRES 9 A 197 LYS LEU ALA SER VAL PHE SER SER THR GLY THR GLY GLY
SEQRES 10 A 197 GLY GLN GLU GLN THR ILE THR SER THR TRP THR THR LEU
SEQRES 11 A 197 ALA HIS HIS GLY MET VAL ILE VAL PRO ILE GLY TYR ALA
SEQRES 12 A 197 ALA GLN GLU LEU PHE ASP VAL SER GLN VAL ARG GLY GLY
SEQRES 13 A 197 THR PRO TYR GLY ALA THR THR ILE ALA GLY GLY ASP GLY
SEQRES 14 A 197 SER ARG GLN PRO SER GLN GLU GLU LEU SER ILE ALA ARG
SEQRES 15 A 197 TYR GLN GLY GLU TYR VAL ALA GLY LEU ALA VAL LYS LEU
SEQRES 16 A 197 ASN GLY
SEQRES 1 B 197 ALA LYS VAL LEU VAL LEU TYR TYR SER MHO TYR GLY HIS
SEQRES 2 B 197 ILE GLU THR MET ALA ARG ALA VAL ALA GLU GLY ALA SER
SEQRES 3 B 197 LYS VAL ASP GLY ALA GLU VAL VAL VAL LYS ARG VAL PRO
SEQRES 4 B 197 GLU THR MET PRO PRO GLN LEU PHE GLU LYS ALA GLY GLY
SEQRES 5 B 197 LYS THR GLN THR ALA PRO VAL ALA THR PRO GLN GLU LEU
SEQRES 6 B 197 ALA ASP TYR ASP ALA ILE ILE PHE GLY THR PRO THR ARG
SEQRES 7 B 197 PHE GLY ASN MET SER GLY GLN MET ARG THR PHE LEU ASP
SEQRES 8 B 197 GLN THR GLY GLY LEU TRP ALA SER GLY ALA LEU TYR GLY
SEQRES 9 B 197 LYS LEU ALA SER VAL PHE SER SER THR GLY THR GLY GLY
SEQRES 10 B 197 GLY GLN GLU GLN THR ILE THR SER THR TRP THR THR LEU
SEQRES 11 B 197 ALA HIS HIS GLY MET VAL ILE VAL PRO ILE GLY TYR ALA
SEQRES 12 B 197 ALA GLN GLU LEU PHE ASP VAL SER GLN VAL ARG GLY GLY
SEQRES 13 B 197 THR PRO TYR GLY ALA THR THR ILE ALA GLY GLY ASP GLY
SEQRES 14 B 197 SER ARG GLN PRO SER GLN GLU GLU LEU SER ILE ALA ARG
SEQRES 15 B 197 TYR GLN GLY GLU TYR VAL ALA GLY LEU ALA VAL LYS LEU
SEQRES 16 B 197 ASN GLY
MODRES 5F12 MHO A 10 MET MODIFIED RESIDUE
MODRES 5F12 MHO B 10 MET MODIFIED RESIDUE
HET MHO A 10 9
HET MHO B 10 9
HET FMN A 201 31
HET FMN B 201 31
HETNAM MHO S-OXYMETHIONINE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 1 MHO 2(C5 H11 N O3 S)
FORMUL 3 FMN 2(C17 H21 N4 O9 P)
FORMUL 5 HOH *206(H2 O)
HELIX 1 AA1 GLY A 12 SER A 26 1 15
HELIX 2 AA2 PRO A 43 ALA A 50 1 8
HELIX 3 AA3 THR A 61 TYR A 68 5 8
HELIX 4 AA4 SER A 83 ASP A 91 1 9
HELIX 5 AA5 THR A 93 GLY A 100 1 8
HELIX 6 AA6 GLY A 118 HIS A 133 1 16
HELIX 7 AA7 ALA A 144 PHE A 148 5 5
HELIX 8 AA8 SER A 174 GLY A 197 1 24
HELIX 9 AA9 GLY B 12 LYS B 27 1 16
HELIX 10 AB1 PRO B 43 ALA B 50 1 8
HELIX 11 AB2 THR B 61 TYR B 68 5 8
HELIX 12 AB3 SER B 83 ASP B 91 1 9
HELIX 13 AB4 THR B 93 GLY B 100 1 8
HELIX 14 AB5 GLY B 118 HIS B 133 1 16
HELIX 15 AB6 ILE B 140 ALA B 144 5 5
HELIX 16 AB7 SER B 174 GLY B 197 1 24
SHEET 1 AA1 5 GLU A 32 ARG A 37 0
SHEET 2 AA1 5 LYS A 2 TYR A 7 1 N VAL A 5 O VAL A 34
SHEET 3 AA1 5 ALA A 70 PRO A 76 1 O ILE A 72 N LEU A 4
SHEET 4 AA1 5 LEU A 106 SER A 112 1 O SER A 108 N PHE A 73
SHEET 5 AA1 5 VAL A 136 ILE A 137 1 O VAL A 136 N ALA A 107
SHEET 1 AA2 5 GLU B 32 ARG B 37 0
SHEET 2 AA2 5 LYS B 2 TYR B 7 1 N VAL B 3 O GLU B 32
SHEET 3 AA2 5 ALA B 70 PRO B 76 1 O ILE B 72 N LEU B 4
SHEET 4 AA2 5 LEU B 106 THR B 113 1 O SER B 108 N PHE B 73
SHEET 5 AA2 5 VAL B 136 ILE B 137 1 O VAL B 136 N ALA B 107
SHEET 1 AA3 5 GLU B 32 ARG B 37 0
SHEET 2 AA3 5 LYS B 2 TYR B 7 1 N VAL B 3 O GLU B 32
SHEET 3 AA3 5 ALA B 70 PRO B 76 1 O ILE B 72 N LEU B 4
SHEET 4 AA3 5 LEU B 106 THR B 113 1 O SER B 108 N PHE B 73
SHEET 5 AA3 5 THR B 162 ILE B 164 1 O THR B 163 N THR B 113
LINK C SER A 9 N MHO A 10 1555 1555 1.31
LINK C MHO A 10 N TYR A 11 1555 1555 1.33
LINK C SER B 9 N MHO B 10 1555 1555 1.33
LINK C MHO B 10 N TYR B 11 1555 1555 1.33
SITE 1 AC1 20 SER A 9 MHO A 10 TYR A 11 GLY A 12
SITE 2 AC1 20 HIS A 13 ILE A 14 PRO A 76 THR A 77
SITE 3 AC1 20 ARG A 78 PHE A 79 SER A 112 THR A 113
SITE 4 AC1 20 GLY A 114 THR A 115 GLY A 116 GLY A 117
SITE 5 AC1 20 HOH A 305 HOH A 337 ASP B 91 HIS B 132
SITE 1 AC2 22 ASP A 91 HIS A 132 SER B 9 MHO B 10
SITE 2 AC2 22 TYR B 11 GLY B 12 HIS B 13 ILE B 14
SITE 3 AC2 22 PRO B 76 THR B 77 ARG B 78 PHE B 79
SITE 4 AC2 22 SER B 112 THR B 113 GLY B 114 THR B 115
SITE 5 AC2 22 GLY B 116 GLY B 117 ALA B 165 HOH B 306
SITE 6 AC2 22 HOH B 326 HOH B 333
CRYST1 60.750 60.750 169.020 90.00 90.00 90.00 P 41 21 2 16
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 0.016461 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005916 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
