HEADER OXIDOREDUCTASE 16-OCT-13 4N82
TITLE X-RAY CRYSTAL STRUCTURE OF STREPTOCOCCUS SANGUINIS NRDIOX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEOTIDE REDUCTASE;
COMPND 3 CHAIN: B, A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SANGUINIS;
SOURCE 3 ORGANISM_TAXID: 388919;
SOURCE 4 STRAIN: SK36;
SOURCE 5 GENE: NRDI, SSA_2263;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS FLAVOPROTEIN, RIBONUCLEOTIDE REDUCTASE, OXIDATION-REDUCTION, FLAVIN
KEYWDS 2 MONONUCLEOTIDE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.BOAL,A.C.ROSENZWEIG
REVDAT 5 20-SEP-23 4N82 1 REMARK SEQADV
REVDAT 4 15-NOV-17 4N82 1 REMARK
REVDAT 3 19-MAR-14 4N82 1 JRNL
REVDAT 2 26-FEB-14 4N82 1 JRNL
REVDAT 1 08-JAN-14 4N82 0
JRNL AUTH O.MAKHLYNETS,A.K.BOAL,D.V.RHODES,T.KITTEN,A.C.ROSENZWEIG,
JRNL AUTH 2 J.STUBBE
JRNL TITL STREPTOCOCCUS SANGUINIS CLASS IB RIBONUCLEOTIDE REDUCTASE:
JRNL TITL 2 HIGH ACTIVITY WITH BOTH IRON AND MANGANESE COFACTORS AND
JRNL TITL 3 STRUCTURAL INSIGHTS.
JRNL REF J.BIOL.CHEM. V. 289 6259 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24381172
JRNL DOI 10.1074/JBC.M113.533554
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 33340
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1675
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) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2141
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2405
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : 1.50000
REMARK 3 B33 (A**2) : -2.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.51000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.143
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.680
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2539 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3440 ; 1.008 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 302 ; 4.720 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;32.470 ;24.880
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 435 ;14.528 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.617 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 373 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1918 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 154
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9770 26.0017 35.8093
REMARK 3 T TENSOR
REMARK 3 T11: 0.0698 T22: 0.0587
REMARK 3 T33: 0.0259 T12: -0.0221
REMARK 3 T13: -0.0051 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.9117 L22: 0.8568
REMARK 3 L33: 0.8412 L12: -0.2930
REMARK 3 L13: -0.4972 L23: -0.0968
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0009 S13: -0.0243
REMARK 3 S21: 0.1196 S22: -0.0733 S23: 0.0140
REMARK 3 S31: -0.0856 S32: 0.0855 S33: 0.0847
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3577 24.5917 3.9833
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: 0.1406
REMARK 3 T33: 0.0170 T12: 0.0163
REMARK 3 T13: 0.0060 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.5605 L22: 1.1788
REMARK 3 L33: 4.2024 L12: 0.1981
REMARK 3 L13: 1.4623 L23: 1.0691
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: 0.1935 S13: -0.0089
REMARK 3 S21: 0.0216 S22: -0.0080 S23: 0.1025
REMARK 3 S31: 0.0278 S32: 0.5326 S33: 0.0328
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4N82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.078
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 33395
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 1RLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULFATE, PH 5.6,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 52.36300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.30600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.36300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.30600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 155
REMARK 465 GLU B 156
REMARK 465 ASN B 157
REMARK 465 GLN B 158
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 67
REMARK 465 GLY A 68
REMARK 465 ASN A 69
REMARK 465 GLY A 70
REMARK 465 VAL A 71
REMARK 465 ASN A 155
REMARK 465 GLU A 156
REMARK 465 ASN A 157
REMARK 465 GLN A 158
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 LEU B 79 -24.21 67.90
REMARK 500 ASN B 108 -116.27 52.42
REMARK 500 MET B 132 -117.53 51.81
REMARK 500 LEU A 79 -25.13 69.79
REMARK 500 ASN A 108 -116.63 52.24
REMARK 500 ASN A 108 -116.09 51.37
REMARK 500 MET A 132 -121.79 51.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N83 RELATED DB: PDB
DBREF 4N82 B 1 158 UNP A3CR20 A3CR20_STRSV 5 162
DBREF 4N82 A 1 158 UNP A3CR20 A3CR20_STRSV 5 162
SEQADV 4N82 MET B -19 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY B -18 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER B -17 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER B -16 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -15 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -14 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -13 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -12 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -11 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B -10 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER B -9 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER B -8 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY B -7 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 LEU B -6 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 VAL B -5 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 PRO B -4 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 ARG B -3 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY B -2 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER B -1 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS B 0 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 MET A -19 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY A -18 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER A -17 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER A -16 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -15 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -14 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -13 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -12 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -11 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A -10 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER A -9 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER A -8 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY A -7 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 LEU A -6 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 VAL A -5 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 PRO A -4 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 ARG A -3 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 GLY A -2 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 SER A -1 UNP A3CR20 EXPRESSION TAG
SEQADV 4N82 HIS A 0 UNP A3CR20 EXPRESSION TAG
SEQRES 1 B 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 178 LEU VAL PRO ARG GLY SER HIS MET THR LYS VAL SER LEU
SEQRES 3 B 178 VAL TYR ILE SER LEU SER GLY ASN THR GLU SER PHE VAL
SEQRES 4 B 178 ARG ARG LEU THR ASP TYR LEU LEU GLU GLN HIS PRO SER
SEQRES 5 B 178 LEU GLU VAL GLU LYS ILE HIS ILE LYS ASP LEU VAL LYS
SEQRES 6 B 178 GLU ARG GLN PRO PHE PHE GLU MET ASP ASN PRO PHE ILE
SEQRES 7 B 178 ALA PHE LEU PRO THR TYR LEU GLU GLY GLY ASN GLY VAL
SEQRES 8 B 178 ASP ASN GLY ASP VAL GLU ILE LEU THR THR ASP VAL GLY
SEQRES 9 B 178 ASP PHE ILE ALA TYR GLY GLN ASN ALA SER LYS CYS LEU
SEQRES 10 B 178 GLY VAL ILE GLY SER GLY ASN ARG ASN PHE ASN ASN GLN
SEQRES 11 B 178 TYR CYS LEU THR ALA LYS GLN TYR SER GLU ARG PHE GLY
SEQRES 12 B 178 PHE PRO VAL LEU ALA ASP PHE GLU MET ARG GLY MET LEU
SEQRES 13 B 178 GLY ASP ILE LYS LYS VAL ALA GLY ILE ILE GLU GLU LEU
SEQRES 14 B 178 TYR HIS ILE GLU LYS ASN GLU ASN GLN
SEQRES 1 A 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 178 LEU VAL PRO ARG GLY SER HIS MET THR LYS VAL SER LEU
SEQRES 3 A 178 VAL TYR ILE SER LEU SER GLY ASN THR GLU SER PHE VAL
SEQRES 4 A 178 ARG ARG LEU THR ASP TYR LEU LEU GLU GLN HIS PRO SER
SEQRES 5 A 178 LEU GLU VAL GLU LYS ILE HIS ILE LYS ASP LEU VAL LYS
SEQRES 6 A 178 GLU ARG GLN PRO PHE PHE GLU MET ASP ASN PRO PHE ILE
SEQRES 7 A 178 ALA PHE LEU PRO THR TYR LEU GLU GLY GLY ASN GLY VAL
SEQRES 8 A 178 ASP ASN GLY ASP VAL GLU ILE LEU THR THR ASP VAL GLY
SEQRES 9 A 178 ASP PHE ILE ALA TYR GLY GLN ASN ALA SER LYS CYS LEU
SEQRES 10 A 178 GLY VAL ILE GLY SER GLY ASN ARG ASN PHE ASN ASN GLN
SEQRES 11 A 178 TYR CYS LEU THR ALA LYS GLN TYR SER GLU ARG PHE GLY
SEQRES 12 A 178 PHE PRO VAL LEU ALA ASP PHE GLU MET ARG GLY MET LEU
SEQRES 13 A 178 GLY ASP ILE LYS LYS VAL ALA GLY ILE ILE GLU GLU LEU
SEQRES 14 A 178 TYR HIS ILE GLU LYS ASN GLU ASN GLN
HET FMN B 201 31
HET SO4 B 202 5
HET FMN A 201 31
HET SO4 A 202 5
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM SO4 SULFATE ION
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 3 FMN 2(C17 H21 N4 O9 P)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *204(H2 O)
HELIX 1 1 GLY B 13 HIS B 30 1 18
HELIX 2 2 ILE B 40 GLU B 46 1 7
HELIX 3 3 GLY B 70 ASP B 75 1 6
HELIX 4 4 THR B 80 TYR B 89 1 10
HELIX 5 5 GLN B 91 LYS B 95 1 5
HELIX 6 6 ASN B 104 TYR B 111 5 8
HELIX 7 7 CYS B 112 GLY B 123 1 12
HELIX 8 8 MET B 135 TYR B 150 1 16
HELIX 9 9 GLY A 13 HIS A 30 1 18
HELIX 10 10 ILE A 40 GLU A 46 1 7
HELIX 11 11 THR A 80 ALA A 88 1 9
HELIX 12 12 GLN A 91 LYS A 95 1 5
HELIX 13 13 ASN A 104 TYR A 111 5 8
HELIX 14 14 CYS A 112 GLY A 123 1 12
HELIX 15 15 MET A 135 TYR A 150 1 16
SHEET 1 A 5 GLU B 34 HIS B 39 0
SHEET 2 A 5 LYS B 3 TYR B 8 1 N VAL B 4 O GLU B 36
SHEET 3 A 5 PHE B 57 PRO B 62 1 O PHE B 60 N VAL B 7
SHEET 4 A 5 CYS B 96 GLY B 103 1 O ILE B 100 N ALA B 59
SHEET 5 A 5 VAL B 126 GLU B 131 1 O LEU B 127 N VAL B 99
SHEET 1 B 5 GLU A 34 HIS A 39 0
SHEET 2 B 5 LYS A 3 TYR A 8 1 N VAL A 4 O GLU A 34
SHEET 3 B 5 PHE A 57 PRO A 62 1 O PHE A 60 N VAL A 7
SHEET 4 B 5 CYS A 96 GLY A 103 1 O LEU A 97 N PHE A 57
SHEET 5 B 5 VAL A 126 GLU A 131 1 O PHE A 130 N GLY A 101
SHEET 1 C 2 LEU A 65 GLU A 66 0
SHEET 2 C 2 VAL A 76 GLU A 77 -1 O VAL A 76 N GLU A 66
SITE 1 AC1 22 TYR A 64 SER B 10 LEU B 11 SER B 12
SITE 2 AC1 22 GLY B 13 ASN B 14 THR B 15 PRO B 62
SITE 3 AC1 22 THR B 63 TYR B 64 LEU B 65 SER B 102
SITE 4 AC1 22 GLY B 103 ASN B 104 PHE B 107 GLN B 110
SITE 5 AC1 22 TYR B 111 CYS B 112 MET B 132 HOH B 306
SITE 6 AC1 22 HOH B 313 HOH B 316
SITE 1 AC2 4 SER B 17 ARG B 20 ARG B 133 HOH B 333
SITE 1 AC3 22 SER A 10 LEU A 11 SER A 12 GLY A 13
SITE 2 AC3 22 ASN A 14 THR A 15 PRO A 62 THR A 63
SITE 3 AC3 22 TYR A 64 LEU A 65 SER A 102 GLY A 103
SITE 4 AC3 22 ASN A 104 PHE A 107 GLN A 110 TYR A 111
SITE 5 AC3 22 CYS A 112 MET A 132 HOH A 306 HOH A 307
SITE 6 AC3 22 HOH A 328 TYR B 64
SITE 1 AC4 4 SER A 17 ARG A 20 ARG A 133 HOH A 326
CRYST1 104.726 56.612 73.387 90.00 106.13 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 0.009549 0.000000 0.002761 0.00000
SCALE2 0.000000 0.017664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
