HEADER OXIDOREDUCTASE 19-DEC-01 1KNR
TITLE L-ASPARTATE OXIDASE: R386L MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-ASPARTATE OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.4.3.16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: NADB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS SUCCINATE DEHYDROGENASE, FUMARATE REDUCTASE FAMILY OF
KEYWDS 2 OXIDOREDUCTASES, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.BOSSI,A.MATTEVI
REVDAT 4 10-NOV-21 1KNR 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1KNR 1 VERSN
REVDAT 2 04-DEC-02 1KNR 1 REMARK
REVDAT 1 17-APR-02 1KNR 0
JRNL AUTH R.T.BOSSI,A.NEGRI,G.TEDESCHI,A.MATTEVI
JRNL TITL STRUCTURE OF FAD-BOUND L-ASPARTATE OXIDASE: INSIGHT INTO
JRNL TITL 2 SUBSTRATE SPECIFICITY AND CATALYSIS.
JRNL REF BIOCHEMISTRY V. 41 3018 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11863440
JRNL DOI 10.1021/BI015939R
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 27964
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1510
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2001
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.4910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4150
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 86.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.99000
REMARK 3 B22 (A**2) : 2.99000
REMARK 3 B33 (A**2) : -5.99000
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): 0.399
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.254
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.703
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4302 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5856 ; 2.583 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 528 ; 5.676 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 725 ;21.355 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 649 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3294 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2182 ; 0.333 ; 0.300
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): 338 ; 0.233 ; 0.500
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): 37 ; 0.302 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.257 ; 0.500
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): 2627 ; 0.845 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4230 ; 1.512 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1675 ; 2.791 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1626 ; 4.236 ; 4.500
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 : 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015152.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.10700
REMARK 200 R SYM FOR SHELL (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 64.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL, HEPES, SODIUM CITRATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 156.96650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.63900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.63900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 78.48325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.63900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.63900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 235.44975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.63900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.63900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 78.48325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.63900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.63900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 235.44975
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 156.96650
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 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 A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 HIS A 536
REMARK 465 TYR A 537
REMARK 465 ILE A 538
REMARK 465 ASN A 539
REMARK 465 ARG A 540
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 425 OG
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 ARG A 91 N GLN A 95 1.31
REMARK 500 O ALA A 90 N CYS A 93 1.72
REMARK 500 O GLU A 404 NH1 ARG A 408 2.04
REMARK 500 N HIS A 107 O SER A 115 2.04
REMARK 500 O ALA A 90 N VAL A 94 2.16
REMARK 500 O ASP A 361 OG SER A 401 2.18
REMARK 500 CD2 LEU A 513 O HOH A 817 2.18
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 ASP A 64 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 69 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 VAL A 86 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 ALA A 90 CA - C - N ANGL. DEV. = -16.3 DEGREES
REMARK 500 ALA A 90 O - C - N ANGL. DEV. = 10.9 DEGREES
REMARK 500 LEU A 130 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 VAL A 210 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP A 218 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 238 CB - CG - CD1 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP A 291 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 307 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 312 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 360 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 MET A 387 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 ASP A 431 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 MET A 469 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU A 499 CB - CG - CD1 ANGL. DEV. = -17.1 DEGREES
REMARK 500 LEU A 499 CB - CG - CD2 ANGL. DEV. = -13.0 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 GLU A 6 -78.93 -47.98
REMARK 500 GLN A 50 -74.36 -106.37
REMARK 500 CYS A 78 157.10 -49.70
REMARK 500 PHE A 85 -82.53 -36.99
REMARK 500 ALA A 90 -99.32 -65.74
REMARK 500 ARG A 91 -53.45 -0.15
REMARK 500 SER A 92 -77.12 -50.93
REMARK 500 HIS A 107 -140.59 -78.42
REMARK 500 ILE A 108 -9.46 -167.10
REMARK 500 GLN A 109 30.13 -150.88
REMARK 500 PRO A 110 176.89 -43.67
REMARK 500 ARG A 128 30.46 -155.18
REMARK 500 ALA A 133 -134.48 42.37
REMARK 500 ALA A 135 42.63 -146.45
REMARK 500 ASN A 150 30.08 -91.78
REMARK 500 ARG A 159 60.02 29.20
REMARK 500 ASP A 169 1.42 -67.51
REMARK 500 TRP A 185 107.20 -57.54
REMARK 500 GLU A 190 39.60 39.82
REMARK 500 ALA A 203 52.88 -145.06
REMARK 500 THR A 259 154.58 -48.57
REMARK 500 PHE A 281 -51.14 -129.94
REMARK 500 HIS A 315 5.33 -56.59
REMARK 500 ALA A 318 -31.30 -38.21
REMARK 500 HIS A 351 -50.70 -122.23
REMARK 500 ASN A 385 125.14 179.44
REMARK 500 ALA A 388 130.62 -37.93
REMARK 500 TRP A 400 -71.44 -51.53
REMARK 500 ILE A 406 -71.15 -69.41
REMARK 500 THR A 407 -45.26 -25.00
REMARK 500 ILE A 416 89.37 -65.34
REMARK 500 GLU A 424 108.30 -20.96
REMARK 500 ARG A 426 12.27 -145.98
REMARK 500 ASN A 429 87.08 -165.35
REMARK 500 VAL A 451 45.42 -144.71
REMARK 500 ALA A 479 -49.91 -22.66
REMARK 500 ARG A 482 118.65 -36.87
REMARK 500 LYS A 508 47.82 -76.25
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 542 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 353 O
REMARK 620 2 GLY A 355 O 72.7
REMARK 620 3 GLU A 375 O 88.8 88.1
REMARK 620 4 SER A 377 O 146.6 74.2 94.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CHU RELATED DB: PDB
REMARK 900 1CHU CONTAINS L-ASPARTATE OXIDASE: WILD TYPE APOFORM
REMARK 900 RELATED ID: 1KNP RELATED DB: PDB
REMARK 900 1KNP CONTAINS L-ASPARTATE OXIDASE: R386L MUTANT HOLOFORM IN COMPLEX
REMARK 900 WITH SUCCINATE
DBREF 1KNR A 1 540 UNP P10902 NADB_ECOLI 1 540
SEQADV 1KNR LEU A 386 UNP P10902 ARG 386 ENGINEERED MUTATION
SEQRES 1 A 540 MET ASN THR LEU PRO GLU HIS SER CYS ASP VAL LEU ILE
SEQRES 2 A 540 ILE GLY SER GLY ALA ALA GLY LEU SER LEU ALA LEU ARG
SEQRES 3 A 540 LEU ALA ASP GLN HIS GLN VAL ILE VAL LEU SER LYS GLY
SEQRES 4 A 540 PRO VAL THR GLU GLY SER THR PHE TYR ALA GLN GLY GLY
SEQRES 5 A 540 ILE ALA ALA VAL PHE ASP GLU THR ASP SER ILE ASP SER
SEQRES 6 A 540 HIS VAL GLU ASP THR LEU ILE ALA GLY ALA GLY ILE CYS
SEQRES 7 A 540 ASP ARG HIS ALA VAL GLU PHE VAL ALA SER ASN ALA ARG
SEQRES 8 A 540 SER CYS VAL GLN TRP LEU ILE ASP GLN GLY VAL LEU PHE
SEQRES 9 A 540 ASP THR HIS ILE GLN PRO ASN GLY GLU GLU SER TYR HIS
SEQRES 10 A 540 LEU THR ARG GLU GLY GLY HIS SER HIS ARG ARG ILE LEU
SEQRES 11 A 540 HIS ALA ALA ASP ALA THR GLY ARG GLU VAL GLU THR THR
SEQRES 12 A 540 LEU VAL SER LYS ALA LEU ASN HIS PRO ASN ILE ARG VAL
SEQRES 13 A 540 LEU GLU ARG THR ASN ALA VAL ASP LEU ILE VAL SER ASP
SEQRES 14 A 540 LYS ILE GLY LEU PRO GLY THR ARG ARG VAL VAL GLY ALA
SEQRES 15 A 540 TRP VAL TRP ASN ARG ASN LYS GLU THR VAL GLU THR CYS
SEQRES 16 A 540 HIS ALA LYS ALA VAL VAL LEU ALA THR GLY GLY ALA SER
SEQRES 17 A 540 LYS VAL TYR GLN TYR THR THR ASN PRO ASP ILE SER SER
SEQRES 18 A 540 GLY ASP GLY ILE ALA MET ALA TRP ARG ALA GLY CYS ARG
SEQRES 19 A 540 VAL ALA ASN LEU GLU PHE ASN GLN PHE HIS PRO THR ALA
SEQRES 20 A 540 LEU TYR HIS PRO GLN ALA ARG ASN PHE LEU LEU THR GLU
SEQRES 21 A 540 ALA LEU ARG GLY GLU GLY ALA TYR LEU LYS ARG PRO ASP
SEQRES 22 A 540 GLY THR ARG PHE MET PRO ASP PHE ASP GLU ARG GLY GLU
SEQRES 23 A 540 LEU ALA PRO ARG ASP ILE VAL ALA ARG ALA ILE ASP HIS
SEQRES 24 A 540 GLU MET LYS ARG LEU GLY ALA ASP CYS MET PHE LEU ASP
SEQRES 25 A 540 ILE SER HIS LYS PRO ALA ASP PHE ILE ARG GLN HIS PHE
SEQRES 26 A 540 PRO MET ILE TYR GLU LYS LEU LEU GLY LEU GLY ILE ASP
SEQRES 27 A 540 LEU THR GLN GLU PRO VAL PRO ILE VAL PRO ALA ALA HIS
SEQRES 28 A 540 TYR THR CYS GLY GLY VAL MET VAL ASP ASP HIS GLY ARG
SEQRES 29 A 540 THR ASP VAL GLU GLY LEU TYR ALA ILE GLY GLU VAL SER
SEQRES 30 A 540 TYR THR GLY LEU HIS GLY ALA ASN LEU MET ALA SER ASN
SEQRES 31 A 540 SER LEU LEU GLU CYS LEU VAL TYR GLY TRP SER ALA ALA
SEQRES 32 A 540 GLU ASP ILE THR ARG ARG MET PRO TYR ALA HIS ASP ILE
SEQRES 33 A 540 SER THR LEU PRO PRO TRP ASP GLU SER ARG VAL GLU ASN
SEQRES 34 A 540 PRO ASP GLU ARG VAL VAL ILE GLN HIS ASN TRP HIS GLU
SEQRES 35 A 540 LEU ARG LEU PHE MET TRP ASP TYR VAL GLY ILE VAL ARG
SEQRES 36 A 540 THR THR LYS ARG LEU GLU ARG ALA LEU ARG ARG ILE THR
SEQRES 37 A 540 MET LEU GLN GLN GLU ILE ASP GLU TYR TYR ALA HIS PHE
SEQRES 38 A 540 ARG VAL SER ASN ASN LEU LEU GLU LEU ARG ASN LEU VAL
SEQRES 39 A 540 GLN VAL ALA GLU LEU ILE VAL ARG CYS ALA MET MET ARG
SEQRES 40 A 540 LYS GLU SER ARG GLY LEU HIS PHE THR LEU ASP TYR PRO
SEQRES 41 A 540 GLU LEU LEU THR HIS SER GLY PRO SER ILE LEU SER PRO
SEQRES 42 A 540 GLY ASN HIS TYR ILE ASN ARG
HET CL A 541 1
HET NA A 542 1
HET FAD A 800 53
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 CL CL 1-
FORMUL 3 NA NA 1+
FORMUL 4 FAD C27 H33 N9 O15 P2
FORMUL 5 HOH *23(H2 O)
HELIX 1 1 GLY A 17 ASP A 29 1 13
HELIX 2 2 GLY A 44 ALA A 49 5 6
HELIX 3 3 SER A 62 GLY A 74 1 13
HELIX 4 4 ASP A 79 SER A 88 1 10
HELIX 5 5 ASN A 89 ASP A 99 1 11
HELIX 6 6 ALA A 135 ASN A 150 1 16
HELIX 7 7 ASP A 169 ILE A 171 5 3
HELIX 8 8 ASN A 188 GLU A 190 5 3
HELIX 9 9 ALA A 207 TYR A 211 5 5
HELIX 10 10 GLY A 222 ALA A 231 1 10
HELIX 11 11 THR A 259 GLU A 265 1 7
HELIX 12 12 PHE A 277 PHE A 281 5 5
HELIX 13 13 ARG A 284 ALA A 288 5 5
HELIX 14 14 PRO A 289 GLY A 305 1 17
HELIX 15 15 PRO A 317 PHE A 325 1 9
HELIX 16 16 PHE A 325 GLY A 334 1 10
HELIX 17 17 ASN A 390 MET A 410 1 21
HELIX 18 18 PRO A 411 ALA A 413 5 3
HELIX 19 19 ASN A 429 VAL A 451 1 23
HELIX 20 20 THR A 456 ALA A 479 1 24
HELIX 21 21 SER A 484 ARG A 507 1 24
SHEET 1 A 4 HIS A 7 SER A 8 0
SHEET 2 A 4 VAL A 192 HIS A 196 1 O HIS A 196 N HIS A 7
SHEET 3 A 4 VAL A 179 ASN A 186 -1 N VAL A 184 O GLU A 193
SHEET 4 A 4 THR A 160 VAL A 167 -1 N ILE A 166 O GLY A 181
SHEET 1 B 5 ILE A 154 LEU A 157 0
SHEET 2 B 5 VAL A 33 LEU A 36 1 N VAL A 33 O ARG A 155
SHEET 3 B 5 VAL A 11 ILE A 14 1 N ILE A 13 O LEU A 36
SHEET 4 B 5 ALA A 199 LEU A 202 1 O ALA A 199 N LEU A 12
SHEET 5 B 5 LEU A 370 ALA A 372 1 O TYR A 371 N LEU A 202
SHEET 1 C 3 ILE A 53 ALA A 54 0
SHEET 2 C 3 ILE A 129 LEU A 130 -1 O LEU A 130 N ILE A 53
SHEET 3 C 3 LEU A 118 THR A 119 -1 N THR A 119 O ILE A 129
SHEET 1 D 4 SER A 377 TYR A 378 0
SHEET 2 D 4 GLY A 356 MET A 358 1 N VAL A 357 O TYR A 378
SHEET 3 D 4 VAL A 235 ALA A 236 -1 N ALA A 236 O GLY A 356
SHEET 4 D 4 ILE A 530 LEU A 531 -1 O LEU A 531 N VAL A 235
SHEET 1 E 4 ASN A 241 LEU A 248 0
SHEET 2 E 4 VAL A 344 THR A 353 -1 O VAL A 347 N ALA A 247
SHEET 3 E 4 MET A 309 ASP A 312 -1 N LEU A 311 O VAL A 344
SHEET 4 E 4 TYR A 268 LYS A 270 -1 N TYR A 268 O ASP A 312
LINK O THR A 353 NA NA A 542 1555 1555 2.77
LINK O GLY A 355 NA NA A 542 1555 1555 2.57
LINK O GLU A 375 NA NA A 542 1555 1555 2.19
LINK O SER A 377 NA NA A 542 1555 1555 2.37
SITE 1 AC1 3 HIS A 244 THR A 259 GLU A 260
SITE 1 AC2 4 THR A 353 GLY A 355 GLU A 375 SER A 377
SITE 1 AC3 31 ILE A 14 GLY A 15 SER A 16 ALA A 18
SITE 2 AC3 31 ALA A 19 LYS A 38 GLY A 44 SER A 45
SITE 3 AC3 31 THR A 46 TYR A 48 ALA A 49 GLN A 50
SITE 4 AC3 31 GLY A 51 GLY A 52 THR A 160 ASN A 161
SITE 5 AC3 31 ALA A 162 ALA A 203 THR A 204 GLY A 205
SITE 6 AC3 31 ASN A 216 ILE A 219 ASP A 223 LEU A 257
SITE 7 AC3 31 HIS A 351 TYR A 352 GLY A 374 GLU A 375
SITE 8 AC3 31 SER A 389 SER A 391 LEU A 392
CRYST1 73.278 73.278 313.933 90.00 90.00 90.00 P 41 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 0.013647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003185 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
