HEADER OXIDOREDUCTASE(OXYGEN AS ACCEPTOR) 09-NOV-93 1POW
TITLE THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE
TITLE 2 PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.2.3.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590
KEYWDS OXIDOREDUCTASE(OXYGEN AS ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.MULLER,G.E.SCHULZ
REVDAT 4 14-FEB-24 1POW 1 REMARK LINK
REVDAT 3 13-JUL-11 1POW 1 VERSN
REVDAT 2 24-FEB-09 1POW 1 VERSN
REVDAT 1 31-JAN-94 1POW 0
JRNL AUTH Y.A.MULLER,G.SCHUMACHER,R.RUDOLPH,G.E.SCHULZ
JRNL TITL THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF
JRNL TITL 2 WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM.
JRNL REF J.MOL.BIOL. V. 237 315 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8145244
JRNL DOI 10.1006/JMBI.1994.1233
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.A.MULLER,G.E.SCHULZ
REMARK 1 TITL STRUCTURE OF THE THIAMINE-AND FLAVIN-DEPENDENT ENZYME
REMARK 1 TITL 2 PYRUVATE OXIDASE
REMARK 1 REF SCIENCE V. 259 965 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 49870
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1POW 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_1000175776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 83.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.70000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.70000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.55000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.70000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.55000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.70000
REMARK 290 SMTRY3 8 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 300 REMARK: THE TETRAMER CAN BE GENERATED FROM THE ASYMMETRIC UNIT BY
REMARK 300 APPLYING THE FOLLOWING TRANSFORMATION:
REMARK 300 1 0 0 0
REMARK 300 0 -1 0 155.36
REMARK 300 0 0 -1 0
REMARK 300
REMARK 300 THE TWO SUBUNITS OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 ARE RELATED BY A LOCAL TWOFOLD AXIS. THE TRANSFORMATION
REMARK 300 PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE
REMARK 300 COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 32430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 70690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -240.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 155.40000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 HIS A 28 NE2 HIS A 28 CD2 -0.070
REMARK 500 HIS A 52 NE2 HIS A 52 CD2 -0.071
REMARK 500 HIS A 58 NE2 HIS A 58 CD2 -0.072
REMARK 500 HIS A 89 NE2 HIS A 89 CD2 -0.077
REMARK 500 HIS A 101 NE2 HIS A 101 CD2 -0.067
REMARK 500 HIS A 148 NE2 HIS A 148 CD2 -0.066
REMARK 500 HIS A 160 NE2 HIS A 160 CD2 -0.071
REMARK 500 HIS A 404 NE2 HIS A 404 CD2 -0.069
REMARK 500 HIS A 413 NE2 HIS A 413 CD2 -0.067
REMARK 500 HIS A 510 NE2 HIS A 510 CD2 -0.072
REMARK 500 HIS A 535 NE2 HIS A 535 CD2 -0.068
REMARK 500 HIS B 28 NE2 HIS B 28 CD2 -0.068
REMARK 500 HIS B 52 NE2 HIS B 52 CD2 -0.070
REMARK 500 HIS B 58 NE2 HIS B 58 CD2 -0.074
REMARK 500 HIS B 89 NE2 HIS B 89 CD2 -0.073
REMARK 500 HIS B 101 NE2 HIS B 101 CD2 -0.071
REMARK 500 HIS B 148 NE2 HIS B 148 CD2 -0.069
REMARK 500 HIS B 316 NE2 HIS B 316 CD2 -0.072
REMARK 500 HIS B 404 NE2 HIS B 404 CD2 -0.076
REMARK 500 HIS B 413 NE2 HIS B 413 CD2 -0.072
REMARK 500 HIS B 464 NE2 HIS B 464 CD2 -0.066
REMARK 500 HIS B 510 NE2 HIS B 510 CD2 -0.072
REMARK 500 HIS B 535 NE2 HIS B 535 CD2 -0.067
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 TRP A 24 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 24 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 174 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 174 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 182 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 182 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 218 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 287 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TRP A 345 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 345 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 346 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 346 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 356 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 356 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 447 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP B 24 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP B 24 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 174 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP B 174 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 182 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP B 182 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 345 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 345 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP B 346 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP B 346 CB - CG - CD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 TRP B 346 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 346 CG - CD2 - CE3 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP B 356 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 356 CB - CG - CD1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 TRP B 356 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 356 CG - CD2 - CE3 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 378 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP B 447 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 515 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 515 NE - CZ - NH2 ANGL. DEV. = -3.8 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 HIS A 101 62.46 37.87
REMARK 500 ASN A 263 -120.09 74.83
REMARK 500 ASP A 393 -152.75 -82.61
REMARK 500 ASN A 517 -7.94 -160.73
REMARK 500 HIS A 535 -33.45 -131.11
REMARK 500 HIS B 101 55.38 39.07
REMARK 500 ASN B 117 12.24 57.28
REMARK 500 SER B 185 28.22 -79.73
REMARK 500 ASN B 263 -123.53 94.48
REMARK 500 ASN B 286 45.14 -154.54
REMARK 500 ASP B 393 -154.60 -88.26
REMARK 500 PRO B 466 76.92 -66.79
REMARK 500 ASN B 517 11.75 -158.61
REMARK 500 ALA B 533 1.14 -66.30
REMARK 500 HIS B 535 -32.47 -136.73
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 MG A 610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 447 OD1
REMARK 620 2 ASN A 474 OD1 85.0
REMARK 620 3 GLN A 476 O 93.2 81.0
REMARK 620 4 TPP A 611 O1A 85.5 170.2 97.4
REMARK 620 5 TPP A 611 O3A 127.8 133.4 122.0 55.4
REMARK 620 6 TPP A 611 O3B 171.8 88.7 90.9 101.0 54.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 447 OD1
REMARK 620 2 ASN B 474 OD1 82.1
REMARK 620 3 GLN B 476 O 91.8 81.7
REMARK 620 4 TPP B 611 O3B 169.9 87.9 87.9
REMARK 620 5 TPP B 611 O3A 127.3 133.9 124.7 60.0
REMARK 620 6 TPP B 611 O1A 82.7 163.1 91.4 107.4 62.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 612
DBREF 1POW A 9 593 UNP P37063 POXB_LACPL 9 593
DBREF 1POW B 9 593 UNP P37063 POXB_LACPL 9 593
SEQRES 1 A 585 THR ASN ILE LEU ALA GLY ALA ALA VAL ILE LYS VAL LEU
SEQRES 2 A 585 GLU ALA TRP GLY VAL ASP HIS LEU TYR GLY ILE PRO GLY
SEQRES 3 A 585 GLY SER ILE ASN SER ILE MET ASP ALA LEU SER ALA GLU
SEQRES 4 A 585 ARG ASP ARG ILE HIS TYR ILE GLN VAL ARG HIS GLU GLU
SEQRES 5 A 585 VAL GLY ALA MET ALA ALA ALA ALA ASP ALA LYS LEU THR
SEQRES 6 A 585 GLY LYS ILE GLY VAL CYS PHE GLY SER ALA GLY PRO GLY
SEQRES 7 A 585 GLY THR HIS LEU MET ASN GLY LEU TYR ASP ALA ARG GLU
SEQRES 8 A 585 ASP HIS VAL PRO VAL LEU ALA LEU ILE GLY GLN PHE GLY
SEQRES 9 A 585 THR THR GLY MET ASN MET ASP THR PHE GLN GLU MET ASN
SEQRES 10 A 585 GLU ASN PRO ILE TYR ALA ASP VAL ALA ASP TYR ASN VAL
SEQRES 11 A 585 THR ALA VAL ASN ALA ALA THR LEU PRO HIS VAL ILE ASP
SEQRES 12 A 585 GLU ALA ILE ARG ARG ALA TYR ALA HIS GLN GLY VAL ALA
SEQRES 13 A 585 VAL VAL GLN ILE PRO VAL ASP LEU PRO TRP GLN GLN ILE
SEQRES 14 A 585 PRO ALA GLU ASP TRP TYR ALA SER ALA ASN SER TYR GLN
SEQRES 15 A 585 THR PRO LEU LEU PRO GLU PRO ASP VAL GLN ALA VAL THR
SEQRES 16 A 585 ARG LEU THR GLN THR LEU LEU ALA ALA GLU ARG PRO LEU
SEQRES 17 A 585 ILE TYR TYR GLY ILE GLY ALA ARG LYS ALA GLY LYS GLU
SEQRES 18 A 585 LEU GLU GLN LEU SER LYS THR LEU LYS ILE PRO LEU MET
SEQRES 19 A 585 SER THR TYR PRO ALA LYS GLY ILE VAL ALA ASP ARG TYR
SEQRES 20 A 585 PRO ALA TYR LEU GLY SER ALA ASN ARG VAL ALA GLN LYS
SEQRES 21 A 585 PRO ALA ASN GLU ALA LEU ALA GLN ALA ASP VAL VAL LEU
SEQRES 22 A 585 PHE VAL GLY ASN ASN TYR PRO PHE ALA GLU VAL SER LYS
SEQRES 23 A 585 ALA PHE LYS ASN THR ARG TYR PHE LEU GLN ILE ASP ILE
SEQRES 24 A 585 ASP PRO ALA LYS LEU GLY LYS ARG HIS LYS THR ASP ILE
SEQRES 25 A 585 ALA VAL LEU ALA ASP ALA GLN LYS THR LEU ALA ALA ILE
SEQRES 26 A 585 LEU ALA GLN VAL SER GLU ARG GLU SER THR PRO TRP TRP
SEQRES 27 A 585 GLN ALA ASN LEU ALA ASN VAL LYS ASN TRP ARG ALA TYR
SEQRES 28 A 585 LEU ALA SER LEU GLU ASP LYS GLN GLU GLY PRO LEU GLN
SEQRES 29 A 585 ALA TYR GLN VAL LEU ARG ALA VAL ASN LYS ILE ALA GLU
SEQRES 30 A 585 PRO ASP ALA ILE TYR SER ILE ASP VAL GLY ASP ILE ASN
SEQRES 31 A 585 LEU ASN ALA ASN ARG HIS LEU LYS LEU THR PRO SER ASN
SEQRES 32 A 585 ARG HIS ILE THR SER ASN LEU PHE ALA THR MET GLY VAL
SEQRES 33 A 585 GLY ILE PRO GLY ALA ILE ALA ALA LYS LEU ASN TYR PRO
SEQRES 34 A 585 GLU ARG GLN VAL PHE ASN LEU ALA GLY ASP GLY GLY ALA
SEQRES 35 A 585 SER MET THR MET GLN ASP LEU ALA THR GLN VAL GLN TYR
SEQRES 36 A 585 HIS LEU PRO VAL ILE ASN VAL VAL PHE THR ASN CYS GLN
SEQRES 37 A 585 TYR GLY PHE ILE LYS ASP GLU GLN GLU ASP THR ASN GLN
SEQRES 38 A 585 ASN ASP PHE ILE GLY VAL GLU PHE ASN ASP ILE ASP PHE
SEQRES 39 A 585 SER LYS ILE ALA ASP GLY VAL HIS MET GLN ALA PHE ARG
SEQRES 40 A 585 VAL ASN LYS ILE GLU GLN LEU PRO ASP VAL PHE GLU GLN
SEQRES 41 A 585 ALA LYS ALA ILE ALA GLN HIS GLU PRO VAL LEU ILE ASP
SEQRES 42 A 585 ALA VAL ILE THR GLY ASP ARG PRO LEU PRO ALA GLU LYS
SEQRES 43 A 585 LEU ARG LEU ASP SER ALA MET SER SER ALA ALA ASP ILE
SEQRES 44 A 585 GLU ALA PHE LYS GLN ARG TYR GLU ALA GLN ASP LEU GLN
SEQRES 45 A 585 PRO LEU SER THR TYR LEU LYS GLN PHE GLY LEU ASP ASP
SEQRES 1 B 585 THR ASN ILE LEU ALA GLY ALA ALA VAL ILE LYS VAL LEU
SEQRES 2 B 585 GLU ALA TRP GLY VAL ASP HIS LEU TYR GLY ILE PRO GLY
SEQRES 3 B 585 GLY SER ILE ASN SER ILE MET ASP ALA LEU SER ALA GLU
SEQRES 4 B 585 ARG ASP ARG ILE HIS TYR ILE GLN VAL ARG HIS GLU GLU
SEQRES 5 B 585 VAL GLY ALA MET ALA ALA ALA ALA ASP ALA LYS LEU THR
SEQRES 6 B 585 GLY LYS ILE GLY VAL CYS PHE GLY SER ALA GLY PRO GLY
SEQRES 7 B 585 GLY THR HIS LEU MET ASN GLY LEU TYR ASP ALA ARG GLU
SEQRES 8 B 585 ASP HIS VAL PRO VAL LEU ALA LEU ILE GLY GLN PHE GLY
SEQRES 9 B 585 THR THR GLY MET ASN MET ASP THR PHE GLN GLU MET ASN
SEQRES 10 B 585 GLU ASN PRO ILE TYR ALA ASP VAL ALA ASP TYR ASN VAL
SEQRES 11 B 585 THR ALA VAL ASN ALA ALA THR LEU PRO HIS VAL ILE ASP
SEQRES 12 B 585 GLU ALA ILE ARG ARG ALA TYR ALA HIS GLN GLY VAL ALA
SEQRES 13 B 585 VAL VAL GLN ILE PRO VAL ASP LEU PRO TRP GLN GLN ILE
SEQRES 14 B 585 PRO ALA GLU ASP TRP TYR ALA SER ALA ASN SER TYR GLN
SEQRES 15 B 585 THR PRO LEU LEU PRO GLU PRO ASP VAL GLN ALA VAL THR
SEQRES 16 B 585 ARG LEU THR GLN THR LEU LEU ALA ALA GLU ARG PRO LEU
SEQRES 17 B 585 ILE TYR TYR GLY ILE GLY ALA ARG LYS ALA GLY LYS GLU
SEQRES 18 B 585 LEU GLU GLN LEU SER LYS THR LEU LYS ILE PRO LEU MET
SEQRES 19 B 585 SER THR TYR PRO ALA LYS GLY ILE VAL ALA ASP ARG TYR
SEQRES 20 B 585 PRO ALA TYR LEU GLY SER ALA ASN ARG VAL ALA GLN LYS
SEQRES 21 B 585 PRO ALA ASN GLU ALA LEU ALA GLN ALA ASP VAL VAL LEU
SEQRES 22 B 585 PHE VAL GLY ASN ASN TYR PRO PHE ALA GLU VAL SER LYS
SEQRES 23 B 585 ALA PHE LYS ASN THR ARG TYR PHE LEU GLN ILE ASP ILE
SEQRES 24 B 585 ASP PRO ALA LYS LEU GLY LYS ARG HIS LYS THR ASP ILE
SEQRES 25 B 585 ALA VAL LEU ALA ASP ALA GLN LYS THR LEU ALA ALA ILE
SEQRES 26 B 585 LEU ALA GLN VAL SER GLU ARG GLU SER THR PRO TRP TRP
SEQRES 27 B 585 GLN ALA ASN LEU ALA ASN VAL LYS ASN TRP ARG ALA TYR
SEQRES 28 B 585 LEU ALA SER LEU GLU ASP LYS GLN GLU GLY PRO LEU GLN
SEQRES 29 B 585 ALA TYR GLN VAL LEU ARG ALA VAL ASN LYS ILE ALA GLU
SEQRES 30 B 585 PRO ASP ALA ILE TYR SER ILE ASP VAL GLY ASP ILE ASN
SEQRES 31 B 585 LEU ASN ALA ASN ARG HIS LEU LYS LEU THR PRO SER ASN
SEQRES 32 B 585 ARG HIS ILE THR SER ASN LEU PHE ALA THR MET GLY VAL
SEQRES 33 B 585 GLY ILE PRO GLY ALA ILE ALA ALA LYS LEU ASN TYR PRO
SEQRES 34 B 585 GLU ARG GLN VAL PHE ASN LEU ALA GLY ASP GLY GLY ALA
SEQRES 35 B 585 SER MET THR MET GLN ASP LEU ALA THR GLN VAL GLN TYR
SEQRES 36 B 585 HIS LEU PRO VAL ILE ASN VAL VAL PHE THR ASN CYS GLN
SEQRES 37 B 585 TYR GLY PHE ILE LYS ASP GLU GLN GLU ASP THR ASN GLN
SEQRES 38 B 585 ASN ASP PHE ILE GLY VAL GLU PHE ASN ASP ILE ASP PHE
SEQRES 39 B 585 SER LYS ILE ALA ASP GLY VAL HIS MET GLN ALA PHE ARG
SEQRES 40 B 585 VAL ASN LYS ILE GLU GLN LEU PRO ASP VAL PHE GLU GLN
SEQRES 41 B 585 ALA LYS ALA ILE ALA GLN HIS GLU PRO VAL LEU ILE ASP
SEQRES 42 B 585 ALA VAL ILE THR GLY ASP ARG PRO LEU PRO ALA GLU LYS
SEQRES 43 B 585 LEU ARG LEU ASP SER ALA MET SER SER ALA ALA ASP ILE
SEQRES 44 B 585 GLU ALA PHE LYS GLN ARG TYR GLU ALA GLN ASP LEU GLN
SEQRES 45 B 585 PRO LEU SER THR TYR LEU LYS GLN PHE GLY LEU ASP ASP
HET MG A 610 1
HET TPP A 611 26
HET FAD A 612 53
HET MG B 610 1
HET TPP B 611 26
HET FAD B 612 53
HETNAM MG MAGNESIUM ION
HETNAM TPP THIAMINE DIPHOSPHATE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 TPP 2(C12 H19 N4 O7 P2 S 1+)
FORMUL 5 FAD 2(C27 H33 N9 O15 P2)
FORMUL 9 HOH *120(H2 O)
HELIX 1 A1 GLY A 14 GLY A 25 1 12
HELIX 2 A2 ILE A 37 SER A 45 1 9
HELIX 3 A3 GLU A 59 THR A 73 1 15
HELIX 4 A4 GLY A 84 HIS A 89 1 6
HELIX 5 A5 LEU A 90 HIS A 101 1 12
HELIX 6 A6 THR A 145 GLN A 161 1 17
HELIX 7 A7 ASP A 198 ALA A 212 1 15
HELIX 8 A8 ALA A 226 LYS A 238 1 13
HELIX 9 A9 LYS A 268 GLN A 276 1 9
HELIX 10 A10 ASP A 325 ALA A 335 1 11
HELIX 11 A11 THR A 343 ASP A 365 1 23
HELIX 12 A12 ALA A 373 ALA A 384 1 12
HELIX 13 A13 ASP A 396 LEU A 405 1 10
HELIX 14 A14 GLY A 425 TYR A 436 1 12
HELIX 15 A15 GLY A 446 MET A 454 1 9
HELIX 16 A16 ALA A 458 HIS A 464 1 7
HELIX 17 A17 TYR A 477 ASN A 488 1 12
HELIX 18 A18 ASP A 501 HIS A 510 1 10
HELIX 19 A19 LEU A 522 ALA A 533 1 12
HELIX 20 A20 SER A 563 GLU A 575 1 13
HELIX 21 A21 LEU A 582 GLY A 590 1 9
HELIX 22 B1 GLY B 14 GLY B 25 1 12
HELIX 23 B2 ILE B 37 SER B 45 1 9
HELIX 24 B3 GLU B 59 THR B 73 1 15
HELIX 25 B4 GLY B 84 HIS B 89 1 6
HELIX 26 B5 LEU B 90 HIS B 101 1 12
HELIX 27 B6 THR B 145 GLN B 161 1 17
HELIX 28 B7 ASP B 198 ALA B 212 1 15
HELIX 29 B8 ALA B 226 LYS B 238 1 13
HELIX 30 B9 LYS B 268 GLN B 276 1 9
HELIX 31 B10 ASP B 325 ALA B 335 1 11
HELIX 32 B11 THR B 343 ASP B 365 1 23
HELIX 33 B12 ALA B 373 ALA B 384 1 12
HELIX 34 B13 ASP B 396 LEU B 405 1 10
HELIX 35 B14 GLY B 425 TYR B 436 1 12
HELIX 36 B15 GLY B 446 MET B 454 1 9
HELIX 37 B16 ALA B 458 HIS B 464 1 7
HELIX 38 B17 TYR B 477 ASN B 488 1 12
HELIX 39 B18 ASP B 501 HIS B 510 1 10
HELIX 40 B19 LEU B 522 ALA B 533 1 12
HELIX 41 B20 SER B 563 GLU B 575 1 13
HELIX 42 B21 LEU B 582 GLY B 590 1 9
SHEET 1 A0 2 THR A 9 ALA A 13 0
SHEET 2 A0 2 GLN A 175 ALA A 179 -1 O GLN A 175 N ALA A 13
SHEET 1 A1 6 HIS A 52 VAL A 56 0
SHEET 2 A1 6 ASP A 27 GLY A 31 1 O ASP A 27 N HIS A 52
SHEET 3 A1 6 GLY A 77 GLY A 81 1 O VAL A 78 N TYR A 30
SHEET 4 A1 6 PRO A 103 GLN A 110 1 O PRO A 103 N GLY A 77
SHEET 5 A1 6 GLY A 162 VAL A 170 1 O GLY A 162 N VAL A 104
SHEET 6 A1 6 TYR A 136 ALA A 140 1 N TYR A 136 O VAL A 163
SHEET 1 A2 6 ALA A 257 GLY A 260 0
SHEET 2 A2 6 PRO A 240 THR A 244 1 N LEU A 241 O ALA A 257
SHEET 3 A2 6 LEU A 216 GLY A 220 1 N ILE A 217 O PRO A 240
SHEET 4 A2 6 ASP A 278 GLY A 284 1 O VAL A 279 N LEU A 216
SHEET 5 A2 6 TYR A 301 ASP A 306 1 N TYR A 301 O ASP A 278
SHEET 6 A2 6 ILE A 320 ALA A 324 1 O ILE A 320 N GLN A 304
SHEET 1 A3 6 ARG A 412 ILE A 414 0
SHEET 2 A3 6 ALA A 388 ASP A 393 1 O ALA A 388 N ARG A 412
SHEET 3 A3 6 GLN A 440 ALA A 445 1 O GLN A 440 N ILE A 389
SHEET 4 A3 6 VAL A 467 THR A 473 1 N ILE A 468 O VAL A 441
SHEET 5 A3 6 VAL A 538 ILE A 544 1 N VAL A 538 O VAL A 467
SHEET 6 A3 6 GLN A 512 VAL A 516 1 O GLN A 512 N LEU A 539
SHEET 1 B0 2 THR B 9 ALA B 13 0
SHEET 2 B0 2 GLN B 175 ALA B 179 -1 O GLN B 175 N ALA B 13
SHEET 1 B1 6 HIS B 52 VAL B 56 0
SHEET 2 B1 6 ASP B 27 GLY B 31 1 O ASP B 27 N HIS B 52
SHEET 3 B1 6 GLY B 77 GLY B 81 1 O VAL B 78 N TYR B 30
SHEET 4 B1 6 PRO B 103 GLN B 110 1 O PRO B 103 N GLY B 77
SHEET 5 B1 6 GLY B 162 VAL B 170 1 O GLY B 162 N VAL B 104
SHEET 6 B1 6 TYR B 136 ALA B 140 1 N TYR B 136 O VAL B 163
SHEET 1 B2 6 ALA B 257 GLY B 260 0
SHEET 2 B2 6 PRO B 240 THR B 244 1 N LEU B 241 O ALA B 257
SHEET 3 B2 6 LEU B 216 GLY B 220 1 N ILE B 217 O PRO B 240
SHEET 4 B2 6 ASP B 278 GLY B 284 1 O VAL B 279 N LEU B 216
SHEET 5 B2 6 TYR B 301 ASP B 306 1 N TYR B 301 O ASP B 278
SHEET 6 B2 6 ILE B 320 ALA B 324 1 O ILE B 320 N GLN B 304
SHEET 1 B3 6 ARG B 412 ILE B 414 0
SHEET 2 B3 6 ALA B 388 ASP B 393 1 O ALA B 388 N ARG B 412
SHEET 3 B3 6 GLN B 440 ALA B 445 1 O GLN B 440 N ILE B 389
SHEET 4 B3 6 VAL B 467 THR B 473 1 N ILE B 468 O VAL B 441
SHEET 5 B3 6 VAL B 538 ILE B 544 1 N VAL B 538 O VAL B 467
SHEET 6 B3 6 GLN B 512 VAL B 516 1 O GLN B 512 N LEU B 539
LINK OD1 ASP A 447 MG MG A 610 1555 1555 2.01
LINK OD1 ASN A 474 MG MG A 610 1555 1555 2.01
LINK O GLN A 476 MG MG A 610 1555 1555 1.99
LINK MG MG A 610 O1A TPP A 611 1555 1555 1.94
LINK MG MG A 610 O3A TPP A 611 1555 1555 2.99
LINK MG MG A 610 O3B TPP A 611 1555 1555 1.85
LINK OD1 ASP B 447 MG MG B 610 1555 1555 2.01
LINK OD1 ASN B 474 MG MG B 610 1555 1555 2.02
LINK O GLN B 476 MG MG B 610 1555 1555 2.03
LINK MG MG B 610 O3B TPP B 611 1555 1555 1.87
LINK MG MG B 610 O3A TPP B 611 1555 1555 2.65
LINK MG MG B 610 O1A TPP B 611 1555 1555 1.91
SITE 1 AC1 4 ASP A 447 ASN A 474 GLN A 476 TPP A 611
SITE 1 AC2 4 ASP B 447 ASN B 474 GLN B 476 TPP B 611
SITE 1 AC3 22 PRO A 33 GLU A 59 SER A 82 PRO A 85
SITE 2 AC3 22 HIS A 89 GLN A 122 ASP A 396 ALA A 420
SITE 3 AC3 22 MET A 422 ASP A 447 GLY A 448 GLY A 449
SITE 4 AC3 22 ASN A 474 GLN A 476 TYR A 477 GLY A 478
SITE 5 AC3 22 PHE A 479 ILE A 480 MG A 610 HOH A 617
SITE 6 AC3 22 HOH A 659 HOH A 664
SITE 1 AC4 27 HIS A 101 PHE A 121 GLY A 220 ILE A 221
SITE 2 AC4 27 GLY A 222 THR A 244 TYR A 245 ALA A 262
SITE 3 AC4 27 ASN A 263 ARG A 264 VAL A 265 GLY A 284
SITE 4 AC4 27 ASN A 285 ASN A 286 TYR A 287 PRO A 288
SITE 5 AC4 27 PHE A 289 ASP A 306 ILE A 307 LYS A 311
SITE 6 AC4 27 ASP A 325 ALA A 326 ASN A 398 SER A 416
SITE 7 AC4 27 ASN A 417 HOH A 614 HOH A 635
SITE 1 AC5 24 PRO B 33 GLU B 59 SER B 82 PRO B 85
SITE 2 AC5 24 HIS B 89 GLN B 122 ASP B 396 ALA B 420
SITE 3 AC5 24 MET B 422 GLY B 446 ASP B 447 GLY B 448
SITE 4 AC5 24 GLY B 449 MET B 452 ASN B 474 GLN B 476
SITE 5 AC5 24 TYR B 477 GLY B 478 PHE B 479 ILE B 480
SITE 6 AC5 24 MG B 610 HOH B 635 HOH B 651 HOH B 662
SITE 1 AC6 27 HIS B 101 PHE B 121 GLY B 220 ILE B 221
SITE 2 AC6 27 GLY B 222 THR B 244 TYR B 245 PRO B 246
SITE 3 AC6 27 ALA B 262 ASN B 263 ARG B 264 VAL B 265
SITE 4 AC6 27 GLY B 284 ASN B 285 ASN B 286 TYR B 287
SITE 5 AC6 27 PRO B 288 PHE B 289 ASP B 306 ILE B 307
SITE 6 AC6 27 LYS B 311 ASP B 325 ALA B 326 ASN B 398
SITE 7 AC6 27 SER B 416 ASN B 417 HOH B 640
CRYST1 121.600 155.400 167.100 90.00 90.00 90.00 C 2 2 21 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 0.008224 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005984 0.00000
MTRIX1 1 -0.999948 0.008221 -0.006109 -9.91500 1
MTRIX2 1 -0.001108 -0.679808 -0.733389 130.53011 1
MTRIX3 1 -0.010182 -0.733344 0.679782 56.62200 1
(ATOM LINES ARE NOT SHOWN.)
END
