HEADER OXIDOREDUCTASE 29-OCT-07 3B6D
TITLE CRYSTAL STRUCTURE OF STREPTOMYCES CHOLESTEROL OXIDASE H447Q/E361Q
TITLE 2 MUTANT (1.2A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHOD;
COMPND 5 EC: 1.1.3.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: FAD COFACTOR NON-COVALENTLY BOUND TO THE ENZYME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP.;
SOURCE 3 ORGANISM_TAXID: 74576;
SOURCE 4 STRAIN: SA-COO;
SOURCE 5 GENE: CHOA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCO202
KEYWDS FLAVOENZYME, FLAVIN, OXIDOREDUCTASE, FLAVIN ACTIVATION, CHOLESTEROL
KEYWDS 2 OXIDASE, CHOLESTEROL METABOLISM, FAD, FLAVOPROTEIN, LIPID
KEYWDS 3 METABOLISM, SECRETED, STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.Y.LYUBIMOV,A.VRIELINK
REVDAT 5 01-NOV-23 3B6D 1 REMARK
REVDAT 4 10-NOV-21 3B6D 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3B6D 1 VERSN
REVDAT 2 24-FEB-09 3B6D 1 VERSN
REVDAT 1 18-DEC-07 3B6D 0
JRNL AUTH A.Y.LYUBIMOV,K.HEARD,H.TANG,N.S.SAMPSON,A.VRIELINK
JRNL TITL DISTORTION OF FLAVIN GEOMETRY IS LINKED TO LIGAND BINDING IN
JRNL TITL 2 CHOLESTEROL OXIDASE
JRNL REF PROTEIN SCI. V. 16 2647 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 18029419
JRNL DOI 10.1110/PS.073168207
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.133
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.132
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6605
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.125
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.124
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 5778
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 115111
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3819
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 560
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 4427.8
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 3714.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 73
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 43986
REMARK 3 NUMBER OF RESTRAINTS : 62007
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.032
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.068
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.075
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.020
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.040
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.094
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3B6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 132078
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 60.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1MXT; ADP, WATERS, LIGANDS AND ACTIVE
REMARK 200 SITE SIDECHAINS REMOVED FROM STARTING MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 75MM MNSO4, 100MM
REMARK 280 CACODYLATE PH 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 36.57000
REMARK 290 SMTRY3 2 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 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: 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 ASP A 6
REMARK 465 ASN A 7
REMARK 465 GLY A 8
REMARK 465 THR A 507
REMARK 465 ALA A 508
REMARK 465 SER A 509
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 ARG A 146 NH1 NH2
REMARK 470 LYS A 183 CD CE NZ
REMARK 470 LYS A 241 NZ
REMARK 470 LYS A 273 NZ
REMARK 470 THR A 435 OG1 CG2
REMARK 470 GLN A 436 CG CD OE1 NE2
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 CYS A 56 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 87 CD - NE - CZ ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLY A 259 CA - C - O ANGL. DEV. = -11.0 DEGREES
REMARK 500 GLY A 259 CA - C - N ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 300 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 PHE A 359 CB - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TYR A 390 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR A 390 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 396 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 396 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 403 CD - NE - CZ ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 419 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 429 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 429 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 500 NE - CZ - NH2 ANGL. DEV. = -4.4 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 THR A 18 31.00 -145.07
REMARK 500 ASN A 46 12.79 -143.81
REMARK 500 ASN A 46 13.01 -143.81
REMARK 500 ASP A 62 -159.51 -141.46
REMARK 500 ARG A 146 -57.91 -126.23
REMARK 500 ARG A 156 35.36 72.61
REMARK 500 SER A 211 -73.18 -137.99
REMARK 500 VAL A 217 -53.80 -168.28
REMARK 500 VAL A 217 -58.12 -168.28
REMARK 500 THR A 231 -94.66 -108.95
REMARK 500 PRO A 320 30.32 -89.13
REMARK 500 LEU A 437 106.46 -49.82
REMARK 500 LYS A 456 -68.70 -109.45
REMARK 500 LYS A 456 -55.50 -120.75
REMARK 500 ASP A 474 -161.78 -124.77
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 SO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAE A 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B3R RELATED DB: PDB
REMARK 900 THE SAME MUTANT PROTEIN WITH GLYCEROL BOUND IN ACTIVE SITE
DBREF 3B6D A 6 509 UNP P12676 CHOD_STRS0 43 546
SEQADV 3B6D GLN A 361 UNP P12676 GLU 398 ENGINEERED MUTATION
SEQADV 3B6D GLN A 447 UNP P12676 HIS 484 ENGINEERED MUTATION
SEQRES 1 A 504 ASP ASN GLY GLY TYR VAL PRO ALA VAL VAL ILE GLY THR
SEQRES 2 A 504 GLY TYR GLY ALA ALA VAL SER ALA LEU ARG LEU GLY GLU
SEQRES 3 A 504 ALA GLY VAL GLN THR LEU MET LEU GLU MET GLY GLN LEU
SEQRES 4 A 504 TRP ASN GLN PRO GLY PRO ASP GLY ASN ILE PHE CYS GLY
SEQRES 5 A 504 MET LEU ASN PRO ASP LYS ARG SER SER TRP PHE LYS ASN
SEQRES 6 A 504 ARG THR GLU ALA PRO LEU GLY SER PHE LEU TRP LEU ASP
SEQRES 7 A 504 VAL VAL ASN ARG ASN ILE ASP PRO TYR ALA GLY VAL LEU
SEQRES 8 A 504 ASP ARG VAL ASN TYR ASP GLN MET SER VAL TYR VAL GLY
SEQRES 9 A 504 ARG GLY VAL GLY GLY GLY SER LEU VAL ASN GLY GLY MET
SEQRES 10 A 504 ALA VAL GLU PRO LYS ARG SER TYR PHE GLU GLU ILE LEU
SEQRES 11 A 504 PRO ARG VAL ASP SER SER GLU MET TYR ASP ARG TYR PHE
SEQRES 12 A 504 PRO ARG ALA ASN SER MET LEU ARG VAL ASN HIS ILE ASP
SEQRES 13 A 504 THR LYS TRP PHE GLU ASP THR GLU TRP TYR LYS PHE ALA
SEQRES 14 A 504 ARG VAL SER ARG GLU GLN ALA GLY LYS ALA GLY LEU GLY
SEQRES 15 A 504 THR VAL PHE VAL PRO ASN VAL TYR ASP PHE GLY TYR MET
SEQRES 16 A 504 GLN ARG GLU ALA ALA GLY GLU VAL PRO LYS SER ALA LEU
SEQRES 17 A 504 ALA THR GLU VAL ILE TYR GLY ASN ASN HIS GLY LYS GLN
SEQRES 18 A 504 SER LEU ASP LYS THR TYR LEU ALA ALA ALA LEU GLY THR
SEQRES 19 A 504 GLY LYS VAL THR ILE GLN THR LEU HIS GLN VAL LYS THR
SEQRES 20 A 504 ILE ARG GLN THR LYS ASP GLY GLY TYR ALA LEU THR VAL
SEQRES 21 A 504 GLU GLN LYS ASP THR ASP GLY LYS LEU LEU ALA THR LYS
SEQRES 22 A 504 GLU ILE SER CYS ARG TYR LEU PHE LEU GLY ALA GLY SER
SEQRES 23 A 504 LEU GLY SER THR GLU LEU LEU VAL ARG ALA ARG ASP THR
SEQRES 24 A 504 GLY THR LEU PRO ASN LEU ASN SER GLU VAL GLY ALA GLY
SEQRES 25 A 504 TRP GLY PRO ASN GLY ASN ILE MET THR ALA ARG ALA ASN
SEQRES 26 A 504 HIS MET TRP ASN PRO THR GLY ALA HIS GLN SER SER ILE
SEQRES 27 A 504 PRO ALA LEU GLY ILE ASP ALA TRP ASP ASN SER ASP SER
SEQRES 28 A 504 SER VAL PHE ALA GLN ILE ALA PRO MET PRO ALA GLY LEU
SEQRES 29 A 504 GLU THR TRP VAL SER LEU TYR LEU ALA ILE THR LYS ASN
SEQRES 30 A 504 PRO GLN ARG GLY THR PHE VAL TYR ASP ALA ALA THR ASP
SEQRES 31 A 504 ARG ALA LYS LEU ASN TRP THR ARG ASP GLN ASN ALA PRO
SEQRES 32 A 504 ALA VAL ASN ALA ALA LYS ALA LEU PHE ASP ARG ILE ASN
SEQRES 33 A 504 LYS ALA ASN GLY THR ILE TYR ARG TYR ASP LEU PHE GLY
SEQRES 34 A 504 THR GLN LEU LYS ALA PHE ALA ASP ASP PHE CYS TYR GLN
SEQRES 35 A 504 PRO LEU GLY GLY CYS VAL LEU GLY LYS ALA THR ASP ASP
SEQRES 36 A 504 TYR GLY ARG VAL ALA GLY TYR LYS ASN LEU TYR VAL THR
SEQRES 37 A 504 ASP GLY SER LEU ILE PRO GLY SER VAL GLY VAL ASN PRO
SEQRES 38 A 504 PHE VAL THR ILE THR ALA LEU ALA GLU ARG ASN VAL GLU
SEQRES 39 A 504 ARG ILE ILE LYS GLN ASP VAL THR ALA SER
HET SO4 A 511 5
HET FAE A 510 85
HETNAM SO4 SULFATE ION
HETNAM FAE FLAVIN-N7 PROTONATED-ADENINE DINUCLEOTIDE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 FAE C27 H34 N9 O15 P2 1+
FORMUL 4 HOH *560(H2 O)
HELIX 1 1 GLY A 19 ALA A 32 1 14
HELIX 2 2 ASP A 62 SER A 66 5 5
HELIX 3 3 SER A 78 ASP A 83 1 6
HELIX 4 4 VAL A 84 ASN A 86 5 3
HELIX 5 5 GLY A 113 VAL A 118 5 6
HELIX 6 6 LYS A 127 LEU A 135 1 9
HELIX 7 7 ASP A 139 ARG A 146 1 8
HELIX 8 8 ARG A 146 ARG A 156 1 11
HELIX 9 9 ASP A 161 THR A 168 1 8
HELIX 10 10 TYR A 171 ALA A 184 1 14
HELIX 11 11 ASP A 196 ALA A 205 1 10
HELIX 12 12 SER A 211 THR A 215 5 5
HELIX 13 13 THR A 231 THR A 239 1 9
HELIX 14 14 ALA A 289 THR A 304 1 16
HELIX 15 15 THR A 402 GLN A 405 5 4
HELIX 16 16 ASN A 406 GLY A 425 1 20
HELIX 17 17 ASP A 474 ILE A 478 5 5
HELIX 18 18 PRO A 486 VAL A 506 1 21
SHEET 1 A 6 VAL A 242 THR A 246 0
SHEET 2 A 6 THR A 36 GLU A 40 1 N MET A 38 O THR A 243
SHEET 3 A 6 TYR A 10 ILE A 16 1 N VAL A 15 O LEU A 37
SHEET 4 A 6 LEU A 274 LEU A 287 1 O PHE A 286 N VAL A 14
SHEET 5 A 6 TYR A 261 LYS A 268 -1 N LEU A 263 O ILE A 280
SHEET 6 A 6 HIS A 248 GLN A 255 -1 N LYS A 251 O THR A 264
SHEET 1 B 5 VAL A 242 THR A 246 0
SHEET 2 B 5 THR A 36 GLU A 40 1 N MET A 38 O THR A 243
SHEET 3 B 5 TYR A 10 ILE A 16 1 N VAL A 15 O LEU A 37
SHEET 4 B 5 LEU A 274 LEU A 287 1 O PHE A 286 N VAL A 14
SHEET 5 B 5 LEU A 470 VAL A 472 1 O TYR A 471 N LEU A 287
SHEET 1 C 3 LEU A 96 ASN A 100 0
SHEET 2 C 3 SER A 105 GLY A 109 -1 O VAL A 106 N VAL A 99
SHEET 3 C 3 PHE A 444 CYS A 445 1 O CYS A 445 N TYR A 107
SHEET 1 D 6 THR A 188 PHE A 190 0
SHEET 2 D 6 LEU A 346 ALA A 350 -1 O GLY A 347 N VAL A 189
SHEET 3 D 6 VAL A 358 ALA A 363 -1 O ALA A 360 N ILE A 348
SHEET 4 D 6 VAL A 373 THR A 380 -1 O LEU A 377 N GLN A 361
SHEET 5 D 6 ILE A 324 ALA A 329 -1 N ILE A 324 O ALA A 378
SHEET 6 D 6 ILE A 427 TYR A 428 -1 O ILE A 427 N ALA A 329
SHEET 1 E 6 THR A 188 PHE A 190 0
SHEET 2 E 6 LEU A 346 ALA A 350 -1 O GLY A 347 N VAL A 189
SHEET 3 E 6 VAL A 358 ALA A 363 -1 O ALA A 360 N ILE A 348
SHEET 4 E 6 VAL A 373 THR A 380 -1 O LEU A 377 N GLN A 361
SHEET 5 E 6 ILE A 324 ALA A 329 -1 N ILE A 324 O ALA A 378
SHEET 6 E 6 PHE A 440 ALA A 441 -1 O ALA A 441 N MET A 325
SHEET 1 F 2 PHE A 388 ASP A 391 0
SHEET 2 F 2 ARG A 396 LEU A 399 -1 O LYS A 398 N VAL A 389
SITE 1 AC1 7 GLU A 179 GLN A 180 ARG A 283 HIS A 331
SITE 2 AC1 7 TRP A 333 ASN A 334 HOH A 719
SITE 1 AC2 42 ILE A 16 GLY A 17 GLY A 19 TYR A 20
SITE 2 AC2 42 GLY A 21 LEU A 39 GLU A 40 MET A 41
SITE 3 AC2 42 TYR A 107 GLY A 109 ARG A 110 GLY A 111
SITE 4 AC2 42 GLY A 114 GLY A 115 ASN A 119 GLY A 120
SITE 5 AC2 42 GLY A 121 MET A 122 ILE A 218 HIS A 248
SITE 6 AC2 42 GLN A 249 VAL A 250 GLY A 288 ALA A 289
SITE 7 AC2 42 GLY A 290 TYR A 446 ASP A 474 GLY A 475
SITE 8 AC2 42 ASN A 485 PRO A 486 PHE A 487 HOH A 512
SITE 9 AC2 42 HOH A 514 HOH A 517 HOH A 521 HOH A 522
SITE 10 AC2 42 HOH A 539 HOH A 541 HOH A 554 HOH A 581
SITE 11 AC2 42 HOH A 715 HOH A 998
CRYST1 51.300 73.140 63.140 90.00 105.05 90.00 P 1 21 1 2
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 0.019493 0.000000 0.005241 0.00000
SCALE2 0.000000 0.013672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016400 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
