HEADER OXIDOREDUCTASE 25-MAR-08 3CNJ
TITLE CHOLESTEROL OXIDASE FROM STREPTOMYCES SP. F359W MUTANT (0.95A)
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, OXYGEN TUNNEL, CHOLESTEROL
KEYWDS 2 OXIDASE, CHOLESTEROL METABOLISM, FAD, FLAVOPROTEIN, LIPID
KEYWDS 3 METABOLISM, SECRETED, STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.Y.LYUBIMOV,L.BRAMMER,A.VRIELINK
REVDAT 6 01-NOV-23 3CNJ 1 REMARK
REVDAT 5 10-NOV-21 3CNJ 1 REMARK SEQADV
REVDAT 4 13-JUL-11 3CNJ 1 VERSN
REVDAT 3 24-FEB-09 3CNJ 1 VERSN
REVDAT 2 10-JUN-08 3CNJ 1 JRNL
REVDAT 1 29-APR-08 3CNJ 0
JRNL AUTH L.CHEN,A.Y.LYUBIMOV,L.BRAMMER,A.VRIELINK,N.S.SAMPSON
JRNL TITL THE BINDING AND RELEASE OF OXYGEN AND HYDROGEN PEROXIDE ARE
JRNL TITL 2 DIRECTED BY A HYDROPHOBIC TUNNEL IN CHOLESTEROL OXIDASE
JRNL REF BIOCHEMISTRY V. 47 5368 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18410129
JRNL DOI 10.1021/BI800228W
REMARK 2
REMARK 2 RESOLUTION. 0.95 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) : 0.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
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) : 0.151
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.140
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 13529
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 270322
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.143
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.132
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 11953
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 238784
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3828
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 695
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 4549.3
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 3545.7
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 101
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 48651
REMARK 3 NUMBER OF RESTRAINTS : 71611
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.033
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.084
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.089
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.028
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.041
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.104
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:
REMARK 3 HYDROGEN ATOMS REFINED USING THE "RIDING" MODEL, WITH BOND LENGTH
REMARK 3 AND ANGLE CONSTRAINTS. HYDROGEN ATOMS ARE NOT INCLUDED IN THE
REMARK 3 DEPOSITED COORDINATE FILE.
REMARK 3 CLOSE CONTACTS ARE CAUSED BY PARTIAL WATERS IN CLOSE PROXIMITY TO
REMARK 3 ALTERNATE CONFORMATIONS OF DISORDERED RESIDUES. THEY WERE MODELED
REMARK 3 MANUALLY AND THEIR POSITIONS WERE CONFIRMED THROUGH SEVERAL ROUNDS
REMARK 3 OF REFINEMENT.
REMARK 4
REMARK 4 3CNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046989.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 270322
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.950
REMARK 200 RESOLUTION RANGE LOW (A) : 46.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.220
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1MXT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MANGANESE SULFATE,
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 36.43500
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 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 LYS A 163 CE NZ
REMARK 470 LYS A 183 CE NZ
REMARK 470 LYS A 241 NZ
REMARK 470 THR A 435 OG1 CG2
REMARK 470 GLN A 436 CG CD OE1 NE2
REMARK 470 VAL A 488 CG1 CG2
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 OD2 ASP A 404 O HOH A 940 2.05
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 CYS A 56 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 MET A 122 CG - SD - CE ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ASP A 139 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 145 CB - CG - OD1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 156 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 GLY A 259 CA - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 352 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 PHE A 388 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 390 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR A 390 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 403 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 429 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 429 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 500 NE - CZ - NH2 ANGL. DEV. = -7.5 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 30.16 -143.15
REMARK 500 ASN A 46 13.21 -144.73
REMARK 500 ASN A 46 13.03 -144.73
REMARK 500 ASN A 60 53.76 -146.54
REMARK 500 ARG A 146 -54.87 -125.30
REMARK 500 ARG A 146 -56.78 -122.45
REMARK 500 ARG A 156 38.65 70.59
REMARK 500 SER A 211 -72.86 -139.45
REMARK 500 VAL A 217 -53.85 -168.72
REMARK 500 THR A 231 -100.25 -111.91
REMARK 500 ALA A 350 40.63 -107.73
REMARK 500 ASN A 353 -6.13 81.99
REMARK 500 CYS A 452 55.93 -143.34
REMARK 500 LYS A 456 -54.89 -124.33
REMARK 500 ASP A 474 -160.01 -124.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 259 GLY A 260 148.33
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 SO4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MXT RELATED DB: PDB
REMARK 900 WT CHOLESTEROL OXIDASE AT ATOMIC RESOLUTION
DBREF 3CNJ A 8 506 UNP P12676 CHOD_STRS0 45 543
SEQADV 3CNJ TRP A 359 UNP P12676 PHE 396 ENGINEERED MUTATION
SEQRES 1 A 499 GLY GLY TYR VAL PRO ALA VAL VAL ILE GLY THR GLY TYR
SEQRES 2 A 499 GLY ALA ALA VAL SER ALA LEU ARG LEU GLY GLU ALA GLY
SEQRES 3 A 499 VAL GLN THR LEU MET LEU GLU MET GLY GLN LEU TRP ASN
SEQRES 4 A 499 GLN PRO GLY PRO ASP GLY ASN ILE PHE CYS GLY MET LEU
SEQRES 5 A 499 ASN PRO ASP LYS ARG SER SER TRP PHE LYS ASN ARG THR
SEQRES 6 A 499 GLU ALA PRO LEU GLY SER PHE LEU TRP LEU ASP VAL VAL
SEQRES 7 A 499 ASN ARG ASN ILE ASP PRO TYR ALA GLY VAL LEU ASP ARG
SEQRES 8 A 499 VAL ASN TYR ASP GLN MET SER VAL TYR VAL GLY ARG GLY
SEQRES 9 A 499 VAL GLY GLY GLY SER LEU VAL ASN GLY GLY MET ALA VAL
SEQRES 10 A 499 GLU PRO LYS ARG SER TYR PHE GLU GLU ILE LEU PRO ARG
SEQRES 11 A 499 VAL ASP SER SER GLU MET TYR ASP ARG TYR PHE PRO ARG
SEQRES 12 A 499 ALA ASN SER MET LEU ARG VAL ASN HIS ILE ASP THR LYS
SEQRES 13 A 499 TRP PHE GLU ASP THR GLU TRP TYR LYS PHE ALA ARG VAL
SEQRES 14 A 499 SER ARG GLU GLN ALA GLY LYS ALA GLY LEU GLY THR VAL
SEQRES 15 A 499 PHE VAL PRO ASN VAL TYR ASP PHE GLY TYR MET GLN ARG
SEQRES 16 A 499 GLU ALA ALA GLY GLU VAL PRO LYS SER ALA LEU ALA THR
SEQRES 17 A 499 GLU VAL ILE TYR GLY ASN ASN HIS GLY LYS GLN SER LEU
SEQRES 18 A 499 ASP LYS THR TYR LEU ALA ALA ALA LEU GLY THR GLY LYS
SEQRES 19 A 499 VAL THR ILE GLN THR LEU HIS GLN VAL LYS THR ILE ARG
SEQRES 20 A 499 GLN THR LYS ASP GLY GLY TYR ALA LEU THR VAL GLU GLN
SEQRES 21 A 499 LYS ASP THR ASP GLY LYS LEU LEU ALA THR LYS GLU ILE
SEQRES 22 A 499 SER CYS ARG TYR LEU PHE LEU GLY ALA GLY SER LEU GLY
SEQRES 23 A 499 SER THR GLU LEU LEU VAL ARG ALA ARG ASP THR GLY THR
SEQRES 24 A 499 LEU PRO ASN LEU ASN SER GLU VAL GLY ALA GLY TRP GLY
SEQRES 25 A 499 PRO ASN GLY ASN ILE MET THR ALA ARG ALA ASN HIS MET
SEQRES 26 A 499 TRP ASN PRO THR GLY ALA HIS GLN SER SER ILE PRO ALA
SEQRES 27 A 499 LEU GLY ILE ASP ALA TRP ASP ASN SER ASP SER SER VAL
SEQRES 28 A 499 TRP ALA GLU ILE ALA PRO MET PRO ALA GLY LEU GLU THR
SEQRES 29 A 499 TRP VAL SER LEU TYR LEU ALA ILE THR LYS ASN PRO GLN
SEQRES 30 A 499 ARG GLY THR PHE VAL TYR ASP ALA ALA THR ASP ARG ALA
SEQRES 31 A 499 LYS LEU ASN TRP THR ARG ASP GLN ASN ALA PRO ALA VAL
SEQRES 32 A 499 ASN ALA ALA LYS ALA LEU PHE ASP ARG ILE ASN LYS ALA
SEQRES 33 A 499 ASN GLY THR ILE TYR ARG TYR ASP LEU PHE GLY THR GLN
SEQRES 34 A 499 LEU LYS ALA PHE ALA ASP ASP PHE CYS TYR HIS PRO LEU
SEQRES 35 A 499 GLY GLY CYS VAL LEU GLY LYS ALA THR ASP ASP TYR GLY
SEQRES 36 A 499 ARG VAL ALA GLY TYR LYS ASN LEU TYR VAL THR ASP GLY
SEQRES 37 A 499 SER LEU ILE PRO GLY SER VAL GLY VAL ASN PRO PHE VAL
SEQRES 38 A 499 THR ILE THR ALA LEU ALA GLU ARG ASN VAL GLU ARG ILE
SEQRES 39 A 499 ILE LYS GLN ASP VAL
HET SO4 A 511 5
HET SO4 A 512 5
HET FAD A 510 53
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 FAD C27 H33 N9 O15 P2
FORMUL 5 HOH *695(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 LEU A 155 1 10
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 4 GLY A 9 TYR A 10 0
SHEET 2 A 4 LEU A 274 CYS A 282 1 O SER A 281 N GLY A 9
SHEET 3 A 4 TYR A 261 LYS A 268 -1 N GLN A 267 O LEU A 275
SHEET 4 A 4 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 GLN A 245
SHEET 3 B 5 ALA A 13 ILE A 16 1 N VAL A 15 O LEU A 37
SHEET 4 B 5 TYR A 284 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 GLU 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 GLU 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 8 GLU A 179 GLN A 180 ARG A 283 HIS A 331
SITE 2 AC1 8 TRP A 333 ASN A 334 HOH A 612 HOH A1161
SITE 1 AC2 3 ARG A 146 ARG A 150 HOH A 578
SITE 1 AC3 42 ILE A 16 GLY A 17 GLY A 19 TYR A 20
SITE 2 AC3 42 GLY A 21 LEU A 39 GLU A 40 MET A 41
SITE 3 AC3 42 TYR A 107 GLY A 109 ARG A 110 GLY A 111
SITE 4 AC3 42 GLY A 114 GLY A 115 ASN A 119 GLY A 120
SITE 5 AC3 42 GLY A 121 MET A 122 ILE A 218 HIS A 248
SITE 6 AC3 42 GLN A 249 GLY A 288 ALA A 289 GLY A 290
SITE 7 AC3 42 TYR A 446 HIS A 447 ASP A 474 GLY A 475
SITE 8 AC3 42 ASN A 485 PRO A 486 PHE A 487 HOH A 514
SITE 9 AC3 42 HOH A 515 HOH A 516 HOH A 518 HOH A 519
SITE 10 AC3 42 HOH A 539 HOH A 543 HOH A 570 HOH A 755
SITE 11 AC3 42 HOH A 928 HOH A1207
CRYST1 51.280 72.870 62.950 90.00 105.11 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 0.019501 0.000000 0.005265 0.00000
SCALE2 0.000000 0.013723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016455 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
