HEADER OXIDOREDUCTASE 22-JAN-11 3QFS
TITLE CRYSTAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE (FAD/NADPH
TITLE 2 DOMAIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADPH--CYTOCHROME P450 REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FAD/NADPH DOMAIN (UNP RESIDUES 241-677);
COMPND 5 SYNONYM: CPR, P450R;
COMPND 6 EC: 1.6.2.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POR, CYPOR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NADPH-CYTOCHROME P450 REDUCTASE, FLAVOPROTEIN, FAD, NADPH,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.XIA,C.MAROHNIC,S.P.PANDA,B.S.MASTERS,J.-J.P.KIM
REVDAT 4 13-SEP-23 3QFS 1 REMARK SEQADV
REVDAT 3 31-AUG-11 3QFS 1 JRNL
REVDAT 2 24-AUG-11 3QFS 1 JRNL
REVDAT 1 17-AUG-11 3QFS 0
JRNL AUTH C.XIA,S.P.PANDA,C.C.MAROHNIC,P.MARTASEK,B.S.MASTERS,J.J.KIM
JRNL TITL STRUCTURAL BASIS FOR HUMAN NADPH-CYTOCHROME P450
JRNL TITL 2 OXIDOREDUCTASE DEFICIENCY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 13486 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21808038
JRNL DOI 10.1073/PNAS.1106632108
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 228591.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 69748
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 SET) : 0.211
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3544
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8876
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 447
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3476
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 424
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.03000
REMARK 3 B22 (A**2) : 2.40000
REMARK 3 B33 (A**2) : -3.43000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 50.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.980 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.630 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.380 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 53.99
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : COFAC_HUMAN
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : COFAC_HUMAN
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3QFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063589.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0083
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73930
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.71100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1AMO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MAGNESIUM CHLORIDE, 15% PEG5000
REMARK 280 MME, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.32000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.14000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.14000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.32000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.27000
REMARK 290 SMTRY3 4 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 MET A 223
REMARK 465 GLY A 224
REMARK 465 SER A 225
REMARK 465 SER A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 HIS A 230
REMARK 465 HIS A 231
REMARK 465 HIS A 232
REMARK 465 SER A 233
REMARK 465 SER A 234
REMARK 465 GLY A 235
REMARK 465 LEU A 236
REMARK 465 VAL A 237
REMARK 465 PRO A 238
REMARK 465 ARG A 239
REMARK 465 GLY A 240
REMARK 465 SER A 241
REMARK 465 HIS A 242
REMARK 465 MET A 243
REMARK 465 SER A 244
REMARK 465 ILE A 245
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 509 CG CD NE CZ NH1 NH2
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 GLY A 504 O GLY A 507 2.07
REMARK 500 O VAL A 503 O GLY A 508 2.19
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 ASP A 255 59.22 -141.62
REMARK 500 VAL A 423 -60.41 -100.59
REMARK 500 VAL A 503 -96.14 -111.59
REMARK 500 GLU A 505 -179.79 -46.65
REMARK 500 ASN A 506 14.25 53.05
REMARK 500 GLU A 574 -60.41 -123.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAP A 753
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 753
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QE2 RELATED DB: PDB
REMARK 900 FULL-LENGTH WILD TYPE
REMARK 900 RELATED ID: 3QFC RELATED DB: PDB
REMARK 900 FULL-LENGTH V492E MUTANT
REMARK 900 RELATED ID: 3QFR RELATED DB: PDB
REMARK 900 FULL-LENGTH R457H MUTANT
REMARK 900 RELATED ID: 3QFT RELATED DB: PDB
REMARK 900 FAD/NADPH DOMAIN R457H MUTANT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A503V IS A NATURAL VARIANT
DBREF 3QFS A 244 680 UNP P16435 NCPR_HUMAN 241 677
SEQADV 3QFS MET A 223 UNP P16435 EXPRESSION TAG
SEQADV 3QFS GLY A 224 UNP P16435 EXPRESSION TAG
SEQADV 3QFS SER A 225 UNP P16435 EXPRESSION TAG
SEQADV 3QFS SER A 226 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 227 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 228 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 229 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 230 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 231 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 232 UNP P16435 EXPRESSION TAG
SEQADV 3QFS SER A 233 UNP P16435 EXPRESSION TAG
SEQADV 3QFS SER A 234 UNP P16435 EXPRESSION TAG
SEQADV 3QFS GLY A 235 UNP P16435 EXPRESSION TAG
SEQADV 3QFS LEU A 236 UNP P16435 EXPRESSION TAG
SEQADV 3QFS VAL A 237 UNP P16435 EXPRESSION TAG
SEQADV 3QFS PRO A 238 UNP P16435 EXPRESSION TAG
SEQADV 3QFS ARG A 239 UNP P16435 EXPRESSION TAG
SEQADV 3QFS GLY A 240 UNP P16435 EXPRESSION TAG
SEQADV 3QFS SER A 241 UNP P16435 EXPRESSION TAG
SEQADV 3QFS HIS A 242 UNP P16435 EXPRESSION TAG
SEQADV 3QFS MET A 243 UNP P16435 EXPRESSION TAG
SEQADV 3QFS VAL A 503 UNP P16435 ALA 500 SEE REMARK 999
SEQRES 1 A 458 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 458 LEU VAL PRO ARG GLY SER HIS MET SER ILE ARG GLN TYR
SEQRES 3 A 458 GLU LEU VAL VAL HIS THR ASP ILE ASP ALA ALA LYS VAL
SEQRES 4 A 458 TYR MET GLY GLU MET GLY ARG LEU LYS SER TYR GLU ASN
SEQRES 5 A 458 GLN LYS PRO PRO PHE ASP ALA LYS ASN PRO PHE LEU ALA
SEQRES 6 A 458 ALA VAL THR THR ASN ARG LYS LEU ASN GLN GLY THR GLU
SEQRES 7 A 458 ARG HIS LEU MET HIS LEU GLU LEU ASP ILE SER ASP SER
SEQRES 8 A 458 LYS ILE ARG TYR GLU SER GLY ASP HIS VAL ALA VAL TYR
SEQRES 9 A 458 PRO ALA ASN ASP SER ALA LEU VAL ASN GLN LEU GLY LYS
SEQRES 10 A 458 ILE LEU GLY ALA ASP LEU ASP VAL VAL MET SER LEU ASN
SEQRES 11 A 458 ASN LEU ASP GLU GLU SER ASN LYS LYS HIS PRO PHE PRO
SEQRES 12 A 458 CYS PRO THR SER TYR ARG THR ALA LEU THR TYR TYR LEU
SEQRES 13 A 458 ASP ILE THR ASN PRO PRO ARG THR ASN VAL LEU TYR GLU
SEQRES 14 A 458 LEU ALA GLN TYR ALA SER GLU PRO SER GLU GLN GLU LEU
SEQRES 15 A 458 LEU ARG LYS MET ALA SER SER SER GLY GLU GLY LYS GLU
SEQRES 16 A 458 LEU TYR LEU SER TRP VAL VAL GLU ALA ARG ARG HIS ILE
SEQRES 17 A 458 LEU ALA ILE LEU GLN ASP CYS PRO SER LEU ARG PRO PRO
SEQRES 18 A 458 ILE ASP HIS LEU CYS GLU LEU LEU PRO ARG LEU GLN ALA
SEQRES 19 A 458 ARG TYR TYR SER ILE ALA SER SER SER LYS VAL HIS PRO
SEQRES 20 A 458 ASN SER VAL HIS ILE CYS ALA VAL VAL VAL GLU TYR GLU
SEQRES 21 A 458 THR LYS ALA GLY ARG ILE ASN LYS GLY VAL ALA THR ASN
SEQRES 22 A 458 TRP LEU ARG ALA LYS GLU PRO VAL GLY GLU ASN GLY GLY
SEQRES 23 A 458 ARG ALA LEU VAL PRO MET PHE VAL ARG LYS SER GLN PHE
SEQRES 24 A 458 ARG LEU PRO PHE LYS ALA THR THR PRO VAL ILE MET VAL
SEQRES 25 A 458 GLY PRO GLY THR GLY VAL ALA PRO PHE ILE GLY PHE ILE
SEQRES 26 A 458 GLN GLU ARG ALA TRP LEU ARG GLN GLN GLY LYS GLU VAL
SEQRES 27 A 458 GLY GLU THR LEU LEU TYR TYR GLY CYS ARG ARG SER ASP
SEQRES 28 A 458 GLU ASP TYR LEU TYR ARG GLU GLU LEU ALA GLN PHE HIS
SEQRES 29 A 458 ARG ASP GLY ALA LEU THR GLN LEU ASN VAL ALA PHE SER
SEQRES 30 A 458 ARG GLU GLN SER HIS LYS VAL TYR VAL GLN HIS LEU LEU
SEQRES 31 A 458 LYS GLN ASP ARG GLU HIS LEU TRP LYS LEU ILE GLU GLY
SEQRES 32 A 458 GLY ALA HIS ILE TYR VAL CYS GLY ASP ALA ARG ASN MET
SEQRES 33 A 458 ALA ARG ASP VAL GLN ASN THR PHE TYR ASP ILE VAL ALA
SEQRES 34 A 458 GLU LEU GLY ALA MET GLU HIS ALA GLN ALA VAL ASP TYR
SEQRES 35 A 458 ILE LYS LYS LEU MET THR LYS GLY ARG TYR SER LEU ASP
SEQRES 36 A 458 VAL TRP SER
HET FAD A 752 53
HET NAP A 753 31
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 HOH *424(H2 O)
HELIX 1 1 ASP A 257 VAL A 261 5 5
HELIX 2 2 ASP A 330 GLY A 342 1 13
HELIX 3 3 TYR A 370 TYR A 377 1 8
HELIX 4 4 ARG A 385 ALA A 393 1 9
HELIX 5 5 GLN A 394 ALA A 396 5 3
HELIX 6 6 GLU A 398 SER A 410 1 13
HELIX 7 7 SER A 412 VAL A 423 1 12
HELIX 8 8 HIS A 429 CYS A 437 1 9
HELIX 9 9 PRO A 443 LEU A 451 1 9
HELIX 10 10 GLY A 491 ALA A 499 1 9
HELIX 11 11 PRO A 536 GLY A 539 5 4
HELIX 12 12 VAL A 540 GLY A 557 1 18
HELIX 13 13 TYR A 578 ASP A 588 1 11
HELIX 14 14 TYR A 607 ASP A 615 1 9
HELIX 15 15 ASP A 615 GLY A 625 1 11
HELIX 16 16 ASN A 637 GLY A 654 1 18
HELIX 17 17 GLU A 657 LYS A 671 1 15
SHEET 1 A 3 TYR A 248 VAL A 252 0
SHEET 2 A 3 VAL A 348 ASN A 353 -1 O ASN A 352 N GLU A 249
SHEET 3 A 3 THR A 368 SER A 369 -1 O THR A 368 N MET A 349
SHEET 1 B 6 ARG A 457 SER A 460 0
SHEET 2 B 6 HIS A 322 VAL A 325 -1 N VAL A 323 O TYR A 459
SHEET 3 B 6 LEU A 511 ARG A 517 -1 O PHE A 515 N ALA A 324
SHEET 4 B 6 PHE A 285 LYS A 294 -1 N PHE A 285 O MET A 514
SHEET 5 B 6 LEU A 303 ASP A 309 -1 O ASP A 309 N ALA A 288
SHEET 6 B 6 SER A 471 VAL A 477 -1 O ALA A 476 N MET A 304
SHEET 1 C 2 GLU A 480 GLU A 482 0
SHEET 2 C 2 ILE A 488 LYS A 490 -1 O ASN A 489 N TYR A 481
SHEET 1 D 5 GLN A 593 PHE A 598 0
SHEET 2 D 5 THR A 563 CYS A 569 1 N LEU A 565 O ASN A 595
SHEET 3 D 5 VAL A 531 VAL A 534 1 N MET A 533 O TYR A 566
SHEET 4 D 5 HIS A 628 ASP A 634 1 O TYR A 630 N VAL A 534
SHEET 5 D 5 TYR A 674 TRP A 679 1 O SER A 675 N ILE A 629
CISPEP 1 PRO A 277 PRO A 278 0 0.08
CISPEP 2 CYS A 366 PRO A 367 0 -0.08
SITE 1 AC1 26 HOH A 5 HOH A 6 HOH A 23 HOH A 29
SITE 2 AC1 26 HOH A 36 HOH A 37 HOH A 42 HIS A 322
SITE 3 AC1 26 ARG A 427 ARG A 457 TYR A 458 TYR A 459
SITE 4 AC1 26 SER A 460 CYS A 475 ALA A 476 VAL A 477
SITE 5 AC1 26 VAL A 479 TYR A 481 GLY A 491 VAL A 492
SITE 6 AC1 26 ALA A 493 THR A 494 ARG A 517 TRP A 679
SITE 7 AC1 26 HOH A 748 HOH A 854
SITE 1 AC2 20 HOH A 10 HOH A 11 HOH A 89 ARG A 301
SITE 2 AC2 20 GLY A 537 THR A 538 CYS A 569 ARG A 570
SITE 3 AC2 20 SER A 599 ARG A 600 LYS A 605 TYR A 607
SITE 4 AC2 20 GLN A 609 ASN A 637 MET A 638 ASP A 641
SITE 5 AC2 20 HOH A 719 HOH A 775 HOH A 826 HOH A 879
CRYST1 54.640 58.540 130.280 90.00 90.00 90.00 P 21 21 21 4
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 0.018302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017082 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007676 0.00000
(ATOM LINES ARE NOT SHOWN.)
END