HEADER OXIDOREDUCTASE 17-FEB-15 4Y9R
TITLE RAT CYPOR MUTANT - G141DEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADPH--CYTOCHROME P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 57-678;
COMPND 5 SYNONYM: P450R;
COMPND 6 EC: 1.6.2.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 VARIANT: DELTA56;
SOURCE 6 GENE: POR;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS CYTOCHROME P450 REDUCTASE, FMN BINDING, SEMIQUINONE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.XIA,J.J.P.KIM
REVDAT 7 28-FEB-24 4Y9R 1 REMARK
REVDAT 6 25-DEC-19 4Y9R 1 REMARK
REVDAT 5 07-MAR-18 4Y9R 1 REMARK
REVDAT 4 20-SEP-17 4Y9R 1 JRNL REMARK
REVDAT 3 20-JUL-16 4Y9R 1 JRNL
REVDAT 2 01-JUN-16 4Y9R 1 JRNL
REVDAT 1 02-MAR-16 4Y9R 0
JRNL AUTH F.RWERE,C.XIA,S.IM,M.M.HAQUE,D.J.STUEHR,L.WASKELL,J.J.KIM
JRNL TITL MUTANTS OF CYTOCHROME P450 REDUCTASE LACKING EITHER GLY-141
JRNL TITL 2 OR GLY-143 DESTABILIZE ITS FMN SEMIQUINONE.
JRNL REF J.BIOL.CHEM. V. 291 14639 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27189945
JRNL DOI 10.1074/JBC.M116.724625
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 89577.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 53710
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) : 0.195
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2717
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7909
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 411
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 240
REMARK 3 SOLVENT ATOMS : 641
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : -6.06000
REMARK 3 B33 (A**2) : 7.52000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.920 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 37.74
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: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4Y9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000207110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56024
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 37.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.0000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, HEPES, PH
REMARK 280 7.0, 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 51.01300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.82750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.94300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.82750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.01300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.94300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 ILE A 57
REMARK 465 GLN A 58
REMARK 465 THR A 59
REMARK 465 THR A 60
REMARK 465 ALA A 61
REMARK 465 GLY A 237
REMARK 465 GLU A 238
REMARK 465 GLU A 239
REMARK 465 GLY A 501
REMARK 465 GLU A 502
REMARK 465 ASN A 503
REMARK 465 GLY A 504
REMARK 465 GLY A 505
REMARK 465 ILE B 57
REMARK 465 GLN B 58
REMARK 465 THR B 59
REMARK 465 THR B 60
REMARK 465 ALA B 61
REMARK 465 PRO B 62
REMARK 465 GLY B 237
REMARK 465 GLU B 238
REMARK 465 GLU B 239
REMARK 465 SER B 240
REMARK 465 ALA B 500
REMARK 465 GLY B 501
REMARK 465 GLU B 502
REMARK 465 ASN B 503
REMARK 465 GLY B 504
REMARK 465 GLY B 505
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 SER A 68 124.72 -34.67
REMARK 500 MET A 253 149.43 -175.18
REMARK 500 ASP A 277 -169.62 -161.02
REMARK 500 VAL A 420 -60.50 -108.86
REMARK 500 GLU A 477 115.67 -164.52
REMARK 500 GLU A 571 -60.63 -128.92
REMARK 500 ASP A 572 40.50 -141.82
REMARK 500 ASP A 675 74.51 -161.57
REMARK 500 TYR B 105 34.82 -148.85
REMARK 500 ASP B 121 5.25 -67.67
REMARK 500 SER B 124 4.59 -68.98
REMARK 500 GLU B 202 157.41 -49.50
REMARK 500 LEU B 205 79.52 -116.25
REMARK 500 GLU B 353 4.08 -61.17
REMARK 500 TYR B 434 78.24 -119.63
REMARK 500 GLU B 571 -55.34 -125.14
REMARK 500 ASP B 572 49.43 -148.32
REMARK 500 ASP B 675 72.55 -153.94
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 703
REMARK 610 NAP B 703
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y9U RELATED DB: PDB
REMARK 900 RELATED ID: 4YAF RELATED DB: PDB
REMARK 900 RELATED ID: 4YAL RELATED DB: PDB
REMARK 900 RELATED ID: 4YAO RELATED DB: PDB
REMARK 900 RELATED ID: 4YAU RELATED DB: PDB
REMARK 900 RELATED ID: 4YAW RELATED DB: PDB
DBREF 4Y9R A 57 678 UNP P00388 NCPR_RAT 57 678
DBREF 4Y9R B 57 678 UNP P00388 NCPR_RAT 57 678
SEQADV 4Y9R A UNP P00388 GLY 141 DELETION
SEQADV 4Y9R B UNP P00388 GLY 141 DELETION
SEQRES 1 A 621 ILE GLN THR THR ALA PRO PRO VAL LYS GLU SER SER PHE
SEQRES 2 A 621 VAL GLU LYS MET LYS LYS THR GLY ARG ASN ILE ILE VAL
SEQRES 3 A 621 PHE TYR GLY SER GLN THR GLY THR ALA GLU GLU PHE ALA
SEQRES 4 A 621 ASN ARG LEU SER LYS ASP ALA HIS ARG TYR GLY MET ARG
SEQRES 5 A 621 GLY MET SER ALA ASP PRO GLU GLU TYR ASP LEU ALA ASP
SEQRES 6 A 621 LEU SER SER LEU PRO GLU ILE ASP LYS SER LEU VAL VAL
SEQRES 7 A 621 PHE CYS MET ALA THR TYR GLU GLY ASP PRO THR ASP ASN
SEQRES 8 A 621 ALA GLN ASP PHE TYR ASP TRP LEU GLN GLU THR ASP VAL
SEQRES 9 A 621 ASP LEU THR GLY VAL LYS PHE ALA VAL PHE GLY LEU GLY
SEQRES 10 A 621 ASN LYS THR TYR GLU HIS PHE ASN ALA MET GLY LYS TYR
SEQRES 11 A 621 VAL ASP GLN ARG LEU GLU GLN LEU GLY ALA GLN ARG ILE
SEQRES 12 A 621 PHE GLU LEU GLY LEU GLY ASP ASP ASP GLY ASN LEU GLU
SEQRES 13 A 621 GLU ASP PHE ILE THR TRP ARG GLU GLN PHE TRP PRO ALA
SEQRES 14 A 621 VAL CYS GLU PHE PHE GLY VAL GLU ALA THR GLY GLU GLU
SEQRES 15 A 621 SER SER ILE ARG GLN TYR GLU LEU VAL VAL HIS GLU ASP
SEQRES 16 A 621 MET ASP VAL ALA LYS VAL TYR THR GLY GLU MET GLY ARG
SEQRES 17 A 621 LEU LYS SER TYR GLU ASN GLN LYS PRO PRO PHE ASP ALA
SEQRES 18 A 621 LYS ASN PRO PHE LEU ALA ALA VAL THR ALA ASN ARG LYS
SEQRES 19 A 621 LEU ASN GLN GLY THR GLU ARG HIS LEU MET HIS LEU GLU
SEQRES 20 A 621 LEU ASP ILE SER ASP SER LYS ILE ARG TYR GLU SER GLY
SEQRES 21 A 621 ASP HIS VAL ALA VAL TYR PRO ALA ASN ASP SER ALA LEU
SEQRES 22 A 621 VAL ASN GLN ILE GLY GLU ILE LEU GLY ALA ASP LEU ASP
SEQRES 23 A 621 VAL ILE MET SER LEU ASN ASN LEU ASP GLU GLU SER ASN
SEQRES 24 A 621 LYS LYS HIS PRO PHE PRO CYS PRO THR THR TYR ARG THR
SEQRES 25 A 621 ALA LEU THR TYR TYR LEU ASP ILE THR ASN PRO PRO ARG
SEQRES 26 A 621 THR ASN VAL LEU TYR GLU LEU ALA GLN TYR ALA SER GLU
SEQRES 27 A 621 PRO SER GLU GLN GLU HIS LEU HIS LYS MET ALA SER SER
SEQRES 28 A 621 SER GLY GLU GLY LYS GLU LEU TYR LEU SER TRP VAL VAL
SEQRES 29 A 621 GLU ALA ARG ARG HIS ILE LEU ALA ILE LEU GLN ASP TYR
SEQRES 30 A 621 PRO SER LEU ARG PRO PRO ILE ASP HIS LEU CYS GLU LEU
SEQRES 31 A 621 LEU PRO ARG LEU GLN ALA ARG TYR TYR SER ILE ALA SER
SEQRES 32 A 621 SER SER LYS VAL HIS PRO ASN SER VAL HIS ILE CYS ALA
SEQRES 33 A 621 VAL ALA VAL GLU TYR GLU ALA LYS SER GLY ARG VAL ASN
SEQRES 34 A 621 LYS GLY VAL ALA THR SER TRP LEU ARG ALA LYS GLU PRO
SEQRES 35 A 621 ALA GLY GLU ASN GLY GLY ARG ALA LEU VAL PRO MET PHE
SEQRES 36 A 621 VAL ARG LYS SER GLN PHE ARG LEU PRO PHE LYS SER THR
SEQRES 37 A 621 THR PRO VAL ILE MET VAL GLY PRO GLY THR GLY ILE ALA
SEQRES 38 A 621 PRO PHE MET GLY PHE ILE GLN GLU ARG ALA TRP LEU ARG
SEQRES 39 A 621 GLU GLN GLY LYS GLU VAL GLY GLU THR LEU LEU TYR TYR
SEQRES 40 A 621 GLY CYS ARG ARG SER ASP GLU ASP TYR LEU TYR ARG GLU
SEQRES 41 A 621 GLU LEU ALA ARG PHE HIS LYS ASP GLY ALA LEU THR GLN
SEQRES 42 A 621 LEU ASN VAL ALA PHE SER ARG GLU GLN ALA HIS LYS VAL
SEQRES 43 A 621 TYR VAL GLN HIS LEU LEU LYS ARG ASP ARG GLU HIS LEU
SEQRES 44 A 621 TRP LYS LEU ILE HIS GLU GLY GLY ALA HIS ILE TYR VAL
SEQRES 45 A 621 CYS GLY ASP ALA ARG ASN MET ALA LYS ASP VAL GLN ASN
SEQRES 46 A 621 THR PHE TYR ASP ILE VAL ALA GLU PHE GLY PRO MET GLU
SEQRES 47 A 621 HIS THR GLN ALA VAL ASP TYR VAL LYS LYS LEU MET THR
SEQRES 48 A 621 LYS GLY ARG TYR SER LEU ASP VAL TRP SER
SEQRES 1 B 621 ILE GLN THR THR ALA PRO PRO VAL LYS GLU SER SER PHE
SEQRES 2 B 621 VAL GLU LYS MET LYS LYS THR GLY ARG ASN ILE ILE VAL
SEQRES 3 B 621 PHE TYR GLY SER GLN THR GLY THR ALA GLU GLU PHE ALA
SEQRES 4 B 621 ASN ARG LEU SER LYS ASP ALA HIS ARG TYR GLY MET ARG
SEQRES 5 B 621 GLY MET SER ALA ASP PRO GLU GLU TYR ASP LEU ALA ASP
SEQRES 6 B 621 LEU SER SER LEU PRO GLU ILE ASP LYS SER LEU VAL VAL
SEQRES 7 B 621 PHE CYS MET ALA THR TYR GLU GLY ASP PRO THR ASP ASN
SEQRES 8 B 621 ALA GLN ASP PHE TYR ASP TRP LEU GLN GLU THR ASP VAL
SEQRES 9 B 621 ASP LEU THR GLY VAL LYS PHE ALA VAL PHE GLY LEU GLY
SEQRES 10 B 621 ASN LYS THR TYR GLU HIS PHE ASN ALA MET GLY LYS TYR
SEQRES 11 B 621 VAL ASP GLN ARG LEU GLU GLN LEU GLY ALA GLN ARG ILE
SEQRES 12 B 621 PHE GLU LEU GLY LEU GLY ASP ASP ASP GLY ASN LEU GLU
SEQRES 13 B 621 GLU ASP PHE ILE THR TRP ARG GLU GLN PHE TRP PRO ALA
SEQRES 14 B 621 VAL CYS GLU PHE PHE GLY VAL GLU ALA THR GLY GLU GLU
SEQRES 15 B 621 SER SER ILE ARG GLN TYR GLU LEU VAL VAL HIS GLU ASP
SEQRES 16 B 621 MET ASP VAL ALA LYS VAL TYR THR GLY GLU MET GLY ARG
SEQRES 17 B 621 LEU LYS SER TYR GLU ASN GLN LYS PRO PRO PHE ASP ALA
SEQRES 18 B 621 LYS ASN PRO PHE LEU ALA ALA VAL THR ALA ASN ARG LYS
SEQRES 19 B 621 LEU ASN GLN GLY THR GLU ARG HIS LEU MET HIS LEU GLU
SEQRES 20 B 621 LEU ASP ILE SER ASP SER LYS ILE ARG TYR GLU SER GLY
SEQRES 21 B 621 ASP HIS VAL ALA VAL TYR PRO ALA ASN ASP SER ALA LEU
SEQRES 22 B 621 VAL ASN GLN ILE GLY GLU ILE LEU GLY ALA ASP LEU ASP
SEQRES 23 B 621 VAL ILE MET SER LEU ASN ASN LEU ASP GLU GLU SER ASN
SEQRES 24 B 621 LYS LYS HIS PRO PHE PRO CYS PRO THR THR TYR ARG THR
SEQRES 25 B 621 ALA LEU THR TYR TYR LEU ASP ILE THR ASN PRO PRO ARG
SEQRES 26 B 621 THR ASN VAL LEU TYR GLU LEU ALA GLN TYR ALA SER GLU
SEQRES 27 B 621 PRO SER GLU GLN GLU HIS LEU HIS LYS MET ALA SER SER
SEQRES 28 B 621 SER GLY GLU GLY LYS GLU LEU TYR LEU SER TRP VAL VAL
SEQRES 29 B 621 GLU ALA ARG ARG HIS ILE LEU ALA ILE LEU GLN ASP TYR
SEQRES 30 B 621 PRO SER LEU ARG PRO PRO ILE ASP HIS LEU CYS GLU LEU
SEQRES 31 B 621 LEU PRO ARG LEU GLN ALA ARG TYR TYR SER ILE ALA SER
SEQRES 32 B 621 SER SER LYS VAL HIS PRO ASN SER VAL HIS ILE CYS ALA
SEQRES 33 B 621 VAL ALA VAL GLU TYR GLU ALA LYS SER GLY ARG VAL ASN
SEQRES 34 B 621 LYS GLY VAL ALA THR SER TRP LEU ARG ALA LYS GLU PRO
SEQRES 35 B 621 ALA GLY GLU ASN GLY GLY ARG ALA LEU VAL PRO MET PHE
SEQRES 36 B 621 VAL ARG LYS SER GLN PHE ARG LEU PRO PHE LYS SER THR
SEQRES 37 B 621 THR PRO VAL ILE MET VAL GLY PRO GLY THR GLY ILE ALA
SEQRES 38 B 621 PRO PHE MET GLY PHE ILE GLN GLU ARG ALA TRP LEU ARG
SEQRES 39 B 621 GLU GLN GLY LYS GLU VAL GLY GLU THR LEU LEU TYR TYR
SEQRES 40 B 621 GLY CYS ARG ARG SER ASP GLU ASP TYR LEU TYR ARG GLU
SEQRES 41 B 621 GLU LEU ALA ARG PHE HIS LYS ASP GLY ALA LEU THR GLN
SEQRES 42 B 621 LEU ASN VAL ALA PHE SER ARG GLU GLN ALA HIS LYS VAL
SEQRES 43 B 621 TYR VAL GLN HIS LEU LEU LYS ARG ASP ARG GLU HIS LEU
SEQRES 44 B 621 TRP LYS LEU ILE HIS GLU GLY GLY ALA HIS ILE TYR VAL
SEQRES 45 B 621 CYS GLY ASP ALA ARG ASN MET ALA LYS ASP VAL GLN ASN
SEQRES 46 B 621 THR PHE TYR ASP ILE VAL ALA GLU PHE GLY PRO MET GLU
SEQRES 47 B 621 HIS THR GLN ALA VAL ASP TYR VAL LYS LYS LEU MET THR
SEQRES 48 B 621 LYS GLY ARG TYR SER LEU ASP VAL TRP SER
HET FMN A 701 31
HET FAD A 702 53
HET NAP A 703 31
HET PO4 A 704 5
HET FMN B 701 31
HET FAD B 702 53
HET NAP B 703 31
HET PO4 B 704 5
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 FMN 2(C17 H21 N4 O9 P)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 NAP 2(C21 H28 N7 O17 P3)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 11 HOH *641(H2 O)
HELIX 1 AA1 SER A 68 THR A 76 1 9
HELIX 2 AA2 GLY A 89 ALA A 102 1 14
HELIX 3 AA3 HIS A 103 GLY A 106 5 4
HELIX 4 AA4 ASP A 113 TYR A 117 5 5
HELIX 5 AA5 ASP A 118 ILE A 128 5 11
HELIX 6 AA6 ALA A 149 THR A 159 1 11
HELIX 7 AA7 ASN A 182 LEU A 195 1 14
HELIX 8 AA8 ASN A 211 GLY A 232 1 22
HELIX 9 AA9 ASP A 254 VAL A 258 5 5
HELIX 10 AB1 ASP A 327 LEU A 338 1 12
HELIX 11 AB2 TYR A 367 TYR A 374 1 8
HELIX 12 AB3 ARG A 382 ALA A 390 1 9
HELIX 13 AB4 GLN A 391 ALA A 393 5 3
HELIX 14 AB5 GLU A 395 MET A 405 1 11
HELIX 15 AB6 GLY A 410 VAL A 420 1 11
HELIX 16 AB7 HIS A 426 TYR A 434 1 9
HELIX 17 AB8 PRO A 440 LEU A 448 1 9
HELIX 18 AB9 GLY A 488 LYS A 497 1 10
HELIX 19 AC1 PRO A 533 GLY A 536 5 4
HELIX 20 AC2 ILE A 537 GLN A 553 1 17
HELIX 21 AC3 TYR A 575 ASP A 585 1 11
HELIX 22 AC4 TYR A 604 ASP A 612 1 9
HELIX 23 AC5 ASP A 612 GLU A 622 1 11
HELIX 24 AC6 ASN A 635 GLY A 652 1 18
HELIX 25 AC7 GLU A 655 LYS A 669 1 15
HELIX 26 AC8 SER B 68 GLY B 77 1 10
HELIX 27 AC9 GLY B 89 ALA B 102 1 14
HELIX 28 AD1 HIS B 103 GLY B 106 5 4
HELIX 29 AD2 ASP B 113 TYR B 117 5 5
HELIX 30 AD3 ASP B 118 LEU B 125 5 8
HELIX 31 AD4 ALA B 149 THR B 159 1 11
HELIX 32 AD5 ASN B 182 GLN B 194 1 13
HELIX 33 AD6 ASN B 211 GLY B 232 1 22
HELIX 34 AD7 ASP B 254 VAL B 258 5 5
HELIX 35 AD8 ASP B 327 GLY B 339 1 13
HELIX 36 AD9 TYR B 367 TYR B 373 1 7
HELIX 37 AE1 ARG B 382 ALA B 390 1 9
HELIX 38 AE2 GLN B 391 ALA B 393 5 3
HELIX 39 AE3 GLU B 395 LYS B 404 1 10
HELIX 40 AE4 MET B 405 SER B 407 5 3
HELIX 41 AE5 SER B 409 VAL B 420 1 12
HELIX 42 AE6 HIS B 426 TYR B 434 1 9
HELIX 43 AE7 PRO B 440 LEU B 448 1 9
HELIX 44 AE8 GLY B 488 ALA B 496 1 9
HELIX 45 AE9 PRO B 533 GLY B 536 5 4
HELIX 46 AF1 ILE B 537 GLU B 552 1 16
HELIX 47 AF2 TYR B 575 ASP B 585 1 11
HELIX 48 AF3 TYR B 604 ASP B 612 1 9
HELIX 49 AF4 ASP B 612 GLU B 622 1 11
HELIX 50 AF5 ASN B 635 GLY B 652 1 18
HELIX 51 AF6 GLU B 655 LYS B 669 1 15
SHEET 1 AA1 4 GLY A 109 ALA A 112 0
SHEET 2 AA1 4 ILE A 80 GLY A 85 1 N VAL A 82 O MET A 110
SHEET 3 AA1 4 LEU A 132 TYR A 140 1 O CYS A 136 N GLY A 85
SHEET 4 AA1 4 ASP A 144 PRO A 145 -1 O ASP A 144 N TYR A 140
SHEET 1 AA2 5 GLY A 109 ALA A 112 0
SHEET 2 AA2 5 ILE A 80 GLY A 85 1 N VAL A 82 O MET A 110
SHEET 3 AA2 5 LEU A 132 TYR A 140 1 O CYS A 136 N GLY A 85
SHEET 4 AA2 5 LYS A 167 GLY A 174 1 O PHE A 171 N PHE A 135
SHEET 5 AA2 5 GLN A 198 ASP A 207 1 O ILE A 200 N PHE A 168
SHEET 1 AA3 3 TYR A 245 VAL A 249 0
SHEET 2 AA3 3 ILE A 345 ASN A 350 -1 O ASN A 349 N GLU A 246
SHEET 3 AA3 3 THR A 365 THR A 366 -1 O THR A 365 N MET A 346
SHEET 1 AA4 6 ARG A 454 SER A 457 0
SHEET 2 AA4 6 HIS A 319 VAL A 322 -1 N VAL A 320 O TYR A 456
SHEET 3 AA4 6 LEU A 508 ARG A 514 -1 O PHE A 512 N ALA A 321
SHEET 4 AA4 6 PHE A 282 LYS A 291 -1 N PHE A 282 O MET A 511
SHEET 5 AA4 6 LEU A 300 ASP A 306 -1 O ASP A 306 N ALA A 285
SHEET 6 AA4 6 SER A 468 VAL A 474 -1 O ALA A 473 N MET A 301
SHEET 1 AA5 2 GLU A 477 GLU A 479 0
SHEET 2 AA5 2 VAL A 485 LYS A 487 -1 O ASN A 486 N TYR A 478
SHEET 1 AA6 5 GLN A 590 PHE A 595 0
SHEET 2 AA6 5 THR A 560 CYS A 566 1 N LEU A 562 O ASN A 592
SHEET 3 AA6 5 VAL A 528 VAL A 531 1 N VAL A 528 O LEU A 561
SHEET 4 AA6 5 HIS A 626 ASP A 632 1 O TYR A 628 N VAL A 531
SHEET 5 AA6 5 TYR A 672 TRP A 677 1 O SER A 673 N ILE A 627
SHEET 1 AA7 4 GLY B 109 ALA B 112 0
SHEET 2 AA7 4 ILE B 80 GLY B 85 1 N VAL B 82 O ALA B 112
SHEET 3 AA7 4 LEU B 132 TYR B 140 1 O CYS B 136 N PHE B 83
SHEET 4 AA7 4 ASP B 144 PRO B 145 -1 O ASP B 144 N TYR B 140
SHEET 1 AA8 5 GLY B 109 ALA B 112 0
SHEET 2 AA8 5 ILE B 80 GLY B 85 1 N VAL B 82 O ALA B 112
SHEET 3 AA8 5 LEU B 132 TYR B 140 1 O CYS B 136 N PHE B 83
SHEET 4 AA8 5 LYS B 167 GLY B 174 1 O PHE B 171 N PHE B 135
SHEET 5 AA8 5 GLN B 198 ASP B 207 1 O GLY B 204 N GLY B 172
SHEET 1 AA9 3 TYR B 245 VAL B 249 0
SHEET 2 AA9 3 ILE B 345 ASN B 350 -1 O ASN B 349 N GLU B 246
SHEET 3 AA9 3 THR B 365 THR B 366 -1 O THR B 365 N MET B 346
SHEET 1 AB1 6 ARG B 454 SER B 457 0
SHEET 2 AB1 6 HIS B 319 VAL B 322 -1 N VAL B 320 O TYR B 456
SHEET 3 AB1 6 LEU B 508 ARG B 514 -1 O PHE B 512 N ALA B 321
SHEET 4 AB1 6 PHE B 282 LYS B 291 -1 N PHE B 282 O MET B 511
SHEET 5 AB1 6 LEU B 300 ASP B 306 -1 O ASP B 306 N ALA B 285
SHEET 6 AB1 6 SER B 468 VAL B 474 -1 O VAL B 469 N LEU B 305
SHEET 1 AB2 2 GLU B 477 GLU B 479 0
SHEET 2 AB2 2 VAL B 485 LYS B 487 -1 O ASN B 486 N TYR B 478
SHEET 1 AB3 5 GLN B 590 PHE B 595 0
SHEET 2 AB3 5 THR B 560 CYS B 566 1 N TYR B 564 O ASN B 592
SHEET 3 AB3 5 VAL B 528 VAL B 531 1 N MET B 530 O TYR B 563
SHEET 4 AB3 5 HIS B 626 ASP B 632 1 O TYR B 628 N VAL B 531
SHEET 5 AB3 5 TYR B 672 TRP B 677 1 O SER B 673 N ILE B 627
CISPEP 1 PRO A 274 PRO A 275 0 -0.25
CISPEP 2 CYS A 363 PRO A 364 0 0.06
CISPEP 3 GLY A 652 PRO A 653 0 -0.13
CISPEP 4 PRO B 274 PRO B 275 0 0.03
CISPEP 5 CYS B 363 PRO B 364 0 -0.04
CISPEP 6 GLY B 652 PRO B 653 0 -0.46
SITE 1 AC1 20 SER A 86 GLN A 87 THR A 88 GLY A 89
SITE 2 AC1 20 THR A 90 ALA A 91 ALA A 138 THR A 139
SITE 3 AC1 20 TYR A 140 GLU A 142 GLY A 143 LEU A 173
SITE 4 AC1 20 GLY A 174 ASN A 175 TYR A 178 HIS A 180
SITE 5 AC1 20 PHE A 181 ASN A 182 ASP A 208 LEU A 212
SITE 1 AC2 22 ARG A 424 ARG A 454 TYR A 455 TYR A 456
SITE 2 AC2 22 SER A 457 CYS A 472 ALA A 473 VAL A 474
SITE 3 AC2 22 TYR A 478 GLY A 488 VAL A 489 ALA A 490
SITE 4 AC2 22 THR A 491 TRP A 677 HOH A 808 HOH A 827
SITE 5 AC2 22 HOH A 844 HOH A 848 HOH A 855 HOH A 876
SITE 6 AC2 22 HOH A 908 HOH A 977
SITE 1 AC3 18 ARG A 298 GLY A 534 THR A 535 CYS A 566
SITE 2 AC3 18 ARG A 567 SER A 596 ARG A 597 LYS A 602
SITE 3 AC3 18 TYR A 604 GLN A 606 MET A 636 ASP A 639
SITE 4 AC3 18 HOH A 864 HOH A 970 HOH A 979 HOH A1010
SITE 5 AC3 18 HOH A1033 HOH A1069
SITE 1 AC4 4 HIS A 465 PRO A 466 ASN A 467 SER A 468
SITE 1 AC5 20 SER B 86 GLN B 87 THR B 88 GLY B 89
SITE 2 AC5 20 THR B 90 ALA B 91 ALA B 138 THR B 139
SITE 3 AC5 20 TYR B 140 GLU B 142 GLY B 143 LEU B 173
SITE 4 AC5 20 GLY B 174 ASN B 175 TYR B 178 HIS B 180
SITE 5 AC5 20 PHE B 181 ASN B 182 ASP B 208 LEU B 212
SITE 1 AC6 25 HIS B 319 ARG B 424 ARG B 454 TYR B 455
SITE 2 AC6 25 TYR B 456 SER B 457 CYS B 472 ALA B 473
SITE 3 AC6 25 VAL B 474 TYR B 478 GLY B 488 VAL B 489
SITE 4 AC6 25 ALA B 490 THR B 491 TRP B 677 HOH B 814
SITE 5 AC6 25 HOH B 819 HOH B 840 HOH B 863 HOH B 867
SITE 6 AC6 25 HOH B 868 HOH B 878 HOH B 904 HOH B 961
SITE 7 AC6 25 HOH B 979
SITE 1 AC7 18 ARG B 298 GLY B 534 THR B 535 CYS B 566
SITE 2 AC7 18 ARG B 567 SER B 596 ARG B 597 LYS B 602
SITE 3 AC7 18 TYR B 604 GLN B 606 ASN B 635 MET B 636
SITE 4 AC7 18 ASP B 639 HOH B 836 HOH B 864 HOH B 889
SITE 5 AC7 18 HOH B 939 HOH B 978
SITE 1 AC8 3 HIS B 465 PRO B 466 ASN B 467
CRYST1 102.026 115.886 119.655 90.00 90.00 90.00 P 21 21 21 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 0.009801 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008357 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
