HEADER OXIDOREDUCTASE 22-NOV-95 1IUV
TITLE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH
TITLE 2 5.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P-HYDROXYBENZOATE HYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHBH;
COMPND 5 EC: 1.14.13.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PH 5.0 STRUCTURE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: POBA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIE130;
SOURCE 10 EXPRESSION_SYSTEM_GENE: POBA
KEYWDS OXIDOREDUCTASE, MONOOXYGENASE, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.GATTI,B.ENTSCH,D.P.BALLOU,M.L.LUDWIG
REVDAT 5 07-FEB-24 1IUV 1 REMARK
REVDAT 4 29-NOV-17 1IUV 1 HELIX
REVDAT 3 13-JUL-11 1IUV 1 VERSN
REVDAT 2 24-FEB-09 1IUV 1 VERSN
REVDAT 1 20-JUN-96 1IUV 0
JRNL AUTH D.L.GATTI,B.ENTSCH,D.P.BALLOU,M.L.LUDWIG
JRNL TITL PH-DEPENDENT STRUCTURAL CHANGES IN THE ACTIVE SITE OF
JRNL TITL 2 P-HYDROXYBENZOATE HYDROXYLASE POINT TO THE IMPORTANCE OF
JRNL TITL 3 PROTON AND WATER MOVEMENTS DURING CATALYSIS.
JRNL REF BIOCHEMISTRY V. 35 567 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8555229
JRNL DOI 10.1021/BI951344I
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.A.SCHREUDER,A.MATTEVI,G.OBMOLOVA,K.H.KALK,W.G.HOL,
REMARK 1 AUTH 2 F.J.VAN DER BOLT,W.J.VAN BERKEL
REMARK 1 TITL CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE
REMARK 1 TITL 2 HYDROXYLASE COMPLEXED WITH
REMARK 1 TITL 3 4-AMINOBENZOATE,2,4-DIHYDROXYBENZOATE, AND
REMARK 1 TITL 4 2-HYDROXY-4-AMINOBENZOATE AND OF THE TYR222ALA MUTANT
REMARK 1 TITL 5 COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A
REMARK 1 TITL 6 PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING
REMARK 1 REF BIOCHEMISTRY V. 33 10161 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.S.LAH,B.A.PALFEY,H.A.SCHREUDER,M.L.LUDWIG
REMARK 1 TITL CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA
REMARK 1 TITL 2 P-HYDROXYBENZOATE HYDROXYLASES: THE TYR201PHE, TYR385PHE,
REMARK 1 TITL 3 AND ASN300ASP VARIANTS
REMARK 1 REF BIOCHEMISTRY V. 33 1555 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.ENTSCH,B.A.PALFEY,D.P.BALLOU,V.MASSEY
REMARK 1 TITL CATALYTIC FUNCTION OF TYROSINE RESIDUES IN
REMARK 1 TITL 2 PARA-HYDROXYBENZOATE HYDROXYLASE AS DETERMINED BY THE STUDY
REMARK 1 TITL 3 OF SITE-DIRECTED MUTANTS
REMARK 1 REF J.BIOL.CHEM. V. 266 17341 1991
REMARK 1 REFN ISSN 0021-9258
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) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 16343
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) : 0.173
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 : 3124
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 138
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.667
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.98
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.472
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:
REMARK 3 ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON DSSP OUTPUT
REMARK 3 (KABSCH AND SANDER, 1983).
REMARK 3
REMARK 3 THERE IS A MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON
REMARK 3 DENSITY NEAR THE SULFUR AT X=4.90 Y=106.61 Z=72.18:
REMARK 3 CYS 116. THE TYPE OF CHEMICAL MODIFICATION CANNOT BE
REMARK 3 UNAMBIGUOUSLY DETERMINED FROM THE ELECTRON DENSITY.
REMARK 3
REMARK 3 THE SIDE CHAINS OF RESIDUES 23, 136, 144, 173, 311, 321,
REMARK 3 355, 391, 392, 393, AND 394 ARE NOT ORDERED. THE MODEL
REMARK 3 IS DERIVED FROM A COMBINATION OF FIT TO RESIDUAL DENSITY
REMARK 3 AND ENERGY MINIMIZATION.
REMARK 4
REMARK 4 1IUV 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_1000174269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : 0.5 MM COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16343
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.320
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.210
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 (%): 35.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0
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 44.38500
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 44.38500
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 35.82500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.21500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.82500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.21500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.38500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.82500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 73.21500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.38500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.82500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 73.21500
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 146.43000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 88.77000
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 ALA A 10 54.94 -104.22
REMARK 500 ARG A 44 -132.45 43.78
REMARK 500 VAL A 61 52.70 -118.42
REMARK 500 GLN A 82 120.70 -175.78
REMARK 500 ASP A 144 8.60 48.34
REMARK 500 PRO A 182 25.33 -78.93
REMARK 500 ASP A 191 43.38 -91.68
REMARK 500 SER A 212 -169.82 -120.39
REMARK 500 SER A 215 -165.18 -160.08
REMARK 500 ARG A 321 66.43 -119.10
REMARK 500 PRO A 354 -74.07 -56.88
REMARK 500 ILE A 393 140.82 94.45
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 FAD A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHB A 396
DBREF 1IUV A 1 394 UNP P20586 PHHY_PSEAE 1 394
SEQRES 1 A 394 MET LYS THR GLN VAL ALA ILE ILE GLY ALA GLY PRO SER
SEQRES 2 A 394 GLY LEU LEU LEU GLY GLN LEU LEU HIS LYS ALA GLY ILE
SEQRES 3 A 394 ASP ASN VAL ILE LEU GLU ARG GLN THR PRO ASP TYR VAL
SEQRES 4 A 394 LEU GLY ARG ILE ARG ALA GLY VAL LEU GLU GLN GLY MET
SEQRES 5 A 394 VAL ASP LEU LEU ARG GLU ALA GLY VAL ASP ARG ARG MET
SEQRES 6 A 394 ALA ARG ASP GLY LEU VAL HIS GLU GLY VAL GLU ILE ALA
SEQRES 7 A 394 PHE ALA GLY GLN ARG ARG ARG ILE ASP LEU LYS ARG LEU
SEQRES 8 A 394 SER GLY GLY LYS THR VAL THR VAL TYR GLY GLN THR GLU
SEQRES 9 A 394 VAL THR ARG ASP LEU MET GLU ALA ARG GLU ALA CYS GLY
SEQRES 10 A 394 ALA THR THR VAL TYR GLN ALA ALA GLU VAL ARG LEU HIS
SEQRES 11 A 394 ASP LEU GLN GLY GLU ARG PRO TYR VAL THR PHE GLU ARG
SEQRES 12 A 394 ASP GLY GLU ARG LEU ARG LEU ASP CYS ASP TYR ILE ALA
SEQRES 13 A 394 GLY CYS ASP GLY PHE HIS GLY ILE SER ARG GLN SER ILE
SEQRES 14 A 394 PRO ALA GLU ARG LEU LYS VAL PHE GLU ARG VAL TYR PRO
SEQRES 15 A 394 PHE GLY TRP LEU GLY LEU LEU ALA ASP THR PRO PRO VAL
SEQRES 16 A 394 SER HIS GLU LEU ILE TYR ALA ASN HIS PRO ARG GLY PHE
SEQRES 17 A 394 ALA LEU CYS SER GLN ARG SER ALA THR ARG SER ARG TYR
SEQRES 18 A 394 TYR VAL GLN VAL PRO LEU SER GLU LYS VAL GLU ASP TRP
SEQRES 19 A 394 SER ASP GLU ARG PHE TRP THR GLU LEU LYS ALA ARG LEU
SEQRES 20 A 394 PRO SER GLU VAL ALA GLU LYS LEU VAL THR GLY PRO SER
SEQRES 21 A 394 LEU GLU LYS SER ILE ALA PRO LEU ARG SER PHE VAL VAL
SEQRES 22 A 394 GLU PRO MET GLN HIS GLY ARG LEU PHE LEU ALA GLY ASP
SEQRES 23 A 394 ALA ALA HIS ILE VAL PRO PRO THR GLY ALA LYS GLY LEU
SEQRES 24 A 394 ASN LEU ALA ALA SER ASP VAL SER THR LEU TYR ARG LEU
SEQRES 25 A 394 LEU LEU LYS ALA TYR ARG GLU GLY ARG GLY GLU LEU LEU
SEQRES 26 A 394 GLU ARG TYR SER ALA ILE CYS LEU ARG ARG ILE TRP LYS
SEQRES 27 A 394 ALA GLU ARG PHE SER TRP TRP MET THR SER VAL LEU HIS
SEQRES 28 A 394 ARG PHE PRO ASP THR ASP ALA PHE SER GLN ARG ILE GLN
SEQRES 29 A 394 GLN THR GLU LEU GLU TYR TYR LEU GLY SER GLU ALA GLY
SEQRES 30 A 394 LEU ALA THR ILE ALA GLU ASN TYR VAL GLY LEU PRO TYR
SEQRES 31 A 394 GLU GLU ILE GLU
HET FAD A 395 53
HET PHB A 396 10
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PHB P-HYDROXYBENZOIC ACID
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 PHB C7 H6 O3
FORMUL 4 HOH *138(H2 O)
HELIX 1 H1 PRO A 12 LYS A 23 1 12
HELIX 2 H2 PRO A 36 LEU A 40 1 5
HELIX 3 H3 GLN A 50 GLU A 58 1 9
HELIX 4 H4 ARG A 63 ASP A 68 1 6
HELIX 5 H5 LEU A 88 SER A 92 1 5
HELIX 6 H6 GLN A 102 CYS A 116 1 15
HELIX 7 H7 ILE A 164 GLN A 167 1 4
HELIX 8 H8 ASP A 236 ARG A 246 1 11
HELIX 9 H9 SER A 249 ALA A 252 1 4
HELIX 10 H10 GLY A 298 GLU A 319 1 22
HELIX 11 H11 GLY A 322 ARG A 327 5 6
HELIX 12 H12 TYR A 328 LEU A 350 1 23
HELIX 13 H13 ALA A 358 GLY A 373 1 16
HELIX 14 H14 GLU A 375 TYR A 385 1 11
SHEET 1 A 6 THR A 119 TYR A 122 0
SHEET 2 A 6 ASN A 28 LEU A 31 1 N ILE A 30 O THR A 119
SHEET 3 A 6 VAL A 5 ILE A 8 1 O VAL A 5 N VAL A 29
SHEET 4 A 6 TYR A 154 GLY A 157 1 O TYR A 154 N ALA A 6
SHEET 5 A 6 LEU A 281 LEU A 283 1 N PHE A 282 O ILE A 155
SHEET 6 A 6 GLN A 277 HIS A 278 -1 O HIS A 278 N LEU A 281
SHEET 1 B 7 GLN A 82 ASP A 87 0
SHEET 2 B 7 GLY A 74 PHE A 79 -1 O VAL A 75 N ILE A 86
SHEET 3 B 7 ILE A 200 ALA A 202 1 O TYR A 201 N ALA A 78
SHEET 4 B 7 ALA A 209 SER A 215 -1 O ALA A 209 N ALA A 202
SHEET 5 B 7 ARG A 218 VAL A 225 -1 O ARG A 218 N ARG A 214
SHEET 6 B 7 GLY A 184 ALA A 190 -1 N GLY A 184 O VAL A 225
SHEET 7 B 7 SER A 260 ALA A 266 -1 N LEU A 261 O LEU A 189
SHEET 1 C 3 ALA A 125 HIS A 130 0
SHEET 2 C 3 TYR A 138 ARG A 143 -1 O TYR A 138 N HIS A 130
SHEET 3 C 3 GLU A 146 ASP A 151 -1 O GLU A 146 N ARG A 143
SHEET 1 D 3 LYS A 175 TYR A 181 0
SHEET 2 D 3 LEU A 268 GLU A 274 -1 O LEU A 268 N TYR A 181
SHEET 3 D 3 HIS A 289 ILE A 290 -1 O ILE A 290 N PHE A 271
SHEET 1 E 3 VAL A 47 GLU A 49 0
SHEET 2 E 3 VAL A 97 VAL A 99 -1 N THR A 98 O LEU A 48
SHEET 3 E 3 LEU A 70 HIS A 72 -1 N LEU A 70 O VAL A 99
CISPEP 1 GLU A 274 PRO A 275 0 -0.09
SITE 1 AC1 31 ILE A 8 GLY A 9 PRO A 12 SER A 13
SITE 2 AC1 31 LEU A 31 GLU A 32 ARG A 33 ARG A 42
SITE 3 AC1 31 ARG A 44 ALA A 45 GLY A 46 VAL A 47
SITE 4 AC1 31 GLN A 102 VAL A 127 CYS A 158 ASP A 159
SITE 5 AC1 31 GLY A 163 GLY A 285 ASP A 286 ALA A 296
SITE 6 AC1 31 LYS A 297 GLY A 298 LEU A 299 ASN A 300
SITE 7 AC1 31 PHB A 396 HOH A 407 HOH A 409 HOH A 410
SITE 8 AC1 31 HOH A 418 HOH A 420 HOH A 475
SITE 1 AC2 10 ARG A 44 VAL A 47 TYR A 201 SER A 212
SITE 2 AC2 10 ARG A 214 TYR A 222 PRO A 293 THR A 294
SITE 3 AC2 10 ALA A 296 FAD A 395
CRYST1 71.650 146.430 88.770 90.00 90.00 90.00 C 2 2 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 0.013957 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006829 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011265 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
