HEADER OXIDOREDUCTASE 30-APR-07 2YYG
TITLE CRYSTAL STRUCTURE OF THE OXYGENASE COMPONENT (HPAB) OF 4-
TITLE 2 HYDROXYPHENYLACETATE 3-MONOOXYGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXYPHENYLACETATE-3-HYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE;
COMPND 5 EC: 1.14.13.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS STRUCTUROME, RIKEN SPRING-8 CENTER, OXYGNASE COMPONENT, 4-
KEYWDS 2 HYDROXYPHENYLACETATE 3-MONOOXYGENASE, TWO-COMPONENT FLAVIN
KEYWDS 3 DIFFUSIBLE MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-H.KIM,T.HISANO,K.TAKEDA,W.IWASAKI,A.EBIHARA,K.MIKI
REVDAT 5 25-OCT-23 2YYG 1 REMARK
REVDAT 4 13-JUL-11 2YYG 1 VERSN
REVDAT 3 24-FEB-09 2YYG 1 VERSN
REVDAT 2 20-NOV-07 2YYG 1 JRNL
REVDAT 1 04-SEP-07 2YYG 0
JRNL AUTH S.-H.KIM,T.HISANO,K.TAKEDA,W.IWASAKI,A.EBIHARA,K.MIKI
JRNL TITL CRYSTAL STRUCTURE OF THE OXYGENASE COMPONENT (HPAB) OF THE
JRNL TITL 2 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE FROM THERMUS
JRNL TITL 3 THERMOPHILUS HB8
JRNL REF J.BIOL.CHEM. V. 282 33107 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17804419
JRNL DOI 10.1074/JBC.M703440200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.-H.KIM,H.MIYATAKE,T.HISANO,W.IWASAKI,A.EBIHARA,K.MIKI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
REMARK 1 TITL 2 OXYGENASE COMPONENT (HPAB) OF 4-HYDROXYPHENYLACETATE
REMARK 1 TITL 3 3-MONOOXYGENASE FROM THERMUS THERMOPHILUS HB8
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 556 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 17620709
REMARK 1 DOI 10.1107/S174430910702492X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.01
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) (%) : 83.1
REMARK 3 NUMBER OF REFLECTIONS : 38617
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) : 0.180
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1950
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE : 0.2671
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 281
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 : 3734
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.19000
REMARK 3 B22 (A**2) : 19.01000
REMARK 3 B33 (A**2) : -9.82000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 30.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
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) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.840
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 2YYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000027292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38621
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.16500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ARP/WARP
REMARK 200 STARTING MODEL: PDB ENTRY 2YYK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 0.1M TRIS-HCL,
REMARK 280 25% (V/V) GLYCEROL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
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 0.00000
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 45.68850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.60700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.76850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.68850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.60700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.76850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.68850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.60700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.76850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.68850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.60700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.76850
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 29390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -475.0 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 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1329 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1348 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ARG A 153
REMARK 465 PRO A 154
REMARK 465 PRO A 155
REMARK 465 SER A 156
REMARK 465 GLY A 157
REMARK 465 GLN A 158
REMARK 465 GLU A 478
REMARK 465 VAL A 479
REMARK 465 GLN A 480
REMARK 465 ALA A 481
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 151 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 159 CG CD
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 474 CG CD CE NZ
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 145 132.37 71.63
REMARK 500 ASN A 150 98.85 -69.40
REMARK 500 TYR A 162 52.38 -114.04
REMARK 500 PHE A 186 67.16 63.56
REMARK 500 LEU A 188 35.86 -79.66
REMARK 500 ILE A 194 78.27 -116.08
REMARK 500 SER A 197 -100.64 -134.77
REMARK 500 SER A 204 30.27 -91.71
REMARK 500 MET A 246 148.08 72.58
REMARK 500 ALA A 381 -141.48 50.43
REMARK 500 THR A 426 -48.23 -141.96
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 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YYI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (HPAB) COMPLEXED WITH FAD
REMARK 900 RELATED ID: 2YYJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (HPAB) COMPLEXED WITH FAD AND 4-
REMARK 900 HYDROXYPHENYLACETATE
REMARK 900 RELATED ID: 2YYK RELATED DB: PDB
REMARK 900 THE MUTANT OF HPAB
REMARK 900 RELATED ID: 2YYL RELATED DB: PDB
REMARK 900 THE MUTANT OF HPAB COMPLEXED WITH FAD
REMARK 900 RELATED ID: 2YYM RELATED DB: PDB
REMARK 900 THE MUTANT OF HPAB COMPLEXED WITH FAD AND 4-HYDROXYPHENYLACETATE
DBREF 2YYG A 1 481 UNP Q5SJP8 Q5SJP8_THET8 1 481
SEQRES 1 A 481 MET ALA ARG THR GLY ALA GLU TYR ILE GLU ALA LEU LYS
SEQRES 2 A 481 THR ARG PRO PRO ASN LEU TRP TYR LYS GLY GLU LYS VAL
SEQRES 3 A 481 GLU ASP PRO THR THR HIS PRO VAL PHE ARG GLY ILE VAL
SEQRES 4 A 481 ARG THR MET ALA ALA LEU TYR ASP LEU GLN HIS ASP PRO
SEQRES 5 A 481 ARG TYR ARG GLU VAL LEU THR TYR GLU GLU GLU GLY LYS
SEQRES 6 A 481 ARG HIS GLY MET SER PHE LEU ILE PRO LYS THR LYS GLU
SEQRES 7 A 481 ASP LEU LYS ARG ARG GLY GLN ALA TYR LYS LEU TRP ALA
SEQRES 8 A 481 ASP GLN ASN LEU GLY MET MET GLY ARG SER PRO ASP TYR
SEQRES 9 A 481 LEU ASN ALA VAL VAL MET ALA TYR ALA ALA SER ALA ASP
SEQRES 10 A 481 TYR PHE GLY GLU PHE ALA GLU ASN VAL ARG ASN TYR TYR
SEQRES 11 A 481 ARG TYR LEU ARG ASP GLN ASP LEU ALA THR THR HIS ALA
SEQRES 12 A 481 LEU THR ASN PRO GLN VAL ASN ARG ALA ARG PRO PRO SER
SEQRES 13 A 481 GLY GLN PRO ASP PRO TYR ILE PRO VAL GLY VAL VAL LYS
SEQRES 14 A 481 GLN THR GLU LYS GLY ILE VAL VAL ARG GLY ALA ARG MET
SEQRES 15 A 481 THR ALA THR PHE PRO LEU ALA ASP GLU VAL LEU ILE PHE
SEQRES 16 A 481 PRO SER THR LEU LEU GLN ALA GLY SER GLU LYS TYR ALA
SEQRES 17 A 481 LEU ALA PHE ALA LEU PRO THR SER THR PRO GLY LEU HIS
SEQRES 18 A 481 PHE VAL CYS ARG GLU ALA LEU VAL GLY GLY ASP SER PRO
SEQRES 19 A 481 PHE ASP HIS PRO LEU SER SER ARG VAL GLU GLU MET ASP
SEQRES 20 A 481 CYS LEU VAL ILE PHE ASP ASP VAL LEU VAL PRO TRP GLU
SEQRES 21 A 481 ARG VAL PHE ILE LEU GLY ASN VAL GLU LEU CYS ASN ASN
SEQRES 22 A 481 ALA TYR ALA ALA THR GLY ALA LEU ASN HIS MET ALA HIS
SEQRES 23 A 481 GLN VAL VAL ALA LEU LYS THR ALA LYS THR GLU ALA PHE
SEQRES 24 A 481 LEU GLY VAL ALA ALA LEU MET ALA GLU GLY ILE GLY ALA
SEQRES 25 A 481 ASP VAL TYR GLY HIS VAL GLN GLU LYS ILE ALA GLU ILE
SEQRES 26 A 481 ILE VAL TYR LEU GLU ALA MET ARG ALA PHE TRP THR ARG
SEQRES 27 A 481 ALA GLU GLU GLU ALA LYS GLU ASN ALA TYR GLY LEU LEU
SEQRES 28 A 481 VAL PRO ASP ARG GLY ALA LEU ASP GLY ALA ARG ASN LEU
SEQRES 29 A 481 TYR PRO ARG LEU TYR PRO ARG ILE ARG GLU ILE LEU GLU
SEQRES 30 A 481 GLN ILE GLY ALA SER GLY LEU ILE THR LEU PRO SER GLU
SEQRES 31 A 481 LYS ASP PHE LYS GLY PRO LEU GLY PRO PHE LEU GLU LYS
SEQRES 32 A 481 PHE LEU GLN GLY ALA ALA LEU GLU ALA LYS GLU ARG VAL
SEQRES 33 A 481 ALA LEU PHE ARG LEU ALA TRP ASP MET THR LEU SER GLY
SEQRES 34 A 481 PHE GLY ALA ARG GLN GLU LEU TYR GLU ARG PHE PHE PHE
SEQRES 35 A 481 GLY ASP PRO VAL ARG MET TYR GLN THR LEU TYR ASN VAL
SEQRES 36 A 481 TYR ASN LYS GLU PRO TYR LYS GLU ARG ILE ARG ALA PHE
SEQRES 37 A 481 LEU LYS GLU SER LEU LYS VAL PHE GLU GLU VAL GLN ALA
HET SO4 A 600 5
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 7 HOH *357(H2 O)
HELIX 1 1 THR A 4 ARG A 15 1 12
HELIX 2 2 PHE A 35 GLN A 49 1 15
HELIX 3 3 TYR A 54 LEU A 58 1 5
HELIX 4 4 SER A 70 LEU A 72 5 3
HELIX 5 5 THR A 76 GLN A 93 1 18
HELIX 6 6 PRO A 102 SER A 115 1 14
HELIX 7 7 ALA A 116 GLU A 121 5 6
HELIX 8 8 PHE A 122 ASP A 137 1 16
HELIX 9 9 SER A 204 TYR A 207 5 4
HELIX 10 10 ASN A 267 GLY A 279 1 13
HELIX 11 11 GLY A 279 ILE A 310 1 32
HELIX 12 12 GLY A 311 VAL A 314 5 4
HELIX 13 13 TYR A 315 GLU A 342 1 28
HELIX 14 14 ASP A 354 ALA A 381 1 28
HELIX 15 15 SER A 382 ILE A 385 5 4
HELIX 16 16 SER A 389 GLY A 395 1 7
HELIX 17 17 LEU A 397 LEU A 405 1 9
HELIX 18 18 GLU A 411 MET A 425 1 15
HELIX 19 19 SER A 428 PHE A 441 1 14
HELIX 20 20 ASP A 444 TYR A 456 1 13
HELIX 21 21 LYS A 458 LYS A 474 1 17
HELIX 22 22 VAL A 475 GLU A 477 5 3
SHEET 1 A 6 GLU A 24 LYS A 25 0
SHEET 2 A 6 LEU A 19 TYR A 21 -1 N TYR A 21 O GLU A 24
SHEET 3 A 6 LEU A 220 CYS A 224 1 O CYS A 224 N TRP A 20
SHEET 4 A 6 ASP A 247 PRO A 258 -1 O LEU A 249 N VAL A 223
SHEET 5 A 6 GLY A 174 THR A 185 -1 N ILE A 175 O VAL A 257
SHEET 6 A 6 GLY A 166 GLN A 170 -1 N VAL A 168 O VAL A 176
SHEET 1 B 9 GLU A 24 LYS A 25 0
SHEET 2 B 9 LEU A 19 TYR A 21 -1 N TYR A 21 O GLU A 24
SHEET 3 B 9 LEU A 220 CYS A 224 1 O CYS A 224 N TRP A 20
SHEET 4 B 9 ASP A 247 PRO A 258 -1 O LEU A 249 N VAL A 223
SHEET 5 B 9 GLY A 174 THR A 185 -1 N ILE A 175 O VAL A 257
SHEET 6 B 9 THR A 140 LEU A 144 -1 N LEU A 144 O THR A 183
SHEET 7 B 9 GLU A 191 ILE A 194 1 O LEU A 193 N THR A 141
SHEET 8 B 9 LEU A 209 PRO A 214 -1 O PHE A 211 N ILE A 194
SHEET 9 B 9 VAL A 262 LEU A 265 -1 O PHE A 263 N ALA A 210
SHEET 1 C 2 THR A 59 GLU A 62 0
SHEET 2 C 2 LYS A 65 GLY A 68 -1 O LYS A 65 N GLU A 62
SHEET 1 D 2 LYS A 344 GLU A 345 0
SHEET 2 D 2 LEU A 351 VAL A 352 -1 O VAL A 352 N LYS A 344
SITE 1 AC1 6 GLY A 231 ASP A 232 SER A 233 HOH A1069
SITE 2 AC1 6 HOH A1182 HOH A1353
SITE 1 AC2 4 TRP A 336 THR A 337 ARG A 338 HOH A1134
SITE 1 AC3 5 ILE A 73 ARG A 127 TYR A 130 ARG A 131
SITE 2 AC3 5 SO4 A 604
SITE 1 AC4 5 TYR A 456 LYS A 458 GLU A 459 LYS A 462
SITE 2 AC4 5 HOH A1234
SITE 1 AC5 3 ARG A 131 ARG A 134 SO4 A 602
CRYST1 91.377 99.214 131.537 90.00 90.00 90.00 I 2 2 2 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 0.010944 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
