HEADER OXIDOREDUCTASE 04-SEP-02 1MMK
TITLE CRYSTAL STRUCTURE OF TERNARY COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN
TITLE 2 PHENYLALANINE HYDROXYLASE ((FEII)) COMPLEXED WITH TETRAHYDROBIOPTERIN
TITLE 3 AND THIENYLALANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLALANINE-4-HYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 103-427);
COMPND 5 EC: 1.14.16.1;
COMPND 6 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: PAH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL
KEYWDS BASKET-ARRANGEMENT, 13 ALPHA-HELICES, 8 BETA-STRANDS, FERROUS IRON,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.A.ANDERSEN,T.FLATMARK,E.HOUGH
REVDAT 4 25-OCT-23 1MMK 1 REMARK LINK
REVDAT 3 24-FEB-09 1MMK 1 VERSN
REVDAT 2 08-FEB-05 1MMK 1 JRNL
REVDAT 1 04-SEP-03 1MMK 0
JRNL AUTH O.A.ANDERSEN,A.J.STOKKA,T.FLATMARK,E.HOUGH
JRNL TITL 2.0A RESOLUTION CRYSTAL STRUCTURES OF THE TERNARY COMPLEXES
JRNL TITL 2 OF HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN WITH
JRNL TITL 3 TETRAHYDROBIOPTERIN AND 3-(2-THIENYL)-L-ALANINE OR
JRNL TITL 4 L-NORLEUCINE: SUBSTRATE SPECIFICITY AND MOLECULAR MOTIONS
JRNL TITL 5 RELATED TO SUBSTRATE BINDING
JRNL REF J.MOL.BIOL. V. 333 747 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14568534
JRNL DOI 10.1016/J.JMB.2003.09.004
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 20.00
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) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27721
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) : 0.199
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2803
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE : 0.2220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 24
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 : 2532
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.80
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.18
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.140
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL ANISOTROPIC B VALUE
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.23500
REMARK 200 R SYM FOR SHELL (I) : 0.23500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASES ADOPTED FROM 1KW0
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1KW0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2000, 12% ETHYLENE GLYCOL,
REMARK 280 0.12M NA-HEPES, 10MM BH4, 30MM NA-DITHIONITE, PH 6.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 61.71850
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 61.71850
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 32.59700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.93000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.59700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.93000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.71850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.59700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.93000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.71850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.59700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.93000
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL DIMER IS GENERATED BY: -X,
REMARK 300 Y, 1/2-Z
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 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 61.71850
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 GLY A 103
REMARK 465 ALA A 104
REMARK 465 THR A 105
REMARK 465 VAL A 106
REMARK 465 HIS A 107
REMARK 465 GLU A 108
REMARK 465 LEU A 109
REMARK 465 SER A 110
REMARK 465 ARG A 111
REMARK 465 ASP A 112
REMARK 465 LYS A 113
REMARK 465 LYS A 114
REMARK 465 LYS A 115
REMARK 465 ASP A 116
REMARK 465 ASN A 426
REMARK 465 THR A 427
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 222 31.33 -99.90
REMARK 500 ASN A 223 116.22 -171.22
REMARK 500 PRO A 279 41.77 -85.78
REMARK 500 THR A 328 -85.26 -123.69
REMARK 500 PRO A 409 29.51 -69.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A1426 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 285 NE2
REMARK 620 2 HIS A 290 NE2 93.4
REMARK 620 3 GLU A 330 OE1 96.5 103.0
REMARK 620 4 GLU A 330 OE2 149.7 92.7 53.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 429
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TIH A 428
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KW0 RELATED DB: PDB
REMARK 900 1KW0 CONTAINS CATALYTIC DOMAIN OF HUMAN PHENYLALANINE HYDROXYLASE
REMARK 900 (FE(II)) COMPLEXED WITH TETRAHYDROBIOPTERIN AND THIENYLALANINE
REMARK 900 RELATED ID: 1MMT RELATED DB: PDB
REMARK 900 1MMT CONTAINS CATALYTIC DOMAIN OF HUMAN PHENYLALANINE HYDROXYLASE
REMARK 900 (FE(II)) COMPLEXED WITH TETRAHYDROBIOPTERIN AND NORLEUCINE
REMARK 900 RELATED ID: 1J8U RELATED DB: PDB
REMARK 900 1J8U CONTAINS CATALYTIC DOMAIN OF HUMAN PHENYLALANINE HYDROXYLASE
REMARK 900 (FE(II)) COMPLEXED WITH TETRAHYDROBIOPTERIN
REMARK 900 RELATED ID: 1J8T RELATED DB: PDB
REMARK 900 1J8T CONTAINS CATALYTIC DOMAIN OF HUMAN PHENYLALANINE HYDROXYLASE
REMARK 900 (FE(II))
DBREF 1MMK A 103 427 UNP P00439 PH4H_HUMAN 103 427
SEQRES 1 A 325 GLY ALA THR VAL HIS GLU LEU SER ARG ASP LYS LYS LYS
SEQRES 2 A 325 ASP THR VAL PRO TRP PHE PRO ARG THR ILE GLN GLU LEU
SEQRES 3 A 325 ASP ARG PHE ALA ASN GLN ILE LEU SER TYR GLY ALA GLU
SEQRES 4 A 325 LEU ASP ALA ASP HIS PRO GLY PHE LYS ASP PRO VAL TYR
SEQRES 5 A 325 ARG ALA ARG ARG LYS GLN PHE ALA ASP ILE ALA TYR ASN
SEQRES 6 A 325 TYR ARG HIS GLY GLN PRO ILE PRO ARG VAL GLU TYR MET
SEQRES 7 A 325 GLU GLU GLU LYS LYS THR TRP GLY THR VAL PHE LYS THR
SEQRES 8 A 325 LEU LYS SER LEU TYR LYS THR HIS ALA CYS TYR GLU TYR
SEQRES 9 A 325 ASN HIS ILE PHE PRO LEU LEU GLU LYS TYR CYS GLY PHE
SEQRES 10 A 325 HIS GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER GLN
SEQRES 11 A 325 PHE LEU GLN THR CYS THR GLY PHE ARG LEU ARG PRO VAL
SEQRES 12 A 325 ALA GLY LEU LEU SER SER ARG ASP PHE LEU GLY GLY LEU
SEQRES 13 A 325 ALA PHE ARG VAL PHE HIS CYS THR GLN TYR ILE ARG HIS
SEQRES 14 A 325 GLY SER LYS PRO MET TYR THR PRO GLU PRO ASP ILE CYS
SEQRES 15 A 325 HIS GLU LEU LEU GLY HIS VAL PRO LEU PHE SER ASP ARG
SEQRES 16 A 325 SER PHE ALA GLN PHE SER GLN GLU ILE GLY LEU ALA SER
SEQRES 17 A 325 LEU GLY ALA PRO ASP GLU TYR ILE GLU LYS LEU ALA THR
SEQRES 18 A 325 ILE TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN
SEQRES 19 A 325 GLY ASP SER ILE LYS ALA TYR GLY ALA GLY LEU LEU SER
SEQRES 20 A 325 SER PHE GLY GLU LEU GLN TYR CYS LEU SER GLU LYS PRO
SEQRES 21 A 325 LYS LEU LEU PRO LEU GLU LEU GLU LYS THR ALA ILE GLN
SEQRES 22 A 325 ASN TYR THR VAL THR GLU PHE GLN PRO LEU TYR TYR VAL
SEQRES 23 A 325 ALA GLU SER PHE ASN ASP ALA LYS GLU LYS VAL ARG ASN
SEQRES 24 A 325 PHE ALA ALA THR ILE PRO ARG PRO PHE SER VAL ARG TYR
SEQRES 25 A 325 ASP PRO TYR THR GLN ARG ILE GLU VAL LEU ASP ASN THR
HET FE2 A1426 1
HET SO4 A 429 5
HET H4B A1427 17
HET TIH A 428 11
HETNAM FE2 FE (II) ION
HETNAM SO4 SULFATE ION
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM TIH BETA(2-THIENYL)ALANINE
FORMUL 2 FE2 FE 2+
FORMUL 3 SO4 O4 S 2-
FORMUL 4 H4B C9 H15 N5 O3
FORMUL 5 TIH C7 H9 N O2 S
FORMUL 6 HOH *182(H2 O)
HELIX 1 1 ILE A 125 PHE A 131 5 7
HELIX 2 2 ASP A 151 TYR A 168 1 18
HELIX 3 3 MET A 180 ALA A 202 1 23
HELIX 4 4 CYS A 203 CYS A 217 1 15
HELIX 5 5 GLN A 226 GLY A 239 1 14
HELIX 6 6 SER A 250 ALA A 259 1 10
HELIX 7 7 ASP A 282 HIS A 290 1 9
HELIX 8 8 HIS A 290 SER A 295 1 6
HELIX 9 9 ASP A 296 LEU A 311 1 16
HELIX 10 10 PRO A 314 THR A 328 1 15
HELIX 11 11 GLY A 344 SER A 349 1 6
HELIX 12 12 SER A 350 LEU A 358 1 9
HELIX 13 13 GLU A 368 ALA A 373 1 6
HELIX 14 14 SER A 391 ALA A 404 1 14
SHEET 1 A 2 ARG A 241 PRO A 244 0
SHEET 2 A 2 VAL A 262 CYS A 265 1 O PHE A 263 N ARG A 241
SHEET 1 B 4 SER A 339 ALA A 342 0
SHEET 2 B 4 LEU A 333 GLN A 336 -1 N CYS A 334 O LYS A 341
SHEET 3 B 4 LEU A 385 ALA A 389 1 O ALA A 389 N LEU A 333
SHEET 4 B 4 LYS A 363 PRO A 366 1 N LEU A 365 O VAL A 388
SHEET 1 C 2 SER A 411 ASP A 415 0
SHEET 2 C 2 ARG A 420 LEU A 424 -1 O LEU A 424 N SER A 411
LINK NE2 HIS A 285 FE FE2 A1426 1555 1555 2.12
LINK NE2 HIS A 290 FE FE2 A1426 1555 1555 2.18
LINK OE1 GLU A 330 FE FE2 A1426 1555 1555 2.44
LINK OE2 GLU A 330 FE FE2 A1426 1555 1555 2.43
SITE 1 AC1 4 HIS A 285 HIS A 290 GLU A 330 H4B A1427
SITE 1 AC2 9 ARG A 252 MET A 276 PRO A 314 ASP A 315
SITE 2 AC2 9 PHE A 351 GLY A 352 GLN A 355 HOH A 493
SITE 3 AC2 9 HOH A 610
SITE 1 AC3 13 VAL A 245 GLY A 247 LEU A 248 LEU A 249
SITE 2 AC3 13 SER A 251 PHE A 254 HIS A 264 GLU A 286
SITE 3 AC3 13 HIS A 290 TRP A 326 GLU A 330 HOH A 433
SITE 4 AC3 13 FE2 A1426
SITE 1 AC4 11 ARG A 270 TYR A 277 THR A 278 GLU A 280
SITE 2 AC4 11 PRO A 281 HIS A 285 GLU A 330 GLY A 346
SITE 3 AC4 11 SER A 349 SER A 350 HOH A 434
CRYST1 65.194 107.860 123.437 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 0.015339 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008101 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
