HEADER MONOOXYGENASE 20-AUG-98 5PAH
TITLE HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND
TITLE 2 DOPAMINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLALANINE 4-MONOOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 EC: 1.14.16.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: TRUNCATED FORM, DELTA NH 1-102, DELTA COOH 428-452
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NON-HEME IRON-CONTAINING MONOOXYGENASE, OXIDOREDUCTASE, MONOOXYGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ERLANDSEN,T.FLATMARK,R.C.STEVENS
REVDAT 3 06-MAR-24 5PAH 1 REMARK LINK
REVDAT 2 24-FEB-09 5PAH 1 VERSN
REVDAT 1 27-APR-99 5PAH 0
JRNL AUTH H.ERLANDSEN,T.FLATMARK,R.C.STEVENS,E.HOUGH
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF THE HUMAN PHENYLALANINE
JRNL TITL 2 HYDROXYLASE CATALYTIC DOMAIN WITH BOUND CATECHOL INHIBITORS
JRNL TITL 3 AT 2.0 A RESOLUTION.
JRNL REF BIOCHEMISTRY V. 37 15638 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9843368
JRNL DOI 10.1021/BI9815290
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 24638
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) : 0.163
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2393
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3249
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE : 0.2190
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 355
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2525
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28000
REMARK 3 B22 (A**2) : -2.17000
REMARK 3 B33 (A**2) : 2.45000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.120
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 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 5PAH 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_1000179750.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24638
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26700
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS 0.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8
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 62.89750
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 62.89750
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 33.42100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.58300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.42100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.58300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.89750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.42100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.58300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.89750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.42100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.58300
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: MONOMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 264 C CYS A 265 N 0.213
REMARK 500 CYS A 265 CB CYS A 265 SG -0.163
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 264 CA - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 HIS A 264 O - C - N ANGL. DEV. = 12.1 DEGREES
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 ASN A 133 33.72 -93.63
REMARK 500 GLN A 134 21.87 -150.40
REMARK 500 ALA A 246 -76.49 -56.74
REMARK 500 THR A 328 -82.75 -124.86
REMARK 500 PRO A 407 92.44 -66.45
REMARK 500 PRO A 409 32.16 -81.26
REMARK 500 PHE A 410 -179.30 -170.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 254 0.08 SIDE CHAIN
REMARK 500 TYR A 268 0.07 SIDE CHAIN
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 FE A 425 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 285 NE2
REMARK 620 2 HIS A 290 NE2 95.3
REMARK 620 3 GLU A 330 OE2 103.6 85.0
REMARK 620 4 LDP A 600 O1 87.7 174.9 98.3
REMARK 620 5 LDP A 600 O2 172.0 88.9 83.5 87.6
REMARK 620 6 HOH A 649 O 95.7 86.4 159.4 89.2 77.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: IRON BINDING LIGANDS
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDP A 600
DBREF 5PAH A 117 424 UNP P00439 PH4H_HUMAN 117 424
SEQRES 1 A 308 THR VAL PRO TRP PHE PRO ARG THR ILE GLN GLU LEU ASP
SEQRES 2 A 308 ARG PHE ALA ASN GLN ILE LEU SER TYR GLY ALA GLU LEU
SEQRES 3 A 308 ASP ALA ASP HIS PRO GLY PHE LYS ASP PRO VAL TYR ARG
SEQRES 4 A 308 ALA ARG ARG LYS GLN PHE ALA ASP ILE ALA TYR ASN TYR
SEQRES 5 A 308 ARG HIS GLY GLN PRO ILE PRO ARG VAL GLU TYR MET GLU
SEQRES 6 A 308 GLU GLU LYS LYS THR TRP GLY THR VAL PHE LYS THR LEU
SEQRES 7 A 308 LYS SER LEU TYR LYS THR HIS ALA CYS TYR GLU TYR ASN
SEQRES 8 A 308 HIS ILE PHE PRO LEU LEU GLU LYS TYR CYS GLY PHE HIS
SEQRES 9 A 308 GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER GLN PHE
SEQRES 10 A 308 LEU GLN THR CYS THR GLY PHE ARG LEU ARG PRO VAL ALA
SEQRES 11 A 308 GLY LEU LEU SER SER ARG ASP PHE LEU GLY GLY LEU ALA
SEQRES 12 A 308 PHE ARG VAL PHE HIS CYS THR GLN TYR ILE ARG HIS GLY
SEQRES 13 A 308 SER LYS PRO MET TYR THR PRO GLU PRO ASP ILE CYS HIS
SEQRES 14 A 308 GLU LEU LEU GLY HIS VAL PRO LEU PHE SER ASP ARG SER
SEQRES 15 A 308 PHE ALA GLN PHE SER GLN GLU ILE GLY LEU ALA SER LEU
SEQRES 16 A 308 GLY ALA PRO ASP GLU TYR ILE GLU LYS LEU ALA THR ILE
SEQRES 17 A 308 TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN GLY
SEQRES 18 A 308 ASP SER ILE LYS ALA TYR GLY ALA GLY LEU LEU SER SER
SEQRES 19 A 308 PHE GLY GLU LEU GLN TYR CYS LEU SER GLU LYS PRO LYS
SEQRES 20 A 308 LEU LEU PRO LEU GLU LEU GLU LYS THR ALA ILE GLN ASN
SEQRES 21 A 308 TYR THR VAL THR GLU PHE GLN PRO LEU TYR TYR VAL ALA
SEQRES 22 A 308 GLU SER PHE ASN ASP ALA LYS GLU LYS VAL ARG ASN PHE
SEQRES 23 A 308 ALA ALA THR ILE PRO ARG PRO PHE SER VAL ARG TYR ASP
SEQRES 24 A 308 PRO TYR THR GLN ARG ILE GLU VAL LEU
HET FE A 425 1
HET LDP A 600 11
HETNAM FE FE (III) ION
HETNAM LDP L-DOPAMINE
HETSYN LDP DOPAMINE
FORMUL 2 FE FE 3+
FORMUL 3 LDP C8 H11 N O2
FORMUL 4 HOH *130(H2 O)
HELIX 1 1 ILE A 125 GLN A 134 5 10
HELIX 2 2 ALA A 140 LEU A 142 5 3
HELIX 3 3 PRO A 152 ASN A 167 1 16
HELIX 4 4 GLU A 181 HIS A 201 1 21
HELIX 5 5 TYR A 204 CYS A 217 1 14
HELIX 6 6 LEU A 227 THR A 238 1 12
HELIX 7 7 SER A 251 PHE A 260 1 10
HELIX 8 8 GLY A 272 LYS A 274 5 3
HELIX 9 9 ILE A 283 GLY A 289 1 7
HELIX 10 10 LEU A 293 SER A 295 5 3
HELIX 11 11 ARG A 297 SER A 310 1 14
HELIX 12 12 ASP A 315 PHE A 327 1 13
HELIX 13 13 ALA A 345 LEU A 348 1 4
HELIX 14 14 PHE A 351 LEU A 358 1 8
HELIX 15 15 LEU A 369 ILE A 374 1 6
HELIX 16 16 PHE A 392 THR A 405 1 14
SHEET 1 A 2 ARG A 241 PRO A 244 0
SHEET 2 A 2 VAL A 262 CYS A 265 1 N PHE A 263 O ARG A 241
SHEET 1 B 2 LEU A 333 GLN A 336 0
SHEET 2 B 2 SER A 339 ALA A 342 -1 N LYS A 341 O CYS A 334
SHEET 1 C 2 LYS A 363 PRO A 366 0
SHEET 2 C 2 LEU A 385 VAL A 388 1 N TYR A 386 O LYS A 363
SHEET 1 D 2 SER A 411 ASP A 415 0
SHEET 2 D 2 ARG A 420 LEU A 424 -1 N LEU A 424 O SER A 411
LINK NE2 HIS A 285 FE FE A 425 1555 1555 2.20
LINK NE2 HIS A 290 FE FE A 425 1555 1555 2.13
LINK OE2 GLU A 330 FE FE A 425 1555 1555 1.96
LINK FE FE A 425 O1 LDP A 600 1555 1555 1.85
LINK FE FE A 425 O2 LDP A 600 1555 1555 2.29
LINK FE FE A 425 O HOH A 649 1555 1555 2.34
SITE 1 NUL 5 HIS A 285 HIS A 290 GLU A 330 HOH A 649
SITE 2 NUL 5 LDP A 600
SITE 1 AC1 5 HIS A 285 HIS A 290 GLU A 330 LDP A 600
SITE 2 AC1 5 HOH A 649
SITE 1 AC2 7 HIS A 285 HIS A 290 TYR A 325 GLU A 330
SITE 2 AC2 7 FE A 425 HOH A 649 HOH A 725
CRYST1 66.842 109.166 125.795 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 0.014961 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007949 0.00000
(ATOM LINES ARE NOT SHOWN.)
END