HEADER OXIDOREDUCTASE 13-DEC-12 4IEV
TITLE CYS-ONLY BOUND CYSTEINE DIOXYGENASE AT PH 8.0 IN THE PRESENCE OF CYS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I, CDO, CDO-I;
COMPND 5 EC: 1.13.11.20;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CDO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CUPIN FOLD, CATALYZES OXIDATION, CYSTEINE TO CYSTEINE SULFINATE, C93-
KEYWDS 2 Y157 CROSSLINK, CYTOSOL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.DRIGGERS,R.B.COOLEY,P.A.KARPLUS
REVDAT 3 11-SEP-13 4IEV 1 JRNL
REVDAT 2 21-AUG-13 4IEV 1 JRNL
REVDAT 1 26-JUN-13 4IEV 0
JRNL AUTH C.M.DRIGGERS,R.B.COOLEY,B.SANKARAN,L.L.HIRSCHBERGER,
JRNL AUTH 2 M.H.STIPANUK,P.A.KARPLUS
JRNL TITL CYSTEINE DIOXYGENASE STRUCTURES FROM PH4 TO 9: CONSISTENT
JRNL TITL 2 CYS-PERSULFENATE FORMATION AT INTERMEDIATE PH AND A
JRNL TITL 3 CYS-BOUND ENZYME AT HIGHER PH.
JRNL REF J.MOL.BIOL. V. 425 3121 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23747973
JRNL DOI 10.1016/J.JMB.2013.05.028
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 27708
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.820
REMARK 3 FREE R VALUE TEST SET COUNT : 2720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.9145 - 4.2668 1.00 1490 165 0.1478 0.1700
REMARK 3 2 4.2668 - 3.3876 1.00 1377 143 0.1399 0.1610
REMARK 3 3 3.3876 - 2.9597 1.00 1374 154 0.1641 0.1846
REMARK 3 4 2.9597 - 2.6892 1.00 1349 141 0.1770 0.2386
REMARK 3 5 2.6892 - 2.4965 1.00 1310 169 0.1832 0.2607
REMARK 3 6 2.4965 - 2.3494 1.00 1345 138 0.1684 0.2346
REMARK 3 7 2.3494 - 2.2318 1.00 1321 139 0.1701 0.2387
REMARK 3 8 2.2318 - 2.1346 1.00 1321 133 0.1689 0.2514
REMARK 3 9 2.1346 - 2.0525 1.00 1322 149 0.1968 0.2387
REMARK 3 10 2.0525 - 1.9816 1.00 1291 155 0.1982 0.2650
REMARK 3 11 1.9816 - 1.9197 1.00 1324 145 0.2327 0.2769
REMARK 3 12 1.9197 - 1.8648 1.00 1321 135 0.2510 0.2882
REMARK 3 13 1.8648 - 1.8157 1.00 1308 130 0.2555 0.3004
REMARK 3 14 1.8157 - 1.7714 1.00 1315 134 0.2836 0.3158
REMARK 3 15 1.7714 - 1.7312 1.00 1324 125 0.3115 0.3665
REMARK 3 16 1.7312 - 1.6943 1.00 1266 156 0.3328 0.3430
REMARK 3 17 1.6943 - 1.6604 1.00 1314 151 0.3513 0.3670
REMARK 3 18 1.6604 - 1.6291 0.99 1251 152 0.3639 0.3838
REMARK 3 19 1.6291 - 1.6000 0.82 1065 106 0.3811 0.3539
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.140
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 1575
REMARK 3 ANGLE : 1.334 2137
REMARK 3 CHIRALITY : 0.087 228
REMARK 3 PLANARITY : 0.006 276
REMARK 3 DIHEDRAL : 14.651 582
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND (RESID 5:190 OR RESID 501:502 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2383 3.0621 -49.7928
REMARK 3 T TENSOR
REMARK 3 T11: 0.1134 T22: 0.1888
REMARK 3 T33: 0.1350 T12: -0.0040
REMARK 3 T13: -0.0156 T23: -0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.9421 L22: 2.7962
REMARK 3 L33: 2.2293 L12: 0.5804
REMARK 3 L13: -0.2713 L23: 0.1685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0410 S12: -0.0118 S13: 0.0805
REMARK 3 S21: -0.0142 S22: 0.0239 S23: 0.0452
REMARK 3 S31: 0.1261 S32: -0.1352 S33: 0.0070
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB076664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28421
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 42.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED ENZYME WAS CONCENTRATED TO ~8
REMARK 280 MG/ML AND THEN ADDED INTO A CRYSTALLIZATION SCREEN CONTAINING 0.1
REMARK 280 M TRI-SODIUM CITRATE PH=5.6, 24-34% PEG 4K, AND 0.1-0.25 M
REMARK 280 AMMONIUM ACETATE. 1.5L OF PROTEIN SOLUTION WAS ADDED TO EACH WELL
REMARK 280 AND MIXED WITH AN EQUIVALENT VOLUME OF RESERVOIR SOLUTION., PH
REMARK 280 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 61.20000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.80000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.80000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.60000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.80000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.60000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.20000
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 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 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 GLU A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 PHE A 191
REMARK 465 THR A 192
REMARK 465 THR A 193
REMARK 465 SER A 194
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 198
REMARK 465 ASN A 199
REMARK 465 ASN A 200
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 ARG A 141 NE - CZ - NH1 ANGL. DEV. = 3.1 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 128 -10.95 74.83
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 A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS A 140 NE2 95.9
REMARK 620 3 HIS A 88 NE2 101.1 91.6
REMARK 620 4 CYS A 502 SG 107.4 93.3 150.3
REMARK 620 5 CYS A 502 N 91.9 170.9 91.5 79.8
REMARK 620 N 1 2 3 4
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IEO RELATED DB: PDB
REMARK 900 RELATED ID: 4IEP RELATED DB: PDB
REMARK 900 RELATED ID: 4IEQ RELATED DB: PDB
REMARK 900 RELATED ID: 4IER RELATED DB: PDB
REMARK 900 RELATED ID: 4IES RELATED DB: PDB
REMARK 900 RELATED ID: 4IET RELATED DB: PDB
REMARK 900 RELATED ID: 4IEU RELATED DB: PDB
REMARK 900 RELATED ID: 4IEW RELATED DB: PDB
REMARK 900 RELATED ID: 4IEX RELATED DB: PDB
REMARK 900 RELATED ID: 4IEY RELATED DB: PDB
REMARK 900 RELATED ID: 4IEZ RELATED DB: PDB
REMARK 900 RELATED ID: 4IF0 RELATED DB: PDB
REMARK 900 RELATED ID: 4IF1 RELATED DB: PDB
DBREF 4IEV A 1 200 UNP P21816 CDO1_RAT 1 200
SEQRES 1 A 200 MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 200 ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP
SEQRES 3 A 200 GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA
SEQRES 4 A 200 TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS
SEQRES 5 A 200 PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN
SEQRES 6 A 200 GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY
SEQRES 7 A 200 GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER
SEQRES 8 A 200 HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 200 THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 200 ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS
SEQRES 11 A 200 ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU
SEQRES 12 A 200 ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 200 TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN
SEQRES 14 A 200 ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS
SEQRES 15 A 200 SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY
SEQRES 16 A 200 SER LEU GLU ASN ASN
HET FE2 A 501 1
HET CYS A 502 7
HETNAM FE2 FE (II) ION
HETNAM CYS CYSTEINE
FORMUL 2 FE2 FE 2+
FORMUL 3 CYS C3 H7 N O2 S
FORMUL 4 HOH *186(H2 O)
HELIX 1 1 THR A 11 PHE A 23 1 13
HELIX 2 2 ASN A 29 TYR A 40 1 12
HELIX 3 3 ASN A 43 ALA A 48 1 6
HELIX 4 4 LEU A 49 ALA A 51 5 3
SHEET 1 A 7 CYS A 130 ILE A 133 0
SHEET 2 A 7 HIS A 92 GLN A 99 -1 N LEU A 95 O ALA A 131
SHEET 3 A 7 ALA A 151 SER A 158 -1 O LEU A 154 N LYS A 96
SHEET 4 A 7 ASN A 71 TRP A 77 -1 N MET A 73 O HIS A 155
SHEET 5 A 7 THR A 59 ASP A 64 -1 N VAL A 63 O LEU A 72
SHEET 6 A 7 SER A 183 LYS A 184 1 O SER A 183 N LEU A 62
SHEET 7 A 7 ILE A 187 ARG A 188 -1 O ILE A 187 N LYS A 184
SHEET 1 B 3 ILE A 85 HIS A 86 0
SHEET 2 B 3 THR A 163 PHE A 167 -1 O PHE A 167 N ILE A 85
SHEET 3 B 3 LYS A 174 THR A 178 -1 O VAL A 177 N CYS A 164
SHEET 1 C 3 LYS A 119 LEU A 125 0
SHEET 2 C 3 LEU A 102 PHE A 107 -1 N LEU A 106 O LYS A 120
SHEET 3 C 3 LEU A 139 GLU A 143 -1 O GLU A 143 N LYS A 103
LINK SG CYS A 93 CE2 TYR A 157 1555 1555 1.80
LINK NE2 HIS A 86 FE FE2 A 501 1555 1555 2.06
LINK NE2 HIS A 140 FE FE2 A 501 1555 1555 2.15
LINK NE2 HIS A 88 FE FE2 A 501 1555 1555 2.31
LINK FE FE2 A 501 SG CYS A 502 1555 1555 2.35
LINK FE FE2 A 501 N CYS A 502 1555 1555 2.35
CISPEP 1 SER A 158 PRO A 159 0 -5.30
SITE 1 AC1 4 HIS A 86 HIS A 88 HIS A 140 CYS A 502
SITE 1 AC2 10 TYR A 58 ARG A 60 LEU A 75 HIS A 86
SITE 2 AC2 10 HIS A 88 HIS A 140 HIS A 155 TYR A 157
SITE 3 AC2 10 MET A 179 FE2 A 501
CRYST1 57.600 57.600 122.400 90.00 90.00 90.00 P 43 21 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 0.017361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008170 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
