HEADER OXIDOREDUCTASE 23-MAR-13 4JTN
TITLE CYSTEINE DIOXYGENASE AT PH 8.0 IN THE PRESENCE OF DITHIONITE
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, CYSTEINE TO CYSTEINE SULFINIC ACID CATALYSIS, CYTOSOL,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.DRIGGERS,P.A.KARPLUS
REVDAT 3 11-SEP-13 4JTN 1 JRNL
REVDAT 2 21-AUG-13 4JTN 1 JRNL
REVDAT 1 26-JUN-13 4JTN 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. 1.59 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) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 25199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.780
REMARK 3 FREE R VALUE TEST SET COUNT : 2465
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 28.8047 - 4.1720 1.00 1580 168 0.1600 0.1701
REMARK 3 2 4.1720 - 3.3130 0.77 1141 123 0.1594 0.1666
REMARK 3 3 3.3130 - 2.8947 1.00 1441 161 0.1705 0.1834
REMARK 3 4 2.8947 - 2.6302 0.83 1191 131 0.1743 0.2067
REMARK 3 5 2.6302 - 2.4418 1.00 1430 162 0.1679 0.2257
REMARK 3 6 2.4418 - 2.2979 1.00 1428 145 0.1674 0.1911
REMARK 3 7 2.2979 - 2.1829 0.75 1067 102 0.1659 0.2075
REMARK 3 8 2.1829 - 2.0879 1.00 1423 142 0.1628 0.2204
REMARK 3 9 2.0879 - 2.0075 0.76 1057 133 0.1697 0.1983
REMARK 3 10 2.0075 - 1.9382 0.94 1026 133 0.1609 0.2281
REMARK 3 11 1.9382 - 1.8777 0.63 866 87 0.1980 0.2469
REMARK 3 12 1.8777 - 1.8240 1.00 1405 137 0.1701 0.2347
REMARK 3 13 1.8240 - 1.7760 1.00 1403 138 0.1702 0.2232
REMARK 3 14 1.7760 - 1.7327 1.00 1396 147 0.1828 0.2123
REMARK 3 15 1.7327 - 1.6933 0.75 1040 117 0.2016 0.2305
REMARK 3 16 1.6933 - 1.6572 0.99 1373 157 0.2109 0.2415
REMARK 3 17 1.6572 - 1.6241 0.96 1337 155 0.2245 0.2752
REMARK 3 18 1.6241 - 1.5935 0.83 1130 127 0.2378 0.2412
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.120
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 : 0.016 1588
REMARK 3 ANGLE : 1.376 2164
REMARK 3 CHIRALITY : 0.091 229
REMARK 3 PLANARITY : 0.007 284
REMARK 3 DIHEDRAL : 14.005 582
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0531 3.4112 -49.5170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1281 T22: 0.1677
REMARK 3 T33: 0.1503 T12: 0.0030
REMARK 3 T13: -0.0061 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.3059 L22: 1.8002
REMARK 3 L33: 1.2239 L12: 0.5977
REMARK 3 L13: -0.1808 L23: 0.2294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0395 S13: -0.0579
REMARK 3 S21: 0.0342 S22: -0.0232 S23: -0.0150
REMARK 3 S31: 0.0790 S32: -0.0409 S33: 0.0125
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 4JTN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25267
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.593
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3
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: NULL
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: 0.1M TRI-SODIUM CITRATE PH=5.6, 24%
REMARK 280 PEG 4000, 0.15M AMMONIUM ACETATE. 1:1 DROP RATIO WITH
REMARK 280 MICROSEEDING., PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 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 10 NE CZ NH1 NH2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASN A 67 CB LYS A 69 1.98
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 -7.89 73.71
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 88 NE2 102.1
REMARK 620 3 HIS A 140 NE2 95.3 96.1
REMARK 620 4 HOH A 746 O 132.1 119.5 102.2
REMARK 620 5 HOH A 757 O 89.1 89.8 171.8 69.8
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ELN RELATED DB: PDB
REMARK 900 RELATED ID: 2B5H RELATED DB: PDB
REMARK 900 RELATED ID: 4IEZ RELATED DB: PDB
REMARK 900 RELATED ID: 4IEO RELATED DB: PDB
REMARK 900 RELATED ID: 4IEX RELATED DB: PDB
REMARK 900 RELATED ID: 4IEU RELATED DB: PDB
REMARK 900 RELATED ID: 4JTO RELATED DB: PDB
DBREF 4JTN 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
HETNAM FE2 FE (II) ION
FORMUL 2 FE2 FE 2+
FORMUL 3 HOH *237(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 SER A 121 LEU A 125 0
SHEET 2 C 3 LEU A 102 PHE A 107 -1 N LEU A 102 O LEU A 125
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 1.81
LINK NE2 HIS A 86 FE FE2 A 501 1555 1555 1.99
LINK NE2 HIS A 88 FE FE2 A 501 1555 1555 2.06
LINK NE2 HIS A 140 FE FE2 A 501 1555 1555 2.08
LINK FE FE2 A 501 O HOH A 746 1555 1555 2.12
LINK FE FE2 A 501 O HOH A 757 1555 1555 2.35
CISPEP 1 SER A 158 PRO A 159 0 -7.68
SITE 1 AC1 5 HIS A 86 HIS A 88 HIS A 140 HOH A 746
SITE 2 AC1 5 HOH A 757
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
