HEADER ELECTRON TRANSPORT, OXIDOREDUCTASE 28-MAR-09 3GTS
TITLE CRYSTAL STRUCTURE OF DICAMBA MONOOXYGENASE WITH NON-HEME IRON AND
TITLE 2 DICAMBA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DDMC;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STENOTROPHOMONAS MALTOPHILIA;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS MALTOPHILIA;
SOURCE 4 ORGANISM_TAXID: 40324;
SOURCE 5 GENE: DDMC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B(+)(KANAMYCIN RESISTANT)
KEYWDS RIESKE NON-HEME IRON OXYGENASE, ELECTRON TRANSPORT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.RYDEL,E.J.STURMAN,F.MOSHIRI,G.R.BROWN,Y.QI
REVDAT 6 03-APR-24 3GTS 1 REMARK
REVDAT 5 21-FEB-24 3GTS 1 REMARK
REVDAT 4 13-OCT-21 3GTS 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3GTS 1 REMARK
REVDAT 2 06-OCT-09 3GTS 1 JRNL
REVDAT 1 28-JUL-09 3GTS 0
JRNL AUTH R.L.D'ORDINE,T.J.RYDEL,M.J.STOREK,E.J.STURMAN,F.MOSHIRI,
JRNL AUTH 2 R.K.BARTLETT,G.R.BROWN,R.J.EILERS,C.DART,Y.QI,S.FLASINSKI,
JRNL AUTH 3 S.J.FRANKLIN
JRNL TITL DICAMBA MONOOXYGENASE: STRUCTURAL INSIGHTS INTO A DYNAMIC
JRNL TITL 2 RIESKE OXYGENASE THAT CATALYZES AN EXOCYCLIC
JRNL TITL 3 MONOOXYGENATION.
JRNL REF J.MOL.BIOL. V. 392 481 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19616009
JRNL DOI 10.1016/J.JMB.2009.07.022
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
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) (%) : 84.9
REMARK 3 NUMBER OF REFLECTIONS : 50201
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 + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.600
REMARK 3 FREE R VALUE TEST SET COUNT : 5057
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2298
REMARK 3 BIN FREE R VALUE : 0.2729
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 474
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 : 7806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 483
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09800
REMARK 3 B22 (A**2) : -0.09800
REMARK 3 B33 (A**2) : 0.19600
REMARK 3 B12 (A**2) : -0.04000
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) : 0.27
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.320
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.302 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.146 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.618 ; 2.500
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 3GTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052297.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200 WITH HIGH-RESOLUTION DOUBLE-
REMARK 200 CRYSTAL SI(220) SAGITTAL
REMARK 200 FOCUSING.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58874
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 36.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: MR WAS PERFORMED USING A PRELIMINARY DMO
REMARK 200 STRUCTURE. THIS EARLY DMO STRUCTURE WAS OBTAINED LARGELY USING A
REMARK 200 HIGH-REDUNDANCY, 1.5418 A WAVELENGTH DATA SET FOR FE SINGLE
REMARK 200 WAVELENGTH ANOMALOUS DISPERSION (SAD) PHASING, WITH ASSISTANCE
REMARK 200 FROM THE SULFUR ANOMALOUS SIGNAL IN A HIGH-REDUNDANCY, 2.29 A
REMARK 200 WAVELENGTH DATA SET.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PURIFIED PROTEIN WAS CONCENTRATED
REMARK 280 TO 10-20 MG/ML AND BUFFER EXCHANGED INTO 25 MM TRIS-HCL, PH 8.0,
REMARK 280 30-50 MM NACL, 25 MM SODIUM CITRATE. DMO CRYSTALS WERE GROWN
REMARK 280 USING THE VAPOR DIFFUSION BY SITTING DROP METHOD, WITH A
REMARK 280 RESERVOIR SOLUTION OF 8-11% PEG 6000, 100 MM SODIUM ACETATE
REMARK 280 BUFFER-PH 5.5, 1 M LICL, AND 4UL DROPLETS OF VARYING PROTEIN-TO-
REMARK 280 PRECIPITANT RATIOS. TO PREPARE A DMO-NON-HEME IRON-DICAMBA
REMARK 280 CRYSTAL, SOME CRYSTALS WERE TRANSFERRED TO A CRYO-AMENABLE
REMARK 280 STORAGE SOLUTION THAT CONTAINED 25 MM DICAMBA (12.3 % PEG6000,
REMARK 280 95 MM SODIUM ACETATE PH 5.5, 21% GLYCEROL, 1MM NAN3, AND 25 MM
REMARK 280 DICAMBA) FOR 5-6 HOURS PRIOR TO PLUNGE-COOLING FOR CRYO-STORAGE
REMARK 280 AND LOW TEMPERATURE DATA COLLECTION. VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.40000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.20000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
REMARK 465 MET B 1
REMARK 465 GLU B 343
REMARK 465 HIS B 344
REMARK 465 HIS B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
REMARK 465 MET C 1
REMARK 465 TYR C 163
REMARK 465 VAL C 164
REMARK 465 HIS C 165
REMARK 465 ARG C 166
REMARK 465 ALA C 167
REMARK 465 ASN C 168
REMARK 465 ALA C 169
REMARK 465 GLN C 170
REMARK 465 THR C 171
REMARK 465 ASP C 172
REMARK 465 ALA C 173
REMARK 465 PHE C 174
REMARK 465 ASP C 175
REMARK 465 ARG C 176
REMARK 465 GLU C 343
REMARK 465 HIS C 344
REMARK 465 HIS C 345
REMARK 465 HIS C 346
REMARK 465 HIS C 347
REMARK 465 HIS C 348
REMARK 465 HIS C 349
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 SER A 19 -161.72 -166.17
REMARK 500 ASP A 47 48.58 -76.78
REMARK 500 HIS A 51 -72.20 -71.28
REMARK 500 ARG A 208 77.09 61.20
REMARK 500 ASN A 211 -127.06 -75.54
REMARK 500 THR A 212 141.22 72.98
REMARK 500 LYS A 224 110.80 -12.31
REMARK 500 VAL A 225 -90.35 89.80
REMARK 500 SER A 226 42.85 -151.65
REMARK 500 PRO A 236 172.68 -57.64
REMARK 500 GLU A 237 -103.29 31.37
REMARK 500 GLU A 256 -64.40 -102.48
REMARK 500 ASP A 274 64.92 -106.68
REMARK 500 SER B 19 -162.78 -166.32
REMARK 500 ASP B 47 49.78 -76.11
REMARK 500 HIS B 51 -73.32 -70.91
REMARK 500 ARG B 166 -34.71 -28.98
REMARK 500 LEU B 207 24.70 -76.92
REMARK 500 THR B 212 153.53 73.43
REMARK 500 PRO B 213 175.25 -48.80
REMARK 500 LYS B 224 111.46 -12.15
REMARK 500 VAL B 225 -88.08 88.62
REMARK 500 SER B 226 43.40 -154.50
REMARK 500 GLU B 237 -115.69 57.93
REMARK 500 GLU B 256 -62.63 -102.03
REMARK 500 ASP B 274 63.57 -105.83
REMARK 500 LYS B 292 -66.65 -96.19
REMARK 500 ARG B 341 -70.37 -31.66
REMARK 500 SER C 19 -163.51 -167.45
REMARK 500 ASP C 47 49.13 -75.55
REMARK 500 HIS C 51 -72.77 -69.59
REMARK 500 ASP C 115 105.00 -59.08
REMARK 500 ASP C 157 46.83 -105.32
REMARK 500 LEU C 158 95.08 8.93
REMARK 500 HIS C 160 85.09 -61.11
REMARK 500 GLU C 178 -120.94 -100.55
REMARK 500 GLU C 180 121.06 173.63
REMARK 500 THR C 198 -43.90 -138.54
REMARK 500 SER C 200 127.76 174.76
REMARK 500 VAL C 201 -154.45 -130.73
REMARK 500 LEU C 202 -20.14 66.34
REMARK 500 MET C 203 150.32 64.28
REMARK 500 ARG C 208 24.45 -57.90
REMARK 500 ALA C 210 112.39 61.26
REMARK 500 ASN C 211 -152.99 -117.10
REMARK 500 THR C 212 173.11 58.03
REMARK 500 ASN C 218 87.64 -150.29
REMARK 500 LYS C 224 110.61 -11.47
REMARK 500 VAL C 225 -87.27 89.91
REMARK 500 SER C 226 41.96 -154.84
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
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 FES A 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 FES A 501 S1 113.5
REMARK 620 3 FES A 501 S2 105.8 105.9
REMARK 620 4 CYS A 68 SG 114.7 102.8 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 51 ND1
REMARK 620 2 FES A 501 S1 113.4
REMARK 620 3 FES A 501 S2 111.7 105.6
REMARK 620 4 HIS A 71 ND1 93.2 118.2 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 160 NE2
REMARK 620 2 HIS A 165 NE2 113.7
REMARK 620 3 ASP A 294 OD1 89.5 90.9
REMARK 620 4 ASP A 294 OD2 140.1 89.8 57.0
REMARK 620 5 HOH A 700 O 99.9 119.6 139.7 94.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 49 SG
REMARK 620 2 FES B 501 S1 112.5
REMARK 620 3 FES B 501 S2 110.0 105.6
REMARK 620 4 CYS B 68 SG 109.1 108.7 111.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 51 ND1
REMARK 620 2 FES B 501 S1 109.7
REMARK 620 3 FES B 501 S2 113.6 106.2
REMARK 620 4 HIS B 71 ND1 93.1 120.5 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 160 NE2
REMARK 620 2 HIS B 165 NE2 103.0
REMARK 620 3 ASP B 294 OD1 100.3 108.0
REMARK 620 4 ASP B 294 OD2 147.8 105.3 56.2
REMARK 620 5 HOH B 701 O 109.8 97.6 134.6 81.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 49 SG
REMARK 620 2 FES C 501 S1 112.2
REMARK 620 3 FES C 501 S2 108.1 105.9
REMARK 620 4 CYS C 68 SG 107.5 110.7 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 51 ND1
REMARK 620 2 FES C 501 S1 110.4
REMARK 620 3 FES C 501 S2 117.6 106.3
REMARK 620 4 HIS C 71 ND1 93.4 116.4 112.8
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 FES A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3M A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3M B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GB4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DICAMBA MONOOXYGENASE WITH NON-HEME COBALT AND
REMARK 900 DICAMBA
REMARK 900 RELATED ID: 3GOB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DICAMBA MONOOXYGENASE WITH NON-HEME COBALT AND
REMARK 900 DCSA
REMARK 900 RELATED ID: 3GTE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DICAMBA MONOOXYGENASE WITH NON-HEME IRON
DBREF 3GTS A 2 340 UNP Q5S3I3 Q5S3I3_STEMA 1 339
DBREF 3GTS B 2 340 UNP Q5S3I3 Q5S3I3_STEMA 1 339
DBREF 3GTS C 2 340 UNP Q5S3I3 Q5S3I3_STEMA 1 339
SEQADV 3GTS MET A 1 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS ALA A 2 UNP Q5S3I3 MET 1 ENGINEERED MUTATION
SEQADV 3GTS ARG A 341 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS LEU A 342 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS GLU A 343 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 344 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 345 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 346 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 347 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 348 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS A 349 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS ALA B 2 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS ALA B 2 UNP Q5S3I3 MET 1 ENGINEERED MUTATION
SEQADV 3GTS ARG B 341 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS LEU B 342 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS GLU B 343 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 344 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 345 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 346 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 347 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 348 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS B 349 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS ALA C 2 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS ALA C 2 UNP Q5S3I3 MET 1 ENGINEERED MUTATION
SEQADV 3GTS ARG C 341 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS LEU C 342 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS GLU C 343 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 344 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 345 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 346 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 347 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 348 UNP Q5S3I3 EXPRESSION TAG
SEQADV 3GTS HIS C 349 UNP Q5S3I3 EXPRESSION TAG
SEQRES 1 A 349 MET ALA THR PHE VAL ARG ASN ALA TRP TYR VAL ALA ALA
SEQRES 2 A 349 LEU PRO GLU GLU LEU SER GLU LYS PRO LEU GLY ARG THR
SEQRES 3 A 349 ILE LEU ASP THR PRO LEU ALA LEU TYR ARG GLN PRO ASP
SEQRES 4 A 349 GLY VAL VAL ALA ALA LEU LEU ASP ILE CYS PRO HIS ARG
SEQRES 5 A 349 PHE ALA PRO LEU SER ASP GLY ILE LEU VAL ASN GLY HIS
SEQRES 6 A 349 LEU GLN CYS PRO TYR HIS GLY LEU GLU PHE ASP GLY GLY
SEQRES 7 A 349 GLY GLN CYS VAL HIS ASN PRO HIS GLY ASN GLY ALA ARG
SEQRES 8 A 349 PRO ALA SER LEU ASN VAL ARG SER PHE PRO VAL VAL GLU
SEQRES 9 A 349 ARG ASP ALA LEU ILE TRP ILE TRP PRO GLY ASP PRO ALA
SEQRES 10 A 349 LEU ALA ASP PRO GLY ALA ILE PRO ASP PHE GLY CYS ARG
SEQRES 11 A 349 VAL ASP PRO ALA TYR ARG THR VAL GLY GLY TYR GLY HIS
SEQRES 12 A 349 VAL ASP CYS ASN TYR LYS LEU LEU VAL ASP ASN LEU MET
SEQRES 13 A 349 ASP LEU GLY HIS ALA GLN TYR VAL HIS ARG ALA ASN ALA
SEQRES 14 A 349 GLN THR ASP ALA PHE ASP ARG LEU GLU ARG GLU VAL ILE
SEQRES 15 A 349 VAL GLY ASP GLY GLU ILE GLN ALA LEU MET LYS ILE PRO
SEQRES 16 A 349 GLY GLY THR PRO SER VAL LEU MET ALA LYS PHE LEU ARG
SEQRES 17 A 349 GLY ALA ASN THR PRO VAL ASP ALA TRP ASN ASP ILE ARG
SEQRES 18 A 349 TRP ASN LYS VAL SER ALA MET LEU ASN PHE ILE ALA VAL
SEQRES 19 A 349 ALA PRO GLU GLY THR PRO LYS GLU GLN SER ILE HIS SER
SEQRES 20 A 349 ARG GLY THR HIS ILE LEU THR PRO GLU THR GLU ALA SER
SEQRES 21 A 349 CYS HIS TYR PHE PHE GLY SER SER ARG ASN PHE GLY ILE
SEQRES 22 A 349 ASP ASP PRO GLU MET ASP GLY VAL LEU ARG SER TRP GLN
SEQRES 23 A 349 ALA GLN ALA LEU VAL LYS GLU ASP LYS VAL VAL VAL GLU
SEQRES 24 A 349 ALA ILE GLU ARG ARG ARG ALA TYR VAL GLU ALA ASN GLY
SEQRES 25 A 349 ILE ARG PRO ALA MET LEU SER CYS ASP GLU ALA ALA VAL
SEQRES 26 A 349 ARG VAL SER ARG GLU ILE GLU LYS LEU GLU GLN LEU GLU
SEQRES 27 A 349 ALA ALA ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 349 MET ALA THR PHE VAL ARG ASN ALA TRP TYR VAL ALA ALA
SEQRES 2 B 349 LEU PRO GLU GLU LEU SER GLU LYS PRO LEU GLY ARG THR
SEQRES 3 B 349 ILE LEU ASP THR PRO LEU ALA LEU TYR ARG GLN PRO ASP
SEQRES 4 B 349 GLY VAL VAL ALA ALA LEU LEU ASP ILE CYS PRO HIS ARG
SEQRES 5 B 349 PHE ALA PRO LEU SER ASP GLY ILE LEU VAL ASN GLY HIS
SEQRES 6 B 349 LEU GLN CYS PRO TYR HIS GLY LEU GLU PHE ASP GLY GLY
SEQRES 7 B 349 GLY GLN CYS VAL HIS ASN PRO HIS GLY ASN GLY ALA ARG
SEQRES 8 B 349 PRO ALA SER LEU ASN VAL ARG SER PHE PRO VAL VAL GLU
SEQRES 9 B 349 ARG ASP ALA LEU ILE TRP ILE TRP PRO GLY ASP PRO ALA
SEQRES 10 B 349 LEU ALA ASP PRO GLY ALA ILE PRO ASP PHE GLY CYS ARG
SEQRES 11 B 349 VAL ASP PRO ALA TYR ARG THR VAL GLY GLY TYR GLY HIS
SEQRES 12 B 349 VAL ASP CYS ASN TYR LYS LEU LEU VAL ASP ASN LEU MET
SEQRES 13 B 349 ASP LEU GLY HIS ALA GLN TYR VAL HIS ARG ALA ASN ALA
SEQRES 14 B 349 GLN THR ASP ALA PHE ASP ARG LEU GLU ARG GLU VAL ILE
SEQRES 15 B 349 VAL GLY ASP GLY GLU ILE GLN ALA LEU MET LYS ILE PRO
SEQRES 16 B 349 GLY GLY THR PRO SER VAL LEU MET ALA LYS PHE LEU ARG
SEQRES 17 B 349 GLY ALA ASN THR PRO VAL ASP ALA TRP ASN ASP ILE ARG
SEQRES 18 B 349 TRP ASN LYS VAL SER ALA MET LEU ASN PHE ILE ALA VAL
SEQRES 19 B 349 ALA PRO GLU GLY THR PRO LYS GLU GLN SER ILE HIS SER
SEQRES 20 B 349 ARG GLY THR HIS ILE LEU THR PRO GLU THR GLU ALA SER
SEQRES 21 B 349 CYS HIS TYR PHE PHE GLY SER SER ARG ASN PHE GLY ILE
SEQRES 22 B 349 ASP ASP PRO GLU MET ASP GLY VAL LEU ARG SER TRP GLN
SEQRES 23 B 349 ALA GLN ALA LEU VAL LYS GLU ASP LYS VAL VAL VAL GLU
SEQRES 24 B 349 ALA ILE GLU ARG ARG ARG ALA TYR VAL GLU ALA ASN GLY
SEQRES 25 B 349 ILE ARG PRO ALA MET LEU SER CYS ASP GLU ALA ALA VAL
SEQRES 26 B 349 ARG VAL SER ARG GLU ILE GLU LYS LEU GLU GLN LEU GLU
SEQRES 27 B 349 ALA ALA ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 349 MET ALA THR PHE VAL ARG ASN ALA TRP TYR VAL ALA ALA
SEQRES 2 C 349 LEU PRO GLU GLU LEU SER GLU LYS PRO LEU GLY ARG THR
SEQRES 3 C 349 ILE LEU ASP THR PRO LEU ALA LEU TYR ARG GLN PRO ASP
SEQRES 4 C 349 GLY VAL VAL ALA ALA LEU LEU ASP ILE CYS PRO HIS ARG
SEQRES 5 C 349 PHE ALA PRO LEU SER ASP GLY ILE LEU VAL ASN GLY HIS
SEQRES 6 C 349 LEU GLN CYS PRO TYR HIS GLY LEU GLU PHE ASP GLY GLY
SEQRES 7 C 349 GLY GLN CYS VAL HIS ASN PRO HIS GLY ASN GLY ALA ARG
SEQRES 8 C 349 PRO ALA SER LEU ASN VAL ARG SER PHE PRO VAL VAL GLU
SEQRES 9 C 349 ARG ASP ALA LEU ILE TRP ILE TRP PRO GLY ASP PRO ALA
SEQRES 10 C 349 LEU ALA ASP PRO GLY ALA ILE PRO ASP PHE GLY CYS ARG
SEQRES 11 C 349 VAL ASP PRO ALA TYR ARG THR VAL GLY GLY TYR GLY HIS
SEQRES 12 C 349 VAL ASP CYS ASN TYR LYS LEU LEU VAL ASP ASN LEU MET
SEQRES 13 C 349 ASP LEU GLY HIS ALA GLN TYR VAL HIS ARG ALA ASN ALA
SEQRES 14 C 349 GLN THR ASP ALA PHE ASP ARG LEU GLU ARG GLU VAL ILE
SEQRES 15 C 349 VAL GLY ASP GLY GLU ILE GLN ALA LEU MET LYS ILE PRO
SEQRES 16 C 349 GLY GLY THR PRO SER VAL LEU MET ALA LYS PHE LEU ARG
SEQRES 17 C 349 GLY ALA ASN THR PRO VAL ASP ALA TRP ASN ASP ILE ARG
SEQRES 18 C 349 TRP ASN LYS VAL SER ALA MET LEU ASN PHE ILE ALA VAL
SEQRES 19 C 349 ALA PRO GLU GLY THR PRO LYS GLU GLN SER ILE HIS SER
SEQRES 20 C 349 ARG GLY THR HIS ILE LEU THR PRO GLU THR GLU ALA SER
SEQRES 21 C 349 CYS HIS TYR PHE PHE GLY SER SER ARG ASN PHE GLY ILE
SEQRES 22 C 349 ASP ASP PRO GLU MET ASP GLY VAL LEU ARG SER TRP GLN
SEQRES 23 C 349 ALA GLN ALA LEU VAL LYS GLU ASP LYS VAL VAL VAL GLU
SEQRES 24 C 349 ALA ILE GLU ARG ARG ARG ALA TYR VAL GLU ALA ASN GLY
SEQRES 25 C 349 ILE ARG PRO ALA MET LEU SER CYS ASP GLU ALA ALA VAL
SEQRES 26 C 349 ARG VAL SER ARG GLU ILE GLU LYS LEU GLU GLN LEU GLU
SEQRES 27 C 349 ALA ALA ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET FES A 501 4
HET FE A 502 1
HET D3M A 601 13
HET FES B 501 4
HET FE B 502 1
HET D3M B 601 13
HET FES C 501 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FE FE (III) ION
HETNAM D3M 3,6-DICHLORO-2-METHOXYBENZOIC ACID
HETSYN D3M DICAMBA
FORMUL 4 FES 3(FE2 S2)
FORMUL 5 FE 2(FE 3+)
FORMUL 6 D3M 2(C8 H6 CL2 O3)
FORMUL 11 HOH *483(H2 O)
HELIX 1 1 LEU A 14 LEU A 18 5 5
HELIX 2 2 PRO A 55 GLY A 59 5 5
HELIX 3 3 PRO A 92 ASN A 96 5 5
HELIX 4 4 ASP A 115 ALA A 119 5 5
HELIX 5 5 ASP A 120 ILE A 124 5 5
HELIX 6 6 PHE A 127 ASP A 132 5 6
HELIX 7 7 ASN A 147 ASP A 157 1 11
HELIX 8 8 HIS A 160 HIS A 165 1 6
HELIX 9 9 HIS A 165 GLN A 170 1 6
HELIX 10 10 ALA A 173 LEU A 177 5 5
HELIX 11 11 SER A 200 LEU A 207 1 8
HELIX 12 12 PRO A 240 SER A 244 5 5
HELIX 13 13 ASP A 275 LEU A 290 1 16
HELIX 14 14 LYS A 292 ARG A 304 1 13
HELIX 15 15 ARG A 304 ASN A 311 1 8
HELIX 16 16 ASP A 321 ALA A 340 1 20
HELIX 17 17 LEU B 14 LEU B 18 5 5
HELIX 18 18 PRO B 55 GLY B 59 5 5
HELIX 19 19 PRO B 92 ASN B 96 5 5
HELIX 20 20 ASP B 115 ALA B 119 5 5
HELIX 21 21 ASP B 120 ILE B 124 5 5
HELIX 22 22 PHE B 127 ASP B 132 5 6
HELIX 23 23 ASN B 147 ASP B 157 1 11
HELIX 24 24 HIS B 160 HIS B 165 1 6
HELIX 25 25 ALA B 173 LEU B 177 5 5
HELIX 26 26 SER B 200 LEU B 207 1 8
HELIX 27 27 ASP B 275 ALA B 289 1 15
HELIX 28 28 LYS B 292 ARG B 304 1 13
HELIX 29 29 ARG B 304 ASN B 311 1 8
HELIX 30 30 ASP B 321 LEU B 342 1 22
HELIX 31 31 LEU C 14 LEU C 18 5 5
HELIX 32 32 PRO C 55 GLY C 59 5 5
HELIX 33 33 PRO C 92 ASN C 96 5 5
HELIX 34 34 ASP C 120 ILE C 124 5 5
HELIX 35 35 PHE C 127 ASP C 132 5 6
HELIX 36 36 ASN C 147 ASP C 157 1 11
HELIX 37 37 MET C 203 ARG C 208 1 6
HELIX 38 38 PRO C 240 SER C 244 5 5
HELIX 39 39 ASP C 275 ARG C 283 1 9
HELIX 40 40 SER C 284 ALA C 289 1 6
HELIX 41 41 VAL C 291 ARG C 304 1 14
HELIX 42 42 ARG C 304 ASN C 311 1 8
HELIX 43 43 ASP C 321 LEU C 342 1 22
SHEET 1 A 3 TYR A 10 ALA A 13 0
SHEET 2 A 3 LEU A 108 ILE A 111 -1 O ILE A 111 N TYR A 10
SHEET 3 A 3 VAL A 102 ARG A 105 -1 N VAL A 103 O TRP A 110
SHEET 1 B 3 LEU A 23 ILE A 27 0
SHEET 2 B 3 THR A 30 ARG A 36 -1 O LEU A 32 N ARG A 25
SHEET 3 B 3 VAL A 42 LEU A 46 -1 O ALA A 43 N TYR A 35
SHEET 1 C 4 ILE A 60 VAL A 62 0
SHEET 2 C 4 HIS A 65 GLN A 67 -1 O HIS A 65 N VAL A 62
SHEET 3 C 4 GLU A 74 PHE A 75 -1 O PHE A 75 N LEU A 66
SHEET 4 C 4 CYS A 81 HIS A 83 -1 O VAL A 82 N GLU A 74
SHEET 1 D 7 ARG A 136 VAL A 144 0
SHEET 2 D 7 SER A 260 ARG A 269 -1 O SER A 267 N VAL A 138
SHEET 3 D 7 ILE A 245 THR A 257 -1 N THR A 254 O HIS A 262
SHEET 4 D 7 ALA A 227 PRO A 236 -1 N MET A 228 O HIS A 251
SHEET 5 D 7 VAL A 214 ASN A 223 -1 N ASP A 215 O ALA A 235
SHEET 6 D 7 GLU A 187 GLY A 197 -1 N GLY A 197 O VAL A 214
SHEET 7 D 7 GLU A 178 GLY A 184 -1 N GLY A 184 O GLU A 187
SHEET 1 E 3 TYR B 10 ALA B 13 0
SHEET 2 E 3 LEU B 108 ILE B 111 -1 O ILE B 111 N TYR B 10
SHEET 3 E 3 VAL B 102 ARG B 105 -1 N VAL B 103 O TRP B 110
SHEET 1 F 3 LEU B 23 ILE B 27 0
SHEET 2 F 3 THR B 30 ARG B 36 -1 O LEU B 32 N ARG B 25
SHEET 3 F 3 VAL B 42 LEU B 46 -1 O ALA B 43 N TYR B 35
SHEET 1 G 4 ILE B 60 VAL B 62 0
SHEET 2 G 4 HIS B 65 GLN B 67 -1 O HIS B 65 N VAL B 62
SHEET 3 G 4 GLU B 74 PHE B 75 -1 O PHE B 75 N LEU B 66
SHEET 4 G 4 CYS B 81 HIS B 83 -1 O VAL B 82 N GLU B 74
SHEET 1 H 7 ARG B 136 VAL B 144 0
SHEET 2 H 7 SER B 260 ARG B 269 -1 O SER B 267 N VAL B 138
SHEET 3 H 7 ILE B 245 THR B 257 -1 N THR B 254 O HIS B 262
SHEET 4 H 7 ALA B 227 PRO B 236 -1 N MET B 228 O HIS B 251
SHEET 5 H 7 VAL B 214 ASN B 223 -1 N ASP B 219 O PHE B 231
SHEET 6 H 7 GLU B 187 GLY B 197 -1 N ILE B 188 O TRP B 222
SHEET 7 H 7 GLU B 178 GLY B 184 -1 N ILE B 182 O GLN B 189
SHEET 1 I 3 TYR C 10 ALA C 13 0
SHEET 2 I 3 LEU C 108 ILE C 111 -1 O ILE C 111 N TYR C 10
SHEET 3 I 3 VAL C 102 ARG C 105 -1 N VAL C 103 O TRP C 110
SHEET 1 J 3 LEU C 23 ILE C 27 0
SHEET 2 J 3 THR C 30 ARG C 36 -1 O LEU C 34 N LEU C 23
SHEET 3 J 3 VAL C 42 LEU C 46 -1 O ALA C 43 N TYR C 35
SHEET 1 K 4 ILE C 60 VAL C 62 0
SHEET 2 K 4 HIS C 65 GLN C 67 -1 O HIS C 65 N VAL C 62
SHEET 3 K 4 GLU C 74 PHE C 75 -1 O PHE C 75 N LEU C 66
SHEET 4 K 4 CYS C 81 HIS C 83 -1 O VAL C 82 N GLU C 74
SHEET 1 L 7 ARG C 136 VAL C 144 0
SHEET 2 L 7 SER C 260 ARG C 269 -1 O SER C 267 N VAL C 138
SHEET 3 L 7 ILE C 245 THR C 257 -1 N THR C 254 O HIS C 262
SHEET 4 L 7 ALA C 227 PRO C 236 -1 N MET C 228 O HIS C 251
SHEET 5 L 7 VAL C 214 ASN C 223 -1 N ASP C 219 O PHE C 231
SHEET 6 L 7 GLU C 187 ALA C 190 -1 N ILE C 188 O TRP C 222
SHEET 7 L 7 VAL C 181 VAL C 183 -1 N ILE C 182 O GLN C 189
SHEET 1 M 6 ARG C 136 VAL C 144 0
SHEET 2 M 6 SER C 260 ARG C 269 -1 O SER C 267 N VAL C 138
SHEET 3 M 6 ILE C 245 THR C 257 -1 N THR C 254 O HIS C 262
SHEET 4 M 6 ALA C 227 PRO C 236 -1 N MET C 228 O HIS C 251
SHEET 5 M 6 VAL C 214 ASN C 223 -1 N ASP C 219 O PHE C 231
SHEET 6 M 6 LYS C 193 PRO C 195 -1 N ILE C 194 O ALA C 216
LINK SG CYS A 49 FE1 FES A 501 1555 1555 2.24
LINK ND1 HIS A 51 FE2 FES A 501 1555 1555 2.23
LINK SG CYS A 68 FE1 FES A 501 1555 1555 2.32
LINK ND1 HIS A 71 FE2 FES A 501 1555 1555 2.27
LINK NE2 HIS A 160 FE FE A 502 1555 1555 2.07
LINK NE2 HIS A 165 FE FE A 502 1555 1555 2.27
LINK OD1 ASP A 294 FE FE A 502 1555 1555 2.35
LINK OD2 ASP A 294 FE FE A 502 1555 1555 2.25
LINK FE FE A 502 O HOH A 700 1555 1555 2.24
LINK SG CYS B 49 FE1 FES B 501 1555 1555 2.36
LINK ND1 HIS B 51 FE2 FES B 501 1555 1555 2.23
LINK SG CYS B 68 FE1 FES B 501 1555 1555 2.41
LINK ND1 HIS B 71 FE2 FES B 501 1555 1555 2.24
LINK NE2 HIS B 160 FE FE B 502 1555 1555 2.29
LINK NE2 HIS B 165 FE FE B 502 1555 1555 2.22
LINK OD1 ASP B 294 FE FE B 502 1555 1555 2.18
LINK OD2 ASP B 294 FE FE B 502 1555 1555 2.47
LINK FE FE B 502 O HOH B 701 1555 1555 2.18
LINK SG CYS C 49 FE1 FES C 501 1555 1555 2.39
LINK ND1 HIS C 51 FE2 FES C 501 1555 1555 2.14
LINK SG CYS C 68 FE1 FES C 501 1555 1555 2.29
LINK ND1 HIS C 71 FE2 FES C 501 1555 1555 2.34
SITE 1 AC1 7 CYS A 49 HIS A 51 ARG A 52 CYS A 68
SITE 2 AC1 7 TYR A 70 HIS A 71 LEU A 73
SITE 1 AC2 5 ASN A 154 HIS A 160 HIS A 165 ASP A 294
SITE 2 AC2 5 HOH A 700
SITE 1 AC3 7 ASN A 230 GLY A 249 HIS A 251 TRP A 285
SITE 2 AC3 7 HOH A 700 HOH A 707 HOH A 847
SITE 1 AC4 8 CYS B 49 HIS B 51 ARG B 52 ALA B 54
SITE 2 AC4 8 CYS B 68 TYR B 70 HIS B 71 LEU B 73
SITE 1 AC5 5 ASN B 154 HIS B 160 HIS B 165 ASP B 294
SITE 2 AC5 5 HOH B 701
SITE 1 AC6 10 LEU B 202 ASN B 230 ILE B 232 GLY B 249
SITE 2 AC6 10 HIS B 251 TRP B 285 LEU B 290 HOH B 701
SITE 3 AC6 10 HOH B 711 HOH B 888
SITE 1 AC7 7 CYS C 49 HIS C 51 ARG C 52 CYS C 68
SITE 2 AC7 7 TYR C 70 HIS C 71 LEU C 73
CRYST1 80.800 80.800 159.600 90.00 90.00 120.00 P 32 9
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 0.012376 0.007145 0.000000 0.00000
SCALE2 0.000000 0.014291 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006266 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
