HEADER OXIDOREDUCTASE 11-OCT-05 2C3O
TITLE CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF
TITLE 2 PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE-FERREDOXIN OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.2.7.1;
COMPND 5 OTHER_DETAILS: COMPLEXED WITH IRON/SULFUR CLUSTER, THIAMIN
COMPND 6 DIPHOSPHATE, CRYSTAL SOAKED 15 MINUTES WITH PYRUVATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO AFRICANUS;
SOURCE 3 ORGANISM_TAXID: 873
KEYWDS OXIDOREDUCTASE, 4FE-4S, IRON, IRON-SULFUR, IRON-SULFUR CLUSTER,
KEYWDS 2 PYRUVATE CATABOLISM, TPP-DEPENDENT ENZYME, METAL-BINDING, ELECTRON
KEYWDS 3 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CAVAZZA,C.CONTRERAS-MARTEL,L.PIEULLE,E.CHABRIERE,E.C.HATCHIKIAN,
AUTHOR 2 J.C.FONTECILLA-CAMPS
REVDAT 4 13-DEC-23 2C3O 1 REMARK
REVDAT 3 15-NOV-23 2C3O 1 LINK ATOM
REVDAT 2 24-FEB-09 2C3O 1 VERSN
REVDAT 1 15-FEB-06 2C3O 0
JRNL AUTH C.CAVAZZA,C.CONTRERAS-MARTEL,L.PIEULLE,E.CHABRIERE,
JRNL AUTH 2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS
JRNL TITL FLEXIBILITY OF THIAMINE DIPHOSPHATE REVEALED BY KINETIC
JRNL TITL 2 CRYSTALLOGRAPHIC STUDIES OF THE REACTION OF
JRNL TITL 3 PYRUVATE-FERREDOXIN OXIDOREDUCTASE WITH PYRUVATE.
JRNL REF STRUCTURE V. 14 217 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16472741
JRNL DOI 10.1016/J.STR.2005.10.013
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.CHABRIERE,X.VERNEDE,B.GUIGLIARELLI,M.-H.CHARON,
REMARK 1 AUTH 2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS
REMARK 1 TITL CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF
REMARK 1 TITL 2 PYRUVATE:FERREDOXIN OXIDOREDUCTASE.
REMARK 1 REF SCIENCE V.2559 294 2001
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 11752578
REMARK 1 DOI 10.1126/SCIENCE.1066198
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3177736.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 66515
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) : 0.205
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3341
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10094
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 487
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18766
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.12000
REMARK 3 B22 (A**2) : -8.88000
REMARK 3 B33 (A**2) : 13.00000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.38
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.55
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.730
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.360 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.690 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.610 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.020 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 33.94
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 : PARA_FES.PAR
REMARK 3 PARAMETER FILE 3 : TPP_PYR_HTL_CO2.PAR
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : WATER.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PARA_FES.TOP
REMARK 3 TOPOLOGY FILE 3 : TPP_PYR_HTL_CO2.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2C3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290025956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979821
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66272
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1KEK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG6000, 100MM MGCL2, 100 MM NA
REMARK 280 CACODYLATE PH 6, PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 42.82500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.14650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.61800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.14650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.82500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.61800
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 LYS A 3 -166.17 -108.48
REMARK 500 LYS A 4 106.93 172.38
REMARK 500 ILE A 30 135.00 -173.43
REMARK 500 SER A 87 -121.23 19.57
REMARK 500 LEU A 104 78.53 33.17
REMARK 500 PRO A 106 32.21 -65.26
REMARK 500 ALA A 118 -92.17 -112.21
REMARK 500 PHE A 174 -43.61 72.48
REMARK 500 THR A 176 -40.60 -132.32
REMARK 500 ASN A 209 124.68 -175.55
REMARK 500 HIS A 212 61.38 -161.32
REMARK 500 ARG A 329 50.05 -100.82
REMARK 500 PRO A 339 -83.76 -30.57
REMARK 500 GLU A 353 -118.11 -144.76
REMARK 500 ALA A 427 12.73 85.41
REMARK 500 ILE A 440 -72.38 -54.58
REMARK 500 ASP A 443 33.60 -97.61
REMARK 500 ASN A 444 -12.55 -157.99
REMARK 500 ASP A 446 45.56 -102.12
REMARK 500 LEU A 480 173.62 -55.84
REMARK 500 ILE A 497 -9.90 -149.18
REMARK 500 TRP A 516 65.02 -104.52
REMARK 500 GLU A 577 -76.55 -55.02
REMARK 500 LYS A 589 -71.72 -50.40
REMARK 500 ALA A 590 -164.93 -70.38
REMARK 500 TYR A 591 -135.37 40.96
REMARK 500 LEU A 613 77.17 -66.72
REMARK 500 LYS A 617 80.10 -68.59
REMARK 500 LYS A 623 -19.94 -42.00
REMARK 500 GLU A 628 -177.78 -60.52
REMARK 500 ALA A 631 42.28 -164.22
REMARK 500 PRO A 633 -168.05 -57.41
REMARK 500 VAL A 642 -65.32 -121.38
REMARK 500 THR A 648 32.09 -98.99
REMARK 500 LYS A 674 47.91 29.35
REMARK 500 PRO A 686 1.56 -55.16
REMARK 500 ALA A 703 20.11 -78.93
REMARK 500 GLU A 711 -14.04 -47.45
REMARK 500 LEU A 714 56.84 -100.64
REMARK 500 VAL A 715 -64.07 -93.41
REMARK 500 PHE A 721 47.63 -82.90
REMARK 500 THR A 722 129.24 -39.95
REMARK 500 ALA A 726 140.41 -25.33
REMARK 500 LYS A 729 -67.42 -93.18
REMARK 500 LYS A 732 -70.94 -112.96
REMARK 500 ARG A 737 149.38 -172.95
REMARK 500 CYS A 755 108.79 -49.08
REMARK 500 LYS A 760 130.70 -27.00
REMARK 500 GLN A 770 -44.10 -141.88
REMARK 500 LEU A 805 40.66 -89.70
REMARK 500
REMARK 500 THIS ENTRY HAS 145 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 SF4 A2233 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 689 SG
REMARK 620 2 SF4 A2233 S2 113.1
REMARK 620 3 SF4 A2233 S3 113.1 106.8
REMARK 620 4 SF4 A2233 S4 111.2 106.3 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2233 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 692 SG
REMARK 620 2 SF4 A2233 S1 107.6
REMARK 620 3 SF4 A2233 S2 117.0 105.2
REMARK 620 4 SF4 A2233 S4 114.3 105.7 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2233 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 695 SG
REMARK 620 2 SF4 A2233 S1 109.9
REMARK 620 3 SF4 A2233 S3 114.8 105.4
REMARK 620 4 SF4 A2233 S4 113.5 106.5 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2234 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 699 SG
REMARK 620 2 SF4 A2234 S2 112.8
REMARK 620 3 SF4 A2234 S3 112.1 106.4
REMARK 620 4 SF4 A2234 S4 112.9 107.1 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2234 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 745 SG
REMARK 620 2 SF4 A2234 S1 112.8
REMARK 620 3 SF4 A2234 S2 113.1 105.7
REMARK 620 4 SF4 A2234 S4 111.9 106.1 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2234 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 748 SG
REMARK 620 2 SF4 A2234 S1 114.3
REMARK 620 3 SF4 A2234 S2 116.6 105.7
REMARK 620 4 SF4 A2234 S3 106.9 106.5 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2234 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 751 SG
REMARK 620 2 SF4 A2234 S1 112.0
REMARK 620 3 SF4 A2234 S3 111.4 106.8
REMARK 620 4 SF4 A2234 S4 114.7 106.2 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2233 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 755 SG
REMARK 620 2 SF4 A2233 S1 113.0
REMARK 620 3 SF4 A2233 S2 112.5 105.6
REMARK 620 4 SF4 A2233 S3 113.1 105.3 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2235 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 812 SG
REMARK 620 2 SF4 A2235 S2 111.4
REMARK 620 3 SF4 A2235 S3 115.3 105.6
REMARK 620 4 SF4 A2235 S4 110.6 107.5 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2235 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 815 SG
REMARK 620 2 SF4 A2235 S1 115.3
REMARK 620 3 SF4 A2235 S2 112.4 104.9
REMARK 620 4 SF4 A2235 S4 110.5 105.0 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2235 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 840 SG
REMARK 620 2 SF4 A2235 S1 112.4
REMARK 620 3 SF4 A2235 S3 110.7 108.2
REMARK 620 4 SF4 A2235 S4 114.6 104.9 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2237 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 963 OD1
REMARK 620 2 THR A 991 OG1 90.1
REMARK 620 3 VAL A 993 O 110.3 77.3
REMARK 620 4 HOH A2209 O 70.4 81.1 158.5
REMARK 620 5 TPP A2236 O1B 151.6 78.5 92.6 82.1
REMARK 620 6 TPP A2236 O2A 89.6 171.2 111.0 90.4 97.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2238 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 983 OD2
REMARK 620 2 ASN A 985 OD1 118.3
REMARK 620 3 PHE A1059 O 84.5 146.0
REMARK 620 4 GLY A1061 O 92.2 114.7 87.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2235 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1071 SG
REMARK 620 2 SF4 A2235 S1 112.4
REMARK 620 3 SF4 A2235 S2 117.3 104.6
REMARK 620 4 SF4 A2235 S3 108.0 108.1 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2233 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 689 SG
REMARK 620 2 SF4 B2233 S2 113.1
REMARK 620 3 SF4 B2233 S3 113.6 106.7
REMARK 620 4 SF4 B2233 S4 110.3 105.9 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2233 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 692 SG
REMARK 620 2 SF4 B2233 S1 107.4
REMARK 620 3 SF4 B2233 S2 116.0 105.0
REMARK 620 4 SF4 B2233 S4 114.9 106.5 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2233 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 695 SG
REMARK 620 2 SF4 B2233 S1 109.0
REMARK 620 3 SF4 B2233 S3 116.8 104.9
REMARK 620 4 SF4 B2233 S4 111.7 106.5 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2234 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 699 SG
REMARK 620 2 SF4 B2234 S2 111.2
REMARK 620 3 SF4 B2234 S3 112.0 106.9
REMARK 620 4 SF4 B2234 S4 113.7 107.1 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2234 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 745 SG
REMARK 620 2 SF4 B2234 S1 109.3
REMARK 620 3 SF4 B2234 S2 113.6 104.5
REMARK 620 4 SF4 B2234 S4 114.4 107.1 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2234 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 748 SG
REMARK 620 2 SF4 B2234 S1 117.1
REMARK 620 3 SF4 B2234 S2 117.5 104.1
REMARK 620 4 SF4 B2234 S3 103.9 106.5 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2234 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 751 SG
REMARK 620 2 SF4 B2234 S1 110.8
REMARK 620 3 SF4 B2234 S3 111.7 107.0
REMARK 620 4 SF4 B2234 S4 115.1 106.6 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2233 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 755 SG
REMARK 620 2 SF4 B2233 S1 112.7
REMARK 620 3 SF4 B2233 S2 111.0 105.9
REMARK 620 4 SF4 B2233 S3 114.8 105.2 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2235 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 812 SG
REMARK 620 2 SF4 B2235 S2 112.1
REMARK 620 3 SF4 B2235 S3 114.1 104.9
REMARK 620 4 SF4 B2235 S4 111.8 107.4 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2235 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 815 SG
REMARK 620 2 SF4 B2235 S1 116.7
REMARK 620 3 SF4 B2235 S2 112.9 105.1
REMARK 620 4 SF4 B2235 S4 108.2 106.5 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2235 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 840 SG
REMARK 620 2 SF4 B2235 S1 111.3
REMARK 620 3 SF4 B2235 S3 110.0 107.8
REMARK 620 4 SF4 B2235 S4 115.6 105.9 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2237 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 963 OD1
REMARK 620 2 THR B 991 OG1 88.7
REMARK 620 3 VAL B 993 O 100.2 78.7
REMARK 620 4 TPP B2236 O1B 170.8 86.4 86.4
REMARK 620 5 TPP B2236 O2A 98.2 172.2 103.6 86.3
REMARK 620 6 HOH B2255 O 80.2 72.9 151.6 91.0 104.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2238 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 983 OD2
REMARK 620 2 ASN B 985 OD1 108.1
REMARK 620 3 ALA B1056 O 161.7 78.0
REMARK 620 4 GLU B1057 O 94.3 84.2 68.8
REMARK 620 5 PHE B1059 O 79.5 168.7 92.3 87.1
REMARK 620 6 GLY B1061 O 79.5 120.8 112.8 155.1 68.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2235 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1071 SG
REMARK 620 2 SF4 B2235 S1 112.7
REMARK 620 3 SF4 B2235 S2 115.7 105.5
REMARK 620 4 SF4 B2235 S3 109.6 108.1 104.6
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 MG A2237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A2236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A2239
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2233
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2234
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2235
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B2236
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B2239
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM
REMARK 900 DESULFOVIBRIO AFRICANUS
REMARK 900 RELATED ID: 1KEK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OFPYRUVATE:
REMARK 900 FERREDOXIN OXIDOREDUCTASE
REMARK 900 RELATED ID: 2C3M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM
REMARK 900 DESULFOVIBRIO AFRICANUS
REMARK 900 RELATED ID: 2C3P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:
REMARK 900 FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
REMARK 900 RELATED ID: 2C3U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM
REMARK 900 DESULFOVIBRIO AFRICANUS, OXYGEN INHIBITED FORM
REMARK 900 RELATED ID: 2C3Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RADICAL FORM OF PYRUVATE:FERREDOXIN
REMARK 900 OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
REMARK 900 RELATED ID: 2C42 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM
REMARK 900 DESULFOVIBRIO AFRICANUS
REMARK 900 RELATED ID: 2PDA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PYRUVATE- FERREDOXIN
REMARK 900 OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS AND PYRUVATE.
DBREF 2C3O A 2 1232 UNP P94692 P94692_DESAF 2 1232
DBREF 2C3O B 2 1232 UNP P94692 P94692_DESAF 2 1232
SEQRES 1 A 1231 GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR
SEQRES 2 A 1231 ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE
SEQRES 3 A 1231 TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA
SEQRES 4 A 1231 ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY
SEQRES 5 A 1231 GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY
SEQRES 6 A 1231 ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA
SEQRES 7 A 1231 LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU
SEQRES 8 A 1231 MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU
SEQRES 9 A 1231 PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA
SEQRES 10 A 1231 HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR
SEQRES 11 A 1231 ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER
SEQRES 12 A 1231 SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS
SEQRES 13 A 1231 LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE
SEQRES 14 A 1231 PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE
SEQRES 15 A 1231 GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN
SEQRES 16 A 1231 GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN
SEQRES 17 A 1231 PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO
SEQRES 18 A 1231 ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR
SEQRES 19 A 1231 TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN
SEQRES 20 A 1231 LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE
SEQRES 21 A 1231 ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL
SEQRES 22 A 1231 SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE
SEQRES 23 A 1231 ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE
SEQRES 24 A 1231 LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE
SEQRES 25 A 1231 PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL
SEQRES 26 A 1231 LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO
SEQRES 27 A 1231 LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY
SEQRES 28 A 1231 GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU
SEQRES 29 A 1231 GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL
SEQRES 30 A 1231 TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR
SEQRES 31 A 1231 VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO
SEQRES 32 A 1231 VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR
SEQRES 33 A 1231 ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR
SEQRES 34 A 1231 VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP
SEQRES 35 A 1231 ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP
SEQRES 36 A 1231 SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG
SEQRES 37 A 1231 PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN
SEQRES 38 A 1231 ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL
SEQRES 39 A 1231 GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY
SEQRES 40 A 1231 THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP
SEQRES 41 A 1231 MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE
SEQRES 42 A 1231 ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL
SEQRES 43 A 1231 LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN
SEQRES 44 A 1231 MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL
SEQRES 45 A 1231 LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER
SEQRES 46 A 1231 ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL
SEQRES 47 A 1231 LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER
SEQRES 48 A 1231 LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA
SEQRES 49 A 1231 PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE
SEQRES 50 A 1231 PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY
SEQRES 51 A 1231 ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG
SEQRES 52 A 1231 PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL
SEQRES 53 A 1231 ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE
SEQRES 54 A 1231 GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA
SEQRES 55 A 1231 ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY
SEQRES 56 A 1231 ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS
SEQRES 57 A 1231 GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR
SEQRES 58 A 1231 LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS
SEQRES 59 A 1231 PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP
SEQRES 60 A 1231 THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA
SEQRES 61 A 1231 ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP
SEQRES 62 A 1231 SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU
SEQRES 63 A 1231 PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR
SEQRES 64 A 1231 VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE
SEQRES 65 A 1231 ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA
SEQRES 66 A 1231 SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY
SEQRES 67 A 1231 GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA
SEQRES 68 A 1231 ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA
SEQRES 69 A 1231 ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU
SEQRES 70 A 1231 GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN
SEQRES 71 A 1231 GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS
SEQRES 72 A 1231 GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN
SEQRES 73 A 1231 LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP
SEQRES 74 A 1231 LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP
SEQRES 75 A 1231 GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS
SEQRES 76 A 1231 VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET
SEQRES 77 A 1231 ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER
SEQRES 78 A 1231 LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA
SEQRES 79 A 1231 ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET
SEQRES 80 A 1231 VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER
SEQRES 81 A 1231 MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS
SEQRES 82 A 1231 GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA
SEQRES 83 A 1231 TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET
SEQRES 84 A 1231 GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER
SEQRES 85 A 1231 GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA
SEQRES 86 A 1231 ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA
SEQRES 87 A 1231 PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN
SEQRES 88 A 1231 ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA
SEQRES 89 A 1231 LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL
SEQRES 90 A 1231 ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE
SEQRES 91 A 1231 PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY
SEQRES 92 A 1231 SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG
SEQRES 93 A 1231 ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU
SEQRES 94 A 1231 ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN
SEQRES 95 A 1231 GLY ASP LEU SER LYS ARG THR LYS LYS
SEQRES 1 B 1231 GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR
SEQRES 2 B 1231 ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE
SEQRES 3 B 1231 TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA
SEQRES 4 B 1231 ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY
SEQRES 5 B 1231 GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY
SEQRES 6 B 1231 ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA
SEQRES 7 B 1231 LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU
SEQRES 8 B 1231 MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU
SEQRES 9 B 1231 PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA
SEQRES 10 B 1231 HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR
SEQRES 11 B 1231 ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER
SEQRES 12 B 1231 SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS
SEQRES 13 B 1231 LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE
SEQRES 14 B 1231 PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE
SEQRES 15 B 1231 GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN
SEQRES 16 B 1231 GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN
SEQRES 17 B 1231 PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO
SEQRES 18 B 1231 ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR
SEQRES 19 B 1231 TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN
SEQRES 20 B 1231 LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE
SEQRES 21 B 1231 ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL
SEQRES 22 B 1231 SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE
SEQRES 23 B 1231 ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE
SEQRES 24 B 1231 LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE
SEQRES 25 B 1231 PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL
SEQRES 26 B 1231 LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO
SEQRES 27 B 1231 LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY
SEQRES 28 B 1231 GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU
SEQRES 29 B 1231 GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL
SEQRES 30 B 1231 TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR
SEQRES 31 B 1231 VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO
SEQRES 32 B 1231 VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR
SEQRES 33 B 1231 ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR
SEQRES 34 B 1231 VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP
SEQRES 35 B 1231 ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP
SEQRES 36 B 1231 SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG
SEQRES 37 B 1231 PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN
SEQRES 38 B 1231 ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL
SEQRES 39 B 1231 GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY
SEQRES 40 B 1231 THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP
SEQRES 41 B 1231 MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE
SEQRES 42 B 1231 ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL
SEQRES 43 B 1231 LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN
SEQRES 44 B 1231 MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL
SEQRES 45 B 1231 LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER
SEQRES 46 B 1231 ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL
SEQRES 47 B 1231 LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER
SEQRES 48 B 1231 LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA
SEQRES 49 B 1231 PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE
SEQRES 50 B 1231 PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY
SEQRES 51 B 1231 ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG
SEQRES 52 B 1231 PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL
SEQRES 53 B 1231 ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE
SEQRES 54 B 1231 GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA
SEQRES 55 B 1231 ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY
SEQRES 56 B 1231 ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS
SEQRES 57 B 1231 GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR
SEQRES 58 B 1231 LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS
SEQRES 59 B 1231 PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP
SEQRES 60 B 1231 THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA
SEQRES 61 B 1231 ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP
SEQRES 62 B 1231 SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU
SEQRES 63 B 1231 PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR
SEQRES 64 B 1231 VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE
SEQRES 65 B 1231 ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA
SEQRES 66 B 1231 SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY
SEQRES 67 B 1231 GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA
SEQRES 68 B 1231 ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA
SEQRES 69 B 1231 ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU
SEQRES 70 B 1231 GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN
SEQRES 71 B 1231 GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS
SEQRES 72 B 1231 GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN
SEQRES 73 B 1231 LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP
SEQRES 74 B 1231 LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP
SEQRES 75 B 1231 GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS
SEQRES 76 B 1231 VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET
SEQRES 77 B 1231 ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER
SEQRES 78 B 1231 LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA
SEQRES 79 B 1231 ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET
SEQRES 80 B 1231 VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER
SEQRES 81 B 1231 MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS
SEQRES 82 B 1231 GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA
SEQRES 83 B 1231 TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET
SEQRES 84 B 1231 GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER
SEQRES 85 B 1231 GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA
SEQRES 86 B 1231 ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA
SEQRES 87 B 1231 PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN
SEQRES 88 B 1231 ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA
SEQRES 89 B 1231 LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL
SEQRES 90 B 1231 ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE
SEQRES 91 B 1231 PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY
SEQRES 92 B 1231 SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG
SEQRES 93 B 1231 ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU
SEQRES 94 B 1231 ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN
SEQRES 95 B 1231 GLY ASP LEU SER LYS ARG THR LYS LYS
HET SF4 A2233 8
HET SF4 A2234 8
HET SF4 A2235 8
HET TPP A2236 26
HET MG A2237 1
HET CA A2238 1
HET PYR A2239 6
HET SF4 B2233 8
HET SF4 B2234 8
HET SF4 B2235 8
HET TPP B2236 26
HET MG B2237 1
HET CA B2238 1
HET PYR B2239 6
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM TPP THIAMINE DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
HETNAM PYR PYRUVIC ACID
FORMUL 3 SF4 6(FE4 S4)
FORMUL 6 TPP 2(C12 H19 N4 O7 P2 S 1+)
FORMUL 7 MG 2(MG 2+)
FORMUL 8 CA 2(CA 2+)
FORMUL 9 PYR 2(C3 H4 O3)
FORMUL 17 HOH *569(H2 O)
HELIX 1 1 GLY A 10 MET A 21 1 12
HELIX 2 2 SER A 33 GLY A 47 1 15
HELIX 3 3 SER A 63 ALA A 77 1 15
HELIX 4 4 ALA A 86 LEU A 92 1 7
HELIX 5 5 MET A 93 GLU A 103 1 11
HELIX 6 6 HIS A 127 ALA A 133 1 7
HELIX 7 7 SER A 145 ASN A 164 1 20
HELIX 8 8 ASP A 187 SER A 193 1 7
HELIX 9 9 ASN A 196 SER A 207 1 12
HELIX 10 10 ILE A 224 ALA A 231 1 8
HELIX 11 11 ALA A 232 GLY A 255 1 24
HELIX 12 12 SER A 278 LYS A 293 1 16
HELIX 13 13 VAL A 309 ALA A 316 1 8
HELIX 14 14 ASP A 338 GLY A 352 1 15
HELIX 15 15 SER A 371 SER A 383 1 13
HELIX 16 16 GLY A 429 ASP A 443 1 15
HELIX 17 17 ASN A 491 ILE A 497 5 7
HELIX 18 18 SER A 518 LEU A 526 1 9
HELIX 19 19 PRO A 527 LYS A 537 1 11
HELIX 20 20 ASP A 545 VAL A 553 1 9
HELIX 21 21 ILE A 559 ALA A 571 1 13
HELIX 22 22 PRO A 575 ALA A 590 1 16
HELIX 23 23 LYS A 594 LEU A 613 1 20
HELIX 24 24 PRO A 619 ALA A 625 5 7
HELIX 25 25 VAL A 642 THR A 648 1 7
HELIX 26 26 GLN A 650 LEU A 654 5 5
HELIX 27 27 PRO A 655 PHE A 659 5 5
HELIX 28 28 GLY A 668 PHE A 672 5 5
HELIX 29 29 ASN A 693 CYS A 699 1 7
HELIX 30 30 GLY A 749 CYS A 755 1 7
HELIX 31 31 GLN A 770 ALA A 782 1 13
HELIX 32 32 SER A 795 GLN A 800 1 6
HELIX 33 33 GLU A 817 GLY A 829 1 13
HELIX 34 34 GLY A 839 SER A 847 1 9
HELIX 35 35 ASP A 871 SER A 900 1 30
HELIX 36 36 SER A 903 LYS A 917 1 15
HELIX 37 37 ASP A 919 ALA A 935 1 17
HELIX 38 38 ASP A 939 ALA A 947 1 9
HELIX 39 39 MET A 948 TYR A 952 5 5
HELIX 40 40 ASP A 963 ASP A 968 1 6
HELIX 41 41 GLY A 970 SER A 980 1 11
HELIX 42 42 ASP A 1024 THR A 1031 1 8
HELIX 43 43 SER A 1045 PHE A 1059 1 15
HELIX 44 44 GLY A 1079 GLY A 1081 5 3
HELIX 45 45 LYS A 1082 SER A 1093 1 12
HELIX 46 46 ASP A 1102 ALA A 1107 1 6
HELIX 47 47 SER A 1123 MET A 1129 1 7
HELIX 48 48 GLN A 1131 VAL A 1136 1 6
HELIX 49 49 VAL A 1136 PHE A 1141 1 6
HELIX 50 50 PHE A 1141 THR A 1169 1 29
HELIX 51 51 THR A 1219 ARG A 1229 1 11
HELIX 52 52 GLY B 10 SER B 22 1 13
HELIX 53 53 SER B 33 GLY B 47 1 15
HELIX 54 54 SER B 63 ALA B 77 1 15
HELIX 55 55 ALA B 86 LEU B 92 1 7
HELIX 56 56 MET B 93 GLU B 103 1 11
HELIX 57 57 HIS B 127 ALA B 132 1 6
HELIX 58 58 SER B 145 ASN B 164 1 20
HELIX 59 59 ASP B 187 LEU B 194 1 8
HELIX 60 60 ASN B 196 SER B 207 1 12
HELIX 61 61 ILE B 224 ALA B 231 1 8
HELIX 62 62 ALA B 232 GLY B 255 1 24
HELIX 63 63 SER B 278 LYS B 293 1 16
HELIX 64 64 VAL B 309 ALA B 316 1 8
HELIX 65 65 ASP B 338 GLY B 352 1 15
HELIX 66 66 GLY B 364 LYS B 368 5 5
HELIX 67 67 SER B 371 GLY B 384 1 14
HELIX 68 68 GLY B 429 ASP B 443 1 15
HELIX 69 69 ASN B 491 ILE B 497 5 7
HELIX 70 70 SER B 518 LEU B 526 1 9
HELIX 71 71 PRO B 527 LYS B 537 1 11
HELIX 72 72 ASP B 545 GLY B 554 1 10
HELIX 73 73 ILE B 559 ALA B 571 1 13
HELIX 74 74 PRO B 575 ALA B 590 1 16
HELIX 75 75 LYS B 594 THR B 611 1 18
HELIX 76 76 PRO B 619 LYS B 623 5 5
HELIX 77 77 ASN B 636 VAL B 642 1 7
HELIX 78 78 VAL B 642 THR B 648 1 7
HELIX 79 79 GLN B 650 LEU B 654 5 5
HELIX 80 80 PRO B 655 PHE B 659 5 5
HELIX 81 81 GLY B 668 PHE B 672 5 5
HELIX 82 82 ASN B 693 CYS B 699 1 7
HELIX 83 83 GLU B 712 LEU B 714 5 3
HELIX 84 84 GLY B 749 CYS B 755 1 7
HELIX 85 85 GLN B 770 ILE B 784 1 15
HELIX 86 86 SER B 795 GLN B 800 1 6
HELIX 87 87 GLU B 817 GLY B 829 1 13
HELIX 88 88 GLY B 839 SER B 847 1 9
HELIX 89 89 ASP B 871 LEU B 898 1 28
HELIX 90 90 SER B 903 GLY B 916 1 14
HELIX 91 91 ASP B 919 LEU B 934 1 16
HELIX 92 92 ASP B 939 ALA B 947 1 9
HELIX 93 93 MET B 948 THR B 953 1 6
HELIX 94 94 ASP B 963 ASP B 968 1 6
HELIX 95 95 GLY B 970 SER B 980 1 11
HELIX 96 96 ASP B 1024 MET B 1030 1 7
HELIX 97 97 SER B 1045 PHE B 1059 1 15
HELIX 98 98 CYS B 1071 GLY B 1075 5 5
HELIX 99 99 GLY B 1079 GLY B 1081 5 3
HELIX 100 100 LYS B 1082 SER B 1093 1 12
HELIX 101 101 ASP B 1102 GLN B 1108 1 7
HELIX 102 102 SER B 1123 ALA B 1130 1 8
HELIX 103 103 GLN B 1131 PHE B 1141 1 11
HELIX 104 104 PHE B 1141 THR B 1169 1 29
HELIX 105 105 THR B 1219 ARG B 1229 1 11
SHEET 1 AA 8 MET A 5 ASP A 9 0
SHEET 2 AA 8 ILE A 180 GLU A 184 -1 O GLN A 181 N THR A 8
SHEET 3 AA 8 PHE A 448 SER A 454 -1 O ALA A 449 N LYS A 182
SHEET 4 AA 8 ILE A 463 GLY A 471 -1 O ILE A 465 N SER A 454
SHEET 5 AA 8 ILE A 418 LEU A 425 -1 O ILE A 418 N PHE A 470
SHEET 6 AA 8 TYR A 486 CYS A 489 1 O TYR A 486 N GLN A 421
SHEET 7 AA 8 THR A 509 ASN A 513 1 O THR A 509 N VAL A 487
SHEET 8 AA 8 LYS A 540 ILE A 544 1 O LYS A 540 N PHE A 510
SHEET 1 AB 7 THR A 57 GLU A 60 0
SHEET 2 AB 7 VAL A 24 ILE A 27 1 O ALA A 25 N ARG A 59
SHEET 3 AB 7 THR A 81 THR A 85 1 O THR A 82 N ALA A 26
SHEET 4 AB 7 VAL A 108 ALA A 113 1 O VAL A 108 N THR A 83
SHEET 5 AB 7 PHE A 167 ASP A 172 1 O PHE A 167 N PHE A 109
SHEET 6 AB 7 ALA A 139 ALA A 142 1 O ALA A 139 N MET A 168
SHEET 7 AB 7 LEU A 304 ARG A 306 -1 N TYR A 305 O MET A 140
SHEET 1 AC 9 VAL A 215 ARG A 216 0
SHEET 2 AC 9 ALA B 863 GLY B 865 1 O TRP B 864 N ARG A 216
SHEET 3 AC 9 MET B 832 ASN B 836 1 O MET B 832 N ALA B 863
SHEET 4 AC 9 SER B 956 GLY B 962 1 O SER B 956 N PHE B 833
SHEET 5 AC 9 ASN B 985 ASP B 990 1 O ASN B 985 N ILE B 959
SHEET 6 AC 9 SER B1063 TYR B1068 1 O SER B1063 N VAL B 986
SHEET 7 AC 9 TYR B1036 VAL B1040 1 O TYR B1036 N LEU B1064
SHEET 8 AC 9 PHE B1099 TYR B1101 -1 O PHE B1099 N THR B1039
SHEET 9 AC 9 PHE B1113 LEU B1115 -1 O GLN B1114 N ARG B1100
SHEET 1 AD 6 PHE A 261 GLY A 265 0
SHEET 2 AD 6 ILE A 297 VAL A 302 -1 O LEU A 299 N VAL A 264
SHEET 3 AD 6 ARG A 271 SER A 275 1 O ARG A 271 N GLY A 298
SHEET 4 AD 6 VAL A 323 ASP A 328 1 O VAL A 323 N VAL A 272
SHEET 5 AD 6 LYS A 357 TYR A 363 1 O LYS A 357 N ILE A 324
SHEET 6 AD 6 PHE A 390 VAL A 392 1 O PHE A 390 N ARG A 362
SHEET 1 AE 2 ASN A 680 TRP A 684 0
SHEET 2 AE 2 LEU A 762 PRO A 766 -1 O VAL A 763 N GLN A 683
SHEET 1 AF 3 ILE A 704 ALA A 709 0
SHEET 2 AF 3 LYS A 735 ILE A 740 -1 O LYS A 735 N ALA A 709
SHEET 3 AF 3 LEU A 724 GLU A 725 -1 O LEU A 724 N PHE A 736
SHEET 1 AG 9 PHE A1113 LEU A1115 0
SHEET 2 AG 9 PHE A1099 TYR A1101 -1 O ARG A1100 N GLN A1114
SHEET 3 AG 9 TYR A1036 VAL A1040 -1 O VAL A1037 N TYR A1101
SHEET 4 AG 9 SER A1063 TYR A1068 1 O LEU A1064 N ALA A1038
SHEET 5 AG 9 ASN A 985 ASP A 990 1 O VAL A 986 N VAL A1065
SHEET 6 AG 9 SER A 956 GLY A 962 1 O VAL A 957 N ASN A 985
SHEET 7 AG 9 MET A 832 ASN A 836 1 O PHE A 833 N TRP A 958
SHEET 8 AG 9 ALA A 863 GLY A 865 1 O ALA A 863 N ILE A 834
SHEET 9 AG 9 VAL B 215 ARG B 216 1 N ARG B 216 O TRP A 864
SHEET 1 BA 8 LYS B 3 ASP B 9 0
SHEET 2 BA 8 ILE B 180 LEU B 186 -1 O GLN B 181 N THR B 8
SHEET 3 BA 8 PHE B 448 SER B 454 -1 O ALA B 449 N LYS B 182
SHEET 4 BA 8 ILE B 463 GLY B 471 -1 O ILE B 465 N SER B 454
SHEET 5 BA 8 ILE B 418 LEU B 425 -1 O ILE B 418 N PHE B 470
SHEET 6 BA 8 TYR B 486 CYS B 489 1 O TYR B 486 N GLN B 421
SHEET 7 BA 8 THR B 509 ASN B 513 1 O THR B 509 N VAL B 487
SHEET 8 BA 8 LYS B 540 ILE B 544 1 O LYS B 540 N PHE B 510
SHEET 1 BB 7 THR B 57 GLU B 60 0
SHEET 2 BB 7 VAL B 24 ILE B 27 1 O ALA B 25 N ARG B 59
SHEET 3 BB 7 THR B 81 THR B 85 1 O THR B 82 N ALA B 26
SHEET 4 BB 7 VAL B 108 ALA B 113 1 O VAL B 108 N THR B 83
SHEET 5 BB 7 PHE B 167 ASP B 172 1 O PHE B 167 N PHE B 109
SHEET 6 BB 7 ALA B 139 ALA B 142 1 O ALA B 139 N MET B 168
SHEET 7 BB 7 LEU B 304 ARG B 306 -1 N TYR B 305 O MET B 140
SHEET 1 BC 6 PHE B 261 GLY B 265 0
SHEET 2 BC 6 ILE B 297 VAL B 302 -1 O LEU B 299 N VAL B 264
SHEET 3 BC 6 ARG B 271 SER B 275 1 O ARG B 271 N GLY B 298
SHEET 4 BC 6 VAL B 323 ASP B 328 1 O VAL B 323 N VAL B 272
SHEET 5 BC 6 ILE B 358 ARG B 362 1 O LEU B 359 N VAL B 326
SHEET 6 BC 6 PHE B 390 THR B 391 1 O PHE B 390 N ARG B 362
SHEET 1 BD 2 ASN B 680 TRP B 684 0
SHEET 2 BD 2 LEU B 762 PRO B 766 -1 O VAL B 763 N GLN B 683
SHEET 1 BE 3 ILE B 704 LYS B 710 0
SHEET 2 BE 3 TYR B 734 ILE B 740 -1 O LYS B 735 N ALA B 709
SHEET 3 BE 3 LEU B 724 GLU B 725 -1 O LEU B 724 N PHE B 736
SSBOND 1 CYS A 1195 CYS A 1212 1555 1555 2.02
SSBOND 2 CYS B 1195 CYS B 1212 1555 1555 2.03
LINK SG CYS A 689 FE1 SF4 A2233 1555 1555 2.31
LINK SG CYS A 692 FE3 SF4 A2233 1555 1555 2.33
LINK SG CYS A 695 FE2 SF4 A2233 1555 1555 2.30
LINK SG CYS A 699 FE1 SF4 A2234 1555 1555 2.30
LINK SG CYS A 745 FE3 SF4 A2234 1555 1555 2.30
LINK SG CYS A 748 FE4 SF4 A2234 1555 1555 2.31
LINK SG CYS A 751 FE2 SF4 A2234 1555 1555 2.30
LINK SG CYS A 755 FE4 SF4 A2233 1555 1555 2.30
LINK SG CYS A 812 FE1 SF4 A2235 1555 1555 2.30
LINK SG CYS A 815 FE3 SF4 A2235 1555 1555 2.30
LINK SG CYS A 840 FE2 SF4 A2235 1555 1555 2.29
LINK OD1 ASP A 963 MG MG A2237 1555 1555 2.05
LINK OD2 ASP A 983 CA CA A2238 1555 1555 2.55
LINK OD1 ASN A 985 CA CA A2238 1555 1555 2.90
LINK OG1 THR A 991 MG MG A2237 1555 1555 2.49
LINK O VAL A 993 MG MG A2237 1555 1555 2.06
LINK O PHE A1059 CA CA A2238 1555 1555 2.54
LINK O GLY A1061 CA CA A2238 1555 1555 2.70
LINK SG CYS A1071 FE4 SF4 A2235 1555 1555 2.30
LINK O HOH A2209 MG MG A2237 1555 1555 2.25
LINK O1B TPP A2236 MG MG A2237 1555 1555 1.96
LINK O2A TPP A2236 MG MG A2237 1555 1555 2.11
LINK SG CYS B 689 FE1 SF4 B2233 1555 1555 2.30
LINK SG CYS B 692 FE3 SF4 B2233 1555 1555 2.30
LINK SG CYS B 695 FE2 SF4 B2233 1555 1555 2.29
LINK SG CYS B 699 FE1 SF4 B2234 1555 1555 2.30
LINK SG CYS B 745 FE3 SF4 B2234 1555 1555 2.30
LINK SG CYS B 748 FE4 SF4 B2234 1555 1555 2.32
LINK SG CYS B 751 FE2 SF4 B2234 1555 1555 2.30
LINK SG CYS B 755 FE4 SF4 B2233 1555 1555 2.31
LINK SG CYS B 812 FE1 SF4 B2235 1555 1555 2.28
LINK SG CYS B 815 FE3 SF4 B2235 1555 1555 2.31
LINK SG CYS B 840 FE2 SF4 B2235 1555 1555 2.30
LINK OD1 ASP B 963 MG MG B2237 1555 1555 1.95
LINK OD2 ASP B 983 CA CA B2238 1555 1555 2.70
LINK OD1 ASN B 985 CA CA B2238 1555 1555 2.65
LINK OG1 THR B 991 MG MG B2237 1555 1555 2.10
LINK O VAL B 993 MG MG B2237 1555 1555 2.11
LINK O ALA B1056 CA CA B2238 1555 1555 2.87
LINK O GLU B1057 CA CA B2238 1555 1555 3.12
LINK O PHE B1059 CA CA B2238 1555 1555 2.53
LINK O GLY B1061 CA CA B2238 1555 1555 2.86
LINK SG CYS B1071 FE4 SF4 B2235 1555 1555 2.30
LINK O1B TPP B2236 MG MG B2237 1555 1555 2.21
LINK O2A TPP B2236 MG MG B2237 1555 1555 2.39
LINK MG MG B2237 O HOH B2255 1555 1555 2.14
CISPEP 1 THR A 31 PRO A 32 0 -0.12
CISPEP 2 ARG A 306 PRO A 307 0 -0.04
CISPEP 3 ALA A 848 PRO A 849 0 0.05
CISPEP 4 THR B 31 PRO B 32 0 -0.24
CISPEP 5 ARG B 306 PRO B 307 0 -0.10
CISPEP 6 ALA B 848 PRO B 849 0 -0.01
SITE 1 AC1 5 ASP A 963 THR A 991 VAL A 993 HOH A2209
SITE 2 AC1 5 TPP A2236
SITE 1 AC2 7 ASP A 983 ASN A 985 ALA A1056 GLU A1057
SITE 2 AC2 7 PHE A1059 GLY A1061 SER A1063
SITE 1 AC3 5 ASP B 963 THR B 991 VAL B 993 TPP B2236
SITE 2 AC3 5 HOH B2255
SITE 1 AC4 7 ASP B 983 ASN B 985 ALA B1056 GLU B1057
SITE 2 AC4 7 PHE B1059 GLY B1061 SER B1063
SITE 1 AC5 7 CYS A 689 ILE A 690 CYS A 692 ASN A 693
SITE 2 AC5 7 CYS A 695 CYS A 755 LEU A 762
SITE 1 AC6 8 PRO A 682 CYS A 699 ILE A 704 CYS A 745
SITE 2 AC6 8 MET A 746 CYS A 748 GLY A 749 CYS A 751
SITE 1 AC7 8 LYS A 459 CYS A 812 CYS A 815 GLU A 817
SITE 2 AC7 8 CYS A 840 TRP A 844 CYS A1071 MET B1203
SITE 1 AC8 27 PRO A 29 ILE A 30 GLU A 64 GLN A 88
SITE 2 AC8 27 LEU A 92 GLU A 817 THR A 838 GLY A 839
SITE 3 AC8 27 CYS A 840 PHE A 869 GLU A 870 GLY A 962
SITE 4 AC8 27 ASP A 963 GLY A 964 TRP A 965 THR A 991
SITE 5 AC8 27 VAL A 993 TYR A 994 SER A 995 ASN A 996
SITE 6 AC8 27 THR A 997 HOH A2179 HOH A2180 HOH A2190
SITE 7 AC8 27 HOH A2209 MG A2237 PYR A2239
SITE 1 AC9 6 THR A 31 ARG A 114 ASN A 996 THR A 997
SITE 2 AC9 6 TPP A2236 MET B1202
SITE 1 BC1 10 TRP B 684 CYS B 689 ILE B 690 CYS B 692
SITE 2 BC1 10 ASN B 693 CYS B 695 CYS B 755 PRO B 756
SITE 3 BC1 10 ALA B 761 LEU B 762
SITE 1 BC2 9 CYS B 699 PRO B 700 ALA B 703 ILE B 704
SITE 2 BC2 9 CYS B 745 MET B 746 CYS B 748 GLY B 749
SITE 3 BC2 9 CYS B 751
SITE 1 BC3 6 LYS B 459 CYS B 812 CYS B 815 GLU B 817
SITE 2 BC3 6 CYS B 840 CYS B1071
SITE 1 BC4 23 TYR B 28 PRO B 29 GLU B 64 GLN B 88
SITE 2 BC4 23 LEU B 92 GLU B 817 GLY B 839 CYS B 840
SITE 3 BC4 23 PHE B 869 GLY B 962 ASP B 963 GLY B 964
SITE 4 BC4 23 TRP B 965 THR B 991 VAL B 993 TYR B 994
SITE 5 BC4 23 SER B 995 ASN B 996 THR B 997 MG B2237
SITE 6 BC4 23 PYR B2239 HOH B2255 HOH B2307
SITE 1 BC5 6 MET A1202 THR B 31 ARG B 114 ASN B 996
SITE 2 BC5 6 THR B 997 TPP B2236
CRYST1 85.650 145.236 204.293 90.00 90.00 90.00 P 21 21 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 0.011675 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004895 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
