HEADER OXIDOREDUCTASE 02-JAN-06 2FJE
TITLE ADENOSINE-5-PHOSPHOSULFATE REDUCTASE OXIDIZED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLYLSULFATE REDUCTASE, SUBUNIT A;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: APRA;
COMPND 5 EC: 1.8.99.2;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ADENYLYLSULFATE REDUCTASE, SUBUNIT B;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: APRB;
COMPND 10 EC: 1.8.99.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 6 ORGANISM_TAXID: 2234
KEYWDS APS REDUCTASE, SULFUR CYCLE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHIFFER,G.FRITZ,P.M.KRONECK,U.ERMLER
REVDAT 5 14-FEB-24 2FJE 1 REMARK
REVDAT 4 18-OCT-17 2FJE 1 REMARK
REVDAT 3 31-MAR-09 2FJE 1 LINK ATOM CONECT
REVDAT 2 24-FEB-09 2FJE 1 VERSN
REVDAT 1 28-MAR-06 2FJE 0
JRNL AUTH A.SCHIFFER,G.FRITZ,P.M.KRONECK,U.ERMLER
JRNL TITL REACTION MECHANISM OF THE IRON-SULFUR FLAVOENZYME
JRNL TITL 2 ADENOSINE-5'-PHOSPHOSULFATE REDUCTASE BASED ON THE
JRNL TITL 3 STRUCTURAL CHARACTERIZATION OF DIFFERENT ENZYMATIC STATES
JRNL REF BIOCHEMISTRY V. 45 2960 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16503650
JRNL DOI 10.1021/BI0521689
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 85.4
REMARK 3 NUMBER OF REFLECTIONS : 127075
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.300
REMARK 3 FREE R VALUE TEST SET COUNT : 6400
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 12669
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 1111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -4.04200
REMARK 3 B33 (A**2) : 4.11200
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 52.83
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : COF.PAR
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : COF.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03800
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 37.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.10900
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: FOURIER SYNTHESIS
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 (%): 44.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6 % PEG 4000, 0.1 M NACL, 0.1 M NAAC
REMARK 280 PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
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 36.30000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.95000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.95000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.30000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.75000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTETRAMER PRESENT
REMARK 300 IN THE ASYMMETRIC UNIT
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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 MET C 2001
REMARK 465 MET B 701
REMARK 465 MET D 2701
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 182 C LYS A 183 N -0.234
REMARK 500 ASP C2182 C LYS C2183 N -0.213
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 ALA A 58 -134.94 -112.68
REMARK 500 ASP A 78 86.01 71.26
REMARK 500 GLU A 141 -70.04 -93.47
REMARK 500 ALA A 213 46.68 -141.66
REMARK 500 ALA A 229 2.71 -65.37
REMARK 500 ASP A 268 -54.43 69.02
REMARK 500 MET A 365 -28.65 -155.05
REMARK 500 HIS A 398 -131.87 -93.70
REMARK 500 PHE A 448 -157.29 55.44
REMARK 500 ALA A 529 41.04 -108.96
REMARK 500 ALA C2058 -129.36 -114.20
REMARK 500 ASP C2078 85.04 73.37
REMARK 500 GLU C2141 -70.87 -93.83
REMARK 500 ALA C2229 1.52 -64.57
REMARK 500 ASP C2268 -52.03 69.34
REMARK 500 MET C2365 -28.94 -154.66
REMARK 500 HIS C2398 -131.40 -96.74
REMARK 500 PHE C2448 -158.49 56.85
REMARK 500 ASN C2473 66.60 -155.62
REMARK 500 ALA C2529 40.79 -108.95
REMARK 500 CYS B 713 76.15 62.64
REMARK 500 LYS B 714 -114.05 -14.32
REMARK 500 LEU B 716 171.30 -56.88
REMARK 500 GLU B 743 74.78 -154.71
REMARK 500 GLU D2743 74.69 -160.05
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 B1110 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 710 SG
REMARK 620 2 SF4 B1110 S2 116.4
REMARK 620 3 SF4 B1110 S3 117.5 101.6
REMARK 620 4 SF4 B1110 S4 116.7 99.9 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1110 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 721 SG
REMARK 620 2 SF4 B1110 S1 108.7
REMARK 620 3 SF4 B1110 S2 119.8 101.9
REMARK 620 4 SF4 B1110 S4 113.6 106.1 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1100 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 725 SG
REMARK 620 2 SF4 B1100 S2 111.7
REMARK 620 3 SF4 B1100 S3 114.5 103.0
REMARK 620 4 SF4 B1100 S4 119.2 104.8 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1100 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 747 SG
REMARK 620 2 SF4 B1100 S1 99.6
REMARK 620 3 SF4 B1100 S3 118.8 104.8
REMARK 620 4 SF4 B1100 S4 120.8 104.4 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1100 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 750 SG
REMARK 620 2 SF4 B1100 S1 119.5
REMARK 620 3 SF4 B1100 S2 100.8 102.9
REMARK 620 4 SF4 B1100 S4 119.7 103.9 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1100 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 753 SG
REMARK 620 2 SF4 B1100 S1 110.6
REMARK 620 3 SF4 B1100 S2 111.6 104.7
REMARK 620 4 SF4 B1100 S3 117.2 103.5 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1110 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 757 SG
REMARK 620 2 SF4 B1110 S1 112.8
REMARK 620 3 SF4 B1110 S2 116.2 100.9
REMARK 620 4 SF4 B1110 S3 111.3 106.8 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3110 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2710 SG
REMARK 620 2 SF4 D3110 S2 117.4
REMARK 620 3 SF4 D3110 S3 116.1 102.1
REMARK 620 4 SF4 D3110 S4 115.7 100.8 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3110 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2713 SG
REMARK 620 2 SF4 D3110 S1 98.2
REMARK 620 3 SF4 D3110 S3 121.8 107.4
REMARK 620 4 SF4 D3110 S4 118.0 102.7 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3110 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2721 SG
REMARK 620 2 SF4 D3110 S1 108.0
REMARK 620 3 SF4 D3110 S2 121.5 102.4
REMARK 620 4 SF4 D3110 S4 111.4 106.2 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3100 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2725 SG
REMARK 620 2 SF4 D3100 S1 105.8
REMARK 620 3 SF4 D3100 S2 115.7 103.0
REMARK 620 4 SF4 D3100 S4 118.9 106.6 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3100 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2747 SG
REMARK 620 2 SF4 D3100 S2 121.9
REMARK 620 3 SF4 D3100 S3 101.2 102.1
REMARK 620 4 SF4 D3100 S4 121.0 103.7 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3100 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2750 SG
REMARK 620 2 SF4 D3100 S1 99.8
REMARK 620 3 SF4 D3100 S3 121.8 104.1
REMARK 620 4 SF4 D3100 S4 118.5 105.5 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3100 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2753 SG
REMARK 620 2 SF4 D3100 S1 109.4
REMARK 620 3 SF4 D3100 S2 118.4 104.3
REMARK 620 4 SF4 D3100 S3 111.5 104.6 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D3110 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2757 SG
REMARK 620 2 SF4 D3110 S1 112.4
REMARK 620 3 SF4 D3110 S2 120.4 100.2
REMARK 620 4 SF4 D3110 S3 110.5 104.9 107.1
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 FAD A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 3100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 3110
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JNR RELATED DB: PDB
REMARK 900 RELATED ID: 1JNZ RELATED DB: PDB
REMARK 900 RELATED ID: 2FJA RELATED DB: PDB
REMARK 900 RELATED ID: 2FJB RELATED DB: PDB
REMARK 900 RELATED ID: 1FJD RELATED DB: PDB
DBREF 2FJE A 1 643 UNP O28603 O28603_ARCFU 1 643
DBREF 2FJE C 2001 2643 UNP O28603 O28603_ARCFU 1 643
DBREF 2FJE B 701 850 UNP O28604 O28604_ARCFU 1 150
DBREF 2FJE D 2701 2850 UNP O28604 O28604_ARCFU 1 150
SEQRES 1 A 643 MET VAL TYR TYR PRO LYS LYS TYR GLU LEU TYR LYS ALA
SEQRES 2 A 643 ASP GLU VAL PRO THR GLU VAL VAL GLU THR ASP ILE LEU
SEQRES 3 A 643 ILE ILE GLY GLY GLY PHE SER GLY CYS GLY ALA ALA TYR
SEQRES 4 A 643 GLU ALA ALA TYR TRP ALA LYS LEU GLY GLY LEU LYS VAL
SEQRES 5 A 643 THR LEU VAL GLU LYS ALA ALA VAL GLU ARG SER GLY ALA
SEQRES 6 A 643 VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR ILE ASP
SEQRES 7 A 643 LEU THR GLY ARG SER GLU ARG GLN ASN THR LEU GLU ASP
SEQRES 8 A 643 TYR VAL ARG TYR VAL THR LEU ASP MET MET GLY LEU ALA
SEQRES 9 A 643 ARG GLU ASP LEU VAL ALA ASP TYR ALA ARG HIS VAL ASP
SEQRES 10 A 643 GLY THR VAL HIS LEU PHE GLU LYS TRP GLY LEU PRO ILE
SEQRES 11 A 643 TRP LYS THR PRO ASP GLY LYS TYR VAL ARG GLU GLY GLN
SEQRES 12 A 643 TRP GLN ILE MET ILE HIS GLY GLU SER TYR LYS PRO ILE
SEQRES 13 A 643 ILE ALA GLU ALA ALA LYS MET ALA VAL GLY GLU GLU ASN
SEQRES 14 A 643 ILE TYR GLU ARG VAL PHE ILE PHE GLU LEU LEU LYS ASP
SEQRES 15 A 643 LYS ASN ASP PRO ASN ALA VAL ALA GLY ALA VAL GLY PHE
SEQRES 16 A 643 SER VAL ARG GLU PRO LYS PHE TYR VAL PHE LYS ALA LYS
SEQRES 17 A 643 ALA VAL ILE LEU ALA THR GLY GLY ALA THR LEU LEU PHE
SEQRES 18 A 643 ARG PRO ARG SER THR GLY GLU ALA ALA GLY ARG THR TRP
SEQRES 19 A 643 TYR ALA ILE PHE ASP THR GLY SER GLY TYR TYR MET GLY
SEQRES 20 A 643 LEU LYS ALA GLY ALA MET LEU THR GLN PHE GLU HIS ARG
SEQRES 21 A 643 PHE ILE PRO PHE ARG PHE LYS ASP GLY TYR GLY PRO VAL
SEQRES 22 A 643 GLY ALA TRP PHE LEU PHE PHE LYS CYS LYS ALA LYS ASN
SEQRES 23 A 643 ALA TYR GLY GLU GLU TYR ILE LYS THR ARG ALA ALA GLU
SEQRES 24 A 643 LEU GLU LYS TYR LYS PRO TYR GLY ALA ALA GLN PRO ILE
SEQRES 25 A 643 PRO THR PRO LEU ARG ASN HIS GLN VAL MET LEU GLU ILE
SEQRES 26 A 643 MET ASP GLY ASN GLN PRO ILE TYR MET HIS THR GLU GLU
SEQRES 27 A 643 ALA LEU ALA GLU LEU ALA GLY GLY ASP LYS LYS LYS LEU
SEQRES 28 A 643 LYS HIS ILE TYR GLU GLU ALA PHE GLU ASP PHE LEU ASP
SEQRES 29 A 643 MET THR VAL SER GLN ALA LEU LEU TRP ALA CYS GLN ASN
SEQRES 30 A 643 ILE ASP PRO GLN GLU GLN PRO SER GLU ALA ALA PRO ALA
SEQRES 31 A 643 GLU PRO TYR ILE MET GLY SER HIS SER GLY GLU ALA GLY
SEQRES 32 A 643 PHE TRP VAL CYS GLY PRO GLU ASP LEU MET PRO GLU GLU
SEQRES 33 A 643 TYR ALA LYS LEU PHE PRO LEU LYS TYR ASN ARG MET THR
SEQRES 34 A 643 THR VAL LYS GLY LEU PHE ALA ILE GLY ASP CYS ALA GLY
SEQRES 35 A 643 ALA ASN PRO HIS LYS PHE SER SER GLY SER PHE THR GLU
SEQRES 36 A 643 GLY ARG ILE ALA ALA LYS ALA ALA VAL ARG PHE ILE LEU
SEQRES 37 A 643 GLU GLN LYS PRO ASN PRO GLU ILE ASP ASP ALA VAL VAL
SEQRES 38 A 643 GLU GLU LEU LYS LYS LYS ALA TYR ALA PRO MET GLU ARG
SEQRES 39 A 643 PHE MET GLN TYR LYS ASP LEU SER THR ALA ASP ASP VAL
SEQRES 40 A 643 ASN PRO GLU TYR ILE LEU PRO TRP GLN GLY LEU VAL ARG
SEQRES 41 A 643 LEU GLN LYS ILE MET ASP GLU TYR ALA ALA GLY ILE ALA
SEQRES 42 A 643 THR ILE TYR LYS THR ASN GLU LYS MET LEU GLN ARG ALA
SEQRES 43 A 643 LEU GLU LEU LEU ALA PHE LEU LYS GLU ASP LEU GLU LYS
SEQRES 44 A 643 LEU ALA ALA ARG ASP LEU HIS GLU LEU MET ARG ALA TRP
SEQRES 45 A 643 GLU LEU VAL HIS ARG VAL TRP THR ALA GLU ALA HIS VAL
SEQRES 46 A 643 ARG HIS MET LEU PHE ARG LYS GLU THR ARG TRP PRO GLY
SEQRES 47 A 643 TYR TYR TYR ARG THR ASP TYR PRO GLU LEU ASN ASP GLU
SEQRES 48 A 643 GLU TRP LYS CYS PHE VAL CYS SER LYS TYR ASP ALA GLU
SEQRES 49 A 643 LYS ASP GLU TRP THR PHE GLU LYS VAL PRO TYR VAL GLN
SEQRES 50 A 643 VAL ILE GLU TRP SER PHE
SEQRES 1 C 643 MET VAL TYR TYR PRO LYS LYS TYR GLU LEU TYR LYS ALA
SEQRES 2 C 643 ASP GLU VAL PRO THR GLU VAL VAL GLU THR ASP ILE LEU
SEQRES 3 C 643 ILE ILE GLY GLY GLY PHE SER GLY CYS GLY ALA ALA TYR
SEQRES 4 C 643 GLU ALA ALA TYR TRP ALA LYS LEU GLY GLY LEU LYS VAL
SEQRES 5 C 643 THR LEU VAL GLU LYS ALA ALA VAL GLU ARG SER GLY ALA
SEQRES 6 C 643 VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR ILE ASP
SEQRES 7 C 643 LEU THR GLY ARG SER GLU ARG GLN ASN THR LEU GLU ASP
SEQRES 8 C 643 TYR VAL ARG TYR VAL THR LEU ASP MET MET GLY LEU ALA
SEQRES 9 C 643 ARG GLU ASP LEU VAL ALA ASP TYR ALA ARG HIS VAL ASP
SEQRES 10 C 643 GLY THR VAL HIS LEU PHE GLU LYS TRP GLY LEU PRO ILE
SEQRES 11 C 643 TRP LYS THR PRO ASP GLY LYS TYR VAL ARG GLU GLY GLN
SEQRES 12 C 643 TRP GLN ILE MET ILE HIS GLY GLU SER TYR LYS PRO ILE
SEQRES 13 C 643 ILE ALA GLU ALA ALA LYS MET ALA VAL GLY GLU GLU ASN
SEQRES 14 C 643 ILE TYR GLU ARG VAL PHE ILE PHE GLU LEU LEU LYS ASP
SEQRES 15 C 643 LYS ASN ASP PRO ASN ALA VAL ALA GLY ALA VAL GLY PHE
SEQRES 16 C 643 SER VAL ARG GLU PRO LYS PHE TYR VAL PHE LYS ALA LYS
SEQRES 17 C 643 ALA VAL ILE LEU ALA THR GLY GLY ALA THR LEU LEU PHE
SEQRES 18 C 643 ARG PRO ARG SER THR GLY GLU ALA ALA GLY ARG THR TRP
SEQRES 19 C 643 TYR ALA ILE PHE ASP THR GLY SER GLY TYR TYR MET GLY
SEQRES 20 C 643 LEU LYS ALA GLY ALA MET LEU THR GLN PHE GLU HIS ARG
SEQRES 21 C 643 PHE ILE PRO PHE ARG PHE LYS ASP GLY TYR GLY PRO VAL
SEQRES 22 C 643 GLY ALA TRP PHE LEU PHE PHE LYS CYS LYS ALA LYS ASN
SEQRES 23 C 643 ALA TYR GLY GLU GLU TYR ILE LYS THR ARG ALA ALA GLU
SEQRES 24 C 643 LEU GLU LYS TYR LYS PRO TYR GLY ALA ALA GLN PRO ILE
SEQRES 25 C 643 PRO THR PRO LEU ARG ASN HIS GLN VAL MET LEU GLU ILE
SEQRES 26 C 643 MET ASP GLY ASN GLN PRO ILE TYR MET HIS THR GLU GLU
SEQRES 27 C 643 ALA LEU ALA GLU LEU ALA GLY GLY ASP LYS LYS LYS LEU
SEQRES 28 C 643 LYS HIS ILE TYR GLU GLU ALA PHE GLU ASP PHE LEU ASP
SEQRES 29 C 643 MET THR VAL SER GLN ALA LEU LEU TRP ALA CYS GLN ASN
SEQRES 30 C 643 ILE ASP PRO GLN GLU GLN PRO SER GLU ALA ALA PRO ALA
SEQRES 31 C 643 GLU PRO TYR ILE MET GLY SER HIS SER GLY GLU ALA GLY
SEQRES 32 C 643 PHE TRP VAL CYS GLY PRO GLU ASP LEU MET PRO GLU GLU
SEQRES 33 C 643 TYR ALA LYS LEU PHE PRO LEU LYS TYR ASN ARG MET THR
SEQRES 34 C 643 THR VAL LYS GLY LEU PHE ALA ILE GLY ASP CYS ALA GLY
SEQRES 35 C 643 ALA ASN PRO HIS LYS PHE SER SER GLY SER PHE THR GLU
SEQRES 36 C 643 GLY ARG ILE ALA ALA LYS ALA ALA VAL ARG PHE ILE LEU
SEQRES 37 C 643 GLU GLN LYS PRO ASN PRO GLU ILE ASP ASP ALA VAL VAL
SEQRES 38 C 643 GLU GLU LEU LYS LYS LYS ALA TYR ALA PRO MET GLU ARG
SEQRES 39 C 643 PHE MET GLN TYR LYS ASP LEU SER THR ALA ASP ASP VAL
SEQRES 40 C 643 ASN PRO GLU TYR ILE LEU PRO TRP GLN GLY LEU VAL ARG
SEQRES 41 C 643 LEU GLN LYS ILE MET ASP GLU TYR ALA ALA GLY ILE ALA
SEQRES 42 C 643 THR ILE TYR LYS THR ASN GLU LYS MET LEU GLN ARG ALA
SEQRES 43 C 643 LEU GLU LEU LEU ALA PHE LEU LYS GLU ASP LEU GLU LYS
SEQRES 44 C 643 LEU ALA ALA ARG ASP LEU HIS GLU LEU MET ARG ALA TRP
SEQRES 45 C 643 GLU LEU VAL HIS ARG VAL TRP THR ALA GLU ALA HIS VAL
SEQRES 46 C 643 ARG HIS MET LEU PHE ARG LYS GLU THR ARG TRP PRO GLY
SEQRES 47 C 643 TYR TYR TYR ARG THR ASP TYR PRO GLU LEU ASN ASP GLU
SEQRES 48 C 643 GLU TRP LYS CYS PHE VAL CYS SER LYS TYR ASP ALA GLU
SEQRES 49 C 643 LYS ASP GLU TRP THR PHE GLU LYS VAL PRO TYR VAL GLN
SEQRES 50 C 643 VAL ILE GLU TRP SER PHE
SEQRES 1 B 150 MET PRO SER PHE VAL ASN PRO GLU LYS CYS ASP GLY CYS
SEQRES 2 B 150 LYS ALA LEU GLU ARG THR ALA CYS GLU TYR ILE CYS PRO
SEQRES 3 B 150 ASN ASP LEU MET THR LEU ASP LYS GLU LYS MET LYS ALA
SEQRES 4 B 150 TYR ASN ARG GLU PRO ASP MET CYS TRP GLU CYS TYR SER
SEQRES 5 B 150 CYS VAL LYS MET CYS PRO GLN GLY ALA ILE ASP VAL ARG
SEQRES 6 B 150 GLY TYR VAL ASP TYR SER PRO LEU GLY GLY ALA CYS VAL
SEQRES 7 B 150 PRO MET ARG GLY THR SER ASP ILE MET TRP THR VAL LYS
SEQRES 8 B 150 TYR ARG ASN GLY LYS VAL LEU ARG PHE LYS PHE ALA ILE
SEQRES 9 B 150 ARG THR THR PRO TRP GLY SER ILE GLN PRO PHE GLU GLY
SEQRES 10 B 150 PHE PRO GLU PRO THR GLU GLU ALA LEU LYS SER GLU LEU
SEQRES 11 B 150 LEU ALA GLY GLU PRO GLU ILE ILE GLY THR SER GLU PHE
SEQRES 12 B 150 PRO GLN VAL LYS LYS LYS ALA
SEQRES 1 D 150 MET PRO SER PHE VAL ASN PRO GLU LYS CYS ASP GLY CYS
SEQRES 2 D 150 LYS ALA LEU GLU ARG THR ALA CYS GLU TYR ILE CYS PRO
SEQRES 3 D 150 ASN ASP LEU MET THR LEU ASP LYS GLU LYS MET LYS ALA
SEQRES 4 D 150 TYR ASN ARG GLU PRO ASP MET CYS TRP GLU CYS TYR SER
SEQRES 5 D 150 CYS VAL LYS MET CYS PRO GLN GLY ALA ILE ASP VAL ARG
SEQRES 6 D 150 GLY TYR VAL ASP TYR SER PRO LEU GLY GLY ALA CYS VAL
SEQRES 7 D 150 PRO MET ARG GLY THR SER ASP ILE MET TRP THR VAL LYS
SEQRES 8 D 150 TYR ARG ASN GLY LYS VAL LEU ARG PHE LYS PHE ALA ILE
SEQRES 9 D 150 ARG THR THR PRO TRP GLY SER ILE GLN PRO PHE GLU GLY
SEQRES 10 D 150 PHE PRO GLU PRO THR GLU GLU ALA LEU LYS SER GLU LEU
SEQRES 11 D 150 LEU ALA GLY GLU PRO GLU ILE ILE GLY THR SER GLU PHE
SEQRES 12 D 150 PRO GLN VAL LYS LYS LYS ALA
HET FAD A1000 53
HET FAD C3000 53
HET SF4 B1100 8
HET SF4 B1110 8
HET SF4 D3100 8
HET SF4 D3110 8
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 5 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 SF4 4(FE4 S4)
FORMUL 11 HOH *1111(H2 O)
HELIX 1 1 LYS A 12 VAL A 16 5 5
HELIX 2 2 GLY A 31 LYS A 46 1 16
HELIX 3 3 THR A 88 MET A 100 1 13
HELIX 4 4 ARG A 105 TRP A 126 1 22
HELIX 5 5 SER A 152 GLY A 166 1 15
HELIX 6 6 GLY A 227 ARG A 232 5 6
HELIX 7 7 GLY A 241 GLY A 251 1 11
HELIX 8 8 VAL A 273 PHE A 279 1 7
HELIX 9 9 GLU A 291 ARG A 296 1 6
HELIX 10 10 ALA A 297 LYS A 304 5 8
HELIX 11 11 PRO A 305 ALA A 309 5 5
HELIX 12 12 PRO A 313 ASP A 327 1 15
HELIX 13 13 HIS A 335 GLY A 345 1 11
HELIX 14 14 ASP A 347 ASP A 364 1 18
HELIX 15 15 THR A 366 GLN A 376 1 11
HELIX 16 16 PRO A 414 LYS A 419 1 6
HELIX 17 17 GLY A 438 ALA A 441 5 4
HELIX 18 18 LYS A 447 LYS A 471 1 25
HELIX 19 19 ASP A 477 LYS A 499 1 23
HELIX 20 20 ASP A 500 SER A 502 5 3
HELIX 21 21 LEU A 513 ALA A 529 1 17
HELIX 22 22 GLY A 531 ILE A 535 5 5
HELIX 23 23 ASN A 539 GLU A 558 1 20
HELIX 24 24 ASP A 564 ARG A 591 1 28
HELIX 25 30 LYS C 2012 VAL C 2016 5 5
HELIX 26 31 GLY C 2031 ALA C 2045 1 15
HELIX 27 32 LYS C 2046 GLY C 2048 5 3
HELIX 28 33 THR C 2088 MET C 2100 1 13
HELIX 29 34 ARG C 2105 TRP C 2126 1 22
HELIX 30 35 SER C 2152 GLY C 2166 1 15
HELIX 31 36 GLY C 2227 ARG C 2232 5 6
HELIX 32 37 GLY C 2241 GLY C 2251 1 11
HELIX 33 38 VAL C 2273 PHE C 2279 1 7
HELIX 34 39 GLU C 2291 ARG C 2296 1 6
HELIX 35 40 ALA C 2297 GLU C 2301 5 5
HELIX 36 41 PRO C 2305 ALA C 2309 5 5
HELIX 37 42 PRO C 2313 GLY C 2328 1 16
HELIX 38 43 HIS C 2335 GLY C 2345 1 11
HELIX 39 44 ASP C 2347 ASP C 2364 1 18
HELIX 40 45 THR C 2366 GLN C 2376 1 11
HELIX 41 46 PRO C 2414 LYS C 2419 1 6
HELIX 42 47 GLY C 2438 ALA C 2441 5 4
HELIX 43 48 LYS C 2447 LYS C 2471 1 25
HELIX 44 49 ASP C 2477 LYS C 2499 1 23
HELIX 45 50 ASP C 2500 SER C 2502 5 3
HELIX 46 51 LEU C 2513 ALA C 2529 1 17
HELIX 47 52 GLY C 2531 ILE C 2535 5 5
HELIX 48 53 ASN C 2539 GLU C 2558 1 20
HELIX 49 54 ASP C 2564 ARG C 2591 1 28
HELIX 50 25 THR B 719 CYS B 725 1 7
HELIX 51 26 GLU B 743 CYS B 747 5 5
HELIX 52 27 TYR B 751 CYS B 757 1 7
HELIX 53 28 GLU B 824 SER B 828 5 5
HELIX 54 29 PRO B 835 GLY B 839 5 5
HELIX 55 55 THR D 2719 CYS D 2725 1 7
HELIX 56 56 GLU D 2743 CYS D 2747 5 5
HELIX 57 57 TYR D 2751 CYS D 2757 1 7
HELIX 58 58 THR D 2822 LYS D 2827 1 6
HELIX 59 59 PRO D 2835 GLY D 2839 5 5
SHEET 1 A 4 THR A 18 GLU A 22 0
SHEET 2 A 4 PHE A 202 LYS A 206 1 O PHE A 202 N GLU A 19
SHEET 3 A 4 VAL A 189 SER A 196 -1 N ALA A 192 O PHE A 205
SHEET 4 A 4 VAL A 174 LYS A 181 -1 N LEU A 180 O ALA A 190
SHEET 1 B 5 ILE A 170 GLU A 172 0
SHEET 2 B 5 VAL A 52 GLU A 56 1 N GLU A 56 O TYR A 171
SHEET 3 B 5 ILE A 25 ILE A 28 1 N ILE A 27 O THR A 53
SHEET 4 B 5 ALA A 209 LEU A 212 1 O ILE A 211 N LEU A 26
SHEET 5 B 5 LEU A 434 ALA A 436 1 O PHE A 435 N VAL A 210
SHEET 1 C 2 LEU A 70 ILE A 73 0
SHEET 2 C 2 ILE A 146 GLY A 150 -1 O ILE A 146 N ILE A 73
SHEET 1 D 4 GLY A 403 PHE A 404 0
SHEET 2 D 4 LEU A 254 THR A 255 -1 N THR A 255 O GLY A 403
SHEET 3 D 4 CYS A 615 ASP A 622 -1 O SER A 619 N LEU A 254
SHEET 4 D 4 GLU A 627 PRO A 634 -1 O VAL A 633 N PHE A 616
SHEET 1 E 4 PHE A 264 PHE A 266 0
SHEET 2 E 4 SER A 385 PRO A 389 -1 O ALA A 388 N ARG A 265
SHEET 3 E 4 ILE A 332 MET A 334 -1 N MET A 334 O SER A 385
SHEET 4 E 4 ALA A 284 LYS A 285 -1 N LYS A 285 O TYR A 333
SHEET 1 F 2 LYS A 537 THR A 538 0
SHEET 2 F 2 TYR A 601 ARG A 602 1 O TYR A 601 N THR A 538
SHEET 1 G 2 SER B 703 VAL B 705 0
SHEET 2 G 2 ILE B 762 VAL B 764 -1 O ASP B 763 N PHE B 704
SHEET 1 H 2 MET B 730 ASP B 733 0
SHEET 2 H 2 LYS B 738 ASN B 741 -1 O LYS B 738 N ASP B 733
SHEET 1 I 3 ALA B 776 ARG B 781 0
SHEET 2 I 3 ASP B 785 LYS B 791 -1 O THR B 789 N VAL B 778
SHEET 3 I 3 VAL B 797 ALA B 803 -1 O LEU B 798 N VAL B 790
SHEET 1 J 4 THR C2018 GLU C2022 0
SHEET 2 J 4 PHE C2202 LYS C2206 1 O PHE C2202 N GLU C2019
SHEET 3 J 4 ASP C2185 SER C2196 -1 N ALA C2192 O PHE C2205
SHEET 4 J 4 VAL C2174 ASP C2182 -1 N LEU C2180 O ALA C2190
SHEET 1 K 5 ILE C2170 TYR C2171 0
SHEET 2 K 5 VAL C2052 VAL C2055 1 N LEU C2054 O TYR C2171
SHEET 3 K 5 ILE C2025 ILE C2028 1 N ILE C2025 O THR C2053
SHEET 4 K 5 ALA C2209 LEU C2212 1 O ILE C2211 N LEU C2026
SHEET 5 K 5 LEU C2434 ALA C2436 1 O PHE C2435 N VAL C2210
SHEET 1 L 2 LEU C2070 ILE C2073 0
SHEET 2 L 2 ILE C2146 GLY C2150 -1 O ILE C2146 N ILE C2073
SHEET 1 M 4 GLY C2403 PHE C2404 0
SHEET 2 M 4 LEU C2254 THR C2255 -1 N THR C2255 O GLY C2403
SHEET 3 M 4 CYS C2615 ASP C2622 -1 O SER C2619 N LEU C2254
SHEET 4 M 4 GLU C2627 PRO C2634 -1 O VAL C2633 N PHE C2616
SHEET 1 N 4 PHE C2264 PHE C2266 0
SHEET 2 N 4 SER C2385 PRO C2389 -1 O ALA C2388 N ARG C2265
SHEET 3 N 4 ILE C2332 MET C2334 -1 N MET C2334 O SER C2385
SHEET 4 N 4 ALA C2284 LYS C2285 -1 N LYS C2285 O TYR C2333
SHEET 1 O 2 LYS C2537 THR C2538 0
SHEET 2 O 2 TYR C2601 ARG C2602 1 O TYR C2601 N THR C2538
SHEET 1 P 2 SER D2703 VAL D2705 0
SHEET 2 P 2 ILE D2762 VAL D2764 -1 O ASP D2763 N PHE D2704
SHEET 1 Q 2 MET D2730 ASP D2733 0
SHEET 2 Q 2 LYS D2738 ASN D2741 -1 O LYS D2738 N ASP D2733
SHEET 1 R 3 ALA D2776 ARG D2781 0
SHEET 2 R 3 ASP D2785 LYS D2791 -1 O LYS D2791 N ALA D2776
SHEET 3 R 3 VAL D2797 ALA D2803 -1 O LEU D2798 N VAL D2790
LINK SG CYS B 710 FE1 SF4 B1110 1555 1555 2.50
LINK SG CYS B 721 FE3 SF4 B1110 1555 1555 2.47
LINK SG CYS B 725 FE1 SF4 B1100 1555 1555 2.40
LINK SG CYS B 747 FE2 SF4 B1100 1555 1555 2.38
LINK SG CYS B 750 FE3 SF4 B1100 1555 1555 2.38
LINK SG CYS B 753 FE4 SF4 B1100 1555 1555 2.40
LINK SG CYS B 757 FE4 SF4 B1110 1555 1555 2.48
LINK SG CYS D2710 FE1 SF4 D3110 1555 1555 2.42
LINK SG CYS D2713 FE2 SF4 D3110 1555 1555 2.44
LINK SG CYS D2721 FE3 SF4 D3110 1555 1555 2.45
LINK SG CYS D2725 FE3 SF4 D3100 1555 1555 2.41
LINK SG CYS D2747 FE1 SF4 D3100 1555 1555 2.36
LINK SG CYS D2750 FE2 SF4 D3100 1555 1555 2.35
LINK SG CYS D2753 FE4 SF4 D3100 1555 1555 2.42
LINK SG CYS D2757 FE4 SF4 D3110 1555 1555 2.37
CISPEP 1 LYS A 304 PRO A 305 0 -0.09
CISPEP 2 GLN A 310 PRO A 311 0 -0.03
CISPEP 3 GLN A 330 PRO A 331 0 0.20
CISPEP 4 LYS C 2304 PRO C 2305 0 0.07
CISPEP 5 GLN C 2310 PRO C 2311 0 0.02
CISPEP 6 GLN C 2330 PRO C 2331 0 0.08
CISPEP 7 GLU B 834 PRO B 835 0 -0.01
CISPEP 8 GLU D 2834 PRO D 2835 0 0.27
SITE 1 AC1 37 GLY A 29 GLY A 30 GLY A 31 PHE A 32
SITE 2 AC1 37 SER A 33 GLU A 56 LYS A 57 SER A 63
SITE 3 AC1 37 GLY A 64 ALA A 65 VAL A 66 LEU A 70
SITE 4 AC1 37 ALA A 72 ILE A 73 ASN A 74 PHE A 175
SITE 5 AC1 37 ILE A 176 ALA A 213 THR A 214 GLY A 215
SITE 6 AC1 37 TRP A 234 TYR A 235 ALA A 236 ASP A 239
SITE 7 AC1 37 SER A 242 MET A 365 SER A 397 GLY A 438
SITE 8 AC1 37 ASP A 439 PHE A 448 SER A 449 SER A 452
SITE 9 AC1 37 HOH A5045 HOH A5121 HOH A5319 HOH A5324
SITE 10 AC1 37 HOH A5747
SITE 1 AC2 38 GLY C2029 GLY C2030 GLY C2031 PHE C2032
SITE 2 AC2 38 SER C2033 GLU C2056 LYS C2057 SER C2063
SITE 3 AC2 38 GLY C2064 ALA C2065 VAL C2066 LEU C2070
SITE 4 AC2 38 ALA C2072 ILE C2073 ASN C2074 PHE C2175
SITE 5 AC2 38 ILE C2176 ALA C2213 THR C2214 GLY C2215
SITE 6 AC2 38 TRP C2234 TYR C2235 ALA C2236 ASP C2239
SITE 7 AC2 38 SER C2242 MET C2365 SER C2397 GLY C2438
SITE 8 AC2 38 ASP C2439 PHE C2448 SER C2449 SER C2452
SITE 9 AC2 38 HOH C5008 HOH C5048 HOH C5059 HOH C5197
SITE 10 AC2 38 HOH C5323 HOH C5642
SITE 1 AC3 8 SER B 703 CYS B 725 ASN B 741 CYS B 747
SITE 2 AC3 8 TRP B 748 CYS B 750 TYR B 751 CYS B 753
SITE 1 AC4 8 CYS B 710 ASP B 711 CYS B 713 THR B 719
SITE 2 AC4 8 ALA B 720 CYS B 721 CYS B 757 ILE B 762
SITE 1 AC5 10 SER D2703 CYS D2725 PRO D2726 ASN D2741
SITE 2 AC5 10 CYS D2747 TRP D2748 CYS D2750 TYR D2751
SITE 3 AC5 10 SER D2752 CYS D2753
SITE 1 AC6 9 CYS D2710 ASP D2711 CYS D2713 THR D2719
SITE 2 AC6 9 ALA D2720 CYS D2721 ALA D2739 CYS D2757
SITE 3 AC6 9 ILE D2762
CRYST1 72.600 113.500 193.900 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 0.013774 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END