HEADER ELECTRON TRANSPORT 24-JUL-00 1FF2
TITLE CRYSTAL STRUCTURE OF THE C42D MUTANT OF AZOTOBACTER VINELANDII 7FE
TITLE 2 FERREDOXIN (FDI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FDI, FERREDOXIN [3FE-4S][4FE-4S];
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;
SOURCE 3 ORGANISM_TAXID: 354;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 7FE FERREDOXIN, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.STOUT,B.K.BURGESS
REVDAT 7 07-FEB-24 1FF2 1 REMARK
REVDAT 6 03-NOV-21 1FF2 1 REMARK SEQADV
REVDAT 5 04-OCT-17 1FF2 1 REMARK
REVDAT 4 24-MAR-09 1FF2 1 ATOM CONECT
REVDAT 3 24-FEB-09 1FF2 1 VERSN
REVDAT 2 08-FEB-05 1FF2 1 JRNL REMARK
REVDAT 1 21-AUG-00 1FF2 0
JRNL AUTH Y.S.JUNG,C.A.BONAGURA,G.J.TILLEY,H.S.GAO-SHERIDAN,
JRNL AUTH 2 F.A.ARMSTRONG,C.D.STOUT,B.K.BURGESS
JRNL TITL STRUCTURE OF C42D AZOTOBACTER VINELANDII FDI. A
JRNL TITL 2 CYS-X-X-ASP-X-X-CYS MOTIF LIGATES AN AIR-STABLE [4FE-4S]2+/+
JRNL TITL 3 CLUSTER
JRNL REF J.BIOL.CHEM. V. 275 36974 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10961993
JRNL DOI 10.1074/JBC.M004947200
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.80
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) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 6320
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) : 0.217
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 316
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 : 843
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.640
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 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 1FF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011531.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48416
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-HCL, PH 7.8,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.29500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.65000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.64750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.65000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.94250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.65000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.65000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.64750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.65000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.65000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 67.94250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 45.29500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A 103 NE2 HIS A 103 CD2 -0.070
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 18 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE A 25 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 42 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 42 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP A 78 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 94 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 94 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 5 -166.78 -105.24
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 F3S A 108 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 F3S A 108 S1 115.9
REMARK 620 3 F3S A 108 S3 115.9 105.8
REMARK 620 4 F3S A 108 S4 103.6 108.2 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 108 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 F3S A 108 S1 107.9
REMARK 620 3 F3S A 108 S2 110.5 107.6
REMARK 620 4 F3S A 108 S3 117.5 105.1 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A 107 S1 108.6
REMARK 620 3 SF4 A 107 S2 118.8 104.5
REMARK 620 4 SF4 A 107 S3 114.6 104.4 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 SF4 A 107 S2 120.5
REMARK 620 3 SF4 A 107 S3 112.5 104.5
REMARK 620 4 SF4 A 107 S4 107.0 106.4 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 42 OD2
REMARK 620 2 SF4 A 107 S1 100.5
REMARK 620 3 SF4 A 107 S3 130.3 104.9
REMARK 620 4 SF4 A 107 S4 109.8 103.3 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 SF4 A 107 S1 112.1
REMARK 620 3 SF4 A 107 S2 118.5 105.5
REMARK 620 4 SF4 A 107 S4 110.3 104.8 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 108 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 F3S A 108 S2 110.6
REMARK 620 3 F3S A 108 S3 112.7 107.1
REMARK 620 4 F3S A 108 S4 112.2 105.9 108.1
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 SF4 A 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 108
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FD1 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE NATIVE PROTEIN AT 1.35 A RESOLUTION.
DBREF 1FF2 A 1 106 UNP P00214 FER1_AZOVI 1 106
SEQADV 1FF2 ASP A 42 UNP P00214 CYS 42 ENGINEERED MUTATION
SEQRES 1 A 106 ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS TYR
SEQRES 2 A 106 THR ASP CYS VAL GLU VAL CYS PRO VAL ASP CYS PHE TYR
SEQRES 3 A 106 GLU GLY PRO ASN PHE LEU VAL ILE HIS PRO ASP GLU CYS
SEQRES 4 A 106 ILE ASP ASP ALA LEU CYS GLU PRO GLU CYS PRO ALA GLN
SEQRES 5 A 106 ALA ILE PHE SER GLU ASP GLU VAL PRO GLU ASP MET GLN
SEQRES 6 A 106 GLU PHE ILE GLN LEU ASN ALA GLU LEU ALA GLU VAL TRP
SEQRES 7 A 106 PRO ASN ILE THR GLU LYS LYS ASP PRO LEU PRO ASP ALA
SEQRES 8 A 106 GLU ASP TRP ASP GLY VAL LYS GLY LYS LEU GLN HIS LEU
SEQRES 9 A 106 GLU ARG
HET SF4 A 107 8
HET F3S A 108 7
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
FORMUL 2 SF4 FE4 S4
FORMUL 3 F3S FE3 S4
FORMUL 4 HOH *48(H2 O)
HELIX 1 1 ASP A 6 ILE A 9 5 4
HELIX 2 2 THR A 14 CYS A 20 5 7
HELIX 3 3 CYS A 45 CYS A 49 5 5
HELIX 4 4 ASP A 58 VAL A 60 5 3
HELIX 5 5 PRO A 61 MET A 64 5 4
HELIX 6 6 GLN A 65 GLU A 76 1 12
HELIX 7 7 ASP A 90 ASP A 95 1 6
HELIX 8 8 GLY A 99 LEU A 104 5 6
SHEET 1 A 2 PHE A 2 VAL A 4 0
SHEET 2 A 2 ILE A 54 SER A 56 -1 O PHE A 55 N VAL A 3
SHEET 1 B 2 PHE A 25 GLU A 27 0
SHEET 2 B 2 LEU A 32 ILE A 34 -1 N VAL A 33 O TYR A 26
LINK SG CYS A 8 FE3 F3S A 108 1555 1555 2.32
LINK SG CYS A 16 FE1 F3S A 108 1555 1555 2.38
LINK SG CYS A 20 FE4 SF4 A 107 1555 1555 2.33
LINK SG CYS A 39 FE1 SF4 A 107 1555 1555 2.29
LINK OD2 ASP A 42 FE2 SF4 A 107 1555 1555 2.11
LINK SG CYS A 45 FE3 SF4 A 107 1555 1555 2.28
LINK SG CYS A 49 FE4 F3S A 108 1555 1555 2.33
SITE 1 AC1 11 PHE A 2 CYS A 20 VAL A 22 CYS A 24
SITE 2 AC1 11 PHE A 25 ILE A 34 CYS A 39 ILE A 40
SITE 3 AC1 11 ASP A 42 ALA A 43 CYS A 45
SITE 1 AC2 9 CYS A 8 LYS A 12 TYR A 13 THR A 14
SITE 2 AC2 9 ASP A 15 CYS A 16 LEU A 32 CYS A 49
SITE 3 AC2 9 ILE A 54
CRYST1 55.300 55.300 90.590 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
