HEADER ELECTRON TRANSPORT 01-OCT-99 1D3W
TITLE CRYSTAL STRUCTURE OF FERREDOXIN 1 D15E MUTANT FROM AZOTOBACTER
TITLE 2 VINELANDII AT 1.7 ANGSTROM RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 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;
SOURCE 6 OTHER_DETAILS: THE SEQUENCE WAS MUTATED BY SITE DIRECTED MUTAGENESIS
SOURCE 7 USING BIORAD MUTAGENE 2 KIT.
KEYWDS BETA SHEET, PROTEIN MONOMER, IRON-SULPHUR PROTEIN, FERREDOXIN,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR K.CHEN,J.HIRST,R.CAMBA,C.A.BONAGURA,C.D.STOUT,B.K.BURGES,
AUTHOR 2 F.A.ARMSTRONG
REVDAT 4 07-FEB-24 1D3W 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1D3W 1 VERSN
REVDAT 2 05-APR-05 1D3W 1 COMPND SOURCE MASTER JRNL
REVDAT 2 2 1 REMARK CRYST1 CONECT
REVDAT 1 14-OCT-99 1D3W 0
JRNL AUTH K.CHEN,J.HIRST,R.CAMBA,C.A.BONAGURA,C.D.STOUT,B.K.BURGESS,
JRNL AUTH 2 F.A.ARMSTRONG
JRNL TITL ATOMICALLY DEFINED MECHANISM FOR PROTON TRANSFER TO A BURIED
JRNL TITL 2 REDOX CENTRE IN A PROTEIN.
JRNL REF NATURE V. 405 814 2000
JRNL REFN ISSN 0028-0836
JRNL PMID 10866206
JRNL DOI 10.1038/35015610
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 10561
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 528
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 : 842
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.895
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 1D3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009771.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-99
REMARK 200 TEMPERATURE (KELVIN) : 100
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 IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16030
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 13.81
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54600
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 (%): 58.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: .4M TRIS PH 7.8, 1.2 M AMMONIUM
REMARK 280 SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 46.26750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.68500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.68500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.13375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.68500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.68500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.40125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.68500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.68500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.13375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.68500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.68500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.40125
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 46.26750
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO A 36 H2 HOH A 157 1.45
REMARK 500 OE2 GLU A 73 H2 HOH A 131 1.47
REMARK 500 OD1 ASP A 41 H1 HOH A 141 1.49
REMARK 500 O ILE A 81 H1 HOH A 114 1.56
REMARK 500 O GLY A 99 H1 HOH A 193 1.59
REMARK 500 O GLU A 59 H2 HOH A 135 1.59
REMARK 500 OE2 GLU A 46 H2 HOH A 201 1.60
REMARK 500 OE1 GLU A 66 H1 HOH A 185 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 H1 HOH A 136 O HOH A 247 3545 1.34
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 -167.82 -105.01
REMARK 500 LYS A 10 -3.39 76.36
REMARK 500 ASN A 30 32.30 -145.76
REMARK 500 ALA A 43 -2.10 62.94
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 112.0
REMARK 620 3 F3S A 108 S3 113.8 103.2
REMARK 620 4 F3S A 108 S4 108.8 111.4 107.5
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 113.6
REMARK 620 3 F3S A 108 S2 108.2 112.0
REMARK 620 4 F3S A 108 S3 114.1 103.3 105.4
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 110.9
REMARK 620 3 SF4 A 107 S2 119.1 103.9
REMARK 620 4 SF4 A 107 S3 112.8 105.4 103.6
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 118.0
REMARK 620 3 SF4 A 107 S3 118.3 103.7
REMARK 620 4 SF4 A 107 S4 105.7 105.5 104.1
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 CYS A 42 SG
REMARK 620 2 SF4 A 107 S1 99.8
REMARK 620 3 SF4 A 107 S3 121.6 105.6
REMARK 620 4 SF4 A 107 S4 119.8 103.9 103.7
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 107.5
REMARK 620 3 SF4 A 107 S2 118.9 104.3
REMARK 620 4 SF4 A 107 S4 114.1 104.6 106.0
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 111.7
REMARK 620 3 F3S A 108 S3 109.5 106.0
REMARK 620 4 F3S A 108 S4 111.1 111.3 107.0
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: 1FDD RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF FERREDOXIN I D15N MUTANT AT 1.9 ANGSTROM
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1BOT RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF FERREDOXIN I D15K, K84D MUTANT AT 2.1
REMARK 900 ANGSTROM RESOLUTION.
REMARK 900 RELATED ID: 6FDR RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DITHIONITE REDUCED FERREDOXIN I WILDTYPE
REMARK 900 FROM AZOTOBACTER VINELANDII AT 1.4 ANGSTROM RESOLUTION.
REMARK 900 RELATED ID: 7FDR RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF FERREDOXIN I
REMARK 900 WILDTYPE FROM AZOTOBACTER VINELANDII AT 1.4 ANGSTROM RESOLUTION.
DBREF 1D3W A 1 106 UNP P00214 FER1_AZOVI 2 107
SEQADV 1D3W GLU A 15 UNP P00214 ASP 15 ENGINEERED MUTATION
SEQRES 1 A 106 ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS TYR
SEQRES 2 A 106 THR GLU 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 CYS 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 *140(H2 O)
HELIX 1 1 ASP A 6 ILE A 9 5 4
HELIX 2 2 CYS A 45 CYS A 49 5 5
HELIX 3 3 ASP A 58 VAL A 60 5 3
HELIX 4 4 PRO A 61 MET A 64 5 4
HELIX 5 5 GLN A 65 TRP A 78 1 14
HELIX 6 6 ASP A 90 ASP A 95 1 6
HELIX 7 7 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 GLY A 28 0
SHEET 2 B 2 PHE A 31 ILE A 34 -1 O PHE A 31 N GLY A 28
LINK SG CYS A 8 FE3 F3S A 108 1555 1555 2.28
LINK SG CYS A 16 FE1 F3S A 108 1555 1555 2.28
LINK SG CYS A 20 FE4 SF4 A 107 1555 1555 2.28
LINK SG CYS A 39 FE1 SF4 A 107 1555 1555 2.29
LINK SG CYS A 42 FE2 SF4 A 107 1555 1555 2.31
LINK SG CYS A 45 FE3 SF4 A 107 1555 1555 2.29
LINK SG CYS A 49 FE4 F3S A 108 1555 1555 2.27
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 CYS 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 GLU A 15 CYS A 16 LEU A 32 CYS A 49
SITE 3 AC2 9 PRO A 50
CRYST1 55.370 55.370 92.535 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 0.018060 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010807 0.00000
(ATOM LINES ARE NOT SHOWN.)
END