HEADER OXIDOREDUCTASE 09-NOV-06 2NUK
TITLE SOLUBLE DOMAIN OF THE RIESKE IRON-SULFUR PROTEIN FROM RHODOBACTER
TITLE 2 SPHAEROIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 47-187;
COMPND 5 SYNONYM: RIESKE IRON-SULFUR PROTEIN, RISP;
COMPND 6 EC: 1.10.2.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 GENE: PETA, FBCF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IRON SULFUR CLUSTER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOLLING,J.BRUNZELLE,S.LHEE,A.R.CROFTS,S.K.NAIR
REVDAT 4 30-AUG-23 2NUK 1 REMARK LINK
REVDAT 3 18-OCT-17 2NUK 1 REMARK
REVDAT 2 24-FEB-09 2NUK 1 VERSN
REVDAT 1 10-APR-07 2NUK 0
JRNL AUTH D.J.KOLLING,J.S.BRUNZELLE,S.LHEE,A.R.CROFTS,S.K.NAIR
JRNL TITL ATOMIC RESOLUTION STRUCTURES OF RIESKE IRON-SULFUR PROTEIN:
JRNL TITL 2 ROLE OF HYDROGEN BONDS IN TUNING THE REDOX POTENTIAL OF
JRNL TITL 3 IRON-SULFUR CLUSTERS.
JRNL REF STRUCTURE V. 15 29 2007
JRNL REFN ISSN 0969-2126
JRNL PMID 17223530
JRNL DOI 10.1016/J.STR.2006.11.012
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 38022
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.120
REMARK 3 R VALUE (WORKING SET) : 0.118
REMARK 3 FREE R VALUE : 0.136
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700
REMARK 3 FREE R VALUE TEST SET COUNT : 3177
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.1020
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.1130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1063
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.05000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.031
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.015
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.669
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1121 ; 0.003 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1013 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1530 ; 1.738 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2354 ; 0.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 5.089 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;33.503 ;23.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 173 ; 8.532 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;11.870 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 169 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1294 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 227 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 203 ; 0.231 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1099 ; 0.192 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 567 ; 0.170 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 646 ; 0.083 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 217 ; 0.126 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 4 ; 0.302 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 23 ; 0.122 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.147 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 926 ; 1.145 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 301 ; 0.533 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1162 ; 1.513 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 459 ; 1.363 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 366 ; 1.869 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1379 ; 0.747 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 198 ;21.201 ;30.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1092 ; 2.547 ;30.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2NUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040319.
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 : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41254
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.02000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.06500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 19.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2NWF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 20% ANHYDROUS
REMARK 280 GLYCEROL, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.28400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.28400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.38450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.28400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.28400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.38450
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 35.28400
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 35.28400
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 27.38450
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 35.28400
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 35.28400
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 27.38450
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 47 CG CD1 CD2
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 H ILE A 162 HD22 ASN A 170 1.33
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 MET A 125 CG - SD - CE ANGL. DEV. = 13.4 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 ALA A 109 46.43 -78.31
REMARK 500 HIS A 131 -79.55 -76.53
REMARK 500 ASP A 180 -166.00 -179.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 200 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 129 SG
REMARK 620 2 FES A 200 S1 111.3
REMARK 620 3 FES A 200 S2 109.5 105.1
REMARK 620 4 CYS A 149 SG 106.4 112.2 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 200 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 131 ND1
REMARK 620 2 FES A 200 S1 112.8
REMARK 620 3 FES A 200 S2 116.8 104.3
REMARK 620 4 HIS A 152 ND1 92.4 119.0 112.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NUM RELATED DB: PDB
REMARK 900 RELATED ID: 2NVE RELATED DB: PDB
REMARK 900 RELATED ID: 2NVF RELATED DB: PDB
REMARK 900 RELATED ID: 2NVG RELATED DB: PDB
REMARK 900 RELATED ID: 2NWF RELATED DB: PDB
DBREF 2NUK A 47 187 UNP Q02762 UCRI_RHOSH 47 187
SEQRES 1 A 141 LEU ALA SER ILE PHE VAL ASP VAL SER SER VAL GLU PRO
SEQRES 2 A 141 GLY VAL GLN LEU THR VAL LYS PHE LEU GLY LYS PRO ILE
SEQRES 3 A 141 PHE ILE ARG ARG ARG THR GLU ALA ASP ILE GLU LEU GLY
SEQRES 4 A 141 ARG SER VAL GLN LEU GLY GLN LEU VAL ASP THR ASN ALA
SEQRES 5 A 141 ARG ASN ALA ASN ILE ASP ALA GLY ALA GLU ALA THR ASP
SEQRES 6 A 141 GLN ASN ARG THR LEU ASP GLU ALA GLY GLU TRP LEU VAL
SEQRES 7 A 141 MET TRP GLY VAL CYS THR HIS LEU GLY CYS VAL PRO ILE
SEQRES 8 A 141 GLY GLY VAL SER GLY ASP PHE GLY GLY TRP PHE CYS PRO
SEQRES 9 A 141 CYS HIS GLY SER HIS TYR ASP SER ALA GLY ARG ILE ARG
SEQRES 10 A 141 LYS GLY PRO ALA PRO GLU ASN LEU PRO ILE PRO LEU ALA
SEQRES 11 A 141 LYS PHE ILE ASP GLU THR THR ILE GLN LEU GLY
HET FES A 200 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
FORMUL 3 HOH *198(H2 O)
HELIX 1 1 THR A 78 SER A 87 1 10
HELIX 2 2 VAL A 88 LEU A 93 5 6
HELIX 3 3 THR A 110 THR A 115 5 6
SHEET 1 A 3 ILE A 50 ASP A 53 0
SHEET 2 A 3 THR A 183 LEU A 186 -1 O ILE A 184 N VAL A 52
SHEET 3 A 3 ALA A 176 PHE A 178 -1 N LYS A 177 O GLN A 185
SHEET 1 B 3 VAL A 61 PHE A 67 0
SHEET 2 B 3 LYS A 70 ARG A 76 -1 O ILE A 72 N VAL A 65
SHEET 3 B 3 TRP A 122 TRP A 126 -1 O MET A 125 N PHE A 73
SHEET 1 C 4 ILE A 137 SER A 141 0
SHEET 2 C 4 GLY A 146 CYS A 149 -1 O PHE A 148 N ILE A 137
SHEET 3 C 4 SER A 154 TYR A 156 -1 O SER A 154 N CYS A 149
SHEET 4 C 4 ILE A 162 LYS A 164 -1 O ARG A 163 N HIS A 155
SSBOND 1 CYS A 134 CYS A 151 1555 1555 2.03
LINK SG CYS A 129 FE1 FES A 200 1555 1555 2.33
LINK ND1 HIS A 131 FE2 FES A 200 1555 1555 2.12
LINK SG CYS A 149 FE1 FES A 200 1555 1555 2.29
LINK ND1 HIS A 152 FE2 FES A 200 1555 1555 2.10
SITE 1 AC1 6 CYS A 129 HIS A 131 LEU A 132 CYS A 149
SITE 2 AC1 6 HIS A 152 SER A 154
CRYST1 70.568 70.568 54.769 90.00 90.00 90.00 I 4 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 0.014171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014171 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
