HEADER OXIDOREDUCTASE 14-JUN-07 2V3A
TITLE CRYSTAL STRUCTURE OF RUBREDOXIN REDUCTASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALKANE DEGRADATION, NADH OXIDOREDUCTASE, RUBREDOXIN REDUCTASE, FAD,
KEYWDS 2 NAD, FLAVOPROTEIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.HAGELUEKEN,L.WIEHLMANN,T.M.ADAMS,H.KOLMAR,D.W.HEINZ,B.TUEMMLER,
AUTHOR 2 W.-D.SCHUBERT
REVDAT 3 13-JUL-11 2V3A 1 VERSN
REVDAT 2 24-FEB-09 2V3A 1 VERSN
REVDAT 1 14-AUG-07 2V3A 0
JRNL AUTH G.HAGELUEKEN,L.WIEHLMANN,T.M.ADAMS,H.KOLMAR,D.W.HEINZ,
JRNL AUTH 2 B.TUEMMLER,W.-D.SCHUBERT
JRNL TITL CRYSTAL STRUCTURE OF THE ELECTRON TRANSFER COMPLEX
JRNL TITL 2 RUBREDOXIN - RUBREDOXIN REDUCTASE FROM PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 12276 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17636129
JRNL DOI 10.1073/PNAS.0702919104
REMARK 2
REMARK 2 RESOLUTION. 2.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 103.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 25303
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1333
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2981
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.47000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 0.70000
REMARK 3 B12 (A**2) : -0.23000
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): 0.214
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.244
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3148 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4295 ; 1.493 ; 2.014
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 421 ; 6.003 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;34.928 ;22.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 511 ;14.987 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;21.153 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 477 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2397 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1371 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2059 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 260 ; 0.151 ; 0.200
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): 67 ; 0.209 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.128 ; 0.200
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): 2026 ; 0.708 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3154 ; 1.079 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1305 ; 1.887 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1126 ; 2.896 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 130
REMARK 3 ORIGIN FOR THE GROUP (A): 83.2847 29.6054 24.8718
REMARK 3 T TENSOR
REMARK 3 T11: -0.1395 T22: -0.1078
REMARK 3 T33: -0.0911 T12: -0.0169
REMARK 3 T13: 0.0717 T23: 0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 1.5729 L22: 2.0179
REMARK 3 L33: 2.1589 L12: -0.1756
REMARK 3 L13: 0.4637 L23: 0.3906
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: -0.1072 S13: -0.1968
REMARK 3 S21: 0.1213 S22: 0.0310 S23: 0.0434
REMARK 3 S31: 0.2540 S32: -0.0323 S33: 0.0045
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 131 A 240
REMARK 3 ORIGIN FOR THE GROUP (A): 79.1395 28.1421 -2.5754
REMARK 3 T TENSOR
REMARK 3 T11: -0.0764 T22: -0.1107
REMARK 3 T33: -0.0766 T12: -0.0141
REMARK 3 T13: -0.0004 T23: -0.0597
REMARK 3 L TENSOR
REMARK 3 L11: 1.3739 L22: 1.6198
REMARK 3 L33: 2.4947 L12: -0.9786
REMARK 3 L13: 0.5631 L23: 0.0517
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: -0.0078 S13: -0.2829
REMARK 3 S21: -0.1683 S22: -0.0199 S23: 0.1833
REMARK 3 S31: 0.2321 S32: -0.0861 S33: 0.0078
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 241 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): 91.3952 42.2053 22.9130
REMARK 3 T TENSOR
REMARK 3 T11: -0.1644 T22: -0.1206
REMARK 3 T33: -0.1292 T12: -0.0170
REMARK 3 T13: 0.0204 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.9388 L22: 2.0051
REMARK 3 L33: 1.8500 L12: -0.6316
REMARK 3 L13: -0.2535 L23: 0.3071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: -0.1191 S13: 0.1235
REMARK 3 S21: 0.0058 S22: 0.0464 S23: -0.2264
REMARK 3 S31: -0.0894 S32: 0.1955 S33: -0.0297
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 311 A 384
REMARK 3 ORIGIN FOR THE GROUP (A): 104.0910 37.7258 0.9397
REMARK 3 T TENSOR
REMARK 3 T11: -0.0771 T22: -0.0141
REMARK 3 T33: -0.0217 T12: 0.0171
REMARK 3 T13: 0.0777 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 3.6774 L22: 1.6911
REMARK 3 L33: 2.7640 L12: 1.3784
REMARK 3 L13: -0.3159 L23: -0.2794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: 0.1877 S13: 0.1856
REMARK 3 S21: -0.3464 S22: -0.0064 S23: -0.1365
REMARK 3 S31: -0.2700 S32: 0.2462 S33: -0.0301
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2V3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-07.
REMARK 100 THE PDBE ID CODE IS EBI-32921.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.981
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 : HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25303
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.7
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.8
REMARK 200 R MERGE FOR SHELL (I) : 0.34
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1XHC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 1000, 40% PEG 300,
REMARK 280 TRIS-CL PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.68800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 105.37600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.03200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 131.72000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.34400
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.68800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 105.37600
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 131.72000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 79.03200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 26.34400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 SER A 2
REMARK 465 GLU A 3
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 125 46.74 -88.14
REMARK 500 ARG A 146 -36.64 -133.80
REMARK 500 ASN A 256 -106.24 -137.81
REMARK 500 CYS A 324 86.22 -152.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1387
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1393
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V3B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ELECTRON TRANSFER
REMARK 900 COMPLEX RUBREDOXIN - RUBREDOXIN REDUCTASE FROM
REMARK 900 PSEUDOMONAS AERUGINOSA.
DBREF 2V3A A 1 384 UNP Q9HTK9 Q9HTK9_PSEAE 1 384
SEQRES 1 A 384 MET SER GLU ARG ALA PRO LEU VAL ILE ILE GLY THR GLY
SEQRES 2 A 384 LEU ALA GLY TYR ASN LEU ALA ARG GLU TRP ARG LYS LEU
SEQRES 3 A 384 ASP GLY GLU THR PRO LEU LEU MET ILE THR ALA ASP ASP
SEQRES 4 A 384 GLY ARG SER TYR SER LYS PRO MET LEU SER THR GLY PHE
SEQRES 5 A 384 SER LYS ASN LYS ASP ALA ASP GLY LEU ALA MET ALA GLU
SEQRES 6 A 384 PRO GLY ALA MET ALA GLU GLN LEU ASN ALA ARG ILE LEU
SEQRES 7 A 384 THR HIS THR ARG VAL THR GLY ILE ASP PRO GLY HIS GLN
SEQRES 8 A 384 ARG ILE TRP ILE GLY GLU GLU GLU VAL ARG TYR ARG ASP
SEQRES 9 A 384 LEU VAL LEU ALA TRP GLY ALA GLU PRO ILE ARG VAL PRO
SEQRES 10 A 384 VAL GLU GLY ASP ALA GLN ASP ALA LEU TYR PRO ILE ASN
SEQRES 11 A 384 ASP LEU GLU ASP TYR ALA ARG PHE ARG GLN ALA ALA ALA
SEQRES 12 A 384 GLY LYS ARG ARG VAL LEU LEU LEU GLY ALA GLY LEU ILE
SEQRES 13 A 384 GLY CYS GLU PHE ALA ASN ASP LEU SER SER GLY GLY TYR
SEQRES 14 A 384 GLN LEU ASP VAL VAL ALA PRO CYS GLU GLN VAL MET PRO
SEQRES 15 A 384 GLY LEU LEU HIS PRO ALA ALA ALA LYS ALA VAL GLN ALA
SEQRES 16 A 384 GLY LEU GLU GLY LEU GLY VAL ARG PHE HIS LEU GLY PRO
SEQRES 17 A 384 VAL LEU ALA SER LEU LYS LYS ALA GLY GLU GLY LEU GLU
SEQRES 18 A 384 ALA HIS LEU SER ASP GLY GLU VAL ILE PRO CYS ASP LEU
SEQRES 19 A 384 VAL VAL SER ALA VAL GLY LEU ARG PRO ARG THR GLU LEU
SEQRES 20 A 384 ALA PHE ALA ALA GLY LEU ALA VAL ASN ARG GLY ILE VAL
SEQRES 21 A 384 VAL ASP ARG SER LEU ARG THR SER HIS ALA ASN ILE TYR
SEQRES 22 A 384 ALA LEU GLY ASP CYS ALA GLU VAL ASP GLY LEU ASN LEU
SEQRES 23 A 384 LEU TYR VAL MET PRO LEU MET ALA CYS ALA ARG ALA LEU
SEQRES 24 A 384 ALA GLN THR LEU ALA GLY ASN PRO SER GLN VAL ALA TYR
SEQRES 25 A 384 GLY PRO MET PRO VAL THR VAL LYS THR PRO ALA CYS PRO
SEQRES 26 A 384 LEU VAL VAL SER PRO PRO PRO ARG GLY MET ASP GLY GLN
SEQRES 27 A 384 TRP LEU VAL GLU GLY SER GLY THR ASP LEU LYS VAL LEU
SEQRES 28 A 384 CYS ARG ASP THR ALA GLY ARG VAL ILE GLY TYR ALA LEU
SEQRES 29 A 384 THR GLY ALA ALA VAL ASN GLU LYS LEU ALA LEU ASN LYS
SEQRES 30 A 384 GLU LEU PRO GLY LEU MET ALA
HET PEG A1385 7
HET PEG A1386 7
HET PEG A1387 7
HET PEG A1388 7
HET PEG A1389 7
HET PEG A1390 7
HET CL A1391 1
HET CL A1392 1
HET FAD A1393 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 CL 2(CL 1-)
FORMUL 4 PEG 6(C4 H10 O3)
FORMUL 5 HOH *231(H2 O)
HELIX 1 1 GLY A 13 LYS A 25 1 13
HELIX 2 2 LYS A 45 GLY A 51 5 7
HELIX 3 3 ASP A 57 LEU A 61 1 5
HELIX 4 4 GLU A 65 LEU A 73 1 9
HELIX 5 5 PRO A 88 HIS A 90 5 3
HELIX 6 6 ASP A 131 ALA A 143 1 13
HELIX 7 7 GLY A 154 GLY A 167 1 14
HELIX 8 8 HIS A 186 GLY A 199 1 14
HELIX 9 9 THR A 245 ALA A 251 1 7
HELIX 10 10 TYR A 288 ALA A 304 1 17
HELIX 11 11 ALA A 367 ASN A 370 5 4
HELIX 12 12 GLU A 371 LYS A 377 1 7
SHEET 1 AA 5 ARG A 76 LEU A 78 0
SHEET 2 AA 5 LEU A 32 ILE A 35 1 O LEU A 32 N ARG A 76
SHEET 3 AA 5 LEU A 7 ILE A 10 1 O LEU A 7 N LEU A 33
SHEET 4 AA 5 ASP A 104 LEU A 107 1 O ASP A 104 N VAL A 8
SHEET 5 AA 5 ILE A 272 ALA A 274 1 O TYR A 273 N LEU A 107
SHEET 1 AB 2 SER A 42 TYR A 43 0
SHEET 2 AB 2 ALA A 62 ALA A 64 -1 N MET A 63 O SER A 42
SHEET 1 AC 3 GLY A 85 ASP A 87 0
SHEET 2 AC 3 ARG A 92 ILE A 95 -1 O ARG A 92 N ASP A 87
SHEET 3 AC 3 GLU A 98 ARG A 101 -1 O GLU A 98 N ILE A 95
SHEET 1 AD 2 ALA A 111 PRO A 113 0
SHEET 2 AD 2 LEU A 241 PRO A 243 -1 O ARG A 242 N GLU A 112
SHEET 1 AE 5 LEU A 126 PRO A 128 0
SHEET 2 AE 5 LEU A 234 SER A 237 1 O VAL A 235 N TYR A 127
SHEET 3 AE 5 ARG A 147 LEU A 151 1 O LEU A 149 N VAL A 236
SHEET 4 AE 5 GLN A 170 ALA A 175 1 O GLN A 170 N VAL A 148
SHEET 5 AE 5 ARG A 203 LEU A 206 1 O ARG A 203 N VAL A 173
SHEET 1 AF 3 LEU A 210 ALA A 216 0
SHEET 2 AF 3 GLY A 219 LEU A 224 -1 O GLY A 219 N ALA A 216
SHEET 3 AF 3 VAL A 229 CYS A 232 -1 O ILE A 230 N ALA A 222
SHEET 1 AG 2 ILE A 259 VAL A 261 0
SHEET 2 AG 2 ALA A 279 VAL A 281 1 O GLU A 280 N VAL A 261
SHEET 1 AH 5 VAL A 317 VAL A 319 0
SHEET 2 AH 5 LEU A 326 SER A 329 -1 O LEU A 326 N VAL A 319
SHEET 3 AH 5 VAL A 359 THR A 365 -1 O TYR A 362 N SER A 329
SHEET 4 AH 5 ASP A 347 ARG A 353 -1 O LEU A 348 N THR A 365
SHEET 5 AH 5 GLN A 338 SER A 344 -1 O GLN A 338 N ARG A 353
SITE 1 AC1 4 LEU A 184 VAL A 317 HOH A2218 HOH A2219
SITE 1 AC2 3 MET A 290 PRO A 314 ASN A 376
SITE 1 AC3 5 GLY A 183 LEU A 184 LEU A 185 HIS A 186
SITE 2 AC3 5 TRP A 339
SITE 1 AC4 5 SER A 264 ARG A 266 PRO A 307 GLN A 309
SITE 2 AC4 5 HOH A2220
SITE 1 AC5 2 ARG A 82 ARG A 244
SITE 1 AC6 7 ARG A 82 VAL A 83 ARG A 115 PRO A 117
SITE 2 AC6 7 GLU A 246 LEU A 247 HOH A2221
SITE 1 AC7 3 LEU A 155 ILE A 156 HOH A2130
SITE 1 AC8 4 ARG A 242 THR A 245 GLU A 246 ARG A 257
SITE 1 AC9 39 ILE A 10 GLY A 11 THR A 12 GLY A 13
SITE 2 AC9 39 LEU A 14 ALA A 15 THR A 36 ALA A 37
SITE 3 AC9 39 ASP A 38 LYS A 45 PRO A 46 THR A 81
SITE 4 AC9 39 ARG A 82 VAL A 83 ALA A 108 TRP A 109
SITE 5 AC9 39 GLY A 110 ILE A 156 GLU A 159 PHE A 160
SITE 6 AC9 39 GLY A 276 ASP A 277 LEU A 287 TYR A 288
SITE 7 AC9 39 VAL A 289 LEU A 292 LYS A 320 HOH A2022
SITE 8 AC9 39 HOH A2091 HOH A2156 HOH A2222 HOH A2223
SITE 9 AC9 39 HOH A2224 HOH A2226 HOH A2227 HOH A2228
SITE 10 AC9 39 HOH A2229 HOH A2230 HOH A2231
CRYST1 119.602 119.602 158.064 90.00 90.00 120.00 P 61 2 2 12
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 0.008361 0.004827 0.000000 0.00000
SCALE2 0.000000 0.009655 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
