HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 13-MAY-14 4QDF
TITLE CRYSTAL STRUCTURE OF APO KSHA5 AND KSHA1 IN COMPLEX WITH 1,4-30Q-COA
TITLE 2 FROM R. RHODOCHROUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-KETOSTEROID 9ALPHA-HYDROXYLASE OXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 3-KETOSTEROID 9ALPHA-HYDROXYLASE OXYGENASE;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: KSHA5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GJ1158;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 11 ORGANISM_TAXID: 1829;
SOURCE 12 GENE: KSHA1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: GJ1158;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MIXED FUNCTION OXYGENASES, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PENFIELD,L.J.WORRALL,N.C.STRYNADKA,L.D.ELTIS
REVDAT 4 28-FEB-24 4QDF 1 REMARK LINK
REVDAT 3 22-NOV-17 4QDF 1 REMARK
REVDAT 2 01-OCT-14 4QDF 1 JRNL
REVDAT 1 30-JUL-14 4QDF 0
JRNL AUTH J.S.PENFIELD,L.J.WORRALL,N.C.STRYNADKA,L.D.ELTIS
JRNL TITL SUBSTRATE SPECIFICITIES AND CONFORMATIONAL FLEXIBILITY OF
JRNL TITL 2 3-KETOSTEROID 9 ALPHA-HYDROXYLASES.
JRNL REF J.BIOL.CHEM. V. 289 25523 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 25049233
JRNL DOI 10.1074/JBC.M114.575886
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 63637
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3222
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) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4428
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5828
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 201
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.999
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6057 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5459 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8225 ; 1.255 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12554 ; 0.743 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 714 ; 6.452 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;33.088 ;23.820
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 949 ;13.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;13.081 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 837 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6907 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1501 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2865 ; 2.946 ; 4.793
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2864 ; 2.942 ; 4.791
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3576 ; 4.780 ; 7.173
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4QDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE CCD X-RAY
REMARK 200 DETECTOR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64010
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 68.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.70
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.30
REMARK 200 R MERGE FOR SHELL (I) : 0.01500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 500 MM NAH2PO4, 125 MM K2HPO4, 4% PEG-
REMARK 280 1000, 20 MM TRIS, 100 MM PHOSPHATE-CITRATE , PH 4.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z+1/2
REMARK 290 15555 -X,Y+1/2,-Z+1/2
REMARK 290 16555 X,-Y+1/2,-Z+1/2
REMARK 290 17555 Z,X+1/2,Y+1/2
REMARK 290 18555 Z,-X+1/2,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y+1/2
REMARK 290 20555 -Z,X+1/2,-Y+1/2
REMARK 290 21555 Y,Z+1/2,X+1/2
REMARK 290 22555 -Y,Z+1/2,-X+1/2
REMARK 290 23555 Y,-Z+1/2,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X+1/2
REMARK 290 25555 X+1/2,Y,Z+1/2
REMARK 290 26555 -X+1/2,-Y,Z+1/2
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X,Y+1/2
REMARK 290 30555 Z+1/2,-X,-Y+1/2
REMARK 290 31555 -Z+1/2,-X,Y+1/2
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y+1/2,Z,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z,-X+1/2
REMARK 290 36555 -Y+1/2,-Z,X+1/2
REMARK 290 37555 X+1/2,Y+1/2,Z
REMARK 290 38555 -X+1/2,-Y+1/2,Z
REMARK 290 39555 -X+1/2,Y+1/2,-Z
REMARK 290 40555 X+1/2,-Y+1/2,-Z
REMARK 290 41555 Z+1/2,X+1/2,Y
REMARK 290 42555 Z+1/2,-X+1/2,-Y
REMARK 290 43555 -Z+1/2,-X+1/2,Y
REMARK 290 44555 -Z+1/2,X+1/2,-Y
REMARK 290 45555 Y+1/2,Z+1/2,X
REMARK 290 46555 -Y+1/2,Z+1/2,-X
REMARK 290 47555 Y+1/2,-Z+1/2,-X
REMARK 290 48555 -Y+1/2,-Z+1/2,X
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 136.84000
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 136.84000
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 136.84000
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 136.84000
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 136.84000
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -173.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 -136.84000
REMARK 350 BIOMT3 2 -1.000000 0.000000 0.000000 136.84000
REMARK 350 BIOMT1 3 0.000000 0.000000 -1.000000 136.84000
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 136.84000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 526 LIES ON A SPECIAL POSITION.
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 ILE A 3
REMARK 465 ASP A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 ASP A 11
REMARK 465 ASP A 12
REMARK 465 ASP A 13
REMARK 465 VAL A 14
REMARK 465 GLU A 15
REMARK 465 ILE A 16
REMARK 465 ARG A 17
REMARK 465 GLU A 18
REMARK 465 ILE A 19
REMARK 465 GLN A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 GLY A 385
REMARK 465 SER A 386
REMARK 465 THR A 387
REMARK 465 ALA A 388
REMARK 465 THR A 389
REMARK 465 PRO A 390
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 SER B 9
REMARK 465 GLU B 10
REMARK 465 ILE B 11
REMARK 465 ARG B 12
REMARK 465 GLU B 13
REMARK 465 ILE B 14
REMARK 465 VAL B 15
REMARK 465 ALA B 16
REMARK 465 GLY B 17
REMARK 465 SER B 18
REMARK 465 ALA B 19
REMARK 465 PRO B 216
REMARK 465 HIS B 217
REMARK 465 ALA B 218
REMARK 465 ASN B 219
REMARK 465 GLY B 220
REMARK 465 GLN B 221
REMARK 465 PRO B 222
REMARK 465 LYS B 223
REMARK 465 SER B 385
REMARK 465 ALA B 386
REMARK 465 PRO B 387
REMARK 465 GLU B 388
REMARK 465 GLN B 389
REMARK 465 SER B 390
REMARK 465 THR B 391
REMARK 465 THR B 392
REMARK 465 ALA B 393
REMARK 465 GLY B 394
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 HIS A 75 -81.20 -72.01
REMARK 500 ASN A 254 -135.38 73.98
REMARK 500 LYS B 37 52.12 -114.30
REMARK 500 ASP B 56 -174.85 -69.13
REMARK 500 HIS B 70 -81.15 -72.36
REMARK 500 THR B 151 44.10 -105.82
REMARK 500 GLU B 248 108.29 -55.04
REMARK 500 LYS B 376 20.86 -77.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 43 GLY A 44 -35.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 30Q B 403
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 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 73 SG
REMARK 620 2 FES A 401 S1 113.8
REMARK 620 3 FES A 401 S2 112.1 99.7
REMARK 620 4 CYS A 92 SG 118.9 108.9 100.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 75 ND1
REMARK 620 2 FES A 401 S1 108.7
REMARK 620 3 FES A 401 S2 119.0 98.8
REMARK 620 4 HIS A 95 ND1 92.3 112.8 125.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 187 NE2
REMARK 620 2 HIS A 192 NE2 99.1
REMARK 620 3 ASP A 311 OD2 138.3 91.7
REMARK 620 4 ASP A 311 OD1 85.5 83.5 55.7
REMARK 620 5 HOH A 602 O 117.6 110.6 95.3 149.0
REMARK 620 6 HOH A 621 O 86.6 173.9 85.2 98.9 64.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 402 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 68 SG
REMARK 620 2 FES B 402 S1 101.8
REMARK 620 3 FES B 402 S2 108.6 95.9
REMARK 620 4 CYS B 87 SG 129.7 115.1 100.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 70 ND1
REMARK 620 2 FES B 402 S1 108.4
REMARK 620 3 FES B 402 S2 125.6 96.3
REMARK 620 4 HIS B 90 ND1 98.8 115.4 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 B 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 186 NE2
REMARK 620 2 ASP B 305 OD1 81.7
REMARK 620 3 ASP B 305 OD2 76.9 54.3
REMARK 620 4 HOH B 533 O 159.5 110.9 97.0
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 FES A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 30Q B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QDC RELATED DB: PDB
REMARK 900 RELATED ID: 4QDD RELATED DB: PDB
REMARK 900 RELATED ID: 4QCK RELATED DB: PDB
DBREF 4QDF A 1 390 UNP F1CMY8 F1CMY8_RHORH 1 390
DBREF 4QDF B 1 394 UNP F1CMX0 F1CMX0_RHORH 1 394
SEQRES 1 A 390 MET SER ILE ASP THR ALA ARG SER GLY SER ASP ASP ASP
SEQRES 2 A 390 VAL GLU ILE ARG GLU ILE GLN ALA ALA ALA ALA PRO THR
SEQRES 3 A 390 ARG PHE ALA ARG GLY TRP HIS CYS LEU GLY LEU LEU ARG
SEQRES 4 A 390 ASP PHE GLN ASP GLY LYS PRO HIS SER ILE GLU ALA PHE
SEQRES 5 A 390 GLY THR LYS LEU VAL VAL PHE ALA ASP SER LYS GLY GLN
SEQRES 6 A 390 LEU ASN VAL LEU ASP ALA TYR CYS ARG HIS MET GLY GLY
SEQRES 7 A 390 ASP LEU SER ARG GLY GLU VAL LYS GLY ASP SER ILE ALA
SEQRES 8 A 390 CYS PRO PHE HIS ASP TRP ARG TRP ASN GLY LYS GLY LYS
SEQRES 9 A 390 CYS THR ASP ILE PRO TYR ALA ARG ARG VAL PRO PRO ILE
SEQRES 10 A 390 ALA LYS THR ARG ALA TRP THR THR LEU GLU ARG ASN GLY
SEQRES 11 A 390 GLN LEU TYR VAL TRP ASN ASP PRO GLN GLY ASN PRO PRO
SEQRES 12 A 390 PRO GLU ASP VAL THR ILE PRO GLU ILE ALA GLY TYR GLY
SEQRES 13 A 390 THR ASP GLU TRP THR ASP TRP SER TRP LYS SER LEU ARG
SEQRES 14 A 390 ILE LYS GLY SER HIS CYS ARG GLU ILE VAL ASP ASN VAL
SEQRES 15 A 390 VAL ASP MET ALA HIS PHE PHE TYR ILE HIS TYR SER PHE
SEQRES 16 A 390 PRO ARG TYR PHE LYS ASN VAL PHE GLU GLY HIS THR ALA
SEQRES 17 A 390 THR GLN TYR MET HIS SER THR GLY ARG GLU ASP VAL ILE
SEQRES 18 A 390 SER GLY THR ASN TYR ASP ASP PRO ASN ALA GLU LEU ARG
SEQRES 19 A 390 SER GLU ALA THR TYR PHE GLY PRO SER TYR MET ILE ASP
SEQRES 20 A 390 TRP LEU GLU SER ASP ALA ASN GLY GLN THR ILE GLU THR
SEQRES 21 A 390 ILE LEU ILE ASN CYS HIS TYR PRO VAL SER ASN ASN GLU
SEQRES 22 A 390 PHE VAL LEU GLN TYR GLY ALA ILE VAL LYS LYS LEU PRO
SEQRES 23 A 390 GLY VAL SER ASP GLU ILE ALA ALA GLY MET ALA GLU GLN
SEQRES 24 A 390 PHE ALA GLU GLY VAL GLN LEU GLY PHE GLU GLN ASP VAL
SEQRES 25 A 390 GLU ILE TRP LYS ASN LYS ALA PRO ILE ASP ASN PRO LEU
SEQRES 26 A 390 LEU SER GLU GLU ASP GLY PRO VAL TYR GLN LEU ARG ARG
SEQRES 27 A 390 TRP TYR GLN GLN PHE TYR VAL ASP VAL GLU ASP ILE THR
SEQRES 28 A 390 GLU ASP MET THR LYS ARG PHE GLU PHE GLU ILE ASP THR
SEQRES 29 A 390 THR ARG ALA VAL ALA SER TRP GLN LYS GLU VAL ALA GLU
SEQRES 30 A 390 ASN LEU ALA LYS GLN ALA GLU GLY SER THR ALA THR PRO
SEQRES 1 B 394 MET SER LEU GLY THR SER GLU GLN SER GLU ILE ARG GLU
SEQRES 2 B 394 ILE VAL ALA GLY SER ALA PRO ALA ARG PHE ALA ARG GLY
SEQRES 3 B 394 TRP HIS CYS LEU GLY LEU ALA LYS ASP PHE LYS ASP GLY
SEQRES 4 B 394 LYS PRO HIS SER VAL HIS ALA PHE GLY THR LYS LEU VAL
SEQRES 5 B 394 VAL TRP ALA ASP SER ASN ASP GLU ILE ARG ILE LEU ASP
SEQRES 6 B 394 ALA TYR CYS ARG HIS MET GLY GLY ASP LEU SER GLN GLY
SEQRES 7 B 394 THR VAL LYS GLY ASP GLU ILE ALA CYS PRO PHE HIS ASP
SEQRES 8 B 394 TRP ARG TRP GLY GLY ASN GLY ARG CYS LYS ASN ILE PRO
SEQRES 9 B 394 TYR ALA ARG ARG VAL PRO PRO ILE ALA LYS THR ARG ALA
SEQRES 10 B 394 TRP HIS THR LEU ASP GLN ASP GLY LEU LEU PHE VAL TRP
SEQRES 11 B 394 HIS ASP PRO GLN GLY ASN PRO PRO PRO ALA ASP VAL THR
SEQRES 12 B 394 ILE PRO ARG ILE ALA GLY ALA THR SER ASP GLU TRP THR
SEQRES 13 B 394 ASP TRP VAL TRP TYR THR THR GLU VAL ASP THR ASN CYS
SEQRES 14 B 394 ARG GLU ILE ILE ASP ASN ILE VAL ASP MET ALA HIS PHE
SEQRES 15 B 394 PHE TYR VAL HIS TYR SER PHE PRO VAL TYR PHE LYS ASN
SEQRES 16 B 394 VAL PHE GLU GLY HIS VAL ALA SER GLN PHE MET ARG GLY
SEQRES 17 B 394 GLN ALA ARG GLU ASP THR ARG PRO HIS ALA ASN GLY GLN
SEQRES 18 B 394 PRO LYS MET ILE GLY SER ARG SER ASP ALA SER TYR PHE
SEQRES 19 B 394 GLY PRO SER PHE MET ILE ASP ASP LEU VAL TYR GLU TYR
SEQRES 20 B 394 GLU GLY TYR ASP VAL GLU SER VAL LEU ILE ASN CYS HIS
SEQRES 21 B 394 TYR PRO VAL SER GLN ASP LYS PHE VAL LEU MET TYR GLY
SEQRES 22 B 394 MET ILE VAL LYS LYS SER ASP ARG LEU GLU GLY GLU LYS
SEQRES 23 B 394 ALA LEU GLN THR ALA GLN GLN PHE GLY ASN PHE ILE ALA
SEQRES 24 B 394 LYS GLY PHE GLU GLN ASP ILE GLU ILE TRP ARG ASN LYS
SEQRES 25 B 394 THR ARG ILE ASP ASN PRO LEU LEU CYS GLU GLU ASP GLY
SEQRES 26 B 394 PRO VAL TYR GLN LEU ARG ARG TRP TYR GLU GLN PHE TYR
SEQRES 27 B 394 VAL ASP VAL GLU ASP VAL ALA PRO GLU MET THR ASP ARG
SEQRES 28 B 394 PHE GLU PHE GLU MET ASP THR THR ARG PRO VAL ALA ALA
SEQRES 29 B 394 TRP MET LYS GLU VAL GLU ALA ASN ILE ALA ARG LYS ALA
SEQRES 30 B 394 ALA LEU ASP THR GLU THR ARG SER ALA PRO GLU GLN SER
SEQRES 31 B 394 THR THR ALA GLY
HET FES A 401 4
HET FE2 A 402 1
HET GOL A 403 6
HET PG4 A 404 13
HET FE2 B 401 1
HET FES B 402 4
HET 30Q B 403 26
HET PO4 B 404 5
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FE2 FE (II) ION
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM 30Q S-[2-(PROPANOYLAMINO)ETHYL] (2S)-2-[(8S,9S,10R,13S,14S,
HETNAM 2 30Q 17R)-10,13-DIMETHYL-3-OXO-6,7,8,9,10,11,12,13,14,15,
HETNAM 3 30Q 16,17-DODECAHYDRO-3H-CYCLOPENTA[A]PHENANTHREN-17-
HETNAM 4 30Q YL]PROPANETHIOATE (NON-PREFERRED NAME)
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FES 2(FE2 S2)
FORMUL 4 FE2 2(FE 2+)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 PG4 C8 H18 O5
FORMUL 9 30Q C27 H39 N O3 S
FORMUL 10 PO4 O4 P 3-
FORMUL 11 HOH *201(H2 O)
HELIX 1 1 LEU A 38 GLN A 42 1 5
HELIX 2 2 ASP A 79 GLY A 83 5 5
HELIX 3 3 CYS A 175 ASP A 180 1 6
HELIX 4 4 ASN A 181 MET A 185 5 5
HELIX 5 5 ALA A 186 ILE A 191 1 6
HELIX 6 6 SER A 289 LYS A 316 1 28
HELIX 7 7 PRO A 332 GLN A 342 1 11
HELIX 8 8 PHE A 343 VAL A 345 5 3
HELIX 9 9 ASP A 346 ILE A 350 5 5
HELIX 10 10 THR A 351 LYS A 356 1 6
HELIX 11 11 THR A 364 GLU A 384 1 21
HELIX 12 12 LYS B 34 LYS B 37 5 4
HELIX 13 13 ASP B 74 GLY B 78 5 5
HELIX 14 14 ILE B 147 SER B 152 5 6
HELIX 15 15 CYS B 169 ASP B 174 1 6
HELIX 16 16 ASN B 175 MET B 179 5 5
HELIX 17 17 ALA B 180 VAL B 185 1 6
HELIX 18 18 LYS B 286 ASN B 311 1 26
HELIX 19 19 PRO B 326 GLU B 335 1 10
HELIX 20 20 GLN B 336 VAL B 339 5 4
HELIX 21 21 ASP B 340 VAL B 344 5 5
HELIX 22 22 ALA B 345 ASP B 350 1 6
HELIX 23 23 THR B 358 LYS B 376 1 19
HELIX 24 24 ALA B 377 LEU B 379 5 3
SHEET 1 A 3 GLY A 31 LEU A 37 0
SHEET 2 A 3 GLN A 131 ASN A 136 -1 O VAL A 134 N HIS A 33
SHEET 3 A 3 THR A 125 ARG A 128 -1 N LEU A 126 O TYR A 133
SHEET 1 B 4 HIS A 47 ALA A 51 0
SHEET 2 B 4 THR A 54 ALA A 60 -1 O LEU A 56 N ILE A 49
SHEET 3 B 4 LEU A 66 ASP A 70 -1 O LEU A 69 N VAL A 57
SHEET 4 B 4 ALA A 122 TRP A 123 -1 O TRP A 123 N VAL A 68
SHEET 1 C 4 GLU A 84 LYS A 86 0
SHEET 2 C 4 SER A 89 ALA A 91 -1 O SER A 89 N LYS A 86
SHEET 3 C 4 ARG A 98 ASN A 100 -1 O TRP A 99 N ILE A 90
SHEET 4 C 4 CYS A 105 ASP A 107 -1 O ASP A 107 N ARG A 98
SHEET 1 D 8 SER A 164 LYS A 171 0
SHEET 2 D 8 GLU A 273 VAL A 282 -1 O LEU A 276 N LEU A 168
SHEET 3 D 8 THR A 257 SER A 270 -1 N CYS A 265 O GLN A 277
SHEET 4 D 8 TYR A 244 ASP A 252 -1 N ASP A 247 O LEU A 262
SHEET 5 D 8 GLU A 232 PHE A 240 -1 N ARG A 234 O GLU A 250
SHEET 6 D 8 THR A 207 GLY A 216 -1 N SER A 214 O LEU A 233
SHEET 7 D 8 SER A 194 GLU A 204 -1 N LYS A 200 O TYR A 211
SHEET 8 D 8 PHE A 358 ILE A 362 -1 O PHE A 358 N PHE A 203
SHEET 1 E 3 GLY B 26 LEU B 32 0
SHEET 2 E 3 LEU B 126 HIS B 131 -1 O LEU B 127 N LEU B 30
SHEET 3 E 3 THR B 120 GLN B 123 -1 N GLN B 123 O LEU B 126
SHEET 1 F 3 HIS B 42 ALA B 46 0
SHEET 2 F 3 THR B 49 ALA B 55 -1 O VAL B 53 N HIS B 42
SHEET 3 F 3 ILE B 61 ASP B 65 -1 O LEU B 64 N VAL B 52
SHEET 1 G 4 THR B 79 LYS B 81 0
SHEET 2 G 4 GLU B 84 ALA B 86 -1 O ALA B 86 N THR B 79
SHEET 3 G 4 ARG B 93 TRP B 94 -1 O TRP B 94 N ILE B 85
SHEET 4 G 4 CYS B 100 ASN B 102 -1 O ASN B 102 N ARG B 93
SHEET 1 H 8 VAL B 159 VAL B 165 0
SHEET 2 H 8 LYS B 267 VAL B 276 -1 O LEU B 270 N THR B 163
SHEET 3 H 8 ASP B 251 SER B 264 -1 N ILE B 257 O GLY B 273
SHEET 4 H 8 PHE B 238 GLU B 246 -1 N ASP B 241 O LEU B 256
SHEET 5 H 8 GLY B 226 PHE B 234 -1 N ASP B 230 O ASP B 242
SHEET 6 H 8 VAL B 201 ALA B 210 -1 N ALA B 202 O TYR B 233
SHEET 7 H 8 SER B 188 GLU B 198 -1 N LYS B 194 O PHE B 205
SHEET 8 H 8 PHE B 352 MET B 356 -1 O MET B 356 N PHE B 193
LINK SG CYS A 73 FE2 FES A 401 1555 1555 2.23
LINK ND1 HIS A 75 FE1 FES A 401 1555 1555 2.11
LINK SG CYS A 92 FE2 FES A 401 1555 1555 2.26
LINK ND1 HIS A 95 FE1 FES A 401 1555 1555 2.25
LINK NE2 HIS A 187 FE FE2 A 402 1555 1555 2.13
LINK NE2 HIS A 192 FE FE2 A 402 1555 1555 2.14
LINK OD2 ASP A 311 FE FE2 A 402 1555 1555 2.23
LINK OD1 ASP A 311 FE FE2 A 402 1555 1555 2.45
LINK FE FE2 A 402 O HOH A 602 1555 1555 1.93
LINK FE FE2 A 402 O HOH A 621 1555 1555 2.48
LINK SG CYS B 68 FE2 FES B 402 1555 1555 2.23
LINK ND1 HIS B 70 FE1 FES B 402 1555 1555 1.96
LINK SG CYS B 87 FE2 FES B 402 1555 1555 2.17
LINK ND1 HIS B 90 FE1 FES B 402 1555 1555 2.09
LINK NE2 HIS B 186 FE FE2 B 401 1555 1555 2.34
LINK OD1 ASP B 305 FE FE2 B 401 1555 1555 2.42
LINK OD2 ASP B 305 FE FE2 B 401 1555 1555 2.42
LINK FE FE2 B 401 O HOH B 533 1555 1555 1.88
SITE 1 AC1 7 CYS A 73 HIS A 75 MET A 76 GLY A 78
SITE 2 AC1 7 CYS A 92 HIS A 95 TRP A 97
SITE 1 AC2 5 HIS A 187 HIS A 192 ASP A 311 HOH A 602
SITE 2 AC2 5 HOH A 621
SITE 1 AC3 2 GLU A 236 THR A 238
SITE 1 AC4 13 ARG A 30 GLY A 31 TRP A 32 TRP A 135
SITE 2 AC4 13 VAL A 147 THR A 148 PHE A 240 GLY A 241
SITE 3 AC4 13 PRO A 242 GLN A 342 PHE A 343 ILE A 350
SITE 4 AC4 13 GLU A 352
SITE 1 AC5 4 HIS B 181 HIS B 186 ASP B 305 HOH B 533
SITE 1 AC6 7 CYS B 68 HIS B 70 MET B 71 GLY B 73
SITE 2 AC6 7 CYS B 87 HIS B 90 TRP B 92
SITE 1 AC7 12 ASN B 175 ILE B 176 HIS B 186 GLN B 204
SITE 2 AC7 12 SER B 229 MET B 239 ASP B 241 LEU B 243
SITE 3 AC7 12 TYR B 245 ASP B 305 HOH B 513 HOH B 533
SITE 1 AC8 5 PHE B 23 PHE B 47 ARG B 116 HIS B 131
SITE 2 AC8 5 HOH B 564
CRYST1 273.680 273.680 273.680 90.00 90.00 90.00 F 2 3 48
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 0.003654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003654 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
