HEADER OXIDOREDUCTASE 22-JUN-07 2V3V
TITLE A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
TITLE 2 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND EPR
TITLE 3 DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC NITRATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.7.99.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO DESULFURICANS;
SOURCE 3 ORGANISM_TAXID: 876;
SOURCE 4 ATCC: 27774
KEYWDS NITRATE ASSIMILATION, NITROGENOUS ACCEPTOR, ELECTRON TRANSPORT,
KEYWDS 2 DISSIMILATORY NITRATE REDUCTASE, MOLYBDOPTERIN COFACTOR, SULFIDO
KEYWDS 3 LIGAND, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NAJMUDIN,P.J.GONZALEZ,J.TRINCAO,C.COELHO,A.MUKHOPADHYAY,C.C.ROMAO,
AUTHOR 2 I.MOURA,J.J.MOURA,C.D.BRONDINO,M.J.ROMAO
REVDAT 4 13-DEC-23 2V3V 1 REMARK LINK
REVDAT 3 13-JUL-11 2V3V 1 VERSN
REVDAT 2 24-FEB-09 2V3V 1 VERSN
REVDAT 1 18-MAR-08 2V3V 0
JRNL AUTH S.NAJMUDIN,P.J.GONZALEZ,J.TRINCAO,C.COELHO,A.MUKHOPADHYAY,
JRNL AUTH 2 N.M.F.S.A.CERQUEIRA,C.C.ROMAO,I.MOURA,J.J.G.MOURA,
JRNL AUTH 3 C.D.BRONDINO,M.J.ROMAO
JRNL TITL PERIPLASMIC NITRATE REDUCTASE REVISITED: A SULFUR ATOM
JRNL TITL 2 COMPLETES THE SIXTH COORDINATION OF THE CATALYTIC
JRNL TITL 3 MOLYBDENUM.
JRNL REF J.BIOL.INORG.CHEM. V. 13 737 2008
JRNL REFN ISSN 0949-8257
JRNL PMID 18327621
JRNL DOI 10.1007/S00775-008-0359-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.J.GONZALEZ,M.G.RIVAS,C.D.BRONDINO,S.A.BURSAKOV,I.MOURA,
REMARK 1 AUTH 2 J.J.G.MOURA
REMARK 1 TITL EPR AND REDOX PROPERTIES OF PERIPLASMIC NITRATE REDUCTASE
REMARK 1 TITL 2 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774
REMARK 1 REF J.BIOL.INORG.CHEM. V. 11 609 2006
REMARK 1 REFN ISSN 0949-8257
REMARK 1 PMID 16791644
REMARK 1 DOI 10.1007/S00775-006-0110-0
REMARK 2
REMARK 2 RESOLUTION. 1.99 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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 57324
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2410
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3370
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5627
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 757
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : UNVERIFIED
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.33000
REMARK 3 B22 (A**2) : -1.33000
REMARK 3 B33 (A**2) : 2.00000
REMARK 3 B12 (A**2) : -0.67000
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): 0.170
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.545
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5965 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8142 ; 1.698 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 740 ; 6.432 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 271 ;36.345 ;22.989
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 952 ;17.287 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;22.004 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 860 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4616 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2999 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3945 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 690 ; 0.239 ; 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): 36 ; 0.150 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 40 ; 0.314 ; 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): 3712 ; 0.589 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5856 ; 0.941 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2589 ; 1.700 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2264 ; 2.617 ; 4.500
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 61
REMARK 3 RESIDUE RANGE : A 464 A 492
REMARK 3 RESIDUE RANGE : A 517 A 561
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3683 21.4829 16.1405
REMARK 3 T TENSOR
REMARK 3 T11: -0.0547 T22: -0.0720
REMARK 3 T33: 0.0141 T12: -0.0328
REMARK 3 T13: 0.0367 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 1.4873 L22: 1.4401
REMARK 3 L33: 0.9175 L12: -0.3316
REMARK 3 L13: 0.6862 L23: -0.5675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.2614 S13: 0.1823
REMARK 3 S21: 0.1488 S22: -0.0127 S23: 0.2884
REMARK 3 S31: -0.0833 S32: -0.1295 S33: -0.0032
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 62 A 135
REMARK 3 RESIDUE RANGE : A 347 A 463
REMARK 3 RESIDUE RANGE : A 493 A 516
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7805 4.0002 1.0706
REMARK 3 T TENSOR
REMARK 3 T11: -0.0483 T22: -0.0785
REMARK 3 T33: 0.0132 T12: -0.0438
REMARK 3 T13: -0.0213 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.0382 L22: 0.7834
REMARK 3 L33: 0.4670 L12: 0.3276
REMARK 3 L13: 0.3492 L23: 0.0260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: -0.0145 S13: -0.0599
REMARK 3 S21: -0.0078 S22: -0.0239 S23: 0.1232
REMARK 3 S31: 0.0616 S32: -0.0833 S33: 0.0006
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 136 A 346
REMARK 3 ORIGIN FOR THE GROUP (A): 89.5862 13.1756 7.6120
REMARK 3 T TENSOR
REMARK 3 T11: -0.0072 T22: -0.0357
REMARK 3 T33: -0.0884 T12: -0.0193
REMARK 3 T13: -0.0170 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.8920 L22: 0.8558
REMARK 3 L33: 0.8572 L12: 0.0801
REMARK 3 L13: 0.2412 L23: -0.1425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0170 S12: 0.0563 S13: -0.0834
REMARK 3 S21: -0.0125 S22: -0.0342 S23: -0.1628
REMARK 3 S31: 0.0165 S32: 0.0776 S33: 0.0172
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 562 A 723
REMARK 3 ORIGIN FOR THE GROUP (A): 78.6350 15.2882 -5.4004
REMARK 3 T TENSOR
REMARK 3 T11: -0.0372 T22: -0.0887
REMARK 3 T33: -0.0725 T12: -0.0365
REMARK 3 T13: 0.0006 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.8402 L22: 0.9032
REMARK 3 L33: 0.8007 L12: 0.1348
REMARK 3 L13: 0.1255 L23: -0.1665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0179 S12: 0.1181 S13: 0.0656
REMARK 3 S21: -0.1292 S22: -0.0200 S23: 0.0079
REMARK 3 S31: -0.0230 S32: 0.0919 S33: 0.0379
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 RIDING
REMARK 3 POSITIONS. THE FIRST 3 RESIDUES ARE DISORDERED.
REMARK 4
REMARK 4 2V3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1290032993.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 454081
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 46.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 1.33000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2NAP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.5, 7.5% PEG 8000 A
REMARK 280 COCRYSTALLISATION WITH 10MM OF KCLO4 (PERCHLORATE) IN 200MM OF
REMARK 280 DDNAPA (IE PROTEIN) WHICH HAD BEEN REDUCED BY DITHIONITE IN
REMARK 280 ANAEROBIC CONDITIONS AND THEN AIR REOXIDISED BEFORE SETTTING UP
REMARK 280 FOR CRYSTALLISATIONS STRAIGHT AFTER THAWING FROM -80C.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.15967
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 90.31933
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 90.31933
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 45.15967
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: PISA
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 ALA A 1
REMARK 465 ASP A 2
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 ASN A 3 CG OD1 ND2
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 HOH A 2024 O HOH A 2223 1.60
REMARK 500 O HOH A 2102 O HOH A 2224 1.78
REMARK 500 O HOH A 2062 O HOH A 2218 1.81
REMARK 500 O HOH A 2158 O HOH A 2422 1.83
REMARK 500 O HOH A 2651 O HOH A 2652 1.83
REMARK 500 O HOH A 2261 O HOH A 2619 1.87
REMARK 500 O HOH A 2646 O HOH A 2651 1.87
REMARK 500 O HOH A 2201 O HOH A 2206 1.91
REMARK 500 O HOH A 2661 O HOH A 2668 1.92
REMARK 500 O HOH A 2220 O HOH A 2230 1.92
REMARK 500 O HOH A 2309 O HOH A 2742 1.95
REMARK 500 O HOH A 2077 O HOH A 2084 1.96
REMARK 500 O HOH A 2266 O HOH A 2628 1.99
REMARK 500 O HOH A 2077 O HOH A 2082 2.03
REMARK 500 NH1 ARG A 540 O HOH A 2557 2.05
REMARK 500 O HOH A 2592 O HOH A 2593 2.05
REMARK 500 O HOH A 2741 O HOH A 2742 2.06
REMARK 500 O2 LCP A 815 O HOH A 2754 2.07
REMARK 500 O ALA A 300 NH2 ARG A 335 2.07
REMARK 500 O HOH A 2180 O HOH A 2181 2.08
REMARK 500 O HOH A 2220 O HOH A 2229 2.09
REMARK 500 O HOH A 2235 O HOH A 2549 2.10
REMARK 500 O HOH A 2260 O HOH A 2261 2.10
REMARK 500 O HOH A 2266 O HOH A 2626 2.10
REMARK 500 O HOH A 2053 O HOH A 2131 2.11
REMARK 500 O3 LCP A 815 O HOH A 2753 2.12
REMARK 500 O HOH A 2264 O HOH A 2622 2.13
REMARK 500 O HOH A 2185 O HOH A 2427 2.13
REMARK 500 O HOH A 2435 O HOH A 2737 2.14
REMARK 500 NE ARG A 91 O HOH A 2136 2.14
REMARK 500 O HOH A 2065 O HOH A 2167 2.14
REMARK 500 ND2 ASN A 102 O HOH A 2159 2.15
REMARK 500 O HOH A 2369 O HOH A 2370 2.19
REMARK 500 O HOH A 2156 O HOH A 2426 2.19
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 O HOH A 2226 O HOH A 2227 6765 1.98
REMARK 500 O HOH A 2226 O HOH A 2239 6765 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 249 CG ARG A 249 CD 0.313
REMARK 500 ARG A 249 CG ARG A 249 CD 0.372
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 LEU A 67 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU A 76 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASN A 209 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASN A 209 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG A 249 CB - CG - CD ANGL. DEV. = -26.0 DEGREES
REMARK 500 ARG A 249 CG - CD - NE ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 617 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 617 NE - CZ - NH2 ANGL. DEV. = -5.5 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 ARG A 4 -116.56 -101.64
REMARK 500 TYR A 15 -122.80 -101.07
REMARK 500 ASN A 132 65.30 -69.87
REMARK 500 CYS A 140 -70.07 -146.92
REMARK 500 GLU A 156 148.74 83.89
REMARK 500 SER A 261 -154.46 -139.34
REMARK 500 CYS A 307 -121.38 -144.57
REMARK 500 ALA A 358 40.88 -99.16
REMARK 500 ASN A 425 60.26 60.42
REMARK 500 TRP A 464 -116.68 51.70
REMARK 500 ASP A 534 110.32 -31.67
REMARK 500 TYR A 565 7.85 80.64
REMARK 500 PHE A 582 99.88 -161.17
REMARK 500 LYS A 599 -134.08 -126.44
REMARK 500 HIS A 623 -114.03 39.36
REMARK 500 MET A 627 -60.54 -107.57
REMARK 500 ASN A 638 75.40 -157.79
REMARK 500 VAL A 707 -63.72 -96.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2135 DISTANCE = 7.40 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE RESIDUE A 813 WAS ORIGINALLY DEPOSITED AS A
REMARK 600 ISOLATED SULFUR ATOM. AS PART OF REMEDIATION, THIS HAS
REMARK 600 BEEN CHANGED TO UNX (UNKNOWN ATOM OR LIGAND) AS THE
REMARK 600 HETEROGEN S IS NOW OBSOLETE IN THE PDB HETGROUP DICTIONARY.
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 SF4 A 800 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 13 SG
REMARK 620 2 SF4 A 800 S1 112.0
REMARK 620 3 SF4 A 800 S2 117.1 107.5
REMARK 620 4 SF4 A 800 S4 112.5 105.2 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 800 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 SF4 A 800 S1 120.3
REMARK 620 3 SF4 A 800 S3 99.8 104.1
REMARK 620 4 SF4 A 800 S4 119.9 105.3 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 800 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A 800 S1 103.7
REMARK 620 3 SF4 A 800 S2 115.4 107.0
REMARK 620 4 SF4 A 800 S3 119.2 103.8 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 800 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 47 SG
REMARK 620 2 SF4 A 800 S2 115.9
REMARK 620 3 SF4 A 800 S3 122.1 107.5
REMARK 620 4 SF4 A 800 S4 103.3 100.5 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO A 810 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 140 SG
REMARK 620 2 MGD A 811 S13 87.6
REMARK 620 3 MGD A 811 S12 129.5 82.4
REMARK 620 4 MGD A 812 S12 80.9 85.7 146.6
REMARK 620 5 MGD A 812 S13 140.7 123.7 82.0 78.9
REMARK 620 6 UNX A 813 UNK 61.9 140.1 97.0 111.8 95.4
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
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 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LCP A 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LCP A 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LCP A 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LCP A 817
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V3V RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2JIQ RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2JIM RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2JIO RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2JIR RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2V45 RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
REMARK 900 RELATED ID: 2JIP RELATED DB: PDB
REMARK 900 A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM
REMARK 900 DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND
REMARK 900 EPR DATA AND BASED ON DETAILED ANALYSIS OF THE SIXTH LIGAND
DBREF 2V3V A 1 723 UNP P81186 NAPA_DESDE 33 755
SEQRES 1 A 723 ALA ASP ASN ARG PRO GLU LYS TRP VAL LYS GLY VAL CYS
SEQRES 2 A 723 ARG TYR CYS GLY THR GLY CYS GLY VAL LEU VAL GLY VAL
SEQRES 3 A 723 LYS ASP GLY LYS ALA VAL ALA ILE GLN GLY ASP PRO ASN
SEQRES 4 A 723 ASN HIS ASN ALA GLY LEU LEU CYS LEU LYS GLY SER LEU
SEQRES 5 A 723 LEU ILE PRO VAL LEU ASN SER LYS GLU ARG VAL THR GLN
SEQRES 6 A 723 PRO LEU VAL ARG ARG HIS LYS GLY GLY LYS LEU GLU PRO
SEQRES 7 A 723 VAL SER TRP ASP GLU ALA LEU ASP LEU MET ALA SER ARG
SEQRES 8 A 723 PHE ARG SER SER ILE ASP MET TYR GLY PRO ASN SER VAL
SEQRES 9 A 723 ALA TRP TYR GLY SER GLY GLN CYS LEU THR GLU GLU SER
SEQRES 10 A 723 TYR VAL ALA ASN LYS ILE PHE LYS GLY GLY PHE GLY THR
SEQRES 11 A 723 ASN ASN VAL ASP GLY ASN PRO ARG LEU CYS MET ALA SER
SEQRES 12 A 723 ALA VAL GLY GLY TYR VAL THR SER PHE GLY LYS ASP GLU
SEQRES 13 A 723 PRO MET GLY THR TYR ALA ASP ILE ASP GLN ALA THR CYS
SEQRES 14 A 723 PHE PHE ILE ILE GLY SER ASN THR SER GLU ALA HIS PRO
SEQRES 15 A 723 VAL LEU PHE ARG ARG ILE ALA ARG ARG LYS GLN VAL GLU
SEQRES 16 A 723 PRO GLY VAL LYS ILE ILE VAL ALA ASP PRO ARG ARG THR
SEQRES 17 A 723 ASN THR SER ARG ILE ALA ASP MET HIS VAL ALA PHE ARG
SEQRES 18 A 723 PRO GLY THR ASP LEU ALA PHE MET HIS SER MET ALA TRP
SEQRES 19 A 723 VAL ILE ILE ASN GLU GLU LEU ASP ASN PRO ARG PHE TRP
SEQRES 20 A 723 GLN ARG TYR VAL ASN PHE MET ASP ALA GLU GLY LYS PRO
SEQRES 21 A 723 SER ASP PHE GLU GLY TYR LYS ALA PHE LEU GLU ASN TYR
SEQRES 22 A 723 ARG PRO GLU LYS VAL ALA GLU ILE CYS ARG VAL PRO VAL
SEQRES 23 A 723 GLU GLN ILE TYR GLY ALA ALA ARG ALA PHE ALA GLU SER
SEQRES 24 A 723 ALA ALA THR MET SER LEU TRP CYS MET GLY ILE ASN GLN
SEQRES 25 A 723 ARG VAL GLN GLY VAL PHE ALA ASN ASN LEU ILE HIS ASN
SEQRES 26 A 723 LEU HIS LEU ILE THR GLY GLN ILE CYS ARG PRO GLY ALA
SEQRES 27 A 723 THR SER PHE SER LEU THR GLY GLN PRO ASN ALA CYS GLY
SEQRES 28 A 723 GLY VAL ARG ASP GLY GLY ALA LEU SER HIS LEU LEU PRO
SEQRES 29 A 723 ALA GLY ARG ALA ILE PRO ASN ALA LYS HIS ARG ALA GLU
SEQRES 30 A 723 MET GLU LYS LEU TRP GLY LEU PRO GLU GLY ARG ILE ALA
SEQRES 31 A 723 PRO GLU PRO GLY TYR HIS THR VAL ALA LEU PHE GLU ALA
SEQRES 32 A 723 LEU GLY ARG GLY ASP VAL LYS CYS MET ILE ILE CYS GLU
SEQRES 33 A 723 THR ASN PRO ALA HIS THR LEU PRO ASN LEU ASN LYS VAL
SEQRES 34 A 723 HIS LYS ALA MET SER HIS PRO GLU SER PHE ILE VAL CYS
SEQRES 35 A 723 ILE GLU ALA PHE PRO ASP ALA VAL THR LEU GLU TYR ALA
SEQRES 36 A 723 ASP LEU VAL LEU PRO PRO ALA PHE TRP CYS GLU ARG ASP
SEQRES 37 A 723 GLY VAL TYR GLY CYS GLY GLU ARG ARG TYR SER LEU THR
SEQRES 38 A 723 GLU LYS ALA VAL ASP PRO PRO GLY GLN CYS ARG PRO THR
SEQRES 39 A 723 VAL ASN THR LEU VAL GLU PHE ALA ARG ARG ALA GLY VAL
SEQRES 40 A 723 ASP PRO GLN LEU VAL ASN PHE ARG ASN ALA GLU ASP VAL
SEQRES 41 A 723 TRP ASN GLU TRP ARG MET VAL SER LYS GLY THR THR TYR
SEQRES 42 A 723 ASP PHE TRP GLY MET THR ARG GLU ARG LEU ARG LYS GLU
SEQRES 43 A 723 SER GLY LEU ILE TRP PRO CYS PRO SER GLU ASP HIS PRO
SEQRES 44 A 723 GLY THR SER LEU ARG TYR VAL ARG GLY GLN ASP PRO CYS
SEQRES 45 A 723 VAL PRO ALA ASP HIS PRO ASP ARG PHE PHE PHE TYR GLY
SEQRES 46 A 723 LYS PRO ASP GLY ARG ALA VAL ILE TRP MET ARG PRO ALA
SEQRES 47 A 723 LYS GLY ALA ALA GLU GLU PRO ASP ALA GLU TYR PRO LEU
SEQRES 48 A 723 TYR LEU THR SER MET ARG VAL ILE ASP HIS TRP HIS THR
SEQRES 49 A 723 ALA THR MET THR GLY LYS VAL PRO GLU LEU GLN LYS ALA
SEQRES 50 A 723 ASN PRO ILE ALA PHE VAL GLU ILE ASN GLU GLU ASP ALA
SEQRES 51 A 723 ALA ARG THR GLY ILE LYS HIS GLY ASP SER VAL ILE VAL
SEQRES 52 A 723 GLU THR ARG ARG ASP ALA MET GLU LEU PRO ALA ARG VAL
SEQRES 53 A 723 SER ASP VAL CYS ARG PRO GLY LEU ILE ALA VAL PRO PHE
SEQRES 54 A 723 PHE ASP PRO LYS LYS LEU VAL ASN LYS LEU PHE LEU ASP
SEQRES 55 A 723 ALA THR ASP PRO VAL SER ARG GLU PRO GLU TYR LYS ILE
SEQRES 56 A 723 CYS ALA ALA ARG VAL ARG LYS ALA
HET SF4 A 800 8
HET MO A 810 1
HET MGD A 811 47
HET MGD A 812 47
HET UNX A 813 1
HET LCP A 814 5
HET LCP A 815 5
HET LCP A 816 5
HET LCP A 817 5
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM MO MOLYBDENUM ATOM
HETNAM MGD 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-
HETNAM 2 MGD OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE
HETNAM 3 MGD DINUCLEOTIDE
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM LCP PERCHLORATE ION
HETSYN MGD MOLYBDOPTERIN GUANOSINE DINUCLEOTIDE
FORMUL 2 SF4 FE4 S4
FORMUL 3 MO MO
FORMUL 4 MGD 2(C20 H26 N10 O13 P2 S2)
FORMUL 6 UNX X
FORMUL 7 LCP 4(CL O4 1-)
FORMUL 11 HOH *757(H2 O)
HELIX 1 1 CYS A 47 LEU A 52 1 6
HELIX 2 2 LEU A 53 ASN A 58 1 6
HELIX 3 3 SER A 80 GLY A 100 1 21
HELIX 4 4 LEU A 113 GLY A 127 1 15
HELIX 5 5 PRO A 137 CYS A 140 5 4
HELIX 6 6 MET A 141 GLY A 153 1 13
HELIX 7 7 THR A 160 GLN A 166 5 7
HELIX 8 8 ASN A 176 HIS A 181 1 6
HELIX 9 9 HIS A 181 GLU A 195 1 15
HELIX 10 10 THR A 208 ALA A 214 5 7
HELIX 11 11 THR A 224 GLU A 239 1 16
HELIX 12 12 ASN A 243 TYR A 250 1 8
HELIX 13 13 ASP A 262 GLU A 271 1 10
HELIX 14 14 ARG A 274 ARG A 283 1 10
HELIX 15 15 PRO A 285 SER A 299 1 15
HELIX 16 16 CYS A 307 GLN A 312 1 6
HELIX 17 17 GLN A 315 GLY A 331 1 17
HELIX 18 18 ASN A 348 VAL A 353 1 6
HELIX 19 19 ASN A 371 TRP A 382 1 12
HELIX 20 20 HIS A 396 GLY A 407 1 12
HELIX 21 21 ASN A 418 LEU A 423 1 6
HELIX 22 22 ASN A 425 SER A 434 1 10
HELIX 23 23 ALA A 449 TYR A 454 5 6
HELIX 24 24 PHE A 463 ARG A 467 5 5
HELIX 25 25 PRO A 493 ALA A 505 1 13
HELIX 26 26 ASP A 508 ASN A 513 5 6
HELIX 27 27 ASN A 516 LYS A 529 1 14
HELIX 28 28 THR A 539 GLU A 546 1 8
HELIX 29 29 MET A 627 LYS A 630 5 4
HELIX 30 30 VAL A 631 ASN A 638 1 8
HELIX 31 31 GLU A 647 ARG A 652 1 6
HELIX 32 32 LEU A 695 LEU A 699 5 5
SHEET 1 AA 3 LYS A 7 VAL A 12 0
SHEET 2 AA 3 GLY A 21 LYS A 27 -1 O VAL A 22 N GLY A 11
SHEET 3 AA 3 LYS A 30 GLY A 36 -1 O LYS A 30 N LYS A 27
SHEET 1 AB 7 LEU A 76 PRO A 78 0
SHEET 2 AB 7 LEU A 67 ARG A 69 -1 O VAL A 68 N GLU A 77
SHEET 3 AB 7 LEU A 457 LEU A 459 -1 O VAL A 458 N LEU A 67
SHEET 4 AB 7 PHE A 439 ILE A 443 1 O CYS A 442 N LEU A 459
SHEET 5 AB 7 CYS A 411 CYS A 415 1 O MET A 412 N VAL A 441
SHEET 6 AB 7 VAL A 104 GLY A 108 1 O ALA A 105 N ILE A 413
SHEET 7 AB 7 VAL A 133 GLY A 135 1 O ASP A 134 N GLY A 108
SHEET 1 AC 5 MET A 216 VAL A 218 0
SHEET 2 AC 5 LYS A 199 ALA A 203 1 O VAL A 202 N VAL A 218
SHEET 3 AC 5 CYS A 169 ILE A 173 1 O PHE A 170 N ILE A 201
SHEET 4 AC 5 THR A 302 TRP A 306 1 O MET A 303 N PHE A 171
SHEET 5 AC 5 THR A 339 SER A 342 1 O THR A 339 N SER A 304
SHEET 1 AD 2 VAL A 251 MET A 254 0
SHEET 2 AD 2 ALA A 591 TRP A 594 1 O ALA A 591 N ASN A 252
SHEET 1 AE 2 LEU A 362 LEU A 363 0
SHEET 2 AE 2 ARG A 367 ALA A 368 -1 O ARG A 367 N LEU A 363
SHEET 1 AF 3 GLY A 469 GLY A 472 0
SHEET 2 AF 3 ARG A 477 THR A 481 -1 O SER A 479 N TYR A 471
SHEET 3 AF 3 LEU A 549 ILE A 550 -1 O LEU A 549 N TYR A 478
SHEET 1 AG 7 LEU A 611 MET A 616 0
SHEET 2 AG 7 CYS A 716 LYS A 722 -1 O CYS A 716 N LEU A 613
SHEET 3 AG 7 SER A 660 GLU A 664 -1 O ILE A 662 N ARG A 721
SHEET 4 AG 7 ALA A 669 SER A 677 -1 O MET A 670 N VAL A 663
SHEET 5 AG 7 VAL A 643 ASN A 646 1 O VAL A 643 N ARG A 675
SHEET 6 AG 7 LEU A 684 PRO A 688 -1 O LEU A 684 N ASN A 646
SHEET 7 AG 7 LEU A 611 MET A 616 1 O TYR A 612 N ILE A 685
LINK SG CYS A 13 FE3 SF4 A 800 1555 1555 2.30
LINK SG CYS A 16 FE2 SF4 A 800 1555 1555 2.23
LINK SG CYS A 20 FE4 SF4 A 800 1555 1555 2.20
LINK SG CYS A 47 FE1 SF4 A 800 1555 1555 2.28
LINK SG CYS A 140 MO MO A 810 1555 1555 2.37
LINK MO MO A 810 S13 MGD A 811 1555 1555 2.21
LINK MO MO A 810 S12 MGD A 811 1555 1555 2.43
LINK MO MO A 810 S12 MGD A 812 1555 1555 2.43
LINK MO MO A 810 S13 MGD A 812 1555 1555 2.37
LINK MO MO A 810 UNK UNX A 813 1555 1555 2.31
CISPEP 1 TRP A 551 PRO A 552 0 -5.78
SITE 1 AC1 7 CYS A 13 TYR A 15 CYS A 16 GLY A 19
SITE 2 AC1 7 CYS A 20 CYS A 47 VAL A 183
SITE 1 AC2 3 CYS A 140 MGD A 811 MGD A 812
SITE 1 AC3 30 ARG A 14 GLN A 111 ASN A 136 CYS A 140
SITE 2 AC3 30 GLN A 312 GLU A 416 THR A 417 ASN A 418
SITE 3 AC3 30 THR A 422 ILE A 443 GLU A 444 ALA A 445
SITE 4 AC3 30 PHE A 446 PRO A 461 ALA A 462 PHE A 463
SITE 5 AC3 30 SER A 615 ARG A 617 TRP A 622 HIS A 623
SITE 6 AC3 30 THR A 624 THR A 626 PHE A 689 ASN A 697
SITE 7 AC3 30 TYR A 713 LYS A 714 MO A 810 MGD A 812
SITE 8 AC3 30 HOH A2514 HOH A2752
SITE 1 AC4 37 CYS A 16 LYS A 49 CYS A 140 ILE A 173
SITE 2 AC4 37 GLY A 174 SER A 175 ASN A 176 GLU A 179
SITE 3 AC4 37 ALA A 180 ASP A 204 PRO A 205 ARG A 206
SITE 4 AC4 37 PHE A 220 PRO A 222 GLY A 223 ASP A 225
SITE 5 AC4 37 CYS A 307 MET A 308 GLY A 309 ARG A 313
SITE 6 AC4 37 GLY A 345 GLN A 346 THR A 614 MET A 616
SITE 7 AC4 37 ARG A 617 VAL A 618 ILE A 619 HIS A 621
SITE 8 AC4 37 TRP A 622 HIS A 623 LYS A 714 MO A 810
SITE 9 AC4 37 MGD A 811 HOH A2068 HOH A2214 HOH A2647
SITE 10 AC4 37 HOH A2748
SITE 1 AC5 9 PRO A 137 ARG A 138 MET A 141 ALA A 142
SITE 2 AC5 9 VAL A 145 VAL A 353 ARG A 354 LEU A 359
SITE 3 AC5 9 LCP A 815
SITE 1 AC6 10 ARG A 138 ALA A 142 VAL A 145 GLY A 146
SITE 2 AC6 10 HIS A 361 VAL A 707 SER A 708 LCP A 814
SITE 3 AC6 10 HOH A2753 HOH A2754
SITE 1 AC7 9 VAL A 145 VAL A 149 ASP A 155 ARG A 354
SITE 2 AC7 9 LEU A 362 TYR A 533 HOH A2388 HOH A2553
SITE 3 AC7 9 HOH A2756
SITE 1 AC8 8 VAL A 68 ARG A 69 ARG A 70 LEU A 87
SITE 2 AC8 8 ARG A 91 PHE A 439 HOH A2098 HOH A2136
CRYST1 106.566 106.566 135.479 90.00 90.00 120.00 P 31 2 1 6
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 0.009384 0.005418 0.000000 0.00000
SCALE2 0.000000 0.010836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
