HEADER LYASE 06-DEC-12 4IAH
TITLE CRYSTAL STRUCTURE OF BAY 60-2770 BOUND C139A H-NOX DOMAIN WITH S-
TITLE 2 NITROSYLATED CONSERVED C122
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALR2278 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HNOX DOMAIN, UNP RESIDUES 1-182;
COMPND 5 EC: 4.6.1.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PC 7120;
SOURCE 5 GENE: ALR2278;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSSETTA 2(DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS H-NOX DOMAIN, SOLUBLE GUANYLYL CYCLASE, BAY 60-2770, S-NITROSYLATION,
KEYWDS 2 CONSERVED C122, HEME BINDING, NO BINDING, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.KUMAR,F.VAN DEN AKKER
REVDAT 3 20-SEP-23 4IAH 1 REMARK SEQADV LINK
REVDAT 2 18-DEC-13 4IAH 1 JRNL
REVDAT 1 20-NOV-13 4IAH 0
JRNL AUTH V.KUMAR,F.MARTIN,M.G.HAHN,M.SCHAEFER,J.S.STAMLER,J.P.STASCH,
JRNL AUTH 2 F.VAN DEN AKKER
JRNL TITL INSIGHTS INTO BAY 60-2770 ACTIVATION AND
JRNL TITL 2 S-NITROSYLATION-DEPENDENT DESENSITIZATION OF SOLUBLE
JRNL TITL 3 GUANYLYL CYCLASE VIA CRYSTAL STRUCTURES OF HOMOLOGOUS NOSTOC
JRNL TITL 4 H-NOX DOMAIN COMPLEXES.
JRNL REF BIOCHEMISTRY V. 52 3601 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23614626
JRNL DOI 10.1021/BI301657W
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.300
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 14472
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 807
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1028
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2866
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3042 ; 0.003 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2012 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4112 ; 0.889 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4902 ; 0.601 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 362 ; 2.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;22.680 ;24.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 491 ;10.399 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;11.844 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 428 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3392 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 626 ; 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): 1798 ; 0.173 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 746 ; 0.014 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2870 ; 0.324 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1244 ; 0.286 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1242 ; 0.512 ; 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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.543
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -K, -H, -L
REMARK 3 TWIN FRACTION : 0.457
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 : 1.40
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
REMARK 4
REMARK 4 4IAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 86.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2O0C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 61.28650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.28650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.28650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.28650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.28650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.28650
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 61.28650
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.28650
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.28650
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.28650
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.28650
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.28650
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 61.28650
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.28650
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.28650
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.28650
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.28650
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.28650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 -61.28650
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -61.28650
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 61.28650
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 -61.28650
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 0.000000 -1.000000 -61.28650
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -61.28650
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 61.28650
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 -61.28650
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 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 SNC B 122 ND OE
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 OE2 GLU A 72 OE2 GLU B 161 5555 2.10
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 ILE A 34 104.79 -44.78
REMARK 500 ASP A 45 -29.51 -39.31
REMARK 500 GLU A 81 48.13 -71.39
REMARK 500 TYR A 83 29.47 -149.55
REMARK 500 ARG A 116 76.89 -114.68
REMARK 500 SER A 126 -156.68 -153.03
REMARK 500 GLN A 157 58.90 24.53
REMARK 500 GLU A 169 -16.28 -48.25
REMARK 500 HIS B 17 -4.62 -146.37
REMARK 500 ASP B 20 -71.32 -31.81
REMARK 500 ALA B 29 -9.41 -51.55
REMARK 500 LEU B 31 82.28 -175.78
REMARK 500 GLU B 81 28.26 -142.62
REMARK 500 ASP B 92 27.66 -151.06
REMARK 500 LEU B 110 -76.05 -58.55
REMARK 500 PHE B 112 71.09 -113.27
REMARK 500 SER B 126 -178.34 171.90
REMARK 500 LYS B 128 -7.18 -146.92
REMARK 500 GLN B 157 61.17 26.45
REMARK 500 GLU B 169 -37.36 -35.33
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 1DX A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1DX B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L6J RELATED DB: PDB
REMARK 900 STRUCTURE OF CINACIGUAT (BAY 58-2667) BOUND TO NOSTOC H-NOX DOMAIN
REMARK 900 RELATED ID: 2O09 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H-NOX DOMAIN FROM NOSTOC SP. PCC 7120
REMARK 900 RELATED ID: 2O0C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H-NOX DOMAIN FROM NOSTOC SP. PCC 7120
REMARK 900 COMPLEXED TO NO
REMARK 900 RELATED ID: 2O0G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H-NOX DOMAIN FROM NOSTOC SP. PCC 7120
REMARK 900 COMPLEXED TO CO
REMARK 900 RELATED ID: 4IAE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BAY 60-2770 BOUND TO NOSTOC H-NOX DOMAIN
REMARK 900 RELATED ID: 4IAM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C139A MUTANT OF NOSTOC H-NOX DOMAIN
DBREF 4IAH A 1 182 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 182
DBREF 4IAH B 1 182 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 182
SEQADV 4IAH ALA A 139 UNP Q8YUQ7 CYS 139 ENGINEERED MUTATION
SEQADV 4IAH ALA B 139 UNP Q8YUQ7 CYS 139 ENGINEERED MUTATION
SEQRES 1 A 182 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 A 182 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 A 182 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 A 182 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 A 182 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 A 182 LEU LEU ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 A 182 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 A 182 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 A 182 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 A 182 PRO ALA PHE GLU SNC GLN HIS THR SER SER LYS SER MET
SEQRES 11 A 182 GLU LEU HIS TYR GLN SER THR ARG ALA GLY LEU ALA PRO
SEQRES 12 A 182 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 A 182 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 A 182 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
SEQRES 1 B 182 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 B 182 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 B 182 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 B 182 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 B 182 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 B 182 LEU LEU ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 B 182 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 B 182 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 B 182 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 B 182 PRO ALA PHE GLU SNC GLN HIS THR SER SER LYS SER MET
SEQRES 11 B 182 GLU LEU HIS TYR GLN SER THR ARG ALA GLY LEU ALA PRO
SEQRES 12 B 182 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 B 182 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 B 182 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
MODRES 4IAH SNC A 122 CYS S-NITROSO-CYSTEINE
MODRES 4IAH SNC B 122 CYS S-NITROSO-CYSTEINE
HET SNC A 122 8
HET SNC B 122 6
HET 1DX A 201 45
HET MLI A 202 7
HET 1DX B 201 45
HET MLI B 202 7
HETNAM SNC S-NITROSO-CYSTEINE
HETNAM 1DX 4-({(4-CARBOXYBUTYL)[2-(5-FLUORO-2-{[4'-
HETNAM 2 1DX (TRIFLUOROMETHYL)BIPHENYL-4-YL]METHOXY}PHENYL)
HETNAM 3 1DX ETHYL]AMINO}METHYL)BENZOIC ACID
HETNAM MLI MALONATE ION
FORMUL 1 SNC 2(C3 H6 N2 O3 S)
FORMUL 3 1DX 2(C35 H33 F4 N O5)
FORMUL 4 MLI 2(C3 H2 O4 2-)
FORMUL 7 HOH *35(H2 O)
HELIX 1 1 TYR A 2 ALA A 29 1 28
HELIX 2 2 SER A 44 GLY A 60 1 17
HELIX 3 3 PRO A 62 GLU A 81 1 20
HELIX 4 4 TYR A 83 SER A 89 1 7
HELIX 5 5 SER A 93 LEU A 110 1 18
HELIX 6 6 LEU A 141 PHE A 156 1 16
HELIX 7 7 PHE A 167 GLY A 171 5 5
HELIX 8 8 TYR B 2 LYS B 15 1 14
HELIX 9 9 HIS B 17 ALA B 29 1 13
HELIX 10 10 ASP B 45 GLY B 60 1 16
HELIX 11 11 PRO B 62 THR B 78 1 17
HELIX 12 12 TYR B 83 SER B 89 1 7
HELIX 13 13 SER B 93 PHE B 112 1 20
HELIX 14 14 LEU B 141 PHE B 156 1 16
HELIX 15 15 PHE B 167 GLY B 171 5 5
SHEET 1 A 4 ALA A 119 GLN A 123 0
SHEET 2 A 4 SER A 129 GLN A 135 -1 O GLU A 131 N GLN A 123
SHEET 3 A 4 ASP A 175 TYR A 181 -1 O PHE A 177 N LEU A 132
SHEET 4 A 4 VAL A 160 ALA A 166 -1 N THR A 163 O SER A 178
SHEET 1 B 4 ALA B 119 HIS B 124 0
SHEET 2 B 4 SER B 129 GLN B 135 -1 O GLU B 131 N GLN B 123
SHEET 3 B 4 ASP B 175 TYR B 181 -1 O ASP B 175 N TYR B 134
SHEET 4 B 4 VAL B 160 ALA B 166 -1 N THR B 165 O ILE B 176
LINK C GLU A 121 N SNC A 122 1555 1555 1.33
LINK C SNC A 122 N GLN A 123 1555 1555 1.33
LINK C GLU B 121 N SNC B 122 1555 1555 1.33
LINK C SNC B 122 N GLN B 123 1555 1555 1.33
SITE 1 AC1 19 MET A 1 TYR A 2 LEU A 4 GLY A 39
SITE 2 AC1 19 TRP A 74 TYR A 83 PHE A 97 HIS A 105
SITE 3 AC1 19 PHE A 112 LEU A 115 ARG A 116 PRO A 118
SITE 4 AC1 19 TYR A 134 SER A 136 ARG A 138 MET A 144
SITE 5 AC1 19 LEU A 148 LEU A 152 HOH A 304
SITE 1 AC2 4 HIS A 16 HIS A 17 LYS A 61 LYS B 180
SITE 1 AC3 18 MET B 1 TYR B 2 LEU B 4 GLY B 39
SITE 2 AC3 18 TRP B 74 TYR B 83 PHE B 97 LEU B 101
SITE 3 AC3 18 HIS B 105 PHE B 112 LEU B 115 ARG B 116
SITE 4 AC3 18 PRO B 118 TYR B 134 SER B 136 ARG B 138
SITE 5 AC3 18 LEU B 148 HOH B 316
SITE 1 AC4 6 MET B 12 HIS B 16 HIS B 17 LEU B 59
SITE 2 AC4 6 LYS B 61 LEU B 66
CRYST1 122.573 122.573 122.573 90.00 90.00 90.00 P 21 3 24
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 0.008158 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008158 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
