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HEADER HORMONE 03-MAR-19 6O5J
TITLE CRYSTAL STRUCTURE OF DAD2 BOUND TO QUINAZOLINONE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE DAD2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN DECREASED APICAL DOMINANCE 2;
COMPND 5 EC: 3.1.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE 3 ORGANISM_COMMON: PETUNIA;
SOURCE 4 ORGANISM_TAXID: 4102;
SOURCE 5 GENE: DAD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST566
KEYWDS ALPHA/BETA HYDROLASE, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX
REVDAT 1 26-JUN-19 6O5J 0
JRNL AUTH C.HAMIAUX,L.LARSEN,H.W.LEE,Z.LUO,P.SHARMA,B.C.HAWKINS,
JRNL AUTH 2 N.B.PERRY,K.C.SNOWDEN
JRNL TITL CHEMICAL SYNTHESIS AND CHARACTERIZATION OF A NEW
JRNL TITL 2 QUINAZOLINEDIONE COMPETITIVE ANTAGONIST FOR STRIGOLACTONE
JRNL TITL 3 RECEPTORS WITH AN UNEXPECTED BINDING MODE.
JRNL REF BIOCHEM.J. 2019
JRNL REFN ESSN 1470-8728
JRNL PMID 31186286
JRNL DOI 10.1042/BCJ20190288
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HAMIAUX,R.S.M.DRUMMOND,Z.LUO,H.W.LEE,P.SHARMA,B.J.JANSSEN,
REMARK 1 AUTH 2 N.B.PERRY,W.A.DENNY,K.C.SNOWDEN
REMARK 1 TITL INHIBITION OF STRIGOLACTONE RECEPTORS BY N-PHENYLANTHRANILIC
REMARK 1 TITL 2 ACID DERIVATIVES: STRUCTURAL AND FUNCTIONAL INSIGHTS
REMARK 1 REF J. BIOL. CHEM. V. 293 6530 2018
REMARK 1 REFN ESSN 1083-351X
REMARK 1 PMID 29523686
REMARK 1 DOI 10.1074/JBC.RA117.001154
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
REMARK 1 AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
REMARK 1 TITL DAD2 IS AN A/B HYDROLASE LIKELY TO BE INVOLVED IN THE
REMARK 1 TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE
REMARK 1 REF CURR. BIOL. V. 22 2032 2012
REMARK 1 REFN ISSN 1879-0445
REMARK 1 PMID 22959345
REMARK 1 DOI 10.1016/J.CUB.2012.08.007
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 56359
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2954
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2613
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4154
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 514
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.10000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : -0.08000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.659
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4445 ; 0.016 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4085 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6070 ; 1.947 ; 1.646
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9401 ; 1.594 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 553 ; 6.042 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 243 ;26.841 ;20.782
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 683 ;13.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;18.613 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 554 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5092 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1031 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 266 B 3 266 8761 0.080 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2770 57.7940 -17.2090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0087 T22: 0.1457
REMARK 3 T33: 0.0220 T12: -0.0342
REMARK 3 T13: 0.0057 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 1.6998 L22: 0.6332
REMARK 3 L33: 1.1198 L12: 0.0936
REMARK 3 L13: 0.2729 L23: 0.1247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.0703 S13: -0.0111
REMARK 3 S21: -0.0067 S22: -0.0244 S23: -0.0158
REMARK 3 S31: 0.0039 S32: -0.0252 S33: 0.0252
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4540 76.3930 17.8040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0087 T22: 0.1708
REMARK 3 T33: 0.0211 T12: -0.0228
REMARK 3 T13: 0.0040 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.8575 L22: 0.8672
REMARK 3 L33: 1.2750 L12: 0.2160
REMARK 3 L13: 0.0734 L23: 0.4164
REMARK 3 S TENSOR
REMARK 3 S11: 0.0561 S12: 0.1568 S13: -0.0267
REMARK 3 S21: -0.0073 S22: 0.0186 S23: 0.0133
REMARK 3 S31: -0.0324 S32: -0.0342 S33: -0.0747
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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 : WITH TLS ADDED
REMARK 4
REMARK 4 6O5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62194
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 31.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER 2.5.7
REMARK 200 STARTING MODEL: 4DNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/ACETATE, 0.2M MGCL2, 31% PEG
REMARK 280 3350, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 B 463 O HOH B 539 1.87
REMARK 500 NE2 HIS A 218 O HOH A 401 2.06
REMARK 500 OD2 ASP A 61 O HOH A 402 2.09
REMARK 500 OE1 GLU B 129 O HOH B 401 2.09
REMARK 500 NH1 ARG B 109 O HOH B 402 2.11
REMARK 500 O HOH B 583 O HOH B 596 2.18
REMARK 500 O HOH A 634 O HOH A 645 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 B 588 O HOH B 596 1455 2.13
REMARK 500 O HOH A 427 O HOH B 424 1554 2.13
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 ASP A 184 C ASP A 184 O 0.119
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 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 PHE A 212 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 108 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH2 ANGL. DEV. = -3.1 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 THR A 29 -169.15 -125.93
REMARK 500 SER A 96 -128.10 60.22
REMARK 500 LEU A 247 61.32 -119.54
REMARK 500 ALA A 252 57.66 -144.11
REMARK 500 SER B 96 -128.76 60.74
REMARK 500 ARG B 124 122.47 -171.61
REMARK 500 LEU B 247 63.80 -118.15
REMARK 500 ALA B 252 58.55 -144.78
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 A 649 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 650 DISTANCE = 6.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LM7 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LM7 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DNP RELATED DB: PDB
REMARK 900 DAD2 APO STRUCTURE
REMARK 900 RELATED ID: 6AP6 RELATED DB: PDB
REMARK 900 DAD2 BOUND TO TOLFENAMIC ACID
REMARK 900 RELATED ID: 6AP7 RELATED DB: PDB
REMARK 900 DAD2 BOUND TO 2-(2-METHYL-3-NITROANILINO)BENZOIC ACID
DBREF 6O5J A 3 266 UNP J9U5U9 DAD2_PETHY 3 266
DBREF 6O5J B 3 266 UNP J9U5U9 DAD2_PETHY 3 266
SEQADV 6O5J GLN A 89 UNP J9U5U9 CYS 89 ENGINEERED MUTATION
SEQADV 6O5J GLN B 89 UNP J9U5U9 CYS 89 ENGINEERED MUTATION
SEQRES 1 A 264 GLN THR LEU LEU ASP ALA LEU ASN VAL ARG VAL VAL GLY
SEQRES 2 A 264 SER GLY GLU ARG VAL LEU VAL LEU ALA HIS GLY PHE GLY
SEQRES 3 A 264 THR ASP GLN SER ALA TRP ASN ARG ILE LEU PRO PHE PHE
SEQRES 4 A 264 LEU ARG ASP TYR ARG VAL VAL LEU TYR ASP LEU VAL CYS
SEQRES 5 A 264 ALA GLY SER VAL ASN PRO ASP PHE PHE ASP PHE ARG ARG
SEQRES 6 A 264 TYR THR THR LEU ASP PRO TYR VAL ASP ASP LEU LEU HIS
SEQRES 7 A 264 ILE LEU ASP ALA LEU GLY ILE ASP GLN CYS ALA TYR VAL
SEQRES 8 A 264 GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU ALA SER
SEQRES 9 A 264 ILE ARG ARG PRO GLU LEU PHE SER LYS LEU ILE LEU ILE
SEQRES 10 A 264 GLY ALA SER PRO ARG PHE LEU ASN ASP GLU ASP TYR HIS
SEQRES 11 A 264 GLY GLY PHE GLU GLN GLY GLU ILE GLU LYS VAL PHE SER
SEQRES 12 A 264 ALA MET GLU ALA ASN TYR GLU ALA TRP VAL ASN GLY PHE
SEQRES 13 A 264 ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA ALA VAL
SEQRES 14 A 264 ARG GLU PHE SER ARG THR LEU PHE ASN MET ARG PRO ASP
SEQRES 15 A 264 ILE THR LEU PHE VAL SER ARG THR VAL PHE ASN SER ASP
SEQRES 16 A 264 MET ARG GLY VAL LEU GLY LEU VAL LYS VAL PRO CYS HIS
SEQRES 17 A 264 ILE PHE GLN THR ALA ARG ASP HIS SER VAL PRO ALA SER
SEQRES 18 A 264 VAL ALA THR TYR LEU LYS ASN HIS LEU GLY GLY LYS ASN
SEQRES 19 A 264 THR VAL HIS TRP LEU ASN ILE GLU GLY HIS LEU PRO HIS
SEQRES 20 A 264 LEU SER ALA PRO THR LEU LEU ALA GLN GLU LEU ARG ARG
SEQRES 21 A 264 ALA LEU SER HIS
SEQRES 1 B 264 GLN THR LEU LEU ASP ALA LEU ASN VAL ARG VAL VAL GLY
SEQRES 2 B 264 SER GLY GLU ARG VAL LEU VAL LEU ALA HIS GLY PHE GLY
SEQRES 3 B 264 THR ASP GLN SER ALA TRP ASN ARG ILE LEU PRO PHE PHE
SEQRES 4 B 264 LEU ARG ASP TYR ARG VAL VAL LEU TYR ASP LEU VAL CYS
SEQRES 5 B 264 ALA GLY SER VAL ASN PRO ASP PHE PHE ASP PHE ARG ARG
SEQRES 6 B 264 TYR THR THR LEU ASP PRO TYR VAL ASP ASP LEU LEU HIS
SEQRES 7 B 264 ILE LEU ASP ALA LEU GLY ILE ASP GLN CYS ALA TYR VAL
SEQRES 8 B 264 GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU ALA SER
SEQRES 9 B 264 ILE ARG ARG PRO GLU LEU PHE SER LYS LEU ILE LEU ILE
SEQRES 10 B 264 GLY ALA SER PRO ARG PHE LEU ASN ASP GLU ASP TYR HIS
SEQRES 11 B 264 GLY GLY PHE GLU GLN GLY GLU ILE GLU LYS VAL PHE SER
SEQRES 12 B 264 ALA MET GLU ALA ASN TYR GLU ALA TRP VAL ASN GLY PHE
SEQRES 13 B 264 ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA ALA VAL
SEQRES 14 B 264 ARG GLU PHE SER ARG THR LEU PHE ASN MET ARG PRO ASP
SEQRES 15 B 264 ILE THR LEU PHE VAL SER ARG THR VAL PHE ASN SER ASP
SEQRES 16 B 264 MET ARG GLY VAL LEU GLY LEU VAL LYS VAL PRO CYS HIS
SEQRES 17 B 264 ILE PHE GLN THR ALA ARG ASP HIS SER VAL PRO ALA SER
SEQRES 18 B 264 VAL ALA THR TYR LEU LYS ASN HIS LEU GLY GLY LYS ASN
SEQRES 19 B 264 THR VAL HIS TRP LEU ASN ILE GLU GLY HIS LEU PRO HIS
SEQRES 20 B 264 LEU SER ALA PRO THR LEU LEU ALA GLN GLU LEU ARG ARG
SEQRES 21 B 264 ALA LEU SER HIS
HET LM7 A 301 22
HET GOL A 302 6
HET ACT A 303 4
HET LM7 B 301 22
HET PEG B 302 7
HET GOL B 303 6
HETNAM LM7 1-(4-HYDROXY-3-NITROPHENYL)QUINAZOLINE-2,4(1H,3H)-DIONE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 LM7 2(C14 H9 N3 O5)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 ACT C2 H3 O2 1-
FORMUL 7 PEG C4 H10 O3
FORMUL 9 HOH *514(H2 O)
HELIX 1 AA1 GLN A 3 LEU A 9 1 7
HELIX 2 AA2 ASP A 30 ASN A 35 5 6
HELIX 3 AA3 ILE A 37 PHE A 41 5 5
HELIX 4 AA4 ASN A 59 PHE A 63 5 5
HELIX 5 AA5 LEU A 71 LEU A 85 1 15
HELIX 6 AA6 SER A 96 ARG A 109 1 14
HELIX 7 AA7 GLU A 136 ASN A 150 1 15
HELIX 8 AA8 ASN A 150 GLY A 164 1 15
HELIX 9 AA9 VAL A 167 MET A 181 1 15
HELIX 10 AB1 ARG A 182 SER A 196 1 15
HELIX 11 AB2 MET A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 ALA A 252 1 6
HELIX 14 AB5 ALA A 252 HIS A 266 1 15
HELIX 15 AB6 THR B 4 LEU B 9 1 6
HELIX 16 AB7 ASP B 30 ASN B 35 5 6
HELIX 17 AB8 ILE B 37 PHE B 41 5 5
HELIX 18 AB9 ASN B 59 PHE B 63 5 5
HELIX 19 AC1 LEU B 71 LEU B 85 1 15
HELIX 20 AC2 SER B 96 ARG B 109 1 14
HELIX 21 AC3 GLU B 136 ASN B 150 1 15
HELIX 22 AC4 ASN B 150 GLY B 164 1 15
HELIX 23 AC5 VAL B 167 PHE B 179 1 13
HELIX 24 AC6 ARG B 182 SER B 196 1 15
HELIX 25 AC7 MET B 198 VAL B 205 5 8
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 ALA B 252 1 6
HELIX 28 AD1 ALA B 252 HIS B 266 1 15
SHEET 1 AA1 7 ARG A 12 VAL A 14 0
SHEET 2 AA1 7 ARG A 46 TYR A 50 -1 O VAL A 47 N VAL A 14
SHEET 3 AA1 7 VAL A 20 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 AA1 7 CYS A 209 ALA A 215 1 O PHE A 212 N LEU A 118
SHEET 7 AA1 7 ASN A 236 GLU A 244 1 O HIS A 239 N ILE A 211
SHEET 1 AA2 7 ARG B 12 VAL B 14 0
SHEET 2 AA2 7 ARG B 46 TYR B 50 -1 O VAL B 47 N VAL B 14
SHEET 3 AA2 7 VAL B 20 ALA B 24 1 N LEU B 21 O VAL B 48
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 22
SHEET 5 AA2 7 PHE B 113 ILE B 119 1 O ILE B 117 N TYR B 92
SHEET 6 AA2 7 CYS B 209 ALA B 215 1 O PHE B 212 N LEU B 118
SHEET 7 AA2 7 ASN B 236 GLU B 244 1 O HIS B 239 N ILE B 211
SITE 1 AC1 17 PHE A 27 SER A 96 PHE A 125 PHE A 135
SITE 2 AC1 17 VAL A 143 TRP A 154 PHE A 158 PHE A 174
SITE 3 AC1 17 SER A 190 PHE A 194 HIS A 218 SER A 219
SITE 4 AC1 17 HIS A 246 HOH A 401 HOH A 448 HOH A 483
SITE 5 AC1 17 HOH A 515
SITE 1 AC2 5 TYR A 131 HIS A 132 SER A 223 VAL A 224
SITE 2 AC2 5 ASN B 230
SITE 1 AC3 5 ARG A 36 ASP A 72 PRO A 253 THR A 254
SITE 2 AC3 5 HOH A 420
SITE 1 AC4 16 PHE B 27 SER B 96 PHE B 125 PHE B 135
SITE 2 AC4 16 VAL B 143 TRP B 154 PHE B 158 PHE B 174
SITE 3 AC4 16 SER B 190 PHE B 194 HIS B 218 SER B 219
SITE 4 AC4 16 HIS B 246 HOH B 425 HOH B 473 HOH B 493
SITE 1 AC5 3 LEU B 6 ASP B 7 VAL B 11
SITE 1 AC6 6 HOH A 423 ASP B 130 HIS B 132 SER B 223
SITE 2 AC6 6 VAL B 224 HOH B 578
CRYST1 36.630 56.830 68.800 95.69 94.59 108.74 P 1 2
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 0.027300 0.009262 0.003447 0.00000
SCALE2 0.000000 0.018581 0.002480 0.00000
SCALE3 0.000000 0.000000 0.014711 0.00000
TER 2122 HIS A 266
TER 4263 HIS B 266
MASTER 440 0 6 28 14 0 16 6 4735 2 67 42
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