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HEADER HYDROLASE 08-FEB-12 4DNP
TITLE CRYSTAL STRUCTURE OF DAD2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DAD2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE 3 ORGANISM_TAXID: 4102;
SOURCE 4 GENE: DAD2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST566
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX
REVDAT 1 14-NOV-12 4DNP 0
JRNL AUTH C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
JRNL AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
JRNL TITL DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE
JRNL TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE
JRNL REF CURR.BIOL. 2012
JRNL REFN ISSN 0960-9822
JRNL PMID 22959345
JRNL DOI 10.1016/J.CUB.2012.08.007
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19671
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1006
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1372
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.2150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.59
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.332
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2137 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1440 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2904 ; 1.491 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3474 ; 0.961 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 5.921 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;30.147 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 332 ;15.762 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;20.005 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2390 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 474 ; 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): 1310 ; 0.766 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 533 ; 0.207 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2111 ; 1.471 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 827 ; 2.500 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 792 ; 4.050 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 265
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5940 -43.4720 8.5130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1078 T22: 0.0499
REMARK 3 T33: 0.0911 T12: 0.0304
REMARK 3 T13: -0.0818 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 3.0324 L22: 1.4501
REMARK 3 L33: 1.2537 L12: -0.3950
REMARK 3 L13: 0.2780 L23: -0.1872
REMARK 3 S TENSOR
REMARK 3 S11: -0.1530 S12: -0.2391 S13: 0.1327
REMARK 3 S21: 0.0647 S22: 0.0455 S23: -0.0938
REMARK 3 S31: -0.1377 S32: 0.0210 S33: 0.1076
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4DNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979417
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19684
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 40.876
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.700
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : 0.12600
REMARK 200 FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 22.10
REMARK 200 R MERGE FOR SHELL (I) : 0.45800
REMARK 200 R SYM FOR SHELL (I) : 0.45800
REMARK 200 FOR SHELL : 7.700
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 (%): 59.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2HPO4 0.6M, PH 7.1, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,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 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 64.63000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 64.63000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 64.63000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 64.63000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 64.63000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 64.63000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 64.63000
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 300 REMARK: THIS PROTEIN BEHAVES AS A MONOMER ON GEL FILTRATION COLUMN
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -129.26000
REMARK 350 BIOMT3 2 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 GLY A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 HIS A 266
REMARK 465 ARG A 267
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 SG CYS A 89 S1 DTV A 301 2.02
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 SG CYS A 89 S4 DTV A 301 4545 2.08
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 SER A 96 -133.39 63.28
REMARK 500 LYS A 115 140.16 -170.68
REMARK 500 ARG A 124 123.74 -174.73
REMARK 500 ASN A 150 86.88 -166.51
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 551 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A 562 DISTANCE = 6.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTV 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DNQ RELATED DB: PDB
DBREF 4DNP A -1 267 PDB 4DNP 4DNP -1 267
SEQRES 1 A 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 A 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 A 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 A 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 A 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 A 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 A 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 A 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 A 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 A 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 A 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 A 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 A 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 A 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 A 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 A 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 A 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 A 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 A 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 A 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
HET DTV A 301 8
HET GOL A 302 6
HETNAM DTV (2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 DTV C4 H10 O2 S2
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *182(H2 O)
HELIX 1 1 GLN A 3 LEU A 9 1 7
HELIX 2 2 ASP A 30 ASN A 35 5 6
HELIX 3 3 ILE A 37 LEU A 42 5 6
HELIX 4 4 ASN A 59 PHE A 63 5 5
HELIX 5 5 LEU A 71 LEU A 85 1 15
HELIX 6 6 SER A 96 ARG A 109 1 14
HELIX 7 7 GLU A 136 ASN A 150 1 15
HELIX 8 8 ASN A 150 GLY A 164 1 15
HELIX 9 9 VAL A 167 MET A 181 1 15
HELIX 10 10 ARG A 182 ASN A 195 1 14
HELIX 11 11 MET A 198 VAL A 205 5 8
HELIX 12 12 PRO A 221 LEU A 232 1 12
HELIX 13 13 LEU A 247 ALA A 252 1 6
HELIX 14 14 ALA A 252 SER A 265 1 14
SHEET 1 A 7 ARG A 12 VAL A 14 0
SHEET 2 A 7 ARG A 46 TYR A 50 -1 O VAL A 47 N VAL A 14
SHEET 3 A 7 VAL A 20 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 A 7 CYS A 90 HIS A 95 1 O ALA A 91 N VAL A 22
SHEET 5 A 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 A 7 CYS A 209 ALA A 215 1 O PHE A 212 N LEU A 118
SHEET 7 A 7 ASN A 236 GLU A 244 1 O THR A 237 N ILE A 211
SITE 1 AC1 1 CYS A 89
SITE 1 AC2 6 SER A 96 VAL A 97 PHE A 125 HIS A 246
SITE 2 AC2 6 HOH A 580 HOH A 582
CRYST1 129.260 129.260 129.260 90.00 90.00 90.00 I 2 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 0.007736 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007736 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007736 0.00000
TER 2073 SER A 265
MASTER 430 0 2 14 7 0 3 6 2260 1 14 21
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