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HEADER SIGNALING PROTEIN 19-OCT-12 3W05
TITLE CRYSTAL STRUCTURE OF ORYZA SATIVA DWARF14 (D14) IN COMPLEX WITH PMSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DWARF 88 ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 55-318;
COMPND 5 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN, EXPRESSED,
COMPND 6 OS03G0203200 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: D88, LOC_OS03G10620, OS03G0203200;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET47B
KEYWDS STRIGOLACTONE SIGNALING, ALPHA/BETA HYDROLASE, STRIGOLACTONE
KEYWDS 2 HYDROLYSIS, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KAGIYAMA,Y.HIRANO,T.MORI,S.Y.KIM,J.KYOZUKA,Y.SETO,S.YAMAGUCHI,
AUTHOR 2 T.HAKOSHIMA
REVDAT 1 23-JAN-13 3W05 0
JRNL AUTH M.KAGIYAMA,Y.HIRANO,T.MORI,S.Y.KIM,J.KYOZUKA,Y.SETO,
JRNL AUTH 2 S.YAMAGUCHI,T.HAKOSHIMA
JRNL TITL STRUCTURES OF D14 AND D14L IN THE STRIGOLACTONE AND KARRIKIN
JRNL TITL 2 SIGNALING PATHWAYS.
JRNL REF GENES CELLS 2013
JRNL REFN ESSN 1365-2443
JRNL PMID 23301669
JRNL DOI 10.1111/GTC.12025
REMARK 2
REMARK 2 RESOLUTION. 1.58 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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 66026
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3501
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4445
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 253
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 431
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : -0.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.096
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4385 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5994 ; 1.481 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 574 ; 5.818 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;26.255 ;22.083
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 688 ;14.126 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;19.777 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 694 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3378 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2737 ; 1.789 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4445 ; 2.787 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1648 ; 4.334 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1534 ; 6.452 ; 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 : 5
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 55 A 318
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5259 14.8312 -18.4063
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: 0.0290
REMARK 3 T33: 0.0242 T12: 0.0098
REMARK 3 T13: -0.0033 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.4400 L22: 0.4250
REMARK 3 L33: 0.4780 L12: 0.1027
REMARK 3 L13: -0.0887 L23: -0.0170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: -0.0411 S13: 0.0312
REMARK 3 S21: -0.0111 S22: 0.0404 S23: -0.0011
REMARK 3 S31: 0.0119 S32: 0.0104 S33: 0.0136
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 55 B 318
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1848 -8.9294 8.5619
REMARK 3 T TENSOR
REMARK 3 T11: 0.0358 T22: 0.0101
REMARK 3 T33: 0.0034 T12: 0.0086
REMARK 3 T13: -0.0048 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.2883 L22: 0.6649
REMARK 3 L33: 0.5155 L12: -0.0782
REMARK 3 L13: 0.0654 L23: -0.1679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0296 S12: 0.0297 S13: 0.0000
REMARK 3 S21: -0.0998 S22: -0.0261 S23: 0.0025
REMARK 3 S31: 0.0949 S32: 0.0042 S33: -0.0035
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 728
REMARK 3 RESIDUE RANGE : B 501 B 703
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8108 3.6230 -7.2421
REMARK 3 T TENSOR
REMARK 3 T11: 0.0272 T22: 0.0165
REMARK 3 T33: 0.0189 T12: 0.0146
REMARK 3 T13: 0.0022 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0744 L22: 0.1859
REMARK 3 L33: 0.4014 L12: 0.0946
REMARK 3 L13: -0.0483 L23: -0.1741
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: 0.0097 S13: 0.0019
REMARK 3 S21: -0.0291 S22: 0.0177 S23: -0.0056
REMARK 3 S31: 0.0581 S32: 0.0076 S33: -0.0098
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1910 0.7032 -4.6171
REMARK 3 T TENSOR
REMARK 3 T11: 0.0619 T22: 0.0817
REMARK 3 T33: 0.0396 T12: 0.0343
REMARK 3 T13: 0.0054 T23: -0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 0.7912 L22: 0.1299
REMARK 3 L33: 0.1169 L12: 0.0490
REMARK 3 L13: 0.0061 L23: 0.1221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0189 S13: 0.0216
REMARK 3 S21: 0.0501 S22: 0.0294 S23: -0.0122
REMARK 3 S31: 0.0458 S32: 0.0415 S33: -0.0283
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 402 A 405
REMARK 3 RESIDUE RANGE : B 402 B 404
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9755 2.2993 -7.3628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1077 T22: 0.0554
REMARK 3 T33: 0.0527 T12: 0.0189
REMARK 3 T13: -0.0048 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0926 L22: 0.6239
REMARK 3 L33: 0.4923 L12: 0.1661
REMARK 3 L13: -0.1523 L23: -0.5117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.0026 S13: 0.0281
REMARK 3 S21: 0.0009 S22: 0.0470 S23: 0.1470
REMARK 3 S31: 0.0416 S32: 0.0099 S33: -0.1012
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 3W05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB095718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR , SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69842
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49300
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLREP
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1WOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG6000, 5% MPD, 0.1M NA-HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 24.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.44200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.25900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.44200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.25900
REMARK 290 SMTRY3 4 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 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 53
REMARK 465 PRO A 54
REMARK 465 GLY B 53
REMARK 465 PRO B 54
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 ARG B 317 CG CD NE CZ NH1 NH2
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 TYR A 119 49.75 -92.09
REMARK 500 SER A 147 -115.04 56.06
REMARK 500 ARG A 175 123.29 -174.03
REMARK 500 ASP A 181 39.16 33.52
REMARK 500 ASN A 201 80.35 -161.01
REMARK 500 ALA A 303 53.78 -145.84
REMARK 500 SER B 147 -118.36 51.99
REMARK 500 ARG B 175 127.67 -170.98
REMARK 500 SER B 180 -128.89 50.72
REMARK 500 ASN B 201 83.98 -153.21
REMARK 500 ALA B 303 55.90 -142.77
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 PMS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W04 RELATED DB: PDB
REMARK 900 RELATED ID: 3W06 RELATED DB: PDB
DBREF 3W05 A 55 318 UNP Q10QA5 Q10QA5_ORYSJ 55 318
DBREF 3W05 B 55 318 UNP Q10QA5 Q10QA5_ORYSJ 55 318
SEQADV 3W05 GLY A 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 3W05 PRO A 54 UNP Q10QA5 EXPRESSION TAG
SEQADV 3W05 GLY B 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 3W05 PRO B 54 UNP Q10QA5 EXPRESSION TAG
SEQRES 1 A 266 GLY PRO LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL VAL
SEQRES 2 A 266 GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY PHE
SEQRES 3 A 266 GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO TYR
SEQRES 4 A 266 LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU VAL
SEQRES 5 A 266 CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE ARG
SEQRES 6 A 266 ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU LEU
SEQRES 7 A 266 ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA PHE
SEQRES 8 A 266 VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU ALA
SEQRES 9 A 266 SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL LEU
SEQRES 10 A 266 ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP TYR
SEQRES 11 A 266 HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL PHE
SEQRES 12 A 266 ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR GLY
SEQRES 13 A 266 TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA ALA
SEQRES 14 A 266 VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG PRO
SEQRES 15 A 266 ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS THR
SEQRES 16 A 266 ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO CYS
SEQRES 17 A 266 VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO ALA
SEQRES 18 A 266 SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY ARG
SEQRES 19 A 266 THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU PRO
SEQRES 20 A 266 HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU ARG
SEQRES 21 A 266 ARG ALA LEU ALA ARG TYR
SEQRES 1 B 266 GLY PRO LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL VAL
SEQRES 2 B 266 GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY PHE
SEQRES 3 B 266 GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO TYR
SEQRES 4 B 266 LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU VAL
SEQRES 5 B 266 CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE ARG
SEQRES 6 B 266 ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU LEU
SEQRES 7 B 266 ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA PHE
SEQRES 8 B 266 VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU ALA
SEQRES 9 B 266 SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL LEU
SEQRES 10 B 266 ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP TYR
SEQRES 11 B 266 HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL PHE
SEQRES 12 B 266 ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR GLY
SEQRES 13 B 266 TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA ALA
SEQRES 14 B 266 VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG PRO
SEQRES 15 B 266 ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS THR
SEQRES 16 B 266 ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO CYS
SEQRES 17 B 266 VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO ALA
SEQRES 18 B 266 SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY ARG
SEQRES 19 B 266 THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU PRO
SEQRES 20 B 266 HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU ARG
SEQRES 21 B 266 ARG ALA LEU ALA ARG TYR
HET PMS A 401 10
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET PMS B 401 10
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HETNAM PMS PHENYLMETHANESULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PMS 2(C7 H8 O3 S)
FORMUL 4 EDO 7(C2 H6 O2)
FORMUL 12 HOH *431(H2 O)
HELIX 1 1 LYS A 55 LEU A 60 1 6
HELIX 2 2 ASP A 81 SER A 86 5 6
HELIX 3 3 VAL A 88 LEU A 92 5 5
HELIX 4 4 ASN A 110 PHE A 114 5 5
HELIX 5 5 ARG A 117 ASP A 120 5 4
HELIX 6 6 ASN A 121 LEU A 136 1 16
HELIX 7 7 SER A 147 ARG A 160 1 14
HELIX 8 8 GLU A 187 ASN A 201 1 15
HELIX 9 9 ASN A 201 GLY A 215 1 15
HELIX 10 10 VAL A 218 PHE A 230 1 13
HELIX 11 11 ARG A 233 LYS A 246 1 14
HELIX 12 12 LEU A 249 VAL A 256 5 8
HELIX 13 13 SER A 274 LEU A 283 1 10
HELIX 14 14 LEU A 298 ALA A 303 1 6
HELIX 15 15 ALA A 303 LEU A 315 1 13
HELIX 16 16 LEU B 56 LEU B 60 1 5
HELIX 17 17 ASP B 81 SER B 86 5 6
HELIX 18 18 VAL B 88 LEU B 92 5 5
HELIX 19 19 ASN B 110 PHE B 114 5 5
HELIX 20 20 ARG B 117 ASP B 120 5 4
HELIX 21 21 ASN B 121 LEU B 136 1 16
HELIX 22 22 SER B 147 ARG B 160 1 14
HELIX 23 23 GLU B 187 ASN B 201 1 15
HELIX 24 24 ASN B 201 GLY B 215 1 15
HELIX 25 25 VAL B 218 MET B 232 1 15
HELIX 26 26 ARG B 233 LYS B 246 1 14
HELIX 27 27 LEU B 249 VAL B 256 5 8
HELIX 28 28 SER B 274 LEU B 283 1 10
HELIX 29 29 LEU B 298 ALA B 303 1 6
HELIX 30 30 ALA B 303 LEU B 315 1 13
SHEET 1 A 7 ARG A 63 GLY A 66 0
SHEET 2 A 7 ARG A 97 LEU A 100 -1 O VAL A 98 N VAL A 65
SHEET 3 A 7 VAL A 71 SER A 75 1 N VAL A 72 O ARG A 97
SHEET 4 A 7 CYS A 141 HIS A 146 1 O VAL A 144 N VAL A 73
SHEET 5 A 7 PHE A 164 ILE A 170 1 O ALA A 165 N CYS A 141
SHEET 6 A 7 CYS A 260 GLN A 264 1 O VAL A 261 N LEU A 169
SHEET 7 A 7 THR A 287 PHE A 291 1 O THR A 288 N VAL A 262
SHEET 1 B 7 ARG B 63 GLY B 66 0
SHEET 2 B 7 ARG B 97 LEU B 100 -1 O VAL B 98 N VAL B 65
SHEET 3 B 7 VAL B 71 SER B 75 1 N VAL B 72 O VAL B 99
SHEET 4 B 7 CYS B 141 HIS B 146 1 O VAL B 144 N VAL B 73
SHEET 5 B 7 PHE B 164 ILE B 170 1 O ALA B 165 N CYS B 141
SHEET 6 B 7 CYS B 260 GLN B 264 1 O VAL B 263 N LEU B 169
SHEET 7 B 7 THR B 287 PHE B 291 1 O GLU B 290 N GLN B 264
LINK OG SER A 147 S PMS A 401 1555 1555 1.60
LINK OG SER B 147 S PMS B 401 1555 1555 1.54
SITE 1 AC1 6 PHE A 78 SER A 147 VAL A 148 PHE A 176
SITE 2 AC1 6 VAL A 244 PHE A 245
SITE 1 AC2 4 TYR A 182 HIS A 183 SER A 274 VAL A 275
SITE 1 AC3 4 PHE A 186 TYR A 209 SER A 270 HOH A 657
SITE 1 AC4 5 ARG A 97 LEU A 136 HOH A 610 HOH A 655
SITE 2 AC4 5 ARG B 94
SITE 1 AC5 8 MET A 198 GLY A 199 ASN A 201 TYR A 202
SITE 2 AC5 8 PRO A 234 HOH A 538 PRO B 90 TYR B 91
SITE 1 AC6 8 PHE B 78 SER B 147 VAL B 148 MET B 151
SITE 2 AC6 8 PHE B 176 VAL B 244 PHE B 245 HIS B 297
SITE 1 AC7 6 ASP B 181 TYR B 182 HIS B 183 SER B 274
SITE 2 AC7 6 VAL B 275 HOH B 574
SITE 1 AC8 5 ASP B 120 HIS B 239 GLN B 242 THR B 243
SITE 2 AC8 5 LYS B 246
SITE 1 AC9 6 SER A 203 TYR B 91 SER B 305 GLN B 309
SITE 2 AC9 6 HOH B 517 HOH B 625
CRYST1 48.300 88.518 118.884 90.00 90.00 90.00 P 21 21 21 8
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 0.020704 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008412 0.00000
TER 2109 TYR A 318
TER 4231 TYR B 318
MASTER 420 0 9 30 14 0 16 6 4565 2 50 42
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