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HEADER PLANT PROTEIN 17-AUG-17 6AP8
TITLE CRYSTAL STRUCTURE OF RICE D14 BOUND TO 2-(2-METHYL-3-NITROANILINO)
TITLE 2 BENZOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 52-318;
COMPND 5 SYNONYM: PROTEIN DWARF 14,PROTEIN DWARF 88,PROTEIN HIGH-TILLERING
COMPND 6 DWARF 2;
COMPND 7 EC: 3.1.-.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: D14, D88, HTD2, OS03G0203200, LOC_OS03G10620;
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, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX
REVDAT 1 21-MAR-18 6AP8 0
JRNL AUTH C.HAMIAUX,R.S.M.DRUMMOND,Z.LUO,H.W.LEE,P.SHARMA,B.J.JANSSEN,
JRNL AUTH 2 N.B.PERRY,W.A.DENNY,K.C.SNOWDEN
JRNL TITL INHIBITION OF STRIGOLACTONE RECEPTORS BY N-PHENYLANTHRANILIC
JRNL TITL 2 ACID DERIVATIVES: STRUCTURAL AND FUNCTIONAL INSIGHTS
JRNL REF J.BIOL.CHEM. 2018
JRNL REFN ESSN 1083-351X
REMARK 1
REMARK 1 REFERENCE 1
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 ALPHA/BETA 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. 1.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 127214
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) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.119
REMARK 3 FREE R VALUE : 0.154
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6862
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) : 1.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9294
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 488
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4116
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 647
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.35000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : 0.67000
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): 0.038
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.029
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.573
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4508 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4334 ; 0.012 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6186 ; 1.958 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9907 ; 1.763 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 598 ; 6.016 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 203 ;26.064 ;21.872
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 702 ;11.348 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;17.387 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 704 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5273 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1147 ; 0.014 ; 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): 8842 ; 3.331 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 139 ;30.654 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 9221 ;11.080 ; 5.000
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 53 317 B 53 317 31812 0.130 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6AP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229531.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.270
REMARK 200 RESOLUTION RANGE LOW (A) : 48.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.30
REMARK 200 R MERGE FOR SHELL (I) : 1.99200
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: 3W04
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES 0.1M, MPD 5%, PEG 6000 8%, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 24.00250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.51300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.21650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.51300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.00250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.21650
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 300 REMARK: MONOMER AS DETERMINED BY GEL FILTRATION
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 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 50
REMARK 465 GLY A 51
REMARK 465 SER A 52
REMARK 465 GLY B 50
REMARK 465 GLY B 51
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 579 O HOH B 733 1.94
REMARK 500 O2 BNY A 401 O HOH A 501 1.97
REMARK 500 OG1 THR A 294 O HOH A 502 1.99
REMARK 500 NH2 ARG B 70 O LEU B 315 2.04
REMARK 500 O HOH A 723 O HOH B 711 2.05
REMARK 500 NH1 ARG B 118 O HOH B 501 2.13
REMARK 500 ND2 ASN B 121 O HOH B 502 2.15
REMARK 500 O HOH B 724 O HOH B 799 2.16
REMARK 500 O HOH A 507 O HOH A 711 2.17
REMARK 500 OD1 ASN B 231 O HOH B 503 2.17
REMARK 500 OD2 ASP B 95 NH2 ARG B 312 2.17
REMARK 500 O HOH A 581 O HOH A 763 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 776 O HOH B 530 2454 1.99
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 GLY A 53 N GLY A 53 CA 0.099
REMARK 500 SER A 147 CA SER A 147 CB 0.125
REMARK 500 SER A 147 CB SER A 147 OG -0.109
REMARK 500 GLN A 193 CD GLN A 193 NE2 -0.157
REMARK 500 TYR A 318 CE1 TYR A 318 CZ -0.081
REMARK 500 SER B 147 CA SER B 147 CB 0.158
REMARK 500 SER B 147 CB SER B 147 OG -0.163
REMARK 500 GLU B 189 CD GLU B 189 OE1 0.079
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 ASP A 95 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 123 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 GLU A 187 OE1 - CD - OE2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 PHE A 230 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 CYS A 260 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 267 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 87 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP B 123 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 SER B 147 N - CA - CB ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG B 250 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 267 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 267 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 313 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 147 -127.23 61.76
REMARK 500 ARG A 175 120.26 -171.18
REMARK 500 ASN A 201 79.04 -159.94
REMARK 500 GLN A 293 36.56 -96.46
REMARK 500 GLN A 293 42.56 -96.46
REMARK 500 ALA A 303 54.38 -146.56
REMARK 500 ASP B 81 -167.27 -119.74
REMARK 500 SER B 147 -124.74 60.94
REMARK 500 ARG B 175 119.50 -173.70
REMARK 500 ASP B 181 17.99 56.63
REMARK 500 ASN B 201 79.45 -157.18
REMARK 500 ALA B 303 53.43 -144.13
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 837 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 808 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 809 DISTANCE = 6.67 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BNY A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BNY B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W04 RELATED DB: PDB
REMARK 900 3W04 IS THE APO STRUCTURE
DBREF 6AP8 A 52 318 UNP Q10QA5 D14_ORYSJ 52 318
DBREF 6AP8 B 52 318 UNP Q10QA5 D14_ORYSJ 52 318
SEQADV 6AP8 GLY A 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 6AP8 GLY A 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 6AP8 GLY B 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 6AP8 GLY B 51 UNP Q10QA5 EXPRESSION TAG
SEQRES 1 A 269 GLY GLY SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL
SEQRES 2 A 269 ARG VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER
SEQRES 3 A 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL
SEQRES 4 A 269 LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR
SEQRES 5 A 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE
SEQRES 6 A 269 ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP
SEQRES 7 A 269 ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG
SEQRES 8 A 269 CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 A 269 ILE LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS
SEQRES 10 A 269 LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 A 269 SER ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN
SEQRES 12 A 269 GLN VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP
SEQRES 13 A 269 ALA THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 A 269 PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 269 MET ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL
SEQRES 16 A 269 PHE LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG
SEQRES 17 A 269 ALA PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER
SEQRES 18 A 269 VAL PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU
SEQRES 19 A 269 GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY
SEQRES 20 A 269 HIS LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN
SEQRES 21 A 269 VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 B 269 GLY GLY SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL
SEQRES 2 B 269 ARG VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER
SEQRES 3 B 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL
SEQRES 4 B 269 LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR
SEQRES 5 B 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE
SEQRES 6 B 269 ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP
SEQRES 7 B 269 ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG
SEQRES 8 B 269 CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 B 269 ILE LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS
SEQRES 10 B 269 LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 B 269 SER ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN
SEQRES 12 B 269 GLN VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP
SEQRES 13 B 269 ALA THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 B 269 PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 B 269 MET ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL
SEQRES 16 B 269 PHE LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG
SEQRES 17 B 269 ALA PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER
SEQRES 18 B 269 VAL PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU
SEQRES 19 B 269 GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY
SEQRES 20 B 269 HIS LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN
SEQRES 21 B 269 VAL LEU ARG ARG ALA LEU ALA ARG TYR
HET BNY A 401 20
HET GOL A 402 6
HET BNY B 401 20
HET GOL B 402 6
HETNAM BNY 2-[(2-METHYL-3-NITROPHENYL)AMINO]BENZOIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BNY 2(C14 H12 N2 O4)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 7 HOH *647(H2 O)
HELIX 1 AA1 GLY A 53 LEU A 60 1 8
HELIX 2 AA2 ASP A 81 SER A 86 5 6
HELIX 3 AA3 VAL A 88 LEU A 92 5 5
HELIX 4 AA4 ASN A 110 PHE A 114 5 5
HELIX 5 AA5 ARG A 117 ASP A 120 5 4
HELIX 6 AA6 ASN A 121 LEU A 136 1 16
HELIX 7 AA7 SER A 147 ARG A 160 1 14
HELIX 8 AA8 GLU A 187 ASN A 201 1 15
HELIX 9 AA9 ASN A 201 GLY A 215 1 15
HELIX 10 AB1 VAL A 218 MET A 232 1 15
HELIX 11 AB2 ARG A 233 LYS A 246 1 14
HELIX 12 AB3 LEU A 249 VAL A 256 5 8
HELIX 13 AB4 PRO A 272 LEU A 283 1 12
HELIX 14 AB5 LEU A 298 ALA A 303 1 6
HELIX 15 AB6 ALA A 303 LEU A 315 1 13
HELIX 16 AB7 GLY B 53 LEU B 60 1 8
HELIX 17 AB8 ASP B 81 SER B 86 5 6
HELIX 18 AB9 VAL B 88 LEU B 92 5 5
HELIX 19 AC1 ASN B 110 PHE B 114 5 5
HELIX 20 AC2 ARG B 117 ASP B 120 5 4
HELIX 21 AC3 ASN B 121 LEU B 136 1 16
HELIX 22 AC4 SER B 147 ARG B 160 1 14
HELIX 23 AC5 GLU B 187 ASN B 201 1 15
HELIX 24 AC6 ASN B 201 GLY B 215 1 15
HELIX 25 AC7 VAL B 218 MET B 232 1 15
HELIX 26 AC8 ARG B 233 LYS B 246 1 14
HELIX 27 AC9 LEU B 249 VAL B 256 5 8
HELIX 28 AD1 PRO B 272 LEU B 283 1 12
HELIX 29 AD2 LEU B 298 ALA B 303 1 6
HELIX 30 AD3 ALA B 303 ALA B 316 1 14
SHEET 1 AA1 7 ARG A 63 GLY A 66 0
SHEET 2 AA1 7 ARG A 97 LEU A 100 -1 O VAL A 98 N VAL A 65
SHEET 3 AA1 7 VAL A 71 SER A 75 1 N VAL A 72 O VAL A 99
SHEET 4 AA1 7 CYS A 141 HIS A 146 1 O VAL A 144 N VAL A 73
SHEET 5 AA1 7 PHE A 164 ILE A 170 1 O ALA A 165 N CYS A 141
SHEET 6 AA1 7 CYS A 260 GLN A 264 1 O VAL A 263 N LEU A 169
SHEET 7 AA1 7 THR A 287 PHE A 291 1 O THR A 288 N VAL A 262
SHEET 1 AA2 7 ARG B 63 GLY B 66 0
SHEET 2 AA2 7 ARG B 97 LEU B 100 -1 O VAL B 98 N VAL B 65
SHEET 3 AA2 7 VAL B 71 SER B 75 1 N LEU B 74 O VAL B 99
SHEET 4 AA2 7 CYS B 141 HIS B 146 1 O VAL B 144 N VAL B 73
SHEET 5 AA2 7 PHE B 164 ILE B 170 1 O VAL B 168 N PHE B 143
SHEET 6 AA2 7 CYS B 260 THR B 265 1 O VAL B 263 N LEU B 169
SHEET 7 AA2 7 THR B 287 LEU B 292 1 O GLU B 290 N VAL B 262
SITE 1 AC1 11 PHE A 78 SER A 147 PHE A 176 PHE A 186
SITE 2 AC1 11 VAL A 194 TRP A 205 CYS A 241 SER A 270
SITE 3 AC1 11 HIS A 297 HOH A 501 HOH A 568
SITE 1 AC2 5 TYR A 182 HIS A 183 SER A 274 VAL A 275
SITE 2 AC2 5 HOH A 538
SITE 1 AC3 13 PHE B 78 SER B 147 PHE B 176 PHE B 186
SITE 2 AC3 13 VAL B 194 CYS B 241 VAL B 244 PHE B 245
SITE 3 AC3 13 SER B 270 HIS B 297 HOH B 544 HOH B 570
SITE 4 AC3 13 HOH B 669
SITE 1 AC4 8 ASP B 181 TYR B 182 HIS B 183 GLY B 208
SITE 2 AC4 8 PRO B 211 LEU B 212 SER B 274 VAL B 275
CRYST1 48.005 88.433 119.026 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 0.020831 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008402 0.00000
TER 2151 TYR A 318
TER 4329 TYR B 318
MASTER 437 0 4 30 14 0 11 6 4815 2 52 42
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