| 6ap7-pdb | HEADER PLANT PROTEIN 17-AUG-17 6AP7
TITLE CRYSTAL STRUCTURE OF DAD2 IN COMPLEX WITH 2-(2-METHYL-3-NITROANILINO)
TITLE 2 BENZOIC ACID
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 ENGINEERED: 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, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX
REVDAT 1 21-MAR-18 6AP7 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. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0124
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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 66090
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3485
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) : 1.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4204
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.3040
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 : 46
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.12000
REMARK 3 B13 (A**2) : -0.09000
REMARK 3 B23 (A**2) : 0.20000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.628
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4403 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4178 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6002 ; 1.760 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9545 ; 1.436 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 547 ; 5.677 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;28.059 ;22.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 685 ;13.102 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;15.842 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 666 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5075 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1111 ; 0.010 ; 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 32876 0.090 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): -12.2690 -51.2530 -34.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: 0.1088
REMARK 3 T33: 0.0103 T12: -0.0052
REMARK 3 T13: -0.0017 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 2.1828 L22: 1.1100
REMARK 3 L33: 2.0289 L12: 0.4644
REMARK 3 L13: -0.1150 L23: -0.9659
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.0617 S13: 0.0411
REMARK 3 S21: 0.0336 S22: 0.0128 S23: -0.0366
REMARK 3 S31: 0.0199 S32: -0.0418 S33: 0.0026
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): -9.3230 -36.3980 -70.3690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0137 T22: 0.1535
REMARK 3 T33: 0.0168 T12: -0.0340
REMARK 3 T13: -0.0111 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 1.3203 L22: 0.8281
REMARK 3 L33: 1.2534 L12: 0.0384
REMARK 3 L13: 0.0404 L23: -0.2835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: 0.0857 S13: 0.0400
REMARK 3 S21: -0.0491 S22: 0.0076 S23: 0.0533
REMARK 3 S31: 0.0338 S32: -0.0190 S33: 0.0278
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
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 6AP7 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_1000229529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-15
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 : AIMLESS 0.5.12
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69577
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 45.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.83000
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: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/ACETATE 0.1M, MGCL2 0.2M, PEG
REMARK 280 3350 27%, PH 8.5, VAPOR DIFFUSION, HANGING DROP, 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 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 ARG A 267
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 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 NE2 HIS B 210 O HOH B 401 1.97
REMARK 500 O HOH B 431 O HOH B 502 2.00
REMARK 500 O HOH B 403 O HOH B 527 2.01
REMARK 500 OD2 ASP B 61 O HOH B 402 2.02
REMARK 500 OD1 ASN B 10 O HOH B 403 2.03
REMARK 500 OD1 ASN A 10 O HOH A 401 2.06
REMARK 500 O HOH A 411 O HOH B 403 2.09
REMARK 500 O HOH A 401 O HOH A 411 2.09
REMARK 500 O HOH B 404 O HOH B 568 2.09
REMARK 500 O HOH A 401 O HOH B 527 2.09
REMARK 500 O HOH B 596 O HOH B 605 2.10
REMARK 500 OE2 GLU B 148 O HOH B 404 2.11
REMARK 500 O HOH A 401 O HOH A 555 2.12
REMARK 500 O HOH B 401 O HOH B 610 2.12
REMARK 500 O HOH A 401 O HOH A 542 2.13
REMARK 500 O HOH A 401 O HOH A 522 2.15
REMARK 500 O HOH A 463 O HOH A 544 2.16
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 76 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.3 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 96 -133.86 54.03
REMARK 500 ARG A 124 119.00 -166.22
REMARK 500 GLU A 129 -75.77 -51.88
REMARK 500 ASN A 150 87.00 -156.05
REMARK 500 ALA A 252 56.94 -141.22
REMARK 500 SER B 96 -132.37 56.32
REMARK 500 ARG B 124 115.60 -172.04
REMARK 500 ASN B 150 86.62 -159.08
REMARK 500 ALA B 252 56.70 -142.47
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 BNY A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BNY B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DNP RELATED DB: PDB
REMARK 900 4DNP IS THE APO PROETIN
DBREF 6AP7 A 1 267 UNP J9U5U9 DAD2_PETHY 1 267
DBREF 6AP7 B 1 267 UNP J9U5U9 DAD2_PETHY 1 267
SEQADV 6AP7 GLY A -1 UNP J9U5U9 EXPRESSION TAG
SEQADV 6AP7 GLY A 0 UNP J9U5U9 EXPRESSION TAG
SEQADV 6AP7 GLN A 89 UNP J9U5U9 CYS 89 ENGINEERED MUTATION
SEQADV 6AP7 GLY B -1 UNP J9U5U9 EXPRESSION TAG
SEQADV 6AP7 GLY B 0 UNP J9U5U9 EXPRESSION TAG
SEQADV 6AP7 GLN B 89 UNP J9U5U9 CYS 89 ENGINEERED MUTATION
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 GLN
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
SEQRES 1 B 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 B 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 B 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 B 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 B 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 B 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 B 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES 8 B 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 B 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 B 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 B 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 B 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 B 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 B 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 B 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 B 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 B 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 B 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 B 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 B 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 B 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
HET BNY A 300 20
HET BNY B 301 20
HET GOL B 302 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 5 GOL C3 H8 O3
FORMUL 6 HOH *450(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 GLY A 86 1 16
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 ASN A 195 1 14
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 MET B 181 1 15
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 TYR A 45 TYR A 50 -1 O VAL A 47 N VAL A 14
SHEET 3 AA1 7 ARG A 19 ALA A 24 1 N ARG A 19 O ARG A 46
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 THR A 237 N ILE A 211
SHEET 1 AA2 7 ARG B 12 VAL B 14 0
SHEET 2 AA2 7 TYR B 45 TYR B 50 -1 O LEU B 49 N ARG B 12
SHEET 3 AA2 7 ARG B 19 ALA B 24 1 N ARG B 19 O ARG B 46
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N ALA B 24
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 14 PHE A 27 SER A 96 PHE A 125 PHE A 135
SITE 2 AC1 14 ILE A 140 VAL A 143 PHE A 158 SER A 190
SITE 3 AC1 14 VAL A 193 HIS A 218 SER A 219 HIS A 246
SITE 4 AC1 14 HOH A 518 HOH A 530
SITE 1 AC2 14 PHE B 27 SER B 96 PHE B 125 PHE B 135
SITE 2 AC2 14 ILE B 140 VAL B 143 PHE B 158 SER B 190
SITE 3 AC2 14 VAL B 193 HIS B 218 SER B 219 HIS B 246
SITE 4 AC2 14 HOH B 579 HOH B 583
SITE 1 AC3 7 THR A 226 LYS A 229 ASN A 230 TYR B 131
SITE 2 AC3 7 HIS B 132 SER B 223 HOH B 440
CRYST1 36.697 48.315 71.942 82.67 86.76 69.95 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 0.027250 -0.009945 -0.000398 0.00000
SCALE2 0.000000 0.022033 -0.002558 0.00000
SCALE3 0.000000 0.000000 0.014016 0.00000
TER 2120 HIS A 266
TER 4244 HIS B 266
MASTER 389 0 3 28 14 0 10 6 4650 2 46 42
END
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