longtext: 6ap8-pdb

content
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
END