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LongText Report for: 3W04-pdb

Name Class
3W04-pdb
HEADER    HYDROLASE                               19-OCT-12   3W04              
TITLE     CRYSTAL STRUCTURE OF ORYZA SATIVA DWARF14 (D14)                       
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, HYDROLASE                                                
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 3W04    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.    1.45 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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 86870                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
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      : 4583                            
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6305                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 321                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 452                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
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): 0.062         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.006         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4362 ; 0.029 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5956 ; 2.540 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   565 ; 5.806 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;28.186 ;22.135       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   680 ;13.230 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;18.593 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   684 ; 0.176 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3340 ; 0.015 ; 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):  2718 ; 1.466 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4403 ; 2.455 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1644 ; 3.522 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1545 ; 5.264 ; 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  : NULL                                       
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 3W04 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 RCSB095717.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAY-10                          
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               : 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                         : MIRROS                             
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   : 91864                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05300                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.61700                            
REMARK 200   FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1WOM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG6000, 5% MPD, 0.1M NA-HEPES, PH    
REMARK 280  7.5, VAPOR DIFFUSION, SITTING 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       23.99400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.61550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.09550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.61550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.99400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.09550            
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     ARG B   317                                                      
REMARK 465     TYR B   318                                                      
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     PRO B  54    CG   CD                                             
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 A   652     O    HOH A   680              2.11            
REMARK 500   O    HOH A   557     O    HOH A   684              2.15            
REMARK 500   O    HOH A   504     O    HOH A   698              2.16            
REMARK 500   NH2  ARG B   267     O1   EDO B   406              2.16            
REMARK 500   OE2  GLU A   224     O    HOH A   629              2.16            
REMARK 500   O    HOH A   652     O    HOH A   701              2.17            
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    TYR A 278   CZ    TYR A 278   CE2     0.079                       
REMARK 500    VAL B 218   CB    VAL B 218   CG1    -0.148                       
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    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP A 115   CB  -  CG  -  OD2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ARG A 118   CG  -  CD  -  NE  ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ASP A 123   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A 134   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A 160   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    LEU A 229   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PHE A 230   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    PHE A 230   CB  -  CG  -  CD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 248   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 248   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP B 112   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG B 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 118   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP B 120   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP B 120   CB  -  CG  -  OD2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP B 123   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP B 127   CB  -  CG  -  OD2 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    ASP B 134   CB  -  CG  -  OD2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG B 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR B 182   CD1 -  CE1 -  CZ  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    PHE B 230   CB  -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    PHE B 230   CB  -  CG  -  CD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG B 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP B 248   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B 250   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 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     -127.02     59.89                                   
REMARK 500    ARG A 175      123.72   -171.61                                   
REMARK 500    ASN A 201       83.17   -162.46                                   
REMARK 500    ALA A 303       54.44   -145.12                                   
REMARK 500    ASP B  81     -167.13   -128.78                                   
REMARK 500    SER B 147     -129.97     63.74                                   
REMARK 500    ARG B 175      124.04   -171.20                                   
REMARK 500    ASP B 179       78.91   -153.94                                   
REMARK 500    SER B 180     -113.40     61.22                                   
REMARK 500    ASN B 201       95.53   -160.87                                   
REMARK 500    ALA B 303       51.92   -140.00                                   
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 MPD 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 EPE B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WO5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WO6   RELATED DB: PDB                                   
DBREF  3W04 A   55   318  UNP    Q10QA5   Q10QA5_ORYSJ    55    318             
DBREF  3W04 B   55   318  UNP    Q10QA5   Q10QA5_ORYSJ    55    318             
SEQADV 3W04 GLY A   53  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 3W04 PRO A   54  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 3W04 GLY B   53  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 3W04 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    MPD  A 401       8                                                       
HET    EDO  A 402       4                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EPE  B 401      15                                                       
HET    MPD  B 402       8                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    EDO  B 405       4                                                       
HET    EDO  B 406       4                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     EPE HEPES                                                            
FORMUL   3  MPD    2(C6 H14 O2)                                                 
FORMUL   4  EDO    7(C2 H6 O2)                                                  
FORMUL   7  EPE    C8 H18 N2 O4 S                                               
FORMUL  13  HOH   *452(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  ASN A  231  1                                  14    
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 ALA A  273  LEU A  283  1                                  11    
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 LYS B   55  LEU B   60  1                                   6    
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  ALA B  316  1                                  14    
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  VAL A  99           
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  GLU A 290   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  SER B  75           
SHEET    5   B 7 PHE B 164  ILE B 170  1  O  VAL B 168   N  GLY B 145           
SHEET    6   B 7 CYS B 260  GLN B 264  1  O  VAL B 261   N  LEU B 169           
SHEET    7   B 7 THR B 287  PHE B 291  1  O  GLU B 290   N  GLN B 264           
SITE     1 AC1  5 TYR A 209  SER A 270  HOH A 652  HOH A 680                    
SITE     2 AC1  5 HOH A 701                                                     
SITE     1 AC2  4 TYR A 182  HIS A 183  SER A 274  VAL A 275                    
SITE     1 AC3  8 MET A 198  GLY A 199  ASN A 201  TYR A 202                    
SITE     2 AC3  8 PRO A 234  HOH A 512  PRO B  90  ARG B 312                    
SITE     1 AC4  4 ALA A 303  PRO A 304  SER A 305  LEU A 306                    
SITE     1 AC5 13 PHE A 230  ALA B 216  THR B 294  GLU B 295                    
SITE     2 AC5 13 SER B 302  ALA B 303  PRO B 304  SER B 305                    
SITE     3 AC5 13 LEU B 306  HOH B 646  HOH B 667  HOH B 703                    
SITE     4 AC5 13 HOH B 712                                                     
SITE     1 AC6  4 TYR B 209  SER B 270  HOH B 629  HOH B 658                    
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 718                                          
SITE     1 AC8  4 ASP B 120  HIS B 239  GLN B 242  THR B 243                    
SITE     1 AC9  5 GLN A 309  ARG A 312  ASP B 112  ARG B 233                    
SITE     2 AC9  5 HOH B 523                                                     
SITE     1 BC1  7 GLY B 185  ARG B 267  ASP B 268  VAL B 269                    
SITE     2 BC1  7 VAL B 271  PRO B 272  LYS B 280                               
CRYST1   47.988   88.191  121.231  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      0.020839  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011339  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008249        0.00000                         
TER    2097      TYR A 318                                                      
TER    4205      ALA B 316                                                      
MASTER      418    0   10   30   14    0   18    6 4584    2   59   42          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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