Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6ap8-pdb

Name Class
6ap8-pdb
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                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer