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Database: PDB
Entry: 5VBC
LinkDB: 5VBC
Original site: 5VBC 
HEADER    TRANSFERASE/DNA BINDING PROTEIN         29-MAR-17   5VBC              
TITLE     CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HISTONE-LYSINE N-METHYLTRANSFERASE ATXR5;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN RESIDUES 146-374;                               
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE H3.1 PEPTIDE;                                      
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 24-37;                                            
COMPND  11 SYNONYM: HISTONE H3.2;                                               
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RICINUS COMMUNIS;                               
SOURCE   3 ORGANISM_COMMON: CASTOR BEAN;                                        
SOURCE   4 ORGANISM_TAXID: 3988;                                                
SOURCE   5 GENE: ATXR5, RCOM_1460410;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  11 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE  12 ORGANISM_TAXID: 3702                                                 
KEYWDS    NUCLEOSOME, METHYLATION, TRANSFERASE-DNA BINDING PROTEIN COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-F.COUTURE,E.BERGAMIN                                               
REVDAT   2   20-SEP-17 5VBC    1       JRNL                                     
REVDAT   1   19-APR-17 5VBC    0                                                
JRNL        AUTH   E.BERGAMIN,S.SARVAN,J.MALETTE,M.S.ERAM,S.YEUNG,V.MONGEON,    
JRNL        AUTH 2 M.JOSHI,J.S.BRUNZELLE,S.D.MICHAELS,A.BLAIS,M.VEDADI,         
JRNL        AUTH 3 J.F.COUTURE                                                  
JRNL        TITL   MOLECULAR BASIS FOR THE METHYLATION SPECIFICITY OF ATXR5 FOR 
JRNL        TITL 2 HISTONE H3.                                                  
JRNL        REF    NUCLEIC ACIDS RES.            V.  45  6375 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28383693                                                     
JRNL        DOI    10.1093/NAR/GKX224                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155)                                 
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.490                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 29390                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1493                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 26.4063 -  4.6626    0.99     2605   154  0.1950 0.2175        
REMARK   3     2  4.6626 -  3.7041    1.00     2583   127  0.1583 0.1816        
REMARK   3     3  3.7041 -  3.2368    0.99     2571   142  0.1899 0.2099        
REMARK   3     4  3.2368 -  2.9413    0.99     2579   120  0.2120 0.2568        
REMARK   3     5  2.9413 -  2.7307    0.99     2533   142  0.2121 0.2687        
REMARK   3     6  2.7307 -  2.5698    0.98     2538   120  0.2221 0.3006        
REMARK   3     7  2.5698 -  2.4412    0.98     2538   129  0.2188 0.2412        
REMARK   3     8  2.4412 -  2.3350    0.98     2525   139  0.2163 0.3313        
REMARK   3     9  2.3350 -  2.2452    0.97     2480   131  0.2195 0.2802        
REMARK   3    10  2.2452 -  2.1678    0.97     2488   148  0.2286 0.2825        
REMARK   3    11  2.1678 -  2.1000    0.96     2457   141  0.2378 0.3147        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3675                                  
REMARK   3   ANGLE     :  0.997           4958                                  
REMARK   3   CHIRALITY :  0.056            544                                  
REMARK   3   PLANARITY :  0.005            651                                  
REMARK   3   DIHEDRAL  : 15.208           2263                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VBC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227166.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29410                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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                                                
REMARK 200 STARTING MODEL: 4O30                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% POLYPROPYLENE GLYCOL 400, 100MM NA   
REMARK 280  -HEPES PH 6.0 AND 5% DMSO, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.58500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.65500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.58500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.65500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     ARG A   146                                                      
REMARK 465     ARG A   147                                                      
REMARK 465     ARG A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     GLY A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     LEU A   152                                                      
REMARK 465     VAL A   153                                                      
REMARK 465     TYR A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     LYS A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     ARG B   146                                                      
REMARK 465     ARG B   147                                                      
REMARK 465     ARG B   148                                                      
REMARK 465     SER B   149                                                      
REMARK 465     GLY B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     LEU B   152                                                      
REMARK 465     VAL B   153                                                      
REMARK 465     TYR B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     ARG B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     ARG B   159                                                      
REMARK 465     LYS D    23                                                      
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     ARG A 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 186    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 190    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     HIS A 281    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 322    CG   CD1  CD2                                       
REMARK 470     GLU B 186    CG   CD   OE1  OE2                                  
REMARK 470     SER B 199    OG                                                  
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 281    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 283    CG   OD1  OD2                                       
REMARK 470     LYS B 294    CG   CD   CE   NZ                                   
REMARK 470     LYS B 298    CG   CD   CE   NZ                                   
REMARK 470     LEU B 322    CG   CD1  CD2                                       
REMARK 470     ASP B 323    CG   OD1  OD2                                       
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   OD1  ASP A   223     O    HOH A   501              1.84            
REMARK 500   NZ   LYS B   306     O    HOH B   501              2.11            
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   OE1  GLN B   259     NZ   LYS C    23     2455     1.82            
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    MET A 201     -148.15   -120.41                                   
REMARK 500    PRO A 304       44.17    -89.38                                   
REMARK 500    ASN A 362       58.57   -110.53                                   
REMARK 500    TYR A 364      -61.84   -152.32                                   
REMARK 500    MET B 201     -100.21   -105.78                                   
REMARK 500    SER B 286       36.39   -143.03                                   
REMARK 500    PRO B 304       39.05    -90.78                                   
REMARK 500    ASN B 362       58.11   -112.75                                   
REMARK 500    TYR B 364      -67.36   -143.81                                   
REMARK 500    ALA C  24       99.74     73.68                                   
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 643        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A 644        DISTANCE =  6.99 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VA6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VAB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VAH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VAC   RELATED DB: PDB                                   
DBREF  5VBC A  146   374  UNP    B9RU15   ATXR5_RICCO    146    374             
DBREF  5VBC B  146   374  UNP    B9RU15   ATXR5_RICCO    146    374             
DBREF  5VBC C   23    36  UNP    P59226   H32_ARATH       24     37             
DBREF  5VBC D   23    36  UNP    P59226   H32_ARATH       24     37             
SEQRES   1 A  229  ARG ARG ARG SER GLY SER LEU VAL TYR GLN LYS ARG ARG          
SEQRES   2 A  229  ARG ARG LEU LEU PRO PHE VAL SER SER GLU ASP PRO ALA          
SEQRES   3 A  229  GLN ARG LEU LYS GLN MET GLY THR LEU ALA SER ALA LEU          
SEQRES   4 A  229  THR GLU LEU GLN MET GLU PHE SER ASP ASP LEU THR TYR          
SEQRES   5 A  229  SER SER GLY MET ALA PRO ARG SER ALA ASN GLN ALA ARG          
SEQRES   6 A  229  PHE GLU GLU GLY GLY MET GLN VAL LEU THR LYS GLU ASP          
SEQRES   7 A  229  ILE GLU THR LEU GLU GLN CYS ARG ALA MET CYS LYS ARG          
SEQRES   8 A  229  GLY ASP CYS PRO PRO LEU LEU VAL VAL PHE ASP SER ARG          
SEQRES   9 A  229  GLU GLY PHE THR VAL GLU ALA ASP GLY GLN ILE LYS ASP          
SEQRES  10 A  229  MET THR PHE ILE ALA GLU TYR THR GLY ASP VAL ASP TYR          
SEQRES  11 A  229  ILE ARG ASN ARG GLU HIS ASP ASP CYS ASP SER MET MET          
SEQRES  12 A  229  THR LEU LEU LEU ALA LYS ASP PRO SER LYS SER LEU VAL          
SEQRES  13 A  229  ILE CYS PRO ASP LYS ARG GLY ASN ILE ALA ARG PHE ILE          
SEQRES  14 A  229  SER GLY ILE ASN ASN HIS THR LEU ASP GLY LYS LYS LYS          
SEQRES  15 A  229  GLN ASN CYS LYS CYS VAL ARG TYR SER VAL ASN GLY GLU          
SEQRES  16 A  229  CYS ARG VAL PHE LEU VAL ALA THR ARG ASP ILE ALA LYS          
SEQRES  17 A  229  GLY GLU ARG LEU TYR TYR ASP TYR ASN GLY TYR GLU HIS          
SEQRES  18 A  229  GLU TYR PRO THR GLN HIS PHE VAL                              
SEQRES   1 B  229  ARG ARG ARG SER GLY SER LEU VAL TYR GLN LYS ARG ARG          
SEQRES   2 B  229  ARG ARG LEU LEU PRO PHE VAL SER SER GLU ASP PRO ALA          
SEQRES   3 B  229  GLN ARG LEU LYS GLN MET GLY THR LEU ALA SER ALA LEU          
SEQRES   4 B  229  THR GLU LEU GLN MET GLU PHE SER ASP ASP LEU THR TYR          
SEQRES   5 B  229  SER SER GLY MET ALA PRO ARG SER ALA ASN GLN ALA ARG          
SEQRES   6 B  229  PHE GLU GLU GLY GLY MET GLN VAL LEU THR LYS GLU ASP          
SEQRES   7 B  229  ILE GLU THR LEU GLU GLN CYS ARG ALA MET CYS LYS ARG          
SEQRES   8 B  229  GLY ASP CYS PRO PRO LEU LEU VAL VAL PHE ASP SER ARG          
SEQRES   9 B  229  GLU GLY PHE THR VAL GLU ALA ASP GLY GLN ILE LYS ASP          
SEQRES  10 B  229  MET THR PHE ILE ALA GLU TYR THR GLY ASP VAL ASP TYR          
SEQRES  11 B  229  ILE ARG ASN ARG GLU HIS ASP ASP CYS ASP SER MET MET          
SEQRES  12 B  229  THR LEU LEU LEU ALA LYS ASP PRO SER LYS SER LEU VAL          
SEQRES  13 B  229  ILE CYS PRO ASP LYS ARG GLY ASN ILE ALA ARG PHE ILE          
SEQRES  14 B  229  SER GLY ILE ASN ASN HIS THR LEU ASP GLY LYS LYS LYS          
SEQRES  15 B  229  GLN ASN CYS LYS CYS VAL ARG TYR SER VAL ASN GLY GLU          
SEQRES  16 B  229  CYS ARG VAL PHE LEU VAL ALA THR ARG ASP ILE ALA LYS          
SEQRES  17 B  229  GLY GLU ARG LEU TYR TYR ASP TYR ASN GLY TYR GLU HIS          
SEQRES  18 B  229  GLU TYR PRO THR GLN HIS PHE VAL                              
SEQRES   1 C   14  LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL          
SEQRES   2 C   14  LYS                                                          
SEQRES   1 D   14  LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL          
SEQRES   2 D   14  LYS                                                          
HET    SAH  A 401      26                                                       
HET    DMS  A 402       4                                                       
HET    SAH  B 401      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   6  DMS    C2 H6 O S                                                    
FORMUL   8  HOH   *287(H2 O)                                                    
HELIX    1 AA1 ASP A  169  LEU A  187  1                                  19    
HELIX    2 AA2 PRO A  203  ASN A  207  5                                   5    
HELIX    3 AA3 GLN A  208  GLU A  212  5                                   5    
HELIX    4 AA4 THR A  220  GLY A  237  1                                  18    
HELIX    5 AA5 ARG A  277  GLU A  280  5                                   4    
HELIX    6 AA6 ASP A  295  LYS A  298  5                                   4    
HELIX    7 AA7 ASN A  309  ILE A  314  5                                   6    
HELIX    8 AA8 ASP A  323  GLN A  328  5                                   6    
HELIX    9 AA9 ASP B  169  LEU B  187  1                                  19    
HELIX   10 AB1 PRO B  203  ASN B  207  5                                   5    
HELIX   11 AB2 GLN B  208  GLU B  212  5                                   5    
HELIX   12 AB3 THR B  220  GLY B  237  1                                  18    
HELIX   13 AB4 ARG B  277  GLU B  280  5                                   4    
HELIX   14 AB5 ASP B  295  LYS B  298  5                                   4    
HELIX   15 AB6 ASN B  309  ILE B  314  5                                   6    
HELIX   16 AB7 ASP B  323  GLN B  328  5                                   6    
SHEET    1 AA1 2 GLU A 190  PHE A 191  0                                        
SHEET    2 AA1 2 ARG A 307  GLY A 308  1  O  GLY A 308   N  GLU A 190           
SHEET    1 AA2 5 LEU A 195  THR A 196  0                                        
SHEET    2 AA2 5 GLY A 271  TYR A 275  1  O  VAL A 273   N  THR A 196           
SHEET    3 AA2 5 LEU A 300  CYS A 303 -1  O  CYS A 303   N  ASP A 272           
SHEET    4 AA2 5 MET A 287  LEU A 291 -1  N  MET A 288   O  ILE A 302           
SHEET    5 AA2 5 ARG C  26  LYS C  27  1  O  LYS C  27   N  MET A 287           
SHEET    1 AA3 2 LEU A 242  ASP A 247  0                                        
SHEET    2 AA3 2 GLY A 251  ALA A 256 -1  O  GLY A 251   N  ASP A 247           
SHEET    1 AA4 3 PHE A 265  GLU A 268  0                                        
SHEET    2 AA4 3 GLU A 340  ALA A 347 -1  O  LEU A 345   N  ALA A 267           
SHEET    3 AA4 3 CYS A 330  VAL A 337 -1  N  VAL A 333   O  PHE A 344           
SHEET    1 AA5 2 SER A 315  GLY A 316  0                                        
SHEET    2 AA5 2 TYR A 358  TYR A 359  1  O  TYR A 359   N  SER A 315           
SHEET    1 AA6 2 GLU B 190  PHE B 191  0                                        
SHEET    2 AA6 2 ARG B 307  GLY B 308  1  O  GLY B 308   N  GLU B 190           
SHEET    1 AA7 2 LEU B 242  ASP B 247  0                                        
SHEET    2 AA7 2 GLY B 251  ALA B 256 -1  O  THR B 253   N  VAL B 245           
SHEET    1 AA8 3 PHE B 265  GLU B 268  0                                        
SHEET    2 AA8 3 GLU B 340  ALA B 347 -1  O  LEU B 345   N  ILE B 266           
SHEET    3 AA8 3 CYS B 330  VAL B 337 -1  N  VAL B 337   O  GLU B 340           
SHEET    1 AA9 4 ASP B 272  TYR B 275  0                                        
SHEET    2 AA9 4 LEU B 300  CYS B 303 -1  O  CYS B 303   N  ASP B 272           
SHEET    3 AA9 4 MET B 287  LEU B 291 -1  N  MET B 288   O  ILE B 302           
SHEET    4 AA9 4 ARG D  26  LYS D  27  1  O  LYS D  27   N  MET B 287           
SHEET    1 AB1 2 SER B 315  GLY B 316  0                                        
SHEET    2 AB1 2 TYR B 358  TYR B 359  1  O  TYR B 359   N  SER B 315           
SITE     1 AC1 18 ARG A 249  GLU A 250  PHE A 252  ASP A 285                    
SITE     2 AC1 18 SER A 286  ARG A 312  SER A 315  GLY A 316                    
SITE     3 AC1 18 TYR A 361  TYR A 368  PHE A 373  VAL A 374                    
SITE     4 AC1 18 HOH A 513  HOH A 539  HOH A 552  HOH A 559                    
SITE     5 AC1 18 HOH A 565  LYS C  27                                          
SITE     1 AC2  1 MET A 177                                                     
SITE     1 AC3 11 GLU B 250  PHE B 252  ARG B 312  SER B 315                    
SITE     2 AC3 11 GLY B 316  TYR B 361  TYR B 368  PHE B 373                    
SITE     3 AC3 11 VAL B 374  HOH B 569  LYS D  27                               
CRYST1  101.170   87.310   74.510  90.00 127.78  90.00 C 1 2 1       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      0.009884  0.000000  0.007662        0.00000                         
SCALE2      0.000000  0.011453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016981        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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