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Database: PDB
Entry: 5VA6
LinkDB: 5VA6
Original site: 5VA6 
HEADER    TRANSFERASE/DNA BINDING PROTEIN         24-MAR-17   5VA6              
TITLE     CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-         
TITLE    2 METHYLATED ON R26                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HISTONE-LYSINE N-METHYLTRANSFERASE ATXR5;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: 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;                                              
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 20-37;                                            
COMPND  11 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE 
COMPND  12 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE     
COMPND  13 H3/L;                                                                
COMPND  14 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: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    NUCLEOSOME, TRANSFERASE-DNA BINDING PROTEIN COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.BERGAMIN,S.SARVAN,J.MALETTE,M.ERAM,S.YEUNG,V.MONGEON,M.JOSHI,       
AUTHOR   2 J.S.BRUNZELLE,S.D.MICHAELS,A.BLAIS,M.VEDADI,J.-F.COUTURE             
REVDAT   2   20-SEP-17 5VA6    1       JRNL                                     
REVDAT   1   19-APR-17 5VA6    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.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17859                          
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)  : 0.249                          
REMARK   3   R VALUE            (WORKING SET)  : 0.246                          
REMARK   3   FREE R VALUE                      : 0.297                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.160                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 922                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.40                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.60                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.83                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2841                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.3598                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2709                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3558                   
REMARK   3   BIN FREE R VALUE                        : 0.4365                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.65                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 132                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3502                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 159                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.41560                                              
REMARK   3    B22 (A**2) : -1.52560                                             
REMARK   3    B33 (A**2) : -1.89000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 10.93330                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.422               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.685               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.331               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.678               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.335               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.866                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3617   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4888   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1260   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 89     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 560    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3617   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 487    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4114   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.23                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.07                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.64                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   24.8428  -17.6453    2.5359           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0882 T22:   -0.1375                                    
REMARK   3     T33:   -0.1457 T12:   -0.0098                                    
REMARK   3     T13:    0.0819 T23:    0.0196                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4817 L22:    0.8744                                    
REMARK   3     L33:    1.0197 L12:    0.0524                                    
REMARK   3     L13:    0.4537 L23:    0.0225                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0847 S12:   -0.1089 S13:   -0.0867                     
REMARK   3     S21:    0.0536 S22:   -0.0465 S23:   -0.0041                     
REMARK   3     S31:    0.0886 S32:    0.0168 S33:   -0.0382                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.8267   -2.9229   30.0561           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0498 T22:   -0.1828                                    
REMARK   3     T33:   -0.1643 T12:    0.0150                                    
REMARK   3     T13:    0.0851 T23:   -0.0144                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4065 L22:    1.2190                                    
REMARK   3     L33:    1.8017 L12:    0.3225                                    
REMARK   3     L13:    0.6470 L23:   -0.0734                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0646 S12:    0.0267 S13:    0.0417                     
REMARK   3     S21:    0.1949 S22:   -0.1099 S23:   -0.0157                     
REMARK   3     S31:   -0.0892 S32:    0.0279 S33:    0.0453                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227105.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-14                          
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                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
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   (%): 50.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% POLYPROPYLENE GLYCOL 400, 5% DMSO,   
REMARK 280  0.1 M HEPES-NAOH (PH 6.0), VAPOR DIFFUSION, HANGING 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       50.65500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.40500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.65500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.40500            
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: 2190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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     THR C    23                                                      
REMARK 465     GLN D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     LYS D    37                                                      
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     GLN A 208    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 213    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     GLU A 228    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 229    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 259    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     LEU A 322    CG   CD1  CD2                                       
REMARK 470     GLN A 371    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 160    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 199    OG                                                  
REMARK 470     GLU B 213    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 222    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 225    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 231    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 248    OG                                                  
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 281    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 294    CG   CD   CE   NZ                                   
REMARK 470     SER B 298    OG                                                  
REMARK 470     LEU B 322    CG   CD1  CD2                                       
REMARK 470     ASP B 323    CG   OD1  OD2                                       
REMARK 470     ALA B 324    CB                                                  
REMARK 470     LYS B 325    CG   CD   CE   NZ                                   
REMARK 470     LYS C  24    CG   CD   CE   NZ                                   
REMARK 470     LYS C  37    CG   CD   CE   NZ                                   
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    MET B 201   N   -  CA  -  C   ANGL. DEV. = -20.3 DEGREES          
REMARK 500    ALA C  25   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ALA C  25   N   -  CA  -  C   ANGL. DEV. =  34.1 DEGREES          
REMARK 500    ALA D  25   CB  -  CA  -  C   ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ALA D  25   N   -  CA  -  C   ANGL. DEV. =  25.4 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    MET A 201     -155.29   -127.61                                   
REMARK 500    PRO A 304       49.50    -92.94                                   
REMARK 500    ASN A 309     -157.45   -128.06                                   
REMARK 500    ASN A 362       55.37   -113.72                                   
REMARK 500    TYR A 364      -64.47   -138.00                                   
REMARK 500    MET B 201     -153.22   -126.82                                   
REMARK 500    MET B 263        8.23     83.82                                   
REMARK 500    ILE B 266      -61.78    -90.69                                   
REMARK 500    PRO B 304       42.80    -89.13                                   
REMARK 500    LEU B 322      -19.03    -48.17                                   
REMARK 500    ASP B 323       30.51   -145.54                                   
REMARK 500    ASN B 362       59.05   -110.42                                   
REMARK 500    TYR B 364      -57.93   -136.14                                   
REMARK 500    ALA C  25       64.55     60.14                                   
REMARK 500    ALA D  25       75.37     49.81                                   
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 578        DISTANCE =  7.47 ANGSTROMS                       
REMARK 525    HOH B 572        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH B 573        DISTANCE =  7.37 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 SAH B 401                 
DBREF  5VA6 A  146   374  UNP    B9RU15   ATXR5_RICCO    146    374             
DBREF  5VA6 B  146   374  UNP    B9RU15   ATXR5_RICCO    146    374             
DBREF  5VA6 C   20    37  UNP    P68431   H31_HUMAN       20     37             
DBREF  5VA6 D   20    37  UNP    P68431   H31_HUMAN       20     37             
SEQADV 5VA6 SER A  298  UNP  B9RU15    LYS   298 CONFLICT                       
SEQADV 5VA6 ALA A  324  UNP  B9RU15    GLY   324 CONFLICT                       
SEQADV 5VA6 SER B  298  UNP  B9RU15    LYS   298 CONFLICT                       
SEQADV 5VA6 ALA B  324  UNP  B9RU15    GLY   324 CONFLICT                       
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 SER 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 ALA 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 SER 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 ALA 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   18  GLN LEU ALA THR LYS ALA ALA NMM LYS SER ALA PRO ALA          
SEQRES   2 C   18  THR GLY GLY VAL LYS                                          
SEQRES   1 D   18  GLN LEU ALA THR LYS ALA ALA NMM LYS SER ALA PRO ALA          
SEQRES   2 D   18  THR GLY GLY VAL LYS                                          
MODRES 5VA6 NMM C   27  ARG  MODIFIED RESIDUE                                   
MODRES 5VA6 NMM D   27  ARG  MODIFIED RESIDUE                                   
HET    NMM  C  27      12                                                       
HET    NMM  D  27      12                                                       
HET    SAH  A 401      26                                                       
HET    SAH  B 401      26                                                       
HETNAM     NMM (2S)-2-AMINO-5-[(N-METHYLCARBAMIMIDOYL)AMINO]PENTANOIC           
HETNAM   2 NMM  ACID                                                            
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETSYN     NMM L-NMMA                                                           
FORMUL   3  NMM    2(C7 H16 N4 O2)                                              
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   7  HOH   *159(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  ARG A  279  5                                   3    
HELIX    6 AA6 ASN A  309  ILE A  314  5                                   6    
HELIX    7 AA7 ASP A  323  GLN A  328  5                                   6    
HELIX    8 AA8 ASP B  169  LEU B  187  1                                  19    
HELIX    9 AA9 PRO B  203  ASN B  207  5                                   5    
HELIX   10 AB1 GLN B  208  GLU B  212  5                                   5    
HELIX   11 AB2 THR B  220  GLY B  237  1                                  18    
HELIX   12 AB3 ARG B  277  ARG B  279  5                                   3    
HELIX   13 AB4 ASN B  309  ILE B  314  5                                   6    
HELIX   14 AB5 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 2 LEU A 242  ASP A 247  0                                        
SHEET    2 AA2 2 GLY A 251  ALA A 256 -1  O  GLY A 251   N  ASP A 247           
SHEET    1 AA3 3 PHE A 265  GLU A 268  0                                        
SHEET    2 AA3 3 GLU A 340  ALA A 347 -1  O  LEU A 345   N  ILE A 266           
SHEET    3 AA3 3 CYS A 330  VAL A 337 -1  N  LYS A 331   O  VAL A 346           
SHEET    1 AA4 3 ASP A 272  TYR A 275  0                                        
SHEET    2 AA4 3 LEU A 300  CYS A 303 -1  O  VAL A 301   N  ASP A 274           
SHEET    3 AA4 3 MET A 288  LEU A 291 -1  N  MET A 288   O  ILE A 302           
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  GLY B 251   N  ASP B 247           
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  ALA B 267           
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  VAL B 301   N  ASP B 274           
SHEET    3 AA9 4 MET B 287  LEU B 291 -1  N  MET B 288   O  ILE B 302           
SHEET    4 AA9 4 NMM D  27  LYS D  28  1  O  LYS D  28   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           
LINK         C   ALA C  26                 N   NMM C  27     1555   1555  1.33  
LINK         C   NMM C  27                 N   LYS C  28     1555   1555  1.31  
LINK         C   ALA D  26                 N   NMM D  27     1555   1555  1.33  
LINK         C   NMM D  27                 N   LYS D  28     1555   1555  1.32  
SITE     1 AC1 14 ARG A 249  GLU A 250  GLY A 251  PHE A 252                    
SITE     2 AC1 14 ASP A 285  ARG A 312  PHE A 313  SER A 315                    
SITE     3 AC1 14 GLY A 316  TYR A 361  TYR A 368  PHE A 373                    
SITE     4 AC1 14 VAL A 374  HOH A 529                                          
SITE     1 AC2 13 GLU B 250  PHE B 252  ASP B 285  ARG B 312                    
SITE     2 AC2 13 PHE B 313  SER B 315  GLY B 316  TYR B 361                    
SITE     3 AC2 13 TYR B 368  PHE B 373  VAL B 374  HOH B 511                    
SITE     4 AC2 13 LYS D  28                                                     
CRYST1  101.310   86.810   74.040  90.00 127.83  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      0.009871  0.000000  0.007665        0.00000                         
SCALE2      0.000000  0.011519  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017100        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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