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Database: PDB
Entry: 4Q5Y
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Original site: 4Q5Y 
HEADER    TRANSCRIPTION                           18-APR-14   4Q5Y              
TITLE     CRYSTAL STRUCTURE OF EXTENDED-TUDOR 10-11 OF DROSOPHILA MELANOGASTER  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATERNAL PROTEIN TUDOR;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTENDED-TUDOR 10-11, UNP RESIDUES 2164-2515;              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: CG9450, TUD, TUDOR;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-SMT3                                
KEYWDS    TUDOR DOMAIN, RECOGNIZE SDMA OF AUBERGINE, SDMA OF AUBERGINE,         
KEYWDS   2 NUCLEUS, TRANSCRIPTION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LIU,R.REN,W.WANG,M.WANG,N.YANG,Y.DONG,W.GONG,R.LEHMANN,R.M.XU       
REVDAT   3   08-NOV-23 4Q5Y    1       SEQADV                                   
REVDAT   2   17-SEP-14 4Q5Y    1       JRNL                                     
REVDAT   1   21-MAY-14 4Q5Y    0                                                
JRNL        AUTH   R.REN,H.LIU,W.WANG,M.WANG,N.YANG,Y.H.DONG,W.GONG,R.LEHMANN,  
JRNL        AUTH 2 R.M.XU                                                       
JRNL        TITL   STRUCTURE AND DOMAIN ORGANIZATION OF DROSOPHILA TUDOR        
JRNL        REF    CELL RES.                     V.  24  1146 2014              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   24810300                                                     
JRNL        DOI    10.1038/CR.2014.63                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 12930                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 676                             
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 2673                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 56                                      
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Q5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085645.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99985                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13606                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 3NTK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TACSIMATE, PH 7.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       35.62350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.87350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.72050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.87350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.62350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.72050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.62350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.72050            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       75.87350            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.72050            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.62350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.87350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       62.72050            
REMARK 350   BIOMT3   2  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     LEU A  2199                                                      
REMARK 465     LYS A  2200                                                      
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     SER A2161    OG                                                  
REMARK 470     GLU A2162    CG   CD   OE1  OE2                                  
REMARK 470     PHE A2163    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ASN A2173    CG   OD1  ND2                                       
REMARK 470     LYS A2176    CG   CD   CE   NZ                                   
REMARK 470     LYS A2183    CG   CD   CE   NZ                                   
REMARK 470     SER A2186    OG                                                  
REMARK 470     ASP A2190    CG   OD1  OD2                                       
REMARK 470     LYS A2194    CG   CD   CE   NZ                                   
REMARK 470     THR A2195    OG1  CG2                                            
REMARK 470     SER A2198    OG                                                  
REMARK 470     LYS A2201    CG   CD   CE   NZ                                   
REMARK 470     GLU A2202    CG   CD   OE1  OE2                                  
REMARK 470     LYS A2203    CG   CD   CE   NZ                                   
REMARK 470     LEU A2204    CG   CD1  CD2                                       
REMARK 470     LYS A2206    CG   CD   CE   NZ                                   
REMARK 470     ASP A2209    CG   OD1  OD2                                       
REMARK 470     GLN A2221    CG   CD   OE1  NE2                                  
REMARK 470     CYS A2225    SG                                                  
REMARK 470     TYR A2226    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A2232    CG   CD   CE   NZ                                   
REMARK 470     VAL A2234    CG1  CG2                                            
REMARK 470     LEU A2252    CG   CD1  CD2                                       
REMARK 470     GLN A2259    CG   CD   OE1  NE2                                  
REMARK 470     LEU A2260    CG   CD1  CD2                                       
REMARK 470     GLN A2262    CG   CD   OE1  NE2                                  
REMARK 470     GLU A2265    CG   CD   OE1  OE2                                  
REMARK 470     GLU A2286    CG   CD   OE1  OE2                                  
REMARK 470     LYS A2287    CG   CD   CE   NZ                                   
REMARK 470     GLU A2312    CG   CD   OE1  OE2                                  
REMARK 470     GLU A2314    CG   CD   OE1  OE2                                  
REMARK 470     THR A2315    OG1  CG2                                            
REMARK 470     LYS A2316    CG   CD   CE   NZ                                   
REMARK 470     GLU A2345    CG   CD   OE1  OE2                                  
REMARK 470     LYS A2394    CG   CD   CE   NZ                                   
REMARK 470     LYS A2465    CG   CD   CE   NZ                                   
REMARK 470     ASP A2467    CG   OD1  OD2                                       
REMARK 470     LYS A2505    CG   CD   CE   NZ                                   
REMARK 470     GLU A2513    CG   CD   OE1  OE2                                  
REMARK 470     CYS A2514    SG                                                  
REMARK 470     GLN A2515    CG   CD   OE1  NE2                                  
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    PHE A  2300     N    GLU A  2302              2.14            
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 A2177      114.92   -165.50                                   
REMARK 500    THR A2195       27.90    -64.57                                   
REMARK 500    LEU A2204     -155.45    169.85                                   
REMARK 500    LYS A2205     -167.96    166.74                                   
REMARK 500    ILE A2208       72.96    -65.43                                   
REMARK 500    PRO A2210      121.31    -19.55                                   
REMARK 500    ASN A2213       -7.41     71.75                                   
REMARK 500    SER A2230      118.68   -174.80                                   
REMARK 500    TYR A2248      -42.99   -141.19                                   
REMARK 500    VAL A2257     -166.16   -107.30                                   
REMARK 500    TRP A2258     -152.56   -156.12                                   
REMARK 500    GLN A2262       56.03    -58.03                                   
REMARK 500    GLU A2263      -56.52   -140.13                                   
REMARK 500    GLU A2265      -29.47    -39.14                                   
REMARK 500    PRO A2280      100.68    -54.82                                   
REMARK 500    GLN A2298       -3.64    -57.15                                   
REMARK 500    HIS A2299      -84.89   -129.81                                   
REMARK 500    PHE A2300     -149.59     68.93                                   
REMARK 500    PRO A2310      170.66    -53.80                                   
REMARK 500    VAL A2340      122.10    -25.12                                   
REMARK 500    GLN A2341     -160.78    -67.75                                   
REMARK 500    GLN A2355      108.77   -166.68                                   
REMARK 500    ASP A2357       29.01   -143.76                                   
REMARK 500    SER A2361      106.51   -169.23                                   
REMARK 500    ASP A2378      -72.15    -72.10                                   
REMARK 500    ASP A2392       71.53    -60.93                                   
REMARK 500    LEU A2393       62.64    -69.93                                   
REMARK 500    CYS A2399      177.22    168.47                                   
REMARK 500    PRO A2404      -78.02    -47.78                                   
REMARK 500    ASP A2420      -40.20    116.87                                   
REMARK 500    LYS A2465        2.83    -61.44                                   
REMARK 500    ALA A2469      -72.87    -60.45                                   
REMARK 500    ARG A2478       50.24   -116.38                                   
REMARK 500    SER A2504       -4.73     65.75                                   
REMARK 500    GLU A2513       34.64    145.82                                   
REMARK 500    CYS A2514       70.73     76.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Q5W   RELATED DB: PDB                                   
DBREF  4Q5Y A 2164  2515  UNP    P25823   TUD_DROME     2164   2515             
SEQADV 4Q5Y SER A 2161  UNP  P25823              EXPRESSION TAG                 
SEQADV 4Q5Y GLU A 2162  UNP  P25823              EXPRESSION TAG                 
SEQADV 4Q5Y PHE A 2163  UNP  P25823              EXPRESSION TAG                 
SEQRES   1 A  355  SER GLU PHE ASN SER GLU CYS ILE ILE SER TYR GLY ASN          
SEQRES   2 A  355  SER PRO LYS SER PHE TYR VAL GLN MET LYS HIS ASN SER          
SEQRES   3 A  355  ALA ASP LEU ASP LEU ILE VAL LYS THR LEU GLN SER LEU          
SEQRES   4 A  355  LYS LYS GLU LYS LEU LYS LYS LEU ILE ASP PRO THR THR          
SEQRES   5 A  355  ASN SER ASN GLY VAL CYS TYR SER GLN GLU ASP ALA CYS          
SEQRES   6 A  355  TYR TYR ARG CYS SER ILE LYS SER VAL LEU ASP PRO SER          
SEQRES   7 A  355  GLN GLY PHE GLU VAL PHE LEU LEU ASP TYR GLY ASN THR          
SEQRES   8 A  355  LEU VAL VAL PRO GLU VAL TRP GLN LEU PRO GLN GLU ILE          
SEQRES   9 A  355  GLU PRO ILE PRO SER LEU ALA LEU HIS CYS GLN LEU SER          
SEQRES  10 A  355  LYS ILE PRO MET ASP VAL SER ASP GLU LYS LEU GLU GLU          
SEQRES  11 A  355  ALA PHE ALA ALA LEU LEU GLU GLN HIS PHE GLY GLU LEU          
SEQRES  12 A  355  TYR GLU ILE THR THR GLN PRO ASN GLU ASP GLU THR LYS          
SEQRES  13 A  355  PRO LEU ILE ALA GLU LEU ARG ILE ASN TYR LYS ASP PHE          
SEQRES  14 A  355  VAL GLN GLU LEU VAL SER THR VAL THR GLY VAL GLN LYS          
SEQRES  15 A  355  PRO LEU GLU ALA GLU LEU HIS ASN CYS VAL VAL VAL GLN          
SEQRES  16 A  355  PHE ASP GLY PRO MET SER PHE TYR VAL GLN MET GLU SER          
SEQRES  17 A  355  ASP VAL PRO ALA LEU GLU GLN MET THR ASP LYS LEU LEU          
SEQRES  18 A  355  ASP ALA GLU GLN ASP LEU PRO ALA PHE SER ASP LEU LYS          
SEQRES  19 A  355  GLU GLY ALA LEU CYS VAL ALA GLN PHE PRO GLU ASP GLU          
SEQRES  20 A  355  VAL PHE TYR ARG ALA GLN ILE ARG LYS VAL LEU ASP ASP          
SEQRES  21 A  355  GLY LYS CYS GLU VAL HIS PHE ILE ASP PHE GLY ASN ASN          
SEQRES  22 A  355  ALA VAL THR GLN GLN PHE ARG GLN LEU PRO GLU GLU LEU          
SEQRES  23 A  355  ALA LYS PRO ALA ARG TYR SER ARG HIS CYS GLU LEU ASP          
SEQRES  24 A  355  ALA SER THR ILE SER LYS CYS ASP ALA ALA LEU LEU GLN          
SEQRES  25 A  355  SER PHE ILE ASP THR ARG PHE SER GLU THR PHE GLN VAL          
SEQRES  26 A  355  GLU ILE LEU ALA THR LYS GLY THR GLY THR HIS VAL VAL          
SEQRES  27 A  355  ARG LEU PHE TYR GLN SER LYS ASN ILE SER GLU LYS LEU          
SEQRES  28 A  355  GLN GLU CYS GLN                                              
FORMUL   2  HOH   *56(H2 O)                                                     
HELIX    1   1 ASN A 2185  THR A 2195  1                                  11    
HELIX    2   2 SER A 2284  GLN A 2298  1                                  15    
HELIX    3   3 PHE A 2329  THR A 2338  1                                  10    
HELIX    4   4 PRO A 2343  ALA A 2346  5                                   4    
HELIX    5   5 ASP A 2369  GLN A 2385  1                                  17    
HELIX    6   6 PRO A 2443  ALA A 2447  5                                   5    
HELIX    7   7 ASP A 2459  CYS A 2466  1                                   8    
HELIX    8   8 ASP A 2467  ARG A 2478  1                                  12    
HELIX    9   9 ILE A 2507  GLN A 2512  1                                   6    
SHEET    1   A 7 LYS A2327  ASP A2328  0                                        
SHEET    2   A 7 LEU A2318  ILE A2324 -1  N  ILE A2324   O  LYS A2327           
SHEET    3   A 7 TYR A2304  GLN A2309 -1  N  GLU A2305   O  ARG A2323           
SHEET    4   A 7 SER A2165  SER A2174 -1  N  CYS A2167   O  TYR A2304           
SHEET    5   A 7 SER A2177  MET A2182 -1  O  TYR A2179   N  TYR A2171           
SHEET    6   A 7 LEU A2272  LEU A2276 -1  O  CYS A2274   N  PHE A2178           
SHEET    7   A 7 LEU A2318  ILE A2324  1  O  ALA A2320   N  GLN A2275           
SHEET    1   B 2 VAL A2217  SER A2220  0                                        
SHEET    2   B 2 CYS A2225  ARG A2228 -1  O  CYS A2225   N  SER A2220           
SHEET    1   C 3 ILE A2231  VAL A2234  0                                        
SHEET    2   C 3 PHE A2241  PHE A2244 -1  O  GLU A2242   N  LYS A2232           
SHEET    3   C 3 THR A2251  VAL A2254 -1  O  LEU A2252   N  VAL A2243           
SHEET    1   D 7 LYS A2505  ASN A2506  0                                        
SHEET    2   D 7 HIS A2496  TYR A2502 -1  N  TYR A2502   O  LYS A2505           
SHEET    3   D 7 THR A2482  THR A2490 -1  N  ALA A2489   O  VAL A2497           
SHEET    4   D 7 LEU A2348  PHE A2356 -1  N  CYS A2351   O  PHE A2483           
SHEET    5   D 7 PHE A2362  MET A2366 -1  O  TYR A2363   N  GLN A2355           
SHEET    6   D 7 ARG A2454  LEU A2458 -1  O  ARG A2454   N  VAL A2364           
SHEET    7   D 7 HIS A2496  TYR A2502  1  O  HIS A2496   N  HIS A2455           
SHEET    1   E 4 LEU A2398  PHE A2403  0                                        
SHEET    2   E 4 VAL A2408  VAL A2417 -1  O  ALA A2412   N  CYS A2399           
SHEET    3   E 4 CYS A2423  PHE A2427 -1  O  GLU A2424   N  ARG A2415           
SHEET    4   E 4 ASN A2433  THR A2436 -1  O  ALA A2434   N  VAL A2425           
SSBOND   1 CYS A 2218    CYS A 2229                          1555   1555  2.05  
CRYST1   71.247  125.441  151.747  90.00  90.00  90.00 I 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      0.014036  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007972  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006590        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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