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Database: PDB
Entry: 2QVL
LinkDB: 2QVL
Original site: 2QVL 
HEADER    TRANSFERASE                             08-AUG-07   2QVL              
TITLE     CRYSTAL STRUCTURE OF DIACYLGLYCEROL KINASE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIACYLGLYCEROL KINASE DGKB;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.1.107;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 GENE: SAR1989;                                                       
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: METHIONINE AUXOTROPH B834;                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PAJ015                                    
KEYWDS    ALPHA-BETA DOMAIN 1, BETA SANDWICH DOMAIN 2, NATIVE PROTEIN,          
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.MILLER,A.JERGA,C.O.ROCK,S.W.WHITE                                 
REVDAT   3   24-FEB-09 2QVL    1       VERSN                                    
REVDAT   2   05-AUG-08 2QVL    1       JRNL                                     
REVDAT   1   17-JUN-08 2QVL    0                                                
JRNL        AUTH   D.J.MILLER,A.JERGA,C.O.ROCK,S.W.WHITE                        
JRNL        TITL   ANALYSIS OF THE STAPHYLOCOCCUS AUREUS DGKB                   
JRNL        TITL 2 STRUCTURE REVEALS A COMMON CATALYTIC MECHANISM FOR           
JRNL        TITL 3 THE SOLUBLE DIACYLGLYCEROL KINASES.                          
JRNL        REF    STRUCTURE                     V.  16  1036 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18611377                                                     
JRNL        DOI    10.1016/J.STR.2008.03.019                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14042                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 730                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.45                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 800                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 41                           
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2171                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.389         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.272         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.200         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.462         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2210 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2986 ; 1.335 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   281 ; 6.828 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;41.432 ;25.152       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   383 ;18.402 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;16.672 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   340 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1659 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   922 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1481 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   144 ; 0.172 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.247 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1434 ; 1.111 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2241 ; 1.336 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   845 ; 2.269 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   745 ; 3.440 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2QVL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044110.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 170                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : SI-220                             
REMARK 200  OPTICS                         : MIRRORS                            
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   : 15472                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP: 0.1 M TRIS PH 8.5, 9%              
REMARK 280  PEG2KMME; WELL: 0.1 M TRIS PH 8.5, 18% PEG2KMME, VAPOR              
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       62.10500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.10500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.25100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.10500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.10500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.25100            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.10500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.10500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.25100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.10500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.10500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       24.25100            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       48.50200            
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     MSE A   -21                                                      
REMARK 465     GLY A   -20                                                      
REMARK 465     SER A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     VAL A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     TYR A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     LYS A   152                                                      
REMARK 465     LEU A   153                                                      
REMARK 465     LYS A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     ILE A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     PHE A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     TYR A   162                                                      
REMARK 465     TYR A   163                                                      
REMARK 465     ILE A   164                                                      
REMARK 465     LYS A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     PHE A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     ASP A   309                                                      
REMARK 465     ASP A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ILE A   313                                                      
REMARK 465     GLU A   314                                                      
REMARK 465     GLU A   315                                                      
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     HIS A  -1    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MSE A   0    CG  SE    CE                                        
REMARK 470     GLN A  17    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 207    CG   CD   CE   NZ                                   
REMARK 470     LEU A 208    CG   CD1  CD2                                       
REMARK 470     GLN A 267    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 295    CG   OD1  ND2                                       
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 306    CG   OD1  OD2                                       
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    THR A  12       41.28   -107.44                                   
REMARK 500    ASP A 183     -121.60     56.16                                   
REMARK 500    LEU A 198      -63.89    -99.74                                   
REMARK 500    LEU A 208      148.18   -178.62                                   
REMARK 500    ASP A 306       -8.90    -57.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  208     VAL A  209                  140.40                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QV7   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH ADP                                      
DBREF  2QVL A    1   315  UNP    Q6GFF9   Q6GFF9_STAAR     1    315             
SEQADV 2QVL MSE A  -21  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL GLY A  -20  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL SER A  -19  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL SER A  -18  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -17  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -16  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -15  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -14  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -13  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -12  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A  -11  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL SER A  -10  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL SER A   -9  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL GLY A   -8  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL LEU A   -7  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL VAL A   -6  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL PRO A   -5  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL ARG A   -4  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL GLY A   -3  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL SER A   -2  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL HIS A   -1  UNP  Q6GFF9              EXPRESSION TAG                 
SEQADV 2QVL MSE A    0  UNP  Q6GFF9              EXPRESSION TAG                 
SEQRES   1 A  337  MSE GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 A  337  GLY LEU VAL PRO ARG GLY SER HIS MSE MSE ARG LYS ARG          
SEQRES   3 A  337  ALA ARG ILE ILE TYR ASN PRO THR SER GLY LYS GLU GLN          
SEQRES   4 A  337  PHE LYS ARG GLU LEU PRO ASP ALA LEU ILE LYS LEU GLU          
SEQRES   5 A  337  LYS ALA GLY TYR GLU THR SER ALA TYR ALA THR GLU LYS          
SEQRES   6 A  337  ILE GLY ASP ALA THR LEU GLU ALA GLU ARG ALA MSE HIS          
SEQRES   7 A  337  GLU ASN TYR ASP VAL LEU ILE ALA ALA GLY GLY ASP GLY          
SEQRES   8 A  337  THR LEU ASN GLU VAL VAL ASN GLY ILE ALA GLU LYS PRO          
SEQRES   9 A  337  ASN ARG PRO LYS LEU GLY VAL ILE PRO MSE GLY THR VAL          
SEQRES  10 A  337  ASN ASP PHE GLY ARG ALA LEU HIS ILE PRO ASN ASP ILE          
SEQRES  11 A  337  MSE GLY ALA LEU ASP VAL ILE ILE GLU GLY HIS SER THR          
SEQRES  12 A  337  LYS VAL ASP ILE GLY LYS MSE ASN ASN ARG TYR PHE ILE          
SEQRES  13 A  337  ASN LEU ALA ALA GLY GLY GLN LEU THR GLN VAL SER TYR          
SEQRES  14 A  337  GLU THR PRO SER LYS LEU LYS SER ILE VAL GLY PRO PHE          
SEQRES  15 A  337  ALA TYR TYR ILE LYS GLY PHE GLU MSE LEU PRO GLN MSE          
SEQRES  16 A  337  LYS ALA VAL ASP LEU ARG ILE GLU TYR ASP GLY ASN VAL          
SEQRES  17 A  337  PHE GLN GLY GLU ALA LEU LEU PHE PHE LEU GLY LEU THR          
SEQRES  18 A  337  ASN SER MSE ALA GLY PHE GLU LYS LEU VAL PRO ASP ALA          
SEQRES  19 A  337  LYS LEU ASP ASP GLY TYR PHE THR LEU ILE ILE VAL GLU          
SEQRES  20 A  337  LYS SER ASN LEU ALA GLU LEU GLY HIS ILE MSE THR LEU          
SEQRES  21 A  337  ALA SER ARG GLY GLU HIS THR LYS HIS PRO LYS VAL ILE          
SEQRES  22 A  337  TYR GLU LYS ALA LYS ALA ILE ASN ILE SER SER PHE THR          
SEQRES  23 A  337  ASP LEU GLN LEU ASN VAL ASP GLY GLU TYR GLY GLY LYS          
SEQRES  24 A  337  LEU PRO ALA ASN PHE LEU ASN LEU GLU ARG HIS ILE ASP          
SEQRES  25 A  337  VAL PHE ALA PRO ASN ASP ILE VAL ASN GLU GLU LEU ILE          
SEQRES  26 A  337  ASN ASN ASP HIS VAL ASP ASP ASN LEU ILE GLU GLU              
MODRES 2QVL MSE A    0  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A   92  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  109  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  128  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  169  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  173  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  202  MET  SELENOMETHIONINE                                   
MODRES 2QVL MSE A  236  MET  SELENOMETHIONINE                                   
HET    MSE  A   0       5                                                       
HET    MSE  A   1       8                                                       
HET    MSE  A  55       8                                                       
HET    MSE  A  92       8                                                       
HET    MSE  A 109       8                                                       
HET    MSE  A 128       8                                                       
HET    MSE  A 169       8                                                       
HET    MSE  A 173       8                                                       
HET    MSE  A 202       8                                                       
HET    MSE  A 236       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   2  HOH   *116(H2 O)                                                    
HELIX    1   1 GLN A   17  ALA A   32  1                                  16    
HELIX    2   2 GLY A   45  MSE A   55  1                                  11    
HELIX    3   3 GLY A   67  ALA A   79  1                                  13    
HELIX    4   4 ASN A   96  LEU A  102  1                                   7    
HELIX    5   5 ASP A  107  GLY A  118  1                                  12    
HELIX    6   6 MSE A  169  MSE A  173  5                                   5    
HELIX    7   7 ASN A  228  SER A  240  1                                  13    
HELIX    8   8 ARG A  241  GLY A  242  5                                   2    
HELIX    9   9 GLU A  243  HIS A  247  5                                   5    
SHEET    1   A 4 TYR A  34  ALA A  40  0                                        
SHEET    2   A 4 LYS A   3  TYR A   9  1  N  LYS A   3   O  GLU A  35           
SHEET    3   A 4 VAL A  61  GLY A  66  1  O  ILE A  63   N  ILE A   8           
SHEET    4   A 4 LYS A  86  PRO A  91  1  O  GLY A  88   N  LEU A  62           
SHEET    1   B 8 ARG A 131  PHE A 133  0                                        
SHEET    2   B 8 SER A 120  MSE A 128 -1  N  GLY A 126   O  PHE A 133           
SHEET    3   B 8 ALA A 280  PHE A 292 -1  O  LEU A 283   N  LYS A 127           
SHEET    4   B 8 ALA A 257  SER A 261 -1  N  ILE A 260   O  ALA A 280           
SHEET    5   B 8 VAL A 176  TYR A 182 -1  N  GLU A 181   O  ASN A 259           
SHEET    6   B 8 ASN A 185  GLY A 197 -1  O  PHE A 187   N  ILE A 180           
SHEET    7   B 8 PHE A 219  GLU A 225 -1  O  VAL A 224   N  LEU A 192           
SHEET    8   B 8 VAL A 250  ALA A 255 -1  O  ILE A 251   N  ILE A 223           
SHEET    1   C 9 ARG A 131  PHE A 133  0                                        
SHEET    2   C 9 SER A 120  MSE A 128 -1  N  GLY A 126   O  PHE A 133           
SHEET    3   C 9 ALA A 280  PHE A 292 -1  O  LEU A 283   N  LYS A 127           
SHEET    4   C 9 ALA A 257  SER A 261 -1  N  ILE A 260   O  ALA A 280           
SHEET    5   C 9 VAL A 176  TYR A 182 -1  N  GLU A 181   O  ASN A 259           
SHEET    6   C 9 ASN A 185  GLY A 197 -1  O  PHE A 187   N  ILE A 180           
SHEET    7   C 9 LEU A 136  GLY A 140 -1  N  ALA A 137   O  LEU A 196           
SHEET    8   C 9 GLN A 267  VAL A 270 -1  O  ASN A 269   N  ALA A 138           
SHEET    9   C 9 GLU A 273  LYS A 277 -1  O  GLU A 273   N  VAL A 270           
LINK         C   HIS A  -1                 N   MSE A   0     1555   1555  1.33  
LINK         C   MSE A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   ARG A   2     1555   1555  1.33  
LINK         C   ALA A  54                 N   MSE A  55     1555   1555  1.34  
LINK         C   MSE A  55                 N   HIS A  56     1555   1555  1.33  
LINK         C   PRO A  91                 N   MSE A  92     1555   1555  1.33  
LINK         C   MSE A  92                 N   GLY A  93     1555   1555  1.33  
LINK         C   ILE A 108                 N   MSE A 109     1555   1555  1.34  
LINK         C   MSE A 109                 N   GLY A 110     1555   1555  1.33  
LINK         C   LYS A 127                 N   MSE A 128     1555   1555  1.33  
LINK         C   MSE A 128                 N   ASN A 129     1555   1555  1.33  
LINK         C   GLU A 168                 N   MSE A 169     1555   1555  1.32  
LINK         C   MSE A 169                 N   LEU A 170     1555   1555  1.33  
LINK         C   GLN A 172                 N   MSE A 173     1555   1555  1.33  
LINK         C   MSE A 173                 N   LYS A 174     1555   1555  1.33  
LINK         C   SER A 201                 N   MSE A 202     1555   1555  1.34  
LINK         C   ILE A 235                 N   MSE A 236     1555   1555  1.34  
LINK         C   MSE A 236                 N   THR A 237     1555   1555  1.33  
CISPEP   1 LEU A  278    PRO A  279          0        -4.43                     
CRYST1  124.210  124.210   48.502  90.00  90.00  90.00 P 42 21 2     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      0.008051  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008051  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020618        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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