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Database: PDB
Entry: 2VLG
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HEADER    TRANSFERASE                             14-JAN-08   2VLG              
TITLE     KINA PAS-A DOMAIN, HOMODIMER                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPORULATION KINASE A;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: PAS-A, RESIDUES 10-117;                                    
COMPND   5 SYNONYM: STAGE II SPORULATION PROTEIN J, KINA PAS-A;                 
COMPND   6 EC: 2.7.13.3;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: STRAIN 1A40;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PHIS6GBETA1;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHIS6GBETA1KINA;                          
SOURCE  10 OTHER_DETAILS: BACILLUS GENETIC STOCK CENTER, COLUMBUS, OH, U.S.A.   
KEYWDS    HISTIDINE KINASE, TWO-COMPONENT REGULATORY SYSTEM, TWO-COMPONENT      
KEYWDS   2 SIGNAL TRANSDUCTION, TRANSFERASE, SPORULATION, PHOSPHORYLATION,      
KEYWDS   3 SCOD, SCOB, GSIC, SPOIIJ, KINASE, SPOIIF, PAS DOMAIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LEE,D.R.TOMCHICK,C.A.BRAUTIGAM,M.MACHIUS,R.KORT,K.J.HELLINGWERF,    
AUTHOR   2 K.H.GARDNER                                                          
REVDAT   5   15-MAY-19 2VLG    1       REMARK                                   
REVDAT   4   08-MAY-19 2VLG    1       REMARK                                   
REVDAT   3   24-FEB-09 2VLG    1       VERSN                                    
REVDAT   2   08-APR-08 2VLG    1       AUTHOR JRNL   REMARK                     
REVDAT   1   18-MAR-08 2VLG    0                                                
JRNL        AUTH   J.LEE,D.R.TOMCHICK,C.A.BRAUTIGAM,M.MACHIUS,R.KORT,           
JRNL        AUTH 2 K.J.HELLINGWERF,K.H.GARDNER                                  
JRNL        TITL   CHANGES AT THE KINA PAS-A DIMERIZATION INTERFACE INFLUENCE   
JRNL        TITL 2 HISTIDINE KINASE FUNCTION.                                   
JRNL        REF    BIOCHEMISTRY                  V.  47  4051 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18324779                                                     
JRNL        DOI    10.1021/BI7021156                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40811                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1499                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1758                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3207                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 301                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.51000                                             
REMARK   3    B22 (A**2) : 2.99000                                              
REMARK   3    B33 (A**2) : -1.53000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.07000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.938         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3320 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4478 ; 1.761 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   390 ; 6.719 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;30.568 ;23.631       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   613 ;13.795 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;13.490 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   509 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2440 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1388 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2313 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   297 ; 0.167 ; 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):    84 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.197 ; 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):  2030 ; 1.222 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3175 ; 1.834 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1471 ; 2.527 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1303 ; 3.732 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2803   9.4970  13.2805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0351 T22:  -0.0820                                     
REMARK   3      T33:  -0.0474 T12:   0.0046                                     
REMARK   3      T13:   0.0085 T23:  -0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1222 L22:   1.0453                                     
REMARK   3      L33:   3.7557 L12:   0.0009                                     
REMARK   3      L13:  -0.1451 L23:  -0.2402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0167 S12:   0.1277 S13:   0.0201                       
REMARK   3      S21:  -0.0471 S22:   0.0003 S23:  -0.0035                       
REMARK   3      S31:  -0.0144 S32:   0.1207 S33:   0.0163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    15        B   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6858   9.7815  -9.8791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0422 T22:  -0.0275                                     
REMARK   3      T33:  -0.0748 T12:  -0.0377                                     
REMARK   3      T13:   0.0019 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3192 L22:   0.7936                                     
REMARK   3      L33:   3.3929 L12:   0.0509                                     
REMARK   3      L13:  -0.8294 L23:   0.3779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:  -0.2193 S13:   0.0674                       
REMARK   3      S21:   0.0230 S22:   0.0341 S23:  -0.0080                       
REMARK   3      S31:  -0.1050 S32:   0.4103 S33:   0.0019                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    15        C   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4442   5.4054 -24.1438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0595 T22:  -0.0144                                     
REMARK   3      T33:  -0.0469 T12:  -0.0586                                     
REMARK   3      T13:   0.0061 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7766 L22:   0.8563                                     
REMARK   3      L33:   2.0694 L12:  -0.3218                                     
REMARK   3      L13:   0.9801 L23:   0.0893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1309 S12:  -0.3748 S13:  -0.0792                       
REMARK   3      S21:   0.0578 S22:  -0.0835 S23:   0.0818                       
REMARK   3      S31:   0.0243 S32:  -0.1008 S33:  -0.0474                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    15        D   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0493   4.9231 -47.2683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0596 T22:  -0.0336                                     
REMARK   3      T33:  -0.0574 T12:   0.0216                                     
REMARK   3      T13:  -0.0075 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9596 L22:   1.3493                                     
REMARK   3      L33:   2.7514 L12:   0.1921                                     
REMARK   3      L13:  -0.1494 L23:   0.3871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0242 S12:   0.1882 S13:   0.0061                       
REMARK   3      S21:  -0.0799 S22:  -0.0447 S23:  -0.0328                       
REMARK   3      S31:   0.0400 S32:  -0.0041 S33:   0.0206                       
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 RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2VLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035011.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42220                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
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: SAD                          
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM                                    
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 DEGREES CELSIUS, HANGING-DROP VAPOR   
REMARK 280  DIFFUSION: 1 MICROLITER KINA (7 MG/ML IN 25 MM TRIS, PH 8, 100      
REMARK 280  MM NACL PLUS 1 MICROLITER WELL SOLUTION (13 TO 15% (W/V) PEG 10,    
REMARK 280  000, 0.1 M AMMONIUM ACETATE, 0.1 M BIS-TRIS, PH 5.5); CRYSTALS      
REMARK 280  APPEARED AFTER ABOUT ONE DAY AND GREW TO A FINAL SIZE OF ABOUT      
REMARK 280  80 X 80 X 100 MICROMETERS WITHIN FOUR DAYS; CRYO-PROTECTION:        
REMARK 280  STEPWISE TRANSFER INTO WELL SOLUTION SUPPLEMENTED WITH UP TO 25%    
REMARK 280  (V/V) GLYCEROL., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       27.75800            
REMARK 290   SMTRY3   2  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: 680 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 440 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     THR A    97                                                      
REMARK 465     THR A    98                                                      
REMARK 465     ARG A    99                                                      
REMARK 465     ALA A   100                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     ARG A   102                                                      
REMARK 465     THR A   103                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     GLU A   117                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     THR B    98                                                      
REMARK 465     ARG B    99                                                      
REMARK 465     ALA B   100                                                      
REMARK 465     GLU B   101                                                      
REMARK 465     ARG B   102                                                      
REMARK 465     THR B   103                                                      
REMARK 465     GLU B   104                                                      
REMARK 465     GLU B   115                                                      
REMARK 465     GLU B   116                                                      
REMARK 465     GLU B   117                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     PHE C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     GLN C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     LYS C    14                                                      
REMARK 465     GLU C   117                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     PHE D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     GLN D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     LYS D    14                                                      
REMARK 465     GLU D    69                                                      
REMARK 465     HIS D    70                                                      
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    LEU A  72      -60.90   -138.43                                   
REMARK 500    LEU B  72      -64.10   -137.22                                   
REMARK 500    HIS C  70       36.40   -151.92                                   
REMARK 500    LEU C  72       16.29     53.45                                   
REMARK 500    ALA C 100     -124.88   -124.83                                   
REMARK 500    ALA D 100      -90.00   -115.84                                   
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 C2009        DISTANCE =  8.02 ANGSTROMS                       
REMARK 525    HOH C2023        DISTANCE =  6.34 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1115                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1115                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1115                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 7-9 (GEF) BELONG TO THE CLONING LINKER                      
DBREF  2VLG A    7     9  PDB    2VLG     2VLG             7      9             
DBREF  2VLG A   10   117  UNP    P16497   KINA_BACSU      10    117             
DBREF  2VLG B    7     9  PDB    2VLG     2VLG             7      9             
DBREF  2VLG B   10   117  UNP    P16497   KINA_BACSU      10    117             
DBREF  2VLG C    7     9  PDB    2VLG     2VLG             7      9             
DBREF  2VLG C   10   117  UNP    P16497   KINA_BACSU      10    117             
DBREF  2VLG D    7     9  PDB    2VLG     2VLG             7      9             
DBREF  2VLG D   10   117  UNP    P16497   KINA_BACSU      10    117             
SEQRES   1 A  111  GLY GLU PHE PRO LEU GLN THR LYS THR ASP ILE HIS ALA          
SEQRES   2 A  111  VAL LEU ALA SER ASN GLY ARG ILE ILE TYR ILE SER ALA          
SEQRES   3 A  111  ASN SER LYS LEU HIS LEU GLY TYR LEU GLN GLY GLU MET          
SEQRES   4 A  111  ILE GLY SER PHE LEU LYS THR PHE LEU HIS GLU GLU ASP          
SEQRES   5 A  111  GLN PHE LEU VAL GLU SER TYR PHE TYR ASN GLU HIS HIS          
SEQRES   6 A  111  LEU MET PRO CYS THR PHE ARG PHE ILE LYS LYS ASP HIS          
SEQRES   7 A  111  THR ILE VAL TRP VAL GLU ALA ALA VAL GLU ILE VAL THR          
SEQRES   8 A  111  THR ARG ALA GLU ARG THR GLU ARG GLU ILE ILE LEU LYS          
SEQRES   9 A  111  MET LYS VAL LEU GLU GLU GLU                                  
SEQRES   1 B  111  GLY GLU PHE PRO LEU GLN THR LYS THR ASP ILE HIS ALA          
SEQRES   2 B  111  VAL LEU ALA SER ASN GLY ARG ILE ILE TYR ILE SER ALA          
SEQRES   3 B  111  ASN SER LYS LEU HIS LEU GLY TYR LEU GLN GLY GLU MET          
SEQRES   4 B  111  ILE GLY SER PHE LEU LYS THR PHE LEU HIS GLU GLU ASP          
SEQRES   5 B  111  GLN PHE LEU VAL GLU SER TYR PHE TYR ASN GLU HIS HIS          
SEQRES   6 B  111  LEU MET PRO CYS THR PHE ARG PHE ILE LYS LYS ASP HIS          
SEQRES   7 B  111  THR ILE VAL TRP VAL GLU ALA ALA VAL GLU ILE VAL THR          
SEQRES   8 B  111  THR ARG ALA GLU ARG THR GLU ARG GLU ILE ILE LEU LYS          
SEQRES   9 B  111  MET LYS VAL LEU GLU GLU GLU                                  
SEQRES   1 C  111  GLY GLU PHE PRO LEU GLN THR LYS THR ASP ILE HIS ALA          
SEQRES   2 C  111  VAL LEU ALA SER ASN GLY ARG ILE ILE TYR ILE SER ALA          
SEQRES   3 C  111  ASN SER LYS LEU HIS LEU GLY TYR LEU GLN GLY GLU MET          
SEQRES   4 C  111  ILE GLY SER PHE LEU LYS THR PHE LEU HIS GLU GLU ASP          
SEQRES   5 C  111  GLN PHE LEU VAL GLU SER TYR PHE TYR ASN GLU HIS HIS          
SEQRES   6 C  111  LEU MET PRO CYS THR PHE ARG PHE ILE LYS LYS ASP HIS          
SEQRES   7 C  111  THR ILE VAL TRP VAL GLU ALA ALA VAL GLU ILE VAL THR          
SEQRES   8 C  111  THR ARG ALA GLU ARG THR GLU ARG GLU ILE ILE LEU LYS          
SEQRES   9 C  111  MET LYS VAL LEU GLU GLU GLU                                  
SEQRES   1 D  111  GLY GLU PHE PRO LEU GLN THR LYS THR ASP ILE HIS ALA          
SEQRES   2 D  111  VAL LEU ALA SER ASN GLY ARG ILE ILE TYR ILE SER ALA          
SEQRES   3 D  111  ASN SER LYS LEU HIS LEU GLY TYR LEU GLN GLY GLU MET          
SEQRES   4 D  111  ILE GLY SER PHE LEU LYS THR PHE LEU HIS GLU GLU ASP          
SEQRES   5 D  111  GLN PHE LEU VAL GLU SER TYR PHE TYR ASN GLU HIS HIS          
SEQRES   6 D  111  LEU MET PRO CYS THR PHE ARG PHE ILE LYS LYS ASP HIS          
SEQRES   7 D  111  THR ILE VAL TRP VAL GLU ALA ALA VAL GLU ILE VAL THR          
SEQRES   8 D  111  THR ARG ALA GLU ARG THR GLU ARG GLU ILE ILE LEU LYS          
SEQRES   9 D  111  MET LYS VAL LEU GLU GLU GLU                                  
HET     CL  B1115       1                                                       
HET     CL  B1116       1                                                       
HET     CL  C1115       1                                                       
HET    ACT  C1117       4                                                       
HET    ACT  C1118       4                                                       
HET     CL  D1115       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   8  ACT    2(C2 H3 O2 1-)                                               
FORMUL  11  HOH   *301(H2 O)                                                    
HELIX    1   1 ASN A   33  GLY A   39  1                                   7    
HELIX    2   2 LEU A   41  ILE A   46  1                                   6    
HELIX    3   3 LEU A   50  PHE A   53  5                                   4    
HELIX    4   4 HIS A   55  GLU A   57  5                                   3    
HELIX    5   5 ASP A   58  ASN A   68  1                                  11    
HELIX    6   6 ASN B   33  GLY B   39  1                                   7    
HELIX    7   7 LEU B   41  ILE B   46  1                                   6    
HELIX    8   8 LEU B   50  PHE B   53  5                                   4    
HELIX    9   9 HIS B   55  GLU B   57  5                                   3    
HELIX   10  10 ASP B   58  ASN B   68  1                                  11    
HELIX   11  11 ASN C   33  GLY C   39  1                                   7    
HELIX   12  12 LEU C   41  ILE C   46  1                                   6    
HELIX   13  13 LEU C   50  PHE C   53  5                                   4    
HELIX   14  14 HIS C   55  PHE C   60  1                                   6    
HELIX   15  15 VAL C   62  ASN C   68  1                                   7    
HELIX   16  16 ASN D   33  GLY D   39  1                                   7    
HELIX   17  17 LEU D   41  ILE D   46  1                                   6    
HELIX   18  18 LEU D   50  LEU D   54  5                                   5    
HELIX   19  19 HIS D   55  PHE D   66  1                                  12    
SHEET    1  AA 5 ILE A  27  ILE A  30  0                                        
SHEET    2  AA 5 ILE A  17  LEU A  21 -1  O  VAL A  20   N  ILE A  28           
SHEET    3  AA 5 ILE A 107  VAL A 113 -1  O  ILE A 107   N  LEU A  21           
SHEET    4  AA 5 ILE A  86  ILE A  95 -1  O  GLU A  90   N  LYS A 112           
SHEET    5  AA 5 CYS A  75  ILE A  80 -1  O  CYS A  75   N  ALA A  91           
SHEET    1  BA 5 ILE B  27  ILE B  30  0                                        
SHEET    2  BA 5 ILE B  17  LEU B  21 -1  O  VAL B  20   N  ILE B  28           
SHEET    3  BA 5 ILE B 107  VAL B 113 -1  O  ILE B 107   N  LEU B  21           
SHEET    4  BA 5 ILE B  86  ILE B  95 -1  O  GLU B  90   N  LYS B 112           
SHEET    5  BA 5 CYS B  75  ILE B  80 -1  O  CYS B  75   N  ALA B  91           
SHEET    1  CA 5 ILE C  27  ILE C  30  0                                        
SHEET    2  CA 5 ILE C  17  ALA C  22 -1  O  VAL C  20   N  ILE C  28           
SHEET    3  CA 5 THR C 103  VAL C 113 -1  O  ILE C 107   N  LEU C  21           
SHEET    4  CA 5 ILE C  86  ARG C  99 -1  O  GLU C  90   N  LYS C 112           
SHEET    5  CA 5 CYS C  75  ILE C  80 -1  O  CYS C  75   N  ALA C  91           
SHEET    1  DA 5 ILE D  27  ILE D  30  0                                        
SHEET    2  DA 5 ILE D  17  ALA D  22 -1  O  VAL D  20   N  ILE D  28           
SHEET    3  DA 5 THR D 103  LEU D 114 -1  O  ILE D 107   N  LEU D  21           
SHEET    4  DA 5 ILE D  86  ARG D  99 -1  O  TRP D  88   N  LEU D 114           
SHEET    5  DA 5 CYS D  75  ILE D  80 -1  O  CYS D  75   N  ALA D  91           
SITE     1 AC1  8 ALA C  19  VAL C  20  ILE C 108  HOH C2004                    
SITE     2 AC1  8 HOH C2084  ALA D  19  VAL D  20  ILE D 108                    
SITE     1 AC2  4 ALA C  92  GLU C  94  ILE C 108  LYS C 110                    
SITE     1 AC3  3 GLU A  69  HIS A  71  HOH D2039                               
SITE     1 AC4  3 TYR A  29  HOH A2006  TYR B  29                               
SITE     1 AC5  1 HOH D2074                                                     
CRYST1   53.568   55.516   78.879  90.00 109.01  90.00 P 1 21 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      0.018668  0.000000  0.006432        0.00000                         
SCALE2      0.000000  0.018013  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013409        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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