GenomeNet

Database: PDB
Entry: 2Y8Q
LinkDB: 2Y8Q
Original site: 2Y8Q 
HEADER    TRANSFERASE                             09-FEB-11   2Y8Q              
TITLE     STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK IN COMPLEX     
TITLE    2 WITH ONE ADP                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 406-555;                                          
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1;                                       
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 187-272;                                          
COMPND  12 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  16 CHAIN: E;                                                            
COMPND  17 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  15 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  16 ORGANISM_TAXID: 10116;                                               
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, ADP, NUCLEOTIDE-BINDING                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,M.J.SANDERS,E.UNDERWOOD,R.HEATH,F.MAYER,D.CARMENA,C.JING,      
AUTHOR   2 P.A.WALKER,J.F.ECCLESTON,L.F.HAIRE,P.SAIU,S.A.HOWELL,R.AASLAND,      
AUTHOR   3 S.R.MARTIN,D.CARLING,S.J.GAMBLIN                                     
REVDAT   3   28-NOV-12 2Y8Q    1       SEQADV REMARK VERSN  DBREF               
REVDAT   2   20-APR-11 2Y8Q    1       JRNL                                     
REVDAT   1   16-MAR-11 2Y8Q    0                                                
JRNL        AUTH   B.XIAO,M.J.SANDERS,E.UNDERWOOD,R.HEATH,F.MAYER,D.CARMENA,    
JRNL        AUTH 2 C.JING,P.A.WALKER,J.F.ECCLESTON,L.F.HAIRE,P.SAIU,S.A.HOWELL, 
JRNL        AUTH 3 R.AASLAND,S.R.MARTIN,D.CARLING,S.J.GAMBLIN                   
JRNL        TITL   STRUCTURE OF MAMMALIAN AMPK AND ITS REGULATION BY ADP        
JRNL        REF    NATURE                        V. 472   230 2011              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   21399626                                                     
JRNL        DOI    10.1038/NATURE09932                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5                                           
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) : 2.8                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17426                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.2                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 952                             
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) : 2.800                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.871                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1261                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.394                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.460                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3881                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
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) : 68.458                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.89                                                
REMARK   3    B22 (A**2) : 3.52                                                 
REMARK   3    B33 (A**2) : -1.63                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.108         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.382         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.288         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.605        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4020 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5456 ; 1.644 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   474 ; 7.024 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;36.358 ;23.314       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   716 ;20.275 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   633 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2924 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2398 ; 0.527 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3921 ; 0.986 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1622 ; 1.038 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1535 ; 1.832 ; 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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   393        A   469                          
REMARK   3    RESIDUE RANGE :   A   524        A   550                          
REMARK   3    RESIDUE RANGE :   B   190        B   221                          
REMARK   3    RESIDUE RANGE :   B   233        B   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3230  44.5330  51.1990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2645 T22:   0.1333                                     
REMARK   3      T33:   0.1527 T12:   0.0855                                     
REMARK   3      T13:   0.0556 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8511 L22:   3.4229                                     
REMARK   3      L33:   7.8242 L12:   1.5587                                     
REMARK   3      L13:  -0.3673 L23:  -4.2044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1454 S12:   0.0540 S13:  -0.0025                       
REMARK   3      S21:  -0.4112 S22:  -0.1909 S23:  -0.2323                       
REMARK   3      S31:   0.7709 S32:   0.2933 S33:   0.3363                       
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 :   E    48        E   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8010  62.0250  33.5460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2216 T22:   0.5928                                     
REMARK   3      T33:   0.3834 T12:   0.0467                                     
REMARK   3      T13:  -0.0575 T23:   0.2714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7005 L22:   0.5539                                     
REMARK   3      L33:   2.1381 L12:   2.4117                                     
REMARK   3      L13:  -4.7423 L23:  -1.0514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0160 S12:  -0.8534 S13:  -0.2487                       
REMARK   3      S21:   0.0339 S22:  -0.1473 S23:  -0.0673                       
REMARK   3      S31:   0.0225 S32:   0.5057 S33:   0.1313                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    23        E    47                          
REMARK   3    RESIDUE RANGE :   E   129        E   183                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1940  71.9700  30.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1245 T22:   0.0924                                     
REMARK   3      T33:   0.2064 T12:   0.0412                                     
REMARK   3      T13:   0.0327 T23:   0.0674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0440 L22:   2.9646                                     
REMARK   3      L33:   6.7351 L12:  -0.3646                                     
REMARK   3      L13:   0.4822 L23:  -1.6709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0866 S12:   0.2364 S13:   0.1589                       
REMARK   3      S21:   0.3985 S22:   0.1207 S23:   0.2224                       
REMARK   3      S31:  -0.7524 S32:  -0.2395 S33:  -0.0341                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   184        E   203                          
REMARK   3    RESIDUE RANGE :   E   275        E   326                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4460  77.2320  10.4020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.0505                                     
REMARK   3      T33:   0.1048 T12:  -0.0479                                     
REMARK   3      T13:  -0.0474 T23:   0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0311 L22:   4.4093                                     
REMARK   3      L33:   5.8891 L12:  -0.3783                                     
REMARK   3      L13:  -0.8900 L23:  -1.0411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1096 S12:   0.1807 S13:   0.1355                       
REMARK   3      S21:  -0.0019 S22:   0.0601 S23:   0.0429                       
REMARK   3      S31:  -0.2886 S32:   0.1418 S33:   0.0496                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   204        E   274                          
REMARK   3    RESIDUE RANGE :   E  1327        E  1328                          
REMARK   3    RESIDUE RANGE :   A  2001        A  2006                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2011                          
REMARK   3    RESIDUE RANGE :   E  2001        E  2039                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2700  62.9340  14.4240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1596 T22:   0.3611                                     
REMARK   3      T33:   0.3961 T12:   0.0471                                     
REMARK   3      T13:   0.0298 T23:   0.0908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0051 L22:   1.5606                                     
REMARK   3      L33:   3.0291 L12:   0.4031                                     
REMARK   3      L13:  -0.6860 L23:  -0.9597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0829 S12:  -0.1609 S13:  -0.4669                       
REMARK   3      S21:  -0.1916 S22:  -0.2801 S23:  -0.2665                       
REMARK   3      S31:   0.2343 S32:   0.6315 S33:   0.3630                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2Y8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-47330.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS IV)             
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17426                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 2.7                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.36                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2V8Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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       24.51300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.07500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.95900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.07500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.51300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.95900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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     MET A   378                                                      
REMARK 465     SER A   379                                                      
REMARK 465     HIS A   380                                                      
REMARK 465     HIS A   381                                                      
REMARK 465     HIS A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     GLY A   387                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     VAL A   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     ARG A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     ILE A   470                                                      
REMARK 465     THR A   471                                                      
REMARK 465     GLU A   472                                                      
REMARK 465     ALA A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     THR A   477                                                      
REMARK 465     ALA A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     ARG A   482                                                      
REMARK 465     SER A   483                                                      
REMARK 465     GLY A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     ILE A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     ASN A   488                                                      
REMARK 465     TYR A   489                                                      
REMARK 465     ARG A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     CYS A   492                                                      
REMARK 465     GLN A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     ASP A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     ASP A   498                                                      
REMARK 465     ALA A   499                                                      
REMARK 465     GLU A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     LYS A   504                                                      
REMARK 465     PRO A   505                                                      
REMARK 465     SER A   506                                                      
REMARK 465     GLU A   507                                                      
REMARK 465     VAL A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     LEU A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     VAL A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     ASP A   518                                                      
REMARK 465     SER A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     VAL A   522                                                      
REMARK 465     ASP A   523                                                      
REMARK 465     MET B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     THR B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     CYS B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     PRO B   227                                                      
REMARK 465     ALA B   228                                                      
REMARK 465     LEU B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     PRO B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     GLU E     7                                                      
REMARK 465     SER E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     PRO E    10                                                      
REMARK 465     ALA E    11                                                      
REMARK 465     PRO E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     ASN E    14                                                      
REMARK 465     GLU E    15                                                      
REMARK 465     HIS E    16                                                      
REMARK 465     SER E    17                                                      
REMARK 465     GLN E    18                                                      
REMARK 465     GLU E    19                                                      
REMARK 465     THR E    20                                                      
REMARK 465     PRO E    21                                                      
REMARK 465     GLU E    22                                                      
REMARK 465     GLU E   327                                                      
REMARK 465     LYS E   328                                                      
REMARK 465     LYS E   329                                                      
REMARK 465     PRO E   330                                                      
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    LEU E   248     O    HOH E  2024              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY E 274   N     GLY E 274   CA      0.123                       
REMARK 500    GLY E 274   CA    GLY E 274   C       0.116                       
REMARK 500    GLU E 273   C     GLY E 274   N       0.288                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 460   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    PRO E 183   C   -  N   -  CA  ANGL. DEV. = -10.6 DEGREES          
REMARK 500    PHE E 272   CA  -  C   -  N   ANGL. DEV. = -23.7 DEGREES          
REMARK 500    PHE E 272   O   -  C   -  N   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLU E 273   C   -  N   -  CA  ANGL. DEV. = -27.2 DEGREES          
REMARK 500    GLY E 274   N   -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    GLY E 274   CA  -  C   -  O   ANGL. DEV. = -15.2 DEGREES          
REMARK 500    GLY E 274   C   -  N   -  CA  ANGL. DEV. = -25.5 DEGREES          
REMARK 500    GLY E 274   CA  -  C   -  N   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    GLY E 274   O   -  C   -  N   ANGL. DEV. =  28.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A 394      -74.49    -74.72                                   
REMARK 500    GLU B 199      -68.10     67.63                                   
REMARK 500    LEU B 208      -77.52    -61.40                                   
REMARK 500    PRO B 210       36.46    -77.53                                   
REMARK 500    HIS B 211       61.00     35.53                                   
REMARK 500    ASN B 239       -2.22     71.73                                   
REMARK 500    ASP B 248       49.22     30.76                                   
REMARK 500    LYS B 260     -111.23     49.20                                   
REMARK 500    GLN E 104       34.56     73.70                                   
REMARK 500    GLN E 122     -111.56     51.64                                   
REMARK 500    THR E 208      -36.68    -34.66                                   
REMARK 500    ASP E 244       -8.99    -58.06                                   
REMARK 500    ILE E 246       -4.37    -58.16                                   
REMARK 500    LYS E 252       41.06    -91.17                                   
REMARK 500    THR E 253      -42.70   -141.35                                   
REMARK 500    TYR E 254      -17.32     77.10                                   
REMARK 500    ASN E 256       94.96    -57.99                                   
REMARK 500    SER E 269      -72.71   -109.96                                   
REMARK 500    TYR E 271     -117.38    135.23                                   
REMARK 500    PHE E 272      100.43    118.68                                   
REMARK 500    THR E 324       80.73     55.91                                   
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 SER A  546     CYS A  547                 -146.69                    
REMARK 500 LEU B  208     PRO B  209                 -149.06                    
REMARK 500 PHE E  182     PRO E  183                  149.90                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE E 272         12.12                                           
REMARK 500    GLU E 273         10.73                                           
REMARK 500    GLY E 274         10.30                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS B 211        21.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE E 182        23.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 ADENOSINE MONOPHOSPHATE (AMP): BINDING SITE 4                        
REMARK 600 ADENOSINE-5'-DIPHOSPHATE (ADP): BINDING SITE 1                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1328                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F15   RELATED DB: PDB                                   
REMARK 900  GLYCOGEN-BINDING DOMAIN OF THE AMP-ACTIVATED PROTEIN                
REMARK 900  KINASEBETA2 SUBUNIT                                                 
REMARK 900 RELATED ID: 2V8Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF                     
REMARK 900  MAMMALIAN AMPK IN COMPLEXES WITH AMP                                
REMARK 900 RELATED ID: 2V92   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF                     
REMARK 900  MAMMALIAN AMPK IN COMPLEXES WITH ATP-AMP                            
REMARK 900 RELATED ID: 2V9J   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF                     
REMARK 900  MAMMALIAN AMPK IN COMPLEXES WITH MG.ATP-AMP                         
REMARK 900 RELATED ID: 2Y8L   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK              
REMARK 900  IN COMPLEX WITH TWO ADP                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DNA SEQUENCE WITH HIS-TAG, MSHHHHHHSGLVPRG AND THE               
REMARK 999 ARTIFACTS, SMA (393-395) AND NSCTVN (545-550) AS A RESULT            
REMARK 999 OF CLONING STRATEGY.                                                 
REMARK 999 B 186 METHIONINE IS AN ARTIFACT, CREATED BY CLONING.                 
DBREF  2Y8Q A  396   544  UNP    P54645   AAPK1_RAT      407    555             
DBREF  2Y8Q B  187   270  UNP    O43741   AAKB2_HUMAN    187    272             
DBREF  2Y8Q E    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 2Y8Q MET A  378  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q SER A  379  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  380  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  381  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  382  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  383  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  384  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q HIS A  385  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q SER A  386  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q GLY A  387  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q LEU A  388  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q VAL A  389  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q PRO A  390  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q ARG A  391  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q GLY A  392  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q SER A  393  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q MET A  394  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q ALA A  395  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q ASN A  545  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q SER A  546  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q CYS A  547  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q THR A  548  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q VAL A  549  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q ASN A  550  UNP  P54645              EXPRESSION TAG                 
SEQADV 2Y8Q MET B  186  UNP  O43741              EXPRESSION TAG                 
SEQRES   1 A  173  MET SER HIS HIS HIS HIS HIS HIS SER GLY LEU VAL PRO          
SEQRES   2 A  173  ARG GLY SER MET ALA TRP HIS LEU GLY ILE ARG SER GLN          
SEQRES   3 A  173  SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA          
SEQRES   4 A  173  ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO          
SEQRES   5 A  173  TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER          
SEQRES   6 A  173  THR PHE SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP          
SEQRES   7 A  173  SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP          
SEQRES   8 A  173  GLU ILE THR GLU ALA LYS SER GLY THR ALA THR PRO GLN          
SEQRES   9 A  173  ARG SER GLY SER ILE SER ASN TYR ARG SER CYS GLN ARG          
SEQRES  10 A  173  SER ASP SER ASP ALA GLU ALA GLN GLY LYS PRO SER GLU          
SEQRES  11 A  173  VAL SER LEU THR SER SER VAL THR SER LEU ASP SER SER          
SEQRES  12 A  173  PRO VAL ASP VAL ALA PRO ARG PRO GLY SER HIS THR ILE          
SEQRES  13 A  173  GLU PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ASN SER          
SEQRES  14 A  173  CYS THR VAL ASN                                              
SEQRES   1 B   87  MET GLY PRO TYR GLY GLN GLU MET TYR ALA PHE ARG SER          
SEQRES   2 B   87  GLU GLU ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS          
SEQRES   3 B   87  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR ASN ILE SER          
SEQRES   4 B   87  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES   5 B   87  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP SER VAL          
SEQRES   6 B   87  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES   7 B   87  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 E  330  MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU          
SEQRES   2 E  330  ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER          
SEQRES   3 E  330  VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP          
SEQRES   4 E  330  LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR          
SEQRES   5 E  330  SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR          
SEQRES   6 E  330  ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS          
SEQRES   7 E  330  GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE          
SEQRES   8 E  330  ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN          
SEQRES   9 E  330  ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG          
SEQRES  10 E  330  GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS          
SEQRES  11 E  330  ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER          
SEQRES  12 E  330  LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP          
SEQRES  13 E  330  PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS          
SEQRES  14 E  330  ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE          
SEQRES  15 E  330  PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU          
SEQRES  16 E  330  GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR          
SEQRES  17 E  330  THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN          
SEQRES  18 E  330  HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY          
SEQRES  19 E  330  ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN          
SEQRES  20 E  330  LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER          
SEQRES  21 E  330  VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU          
SEQRES  22 E  330  GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA          
SEQRES  23 E  330  ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU          
SEQRES  24 E  330  VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL          
SEQRES  25 E  330  SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY          
SEQRES  26 E  330  GLY GLU LYS LYS PRO                                          
HET    ADP  E1327      27                                                       
HET    AMP  E1328      23                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  AMP    C10 H14 N5 O7 P                                              
FORMUL   6  HOH   *56(H2 O)                                                     
HELIX    1   1 ARG A  405  LEU A  420  1                                  16    
HELIX    2   2 SER A  530  CYS A  547  1                                  18    
HELIX    3   3 SER E   26  SER E   34  1                                   9    
HELIX    4   4 CYS E   37  ILE E   41  5                                   5    
HELIX    5   5 GLN E   55  GLY E   67  1                                  13    
HELIX    6   6 ILE E   87  LEU E  102  1                                  16    
HELIX    7   7 GLU E  107  HIS E  111  5                                   5    
HELIX    8   8 LYS E  112  LEU E  121  1                                  10    
HELIX    9   9 SER E  136  ASN E  147  1                                  12    
HELIX   10  10 THR E  167  ILE E  179  1                                  13    
HELIX   11  11 PRO E  185  LYS E  190  5                                   6    
HELIX   12  12 SER E  191  GLN E  196  1                                   6    
HELIX   13  13 PRO E  211  ARG E  223  1                                  13    
HELIX   14  14 LYS E  242  ASN E  247  1                                   6    
HELIX   15  15 LEU E  248  ALA E  250  5                                   3    
HELIX   16  16 SER E  260  LEU E  265  1                                   6    
HELIX   17  17 THR E  283  GLU E  295  1                                  13    
HELIX   18  18 LEU E  314  LEU E  323  1                                  10    
SHEET    1  BA 8 VAL B 215  LEU B 217  0                                        
SHEET    2  BA 8 ALA A 395  LEU A 398 -1  O  TRP A 396   N  ILE B 216           
SHEET    3  BA 8 TYR B 242  ALA B 243 -1  O  ALA B 243   N  HIS A 397           
SHEET    4  BA 8 VAL B 250  TYR B 259 -1  O  SER B 254   N  TYR B 242           
SHEET    5  BA 8 LYS B 262  PRO B 271 -1  O  LYS B 262   N  TYR B 259           
SHEET    6  BA 8 SER E  44  ASP E  51  1  O  SER E  45   N  THR B 265           
SHEET    7  BA 8 ALA E  70  ASP E  75  1  O  PRO E  72   N  PHE E  50           
SHEET    8  BA 8 SER E  80  THR E  86 -1  O  SER E  80   N  ASP E  75           
SHEET    1  AA 5 ILE A 400  SER A 402  0                                        
SHEET    2  AA 5 TYR A 459  ILE A 466 -1  O  TYR A 459   N  SER A 402           
SHEET    3  AA 5 PHE A 444  GLN A 453 -1  O  LYS A 446   N  ILE A 466           
SHEET    4  AA 5 TYR A 431  LYS A 437 -1  O  LEU A 432   N  LEU A 449           
SHEET    5  AA 5 GLU A 423  ASN A 428 -1  O  GLU A 423   N  ARG A 435           
SHEET    1  EA 2 LEU E 152  ILE E 155  0                                        
SHEET    2  EA 2 THR E 162  LEU E 166 -1  N  LEU E 163   O  VAL E 154           
SHEET    1  EB 3 VAL E 206  ARG E 207  0                                        
SHEET    2  EB 3 ALA E 226  VAL E 230  1  O  PRO E 228   N  VAL E 206           
SHEET    3  EB 3 VAL E 236  SER E 241 -1  N  VAL E 237   O  VAL E 229           
SHEET    1  EC 3 LYS E 277  TYR E 279  0                                        
SHEET    2  EC 3 ARG E 298  VAL E 302  1  O  VAL E 300   N  CYS E 278           
SHEET    3  EC 3 VAL E 308  SER E 313 -1  N  LYS E 309   O  VAL E 301           
SITE     1 AC1 11 MET E  84  THR E  86  THR E  88  ASP E  89                    
SITE     2 AC1 11 PRO E 127  LEU E 128  VAL E 129  ILE E 149                    
SITE     3 AC1 11 HIS E 150  ARG E 151  PRO E 153                               
SITE     1 AC2 14 ARG A 457  HIS E 150  THR E 199  ILE E 203                    
SITE     2 AC2 14 ALA E 204  VAL E 224  SER E 225  ALA E 226                    
SITE     3 AC2 14 PRO E 228  ILE E 311  SER E 313  SER E 315                    
SITE     4 AC2 14 ASP E 316  HOH E2039                                          
CRYST1   49.026  119.918  130.150  90.00  90.00  90.00 P 21 21 21    4          
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      0.020397  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008339  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007683        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system