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Database: PDB
Entry: 2V8Q
LinkDB: 2V8Q
Original site: 2V8Q 
HEADER    TRANSFERASE                             13-AUG-07   2V8Q              
TITLE     CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN             
TITLE    2 AMPK IN COMPLEXES WITH AMP                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 396-548;                                          
COMPND   5 SYNONYM: AMP-ACTIVATED PROTEIN KINASE, AMPK ALPHA-1 CHAIN;           
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 GAMMA-1;           
COMPND  10 CHAIN: E;                                                            
COMPND  11 SYNONYM: AMP-ACTIVATED PROTEIN KINASE, AMPK GAMMA-1 CHAIN, AMPKG;    
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  15 CHAIN: B;                                                            
COMPND  16 FRAGMENT: RESIDUES 187-272;                                          
COMPND  17 SYNONYM: AMP-ACTIVATED PROTEIN KINASE, AMPK BETA-2 CHAIN;            
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: 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: RATTUS NORVEGICUS;                              
SOURCE   9 ORGANISM_COMMON: RAT;                                                
SOURCE  10 ORGANISM_TAXID: 10116;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHORYLATION, NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN         
KEYWDS   2 KINASE, KINASE, MAGNESIUM, CBS DOMAIN, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,P.A.WALKER,L.HAIRE,   
AUTHOR   2 J.F.ECCLESTON,C.T.DAVIS,S.R.MARTIN,D.CARLING,S.J.GAMBLIN             
REVDAT   4   13-JUL-11 2V8Q    1       VERSN                                    
REVDAT   3   24-FEB-09 2V8Q    1       VERSN                                    
REVDAT   2   02-OCT-07 2V8Q    1       JRNL                                     
REVDAT   1   25-SEP-07 2V8Q    0                                                
JRNL        AUTH   B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,P.A.WALKER,  
JRNL        AUTH 2 L.HAIRE,J.F.ECCLESTON,C.T.DAVIS,S.R.MARTIN,D.CARLING,        
JRNL        AUTH 3 S.J.GAMBLIN                                                  
JRNL        TITL   STRUCTURAL BASIS FOR AMP BINDING TO MAMMALIAN AMP-           
JRNL        TITL 2 ACTIVATED PROTEIN KINASE                                     
JRNL        REF    NATURE                        V. 449   496 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17851531                                                     
JRNL        DOI    10.1038/NATURE06161                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 42012                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2234                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5903                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 308                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3884                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 428                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.73000                                             
REMARK   3    B22 (A**2) : 3.06000                                              
REMARK   3    B33 (A**2) : -0.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.192         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.164         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.644        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4044 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5491 ; 1.439 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   474 ; 7.475 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;35.233 ;23.314       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   718 ;18.379 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   638 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2935 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1867 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2708 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   364 ; 0.141 ; 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):    51 ; 0.225 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.216 ; 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):  2452 ; 0.682 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3919 ; 1.157 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1803 ; 1.435 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1572 ; 2.233 ; 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  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   393        A   469                          
REMARK   3    RESIDUE RANGE :   A   524        A   548                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7010  73.3050  11.2570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0278 T22:  -0.1773                                     
REMARK   3      T33:  -0.0962 T12:  -0.0765                                     
REMARK   3      T13:  -0.0170 T23:   0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5999 L22:   3.3406                                     
REMARK   3      L33:   5.2180 L12:  -0.6812                                     
REMARK   3      L13:   0.7886 L23:  -1.4749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:   0.0731 S13:   0.0023                       
REMARK   3      S21:  -0.1302 S22:  -0.1409 S23:  -0.0138                       
REMARK   3      S31:  -0.1520 S32:   0.4508 S33:   0.2086                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   190        B   222                          
REMARK   3    RESIDUE RANGE :   B   233        B   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7430  77.1320  18.1730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1817 T22:  -0.1799                                     
REMARK   3      T33:  -0.0418 T12:   0.0020                                     
REMARK   3      T13:  -0.0246 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4078 L22:   3.0635                                     
REMARK   3      L33:   5.2095 L12:  -1.5372                                     
REMARK   3      L13:   1.0423 L23:  -3.6173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1041 S12:  -0.2674 S13:   0.0594                       
REMARK   3      S21:   0.2766 S22:   0.0320 S23:  -0.0624                       
REMARK   3      S31:  -0.6652 S32:  -0.3198 S33:   0.0721                       
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 :   E    48        E   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6820  57.6860  31.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0358 T22:  -0.0019                                     
REMARK   3      T33:   0.0166 T12:   0.0086                                     
REMARK   3      T13:   0.0515 T23:   0.1520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8083 L22:   0.4347                                     
REMARK   3      L33:   1.3436 L12:  -0.5718                                     
REMARK   3      L13:   2.2413 L23:  -0.2442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0345 S12:   0.2486 S13:  -0.0285                       
REMARK   3      S21:  -0.0464 S22:  -0.1273 S23:  -0.1526                       
REMARK   3      S31:   0.0530 S32:   0.3467 S33:   0.0928                       
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    23        E    47                          
REMARK   3    RESIDUE RANGE :   E   129        E   183                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2200  47.9030  35.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0654 T22:  -0.1480                                     
REMARK   3      T33:   0.0045 T12:  -0.0436                                     
REMARK   3      T13:  -0.0308 T23:   0.0727                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0923 L22:   1.7073                                     
REMARK   3      L33:   2.7792 L12:   0.3548                                     
REMARK   3      L13:  -0.4203 L23:  -1.4289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0389 S12:  -0.0185 S13:  -0.0918                       
REMARK   3      S21:  -0.2244 S22:   0.1891 S23:   0.1568                       
REMARK   3      S31:   0.3833 S32:  -0.1929 S33:  -0.1502                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
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):  16.6080  42.7410  54.4130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0347 T22:  -0.1517                                     
REMARK   3      T33:  -0.0376 T12:   0.0329                                     
REMARK   3      T13:   0.0232 T23:   0.0780                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6590 L22:   2.5787                                     
REMARK   3      L33:   2.1885 L12:   0.4806                                     
REMARK   3      L13:   0.4575 L23:   0.1686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0639 S12:  -0.2307 S13:  -0.0784                       
REMARK   3      S21:   0.0459 S22:  -0.0049 S23:   0.1087                       
REMARK   3      S31:   0.1142 S32:  -0.0525 S33:  -0.0590                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   204        E   274                          
REMARK   3    RESIDUE RANGE :   E  1327        E  1329                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3840  57.0290  51.8220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0464 T22:  -0.1225                                     
REMARK   3      T33:   0.0602 T12:  -0.0321                                     
REMARK   3      T13:   0.0514 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6431 L22:   1.8763                                     
REMARK   3      L33:   4.5418 L12:   0.3534                                     
REMARK   3      L13:   0.5907 L23:  -0.2204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1641 S12:  -0.1641 S13:   0.5141                       
REMARK   3      S21:   0.1617 S22:  -0.1040 S23:  -0.0889                       
REMARK   3      S31:  -0.4499 S32:   0.2731 S33:  -0.0602                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2001        E  2291                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7070  58.3520  32.5380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0312 T22:  -0.1249                                     
REMARK   3      T33:  -0.0024 T12:  -0.0135                                     
REMARK   3      T13:   0.0119 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0981 L22:   0.4695                                     
REMARK   3      L33:   1.0409 L12:  -0.2026                                     
REMARK   3      L13:   0.2598 L23:  -0.4026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0441 S12:   0.0103 S13:  -0.0022                       
REMARK   3      S21:  -0.0709 S22:   0.0296 S23:   0.0008                       
REMARK   3      S31:   0.0717 S32:  -0.0023 S33:   0.0144                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2V8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-AUG-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33452.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42012                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.6                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.0                      
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       24.26100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.65500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.65500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.26100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.69500            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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     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     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: 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. =  16.8 DEGREES          
REMARK 500    LEU E  40   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    ASP A 455     -157.52   -125.82                                   
REMARK 500    GLU B 199      -59.67     66.91                                   
REMARK 500    LEU B 208      -80.30    -58.71                                   
REMARK 500    HIS B 211       65.17      0.77                                   
REMARK 500    HIS B 235      -74.50    -45.36                                   
REMARK 500    ASN B 239       -0.80     74.84                                   
REMARK 500    LYS B 260     -109.57     49.37                                   
REMARK 500    ASN E  24      151.25     68.90                                   
REMARK 500    SER E  25     -112.60    -55.90                                   
REMARK 500    LEU E 121       48.29    -75.36                                   
REMARK 500    GLN E 122      -89.09    -56.29                                   
REMARK 500    SER E 124       91.88    -63.41                                   
REMARK 500    TYR E 254      -10.65     60.42                                   
REMARK 500    ASN E 256       48.86    -92.03                                   
REMARK 500    ARG E 268       90.52    -60.26                                   
REMARK 500    HIS E 270     -142.52    131.85                                   
REMARK 500    GLU E 273     -160.30    -76.15                                   
REMARK 500    THR E 324      134.98     64.30                                   
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 PRO B  209     PRO B  210                  144.35                    
REMARK 500 PRO B  210     HIS B  211                 -141.34                    
REMARK 500 PHE E  182     PRO E  183                  136.13                    
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        18.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE E 182        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1329                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F15   RELATED DB: PDB                                   
REMARK 900  GLYCOGEN-BINDING DOMAIN OF THE AMP-ACTIVATED                        
REMARK 900   PROTEIN KINASEBETA2 SUBUNIT                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999  THE FIRST FOUR RESIDUES (GSMA) OF THE SEQUENCE OF CHAIN A           
REMARK 999  ARE GENERATED FROM THE POST HIS-TAG CLEAVAGE                        
REMARK 999  THE FIRST RESIDUES (M) OF THE SEQUENCE OF CHAIN B IS                
REMARK 999  GENERATED BY THE WAY IT WAS CLONED INTO THE VECTOR                  
DBREF  2V8Q A  392   395  PDB    2V8Q     2V8Q           392    395             
DBREF  2V8Q A  396   548  UNP    P54645   AAPK1_RAT      396    548             
DBREF  2V8Q B  186   186  PDB    2V8Q     2V8Q           186    186             
DBREF  2V8Q B  187   272  UNP    O43741   AAKB2_HUMAN    187    272             
DBREF  2V8Q E    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQRES   1 A  157  GLY SER MET ALA TRP HIS LEU GLY ILE ARG SER GLN SER          
SEQRES   2 A  157  ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA ILE          
SEQRES   3 A  157  LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO TYR          
SEQRES   4 A  157  TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER THR          
SEQRES   5 A  157  PHE SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP SER          
SEQRES   6 A  157  ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP GLU          
SEQRES   7 A  157  ILE THR GLU ALA LYS SER GLY THR ALA THR PRO GLN ARG          
SEQRES   8 A  157  SER GLY SER ILE SER ASN TYR ARG SER CYS GLN ARG SER          
SEQRES   9 A  157  ASP SER ASP ALA GLU ALA GLN GLY LYS PRO SER GLU VAL          
SEQRES  10 A  157  SER LEU THR SER SER VAL THR SER LEU ASP SER SER PRO          
SEQRES  11 A  157  VAL ASP VAL ALA PRO ARG PRO GLY SER HIS THR ILE GLU          
SEQRES  12 A  157  PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA          
SEQRES  13 A  157  GLN                                                          
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    AMP  E1327      23                                                       
HET    AMP  E1328      23                                                       
HET    AMP  E1329      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   4  AMP    3(C10 H14 N5 O7 P)                                           
FORMUL   5  HOH   *428(H2 O)                                                    
HELIX    1   1 ARG A  405  LEU A  420  1                                  16    
HELIX    2   2 SER A  530  ILE A  545  1                                  16    
HELIX    3   3 SER E   26  HIS E   35  1                                  10    
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  LYS E  148  1                                  13    
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 PHE E  243  GLU E  251  5                                   9    
HELIX   15  15 SER E  260  LEU E  265  1                                   6    
HELIX   16  16 GLN E  266  ARG E  268  5                                   3    
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  CYS E 278  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 14 ARG E  69  LYS E 169  ILE E 239  SER E 241                    
SITE     2 AC1 14 PHE E 243  ASP E 244  ARG E 268  PHE E 272                    
SITE     3 AC1 14 VAL E 275  LEU E 276  VAL E 296  HIS E 297                    
SITE     4 AC1 14 ARG E 298  HOH E2283                                          
SITE     1 AC2 14 MET E  84  THR E  86  THR E  88  ASP E  89                    
SITE     2 AC2 14 PRO E 127  LEU E 128  VAL E 129  ILE E 149                    
SITE     3 AC2 14 HIS E 150  ARG E 151  PRO E 153  HOH E2284                    
SITE     4 AC2 14 HOH E2286  HOH E2287                                          
SITE     1 AC3 18 ARG A 457  HIS E 150  THR E 199  ASN E 202                    
SITE     2 AC3 18 ILE E 203  ALA E 204  VAL E 224  SER E 225                    
SITE     3 AC3 18 ALA E 226  HIS E 297  ILE E 311  SER E 313                    
SITE     4 AC3 18 SER E 315  ASP E 316  HOH E2238  HOH E2289                    
SITE     5 AC3 18 HOH E2290  HOH E2291                                          
CRYST1   48.522  119.390  129.310  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      0.020609  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008376  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007733        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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