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Database: PDB
Entry: 2YA3
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HEADER    TRANSFERASE                             17-FEB-11   2YA3              
TITLE     STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK IN COMPLEX     
TITLE    2 WITH COUMARIN 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 407-555;                                          
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1;                                       
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: THE RESIDUES FROM A 393-395 AND 545-550 ARE           
COMPND   9  ARTIFICIAL AS A RESULT OF CLONING STRATEGY;                         
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: RESIDUES 187-272;                                          
COMPND  14 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  18 CHAIN: E;                                                            
COMPND  19 FRAGMENT: RESIDUES 1-330;                                            
COMPND  20 SYNONYM: AMPK SUBUNIT ALPHA-1, AMPK GAMMA1, AMPK SUBUNIT GAMMA-1,    
COMPND  21  AMPKG;                                                              
COMPND  22 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, NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN KINASE,     
KEYWDS   2 PHOSPHORYLATION                                                      
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   2   20-APR-11 2YA3    1       JRNL   REMARK                            
REVDAT   1   16-MAR-11 2YA3    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.19                          
REMARK   3   NUMBER OF REFLECTIONS             : 25251                          
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) : 0.22463                         
REMARK   3   R VALUE            (WORKING SET) : 0.22264                         
REMARK   3   FREE R VALUE                     : 0.26271                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1345                            
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) : 2.512                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.577                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1826                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.304                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.348                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3805                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 113                                     
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.337                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.85                                                
REMARK   3    B22 (A**2) : 2.66                                                 
REMARK   3    B33 (A**2) : 0.19                                                 
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): 0.383         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.270         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.976        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4011 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5455 ; 1.230 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   465 ; 5.668 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;37.698 ;23.212       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   704 ;15.892 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;19.476 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   630 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2910 ; 0.006 ; 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):  2354 ; 0.434 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3850 ; 0.806 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1657 ; 0.833 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1605 ; 1.489 ; 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   394        A   469                          
REMARK   3    RESIDUE RANGE :   A   524        A   549                          
REMARK   3    RESIDUE RANGE :   B   190        B   219                          
REMARK   3    RESIDUE RANGE :   B   235        B   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1300 -16.0270  49.8510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0595 T22:   0.0801                                     
REMARK   3      T33:   0.0577 T12:   0.0176                                     
REMARK   3      T13:   0.0262 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8093 L22:   2.3232                                     
REMARK   3      L33:   4.3925 L12:   0.9843                                     
REMARK   3      L13:  -0.5218 L23:  -2.7314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:  -0.0155 S13:   0.0274                       
REMARK   3      S21:  -0.0458 S22:  -0.1263 S23:  -0.0611                       
REMARK   3      S31:   0.1580 S32:   0.1149 S33:   0.1323                       
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):  11.3040   2.0100  32.8810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0427 T22:   0.2520                                     
REMARK   3      T33:   0.1368 T12:  -0.0237                                     
REMARK   3      T13:  -0.0445 T23:   0.1104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5367 L22:   0.1814                                     
REMARK   3      L33:   0.7975 L12:   0.6923                                     
REMARK   3      L13:  -1.8860 L23:  -0.3180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1098 S12:  -0.2429 S13:   0.0939                       
REMARK   3      S21:   0.0698 S22:  -0.1015 S23:  -0.0653                       
REMARK   3      S31:  -0.0659 S32:   0.1415 S33:  -0.0083                       
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    25        E    47                          
REMARK   3    RESIDUE RANGE :   E   129        E   183                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0260  11.9200  30.2180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0441 T22:   0.0976                                     
REMARK   3      T33:   0.0907 T12:   0.0296                                     
REMARK   3      T13:   0.0265 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7699 L22:   2.6707                                     
REMARK   3      L33:   2.4966 L12:  -0.3119                                     
REMARK   3      L13:   0.2964 L23:  -1.3430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:  -0.0359 S13:   0.1000                       
REMARK   3      S21:   0.1994 S22:   0.1264 S23:   0.1826                       
REMARK   3      S31:  -0.3190 S32:  -0.1331 S33:  -0.1315                       
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   324                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6620  18.1690  10.5650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0290 T22:   0.0724                                     
REMARK   3      T33:   0.0595 T12:  -0.0314                                     
REMARK   3      T13:  -0.0358 T23:   0.0502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2010 L22:   2.3088                                     
REMARK   3      L33:   2.6380 L12:  -0.2263                                     
REMARK   3      L13:  -0.8188 L23:  -0.8942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:   0.1193 S13:   0.1492                       
REMARK   3      S21:  -0.0748 S22:   0.0209 S23:   0.1215                       
REMARK   3      S31:  -0.1204 S32:   0.0606 S33:  -0.0118                       
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  1325        E  1327                          
REMARK   3    RESIDUE RANGE :   A  2001        A  2032                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2020                          
REMARK   3    RESIDUE RANGE :   E  2001        E  2090                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2100   3.5000  16.3960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0225 T22:   0.1655                                     
REMARK   3      T33:   0.1365 T12:  -0.0035                                     
REMARK   3      T13:  -0.0137 T23:   0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3658 L22:   0.7686                                     
REMARK   3      L33:   1.3233 L12:   0.2669                                     
REMARK   3      L13:  -0.3829 L23:  -0.7284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0436 S12:   0.0604 S13:  -0.0760                       
REMARK   3      S21:  -0.1094 S22:  -0.1062 S23:  -0.0844                       
REMARK   3      S31:   0.0750 S32:   0.1593 S33:   0.1498                       
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 2YA3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-47410.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25251                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.6                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.26                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.00                               
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   (%): 57                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
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       24.47150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.65750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.65750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.47150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.03000            
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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     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     SER A   393                                                      
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     ASN A   550                                                      
REMARK 465     MET B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     ASP B   220                                                      
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     PRO B   233                                                      
REMARK 465     ASN B   234                                                      
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     SER E    23                                                      
REMARK 465     ASN E    24                                                      
REMARK 465     GLY E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLU E   327                                                      
REMARK 465     LYS E   328                                                      
REMARK 465     LYS E   329                                                      
REMARK 465     PRO E   330                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR E 271    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU E 273    CG   CD   OE1  OE2                                  
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 468     -163.59    -73.65                                   
REMARK 500    GLU B 199      -59.77     63.39                                   
REMARK 500    ASN B 239       -7.18     76.80                                   
REMARK 500    LYS B 260     -114.30     50.63                                   
REMARK 500    GLU E 107      -63.51   -122.45                                   
REMARK 500    LEU E 121      -71.21   -131.54                                   
REMARK 500    GLN E 122       81.17     46.17                                   
REMARK 500    SER E 124      111.79    -35.62                                   
REMARK 500    PRO E 183       68.51     29.12                                   
REMARK 500    LYS E 252       46.12    -75.46                                   
REMARK 500    THR E 253      -98.56    -66.40                                   
REMARK 500    TYR E 254      -19.90     58.38                                   
REMARK 500    GLU E 273      -70.01    -73.65                                   
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 PHE E  182     PRO E  183                 -134.67                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: 3'-(7-DIETHYLAMINOCOUMARIN-3-CARBONYLAMINO)           
REMARK 630 -3'-DEOXY-ADP                                                        
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     J7V E  1325                                                      
REMARK 630     J7V E  1326                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 SUBCOMP: ADP CNW                                                     
REMARK 630 STRUCTURE DETAILS: NULL                                              
REMARK 630 OTHER DETAILS: NULL                                                  
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J7V E1325                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J7V E1326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1327                 
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: 2Y94   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF AN ACTIVE FORM OF MAMMALIAN AMPK                       
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: 2Y8Q   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK              
REMARK 900  IN COMPLEX WITH ONE ADP                                             
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 PROTEIN SEQUENCE HAS HIS-TAG MSHHHHHHSGLVPRG AT THE N-           
REMARK 999 TERMINAL, AND SMA 393-395 AND NSCTVN 545-550 ARE CLONING             
REMARK 999 ARTIFACTS. B 186 METHIONINE IS AN ARTIFACT, CREATED BY CLONING.      
DBREF  2YA3 A  396   544  UNP    P54645   AAPK1_RAT      407    555             
DBREF  2YA3 B  187   272  UNP    O43741   AAKB2_HUMAN    187    272             
DBREF  2YA3 E    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 2YA3 MET A  378  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 SER A  379  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  380  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  381  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  382  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  383  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  384  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 HIS A  385  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 SER A  386  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 GLY A  387  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 LEU A  388  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 VAL A  389  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 PRO A  390  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 ARG A  391  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 GLY A  392  UNP  P54645              EXPRESSION TAG                 
SEQADV 2YA3 SER A  393  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 MET A  394  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 ALA A  395  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 ASN A  545  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 SER A  546  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 CYS A  547  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 THR A  548  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 VAL A  549  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 ASN A  550  UNP  P54645              CLONING ARTIFACT               
SEQADV 2YA3 MET B  186  UNP  O43741              CLONING ARTIFACT               
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    J7V  E1325      45                                                       
HET    J7V  E1326      45                                                       
HET    AMP  E1327      23                                                       
HETNAM     J7V 3'-(7-DIETHYLAMINOCOUMARIN-3-CARBONYLAMINO)-3'-DEOXY-ADP         
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   5  J7V    2(C24 H29 N7 O12 P2)                                         
FORMUL   6  HOH   *142(H2 O)                                                    
FORMUL   4  AMP    C10 H14 N5 O7 P                                              
FORMUL   6  HOH   *142(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 GLU B  199  LYS B  203  5                                   5    
HELIX    4   4 SER E   26  SER E   34  1                                   9    
HELIX    5   5 CYS E   37  ILE E   41  5                                   5    
HELIX    6   6 GLN E   55  GLY E   67  1                                  13    
HELIX    7   7 ILE E   87  LEU E  102  1                                  16    
HELIX    8   8 GLU E  107  HIS E  111  5                                   5    
HELIX    9   9 LYS E  112  LEU E  121  1                                  10    
HELIX   10  10 SER E  136  LYS E  148  1                                  13    
HELIX   11  11 THR E  167  ILE E  179  1                                  13    
HELIX   12  12 PRO E  185  LYS E  190  5                                   6    
HELIX   13  13 SER E  191  GLN E  196  1                                   6    
HELIX   14  14 PRO E  211  ARG E  223  1                                  13    
HELIX   15  15 LYS E  242  GLU E  251  1                                  10    
HELIX   16  16 SER E  260  LEU E  265  1                                   6    
HELIX   17  17 GLN E  266  SER E  269  5                                   4    
HELIX   18  18 THR E  283  GLU E  295  1                                  13    
HELIX   19  19 LEU E  314  THR E  324  1                                  11    
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 THR A 458  SER A 465 -1  O  TYR A 459   N  SER A 402           
SHEET    3  AA 5 PHE A 444  ASP A 455 -1  O  SER A 448   N  ARG A 464           
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           
CISPEP   1 ASN B  218    LYS B  219          0        14.03                     
CISPEP   2 ASP E  123    SER E  124          0        14.38                     
SITE     1 AC1 17 MET E  84  THR E  86  THR E  88  ASP E  89                    
SITE     2 AC1 17 ASN E  92  ARG E  96  TYR E 120  LYS E 126                    
SITE     3 AC1 17 LEU E 128  VAL E 129  ILE E 149  HIS E 150                    
SITE     4 AC1 17 ARG E 151  PRO E 153  LYS E 242  HOH E2014                    
SITE     5 AC1 17 HOH E2018                                                     
SITE     1 AC2 15 ARG E  69  LYS E 169  SER E 225  SER E 241                    
SITE     2 AC2 15 LYS E 242  PHE E 243  GLY E 274  VAL E 275                    
SITE     3 AC2 15 LEU E 276  VAL E 296  HIS E 297  ARG E 298                    
SITE     4 AC2 15 HOH E2066  HOH E2087  HOH E2088                               
SITE     1 AC3 15 ARG A 457  HIS E 150  THR E 199  ILE E 203                    
SITE     2 AC3 15 ALA E 204  VAL E 224  SER E 225  ALA E 226                    
SITE     3 AC3 15 HIS E 297  ILE E 311  SER E 313  SER E 315                    
SITE     4 AC3 15 ASP E 316  HOH E2089  HOH E2090                               
CRYST1   48.943  124.060  125.315  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      0.020432  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008061  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007980        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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