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Database: PDB
Entry: 4REW
LinkDB: 4REW
Original site: 4REW 
HEADER    TRANSFERASE                             24-SEP-14   4REW              
TITLE     CRYSTAL STRUCTURE OF THE NON-PHOSPHORYLATED HUMAN ALPHA1 BETA2 GAMMA1 
TITLE    2 HOLO-AMPK COMPLEX                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HUMAN AMPK ALPHA1 SUBUNIT [G11-Q550];                      
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1, ACETYL-COA CARBOXYLASE KINASE, ACACA  
COMPND   6 KINASE, HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE, HMGCR KINASE,    
COMPND   7 TAU-PROTEIN KINASE PRKAA1;                                           
COMPND   8 EC: 2.7.11.1, 2.7.11.27, 2.7.11.31, 2.7.11.26;                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: HUMAN AMPK BETA2 SUBUNIT [A76-I272];                       
COMPND  15 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  19 CHAIN: G;                                                            
COMPND  20 FRAGMENT: HUMAN AMPK GAMMA1 SUBUNIT [S24-G327];                      
COMPND  21 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AMPK1, HUMAN HOLO-AMPK ALPHA1 SUBUNIT, PRKAA1;                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HUMAN HOLO-AMPK BETA2 SUBUNIT, PRKAB2;                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: HUMAN HOLO-AMPK GAMMA1 SUBUNIT, PRKAG1;                        
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    HUMAN ALPHA1 BETA2 GAMMA1 HOLO-AMPK COMPLEX, SERINE/THREONINE PROTEIN 
KEYWDS   2 KINASE, AXIN, CAMKKBETA, LKB1, GLYCOGEN, PHOSPHORYLATION,            
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.E.ZHOU,J.KE,X.LI,L.WANG,X.GU,P.W.DE WAAL,M.H.E.TAN,D.WANG,D.WU,     
AUTHOR   2 H.E.XU,K.MELCHER                                                     
REVDAT   3   11-MAR-15 4REW    1       AUTHOR                                   
REVDAT   2   14-JAN-15 4REW    1       JRNL                                     
REVDAT   1   10-DEC-14 4REW    0                                                
JRNL        AUTH   X.LI,L.WANG,X.E.ZHOU,J.KE,P.W.DE WAAL,X.GU,M.H.TAN,D.WANG,   
JRNL        AUTH 2 D.WU,H.E.XU,K.MELCHER                                        
JRNL        TITL   STRUCTURAL BASIS OF AMPK REGULATION BY ADENINE NUCLEOTIDES   
JRNL        TITL 2 AND GLYCOGEN.                                                
JRNL        REF    CELL RES.                     V.  25    50 2015              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   25412657                                                     
JRNL        DOI    10.1038/CR.2014.150                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 10260                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 729                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.0063 -  7.7873    1.00     1972   179  0.1769 0.2129        
REMARK   3     2  7.7873 -  6.2008    1.00     1903   167  0.2752 0.3157        
REMARK   3     3  6.2008 -  5.4228    1.00     1898   128  0.2907 0.2956        
REMARK   3     4  5.4228 -  4.9296    1.00     1893   140  0.2955 0.3258        
REMARK   3     5  4.9296 -  4.5778    0.99     1865   115  0.2926 0.3026        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.000           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           6661                                  
REMARK   3   ANGLE     :  0.916           9040                                  
REMARK   3   CHIRALITY :  0.036           1014                                  
REMARK   3   PLANARITY :  0.005           1116                                  
REMARK   3   DIHEDRAL  : 18.665           2518                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  61.9453 -38.6445  15.3947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1447 T22:   2.4726                                     
REMARK   3      T33:   2.2666 T12:  -0.0173                                     
REMARK   3      T13:   0.0605 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2236 L22:   5.0648                                     
REMARK   3      L33:   2.0617 L12:  -0.5606                                     
REMARK   3      L13:   0.7321 L23:  -0.4762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:  -0.0897 S13:  -0.2024                       
REMARK   3      S21:   0.2094 S22:   0.0233 S23:   0.2173                       
REMARK   3      S31:  -0.0750 S32:  -0.1555 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  58.2119 -23.3274   8.6703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2311 T22:   2.6010                                     
REMARK   3      T33:   2.1862 T12:  -0.1831                                     
REMARK   3      T13:   0.0448 T23:   0.1153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1963 L22:   1.8942                                     
REMARK   3      L33:   1.8562 L12:  -0.6093                                     
REMARK   3      L13:   0.2168 L23:   1.6169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0894 S12:  -0.2179 S13:  -0.3628                       
REMARK   3      S21:  -0.0440 S22:  -0.2602 S23:  -0.2343                       
REMARK   3      S31:   0.0362 S32:  -0.0967 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain G                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3176 -19.1732 -16.3325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8017 T22:   2.0233                                     
REMARK   3      T33:   2.2113 T12:   0.0832                                     
REMARK   3      T13:  -0.1604 T23:  -0.0857                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3202 L22:   4.2070                                     
REMARK   3      L33:   6.3226 L12:   0.5863                                     
REMARK   3      L13:   0.4323 L23:  -0.8544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0171 S12:  -0.1845 S13:  -0.0707                       
REMARK   3      S21:  -0.1531 S22:   0.0018 S23:   0.6670                       
REMARK   3      S31:   0.1254 S32:  -0.6073 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4REW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087259.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.078                              
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10287                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2Y94                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M N-ACETAMIDO-IMINODIACETIC ACID,    
REMARK 280  PH 6.8, 9% 2-METHYL-2,4-PENTANEDIOL, AND 11.5 MM C-HEGA, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      125.86267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.93133            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.93133            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      125.86267            
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 300 REMARK: HUMAN ALPHA1 BETA2 GAMMA1 HETEROTRIMERIC COMPLEX             
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: 14120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G                               
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     ASP A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     TYR A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     SER A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     MET A   289                                                      
REMARK 465     ILE A   290                                                      
REMARK 465     ASP A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     VAL A   298                                                      
REMARK 465     CYS A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     PHE A   302                                                      
REMARK 465     GLU A   303                                                      
REMARK 465     CYS A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     CYS A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     GLN A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     VAL A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     TYR A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     ILE A   329                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     ASN A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     GLN A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     THR A   473                                                      
REMARK 465     ALA A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     ALA A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     GLY A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 465     ALA A   480                                                      
REMARK 465     THR A   481                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     GLN A   483                                                      
REMARK 465     ARG A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     GLY A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     VAL A   488                                                      
REMARK 465     SER A   489                                                      
REMARK 465     ASN A   490                                                      
REMARK 465     TYR A   491                                                      
REMARK 465     ARG A   492                                                      
REMARK 465     SER A   493                                                      
REMARK 465     CYS A   494                                                      
REMARK 465     GLN A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     ASP A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     ASP A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     LYS A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     VAL A   510                                                      
REMARK 465     SER A   511                                                      
REMARK 465     LEU A   512                                                      
REMARK 465     THR A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     SER A   515                                                      
REMARK 465     VAL A   516                                                      
REMARK 465     THR A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     LEU A   519                                                      
REMARK 465     ASP A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     SER A   522                                                      
REMARK 465     PRO A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     ASP A   525                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     THR A   527                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     ARG B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     VAL B    80                                                      
REMARK 465     ILE B    81                                                      
REMARK 465     ARG B    82                                                      
REMARK 465     TRP B    83                                                      
REMARK 465     SER B    84                                                      
REMARK 465     GLU B    85                                                      
REMARK 465     GLY B    86                                                      
REMARK 465     GLY B    87                                                      
REMARK 465     LYS B    88                                                      
REMARK 465     GLU B    89                                                      
REMARK 465     VAL B    90                                                      
REMARK 465     PHE B    91                                                      
REMARK 465     ILE B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     SER B    95                                                      
REMARK 465     PHE B    96                                                      
REMARK 465     ASN B    97                                                      
REMARK 465     ASN B    98                                                      
REMARK 465     TRP B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     THR B   101                                                      
REMARK 465     LYS B   102                                                      
REMARK 465     ILE B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     LEU B   105                                                      
REMARK 465     ILE B   106                                                      
REMARK 465     LYS B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     HIS B   109                                                      
REMARK 465     ASN B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     PHE B   112                                                      
REMARK 465     VAL B   113                                                      
REMARK 465     ALA B   114                                                      
REMARK 465     ILE B   115                                                      
REMARK 465     LEU B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     LEU B   118                                                      
REMARK 465     PRO B   119                                                      
REMARK 465     GLU B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     HIS B   123                                                      
REMARK 465     GLN B   124                                                      
REMARK 465     TYR B   125                                                      
REMARK 465     LYS B   126                                                      
REMARK 465     PHE B   127                                                      
REMARK 465     PHE B   128                                                      
REMARK 465     VAL B   129                                                      
REMARK 465     ASP B   130                                                      
REMARK 465     GLY B   131                                                      
REMARK 465     GLN B   132                                                      
REMARK 465     TRP B   133                                                      
REMARK 465     VAL B   134                                                      
REMARK 465     HIS B   135                                                      
REMARK 465     ASP B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     SER B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     VAL B   141                                                      
REMARK 465     VAL B   142                                                      
REMARK 465     THR B   143                                                      
REMARK 465     SER B   144                                                      
REMARK 465     GLN B   145                                                      
REMARK 465     LEU B   146                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     THR B   148                                                      
REMARK 465     ILE B   149                                                      
REMARK 465     ASN B   150                                                      
REMARK 465     ASN B   151                                                      
REMARK 465     LEU B   152                                                      
REMARK 465     ILE B   153                                                      
REMARK 465     HIS B   154                                                      
REMARK 465     VAL B   155                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     LYS B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     ASP B   159                                                      
REMARK 465     PHE B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     VAL B   162                                                      
REMARK 465     PHE B   163                                                      
REMARK 465     ASP B   164                                                      
REMARK 465     ALA B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     LEU B   168                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     SER B   170                                                      
REMARK 465     MET B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     CYS B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     ASP B   180                                                      
REMARK 465     LEU B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     PRO B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     GLN B   191                                                      
REMARK 465     GLU B   192                                                      
REMARK 465     MET B   193                                                      
REMARK 465     SER G    23                                                      
REMARK 465     GLY G   325                                                      
REMARK 465     GLY G   326                                                      
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     TRP A 426    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 426    CZ3  CH2                                            
REMARK 470     THR G 286    OG1  CG2                                            
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    PHE A  29      -75.87    -99.53                                   
REMARK 500    LEU A  39      -69.06    -90.92                                   
REMARK 500    THR A  87      149.24   -175.42                                   
REMARK 500    GLU A 117      -61.96    -95.18                                   
REMARK 500    ALA A 158      -78.30   -106.98                                   
REMARK 500    PRO A 280       74.05    -67.28                                   
REMARK 500    LYS A 340     -166.91    -78.75                                   
REMARK 500    GLU A 372      -60.91    -99.99                                   
REMARK 500    HIS A 399      -74.28    -83.15                                   
REMARK 500    ASP A 457     -168.56   -164.71                                   
REMARK 500    ILE A 468     -155.02   -129.20                                   
REMARK 500    ARG A 529      133.43   -174.62                                   
REMARK 500    ALA A 549      -65.41   -105.41                                   
REMARK 500    PHE B 196     -161.22   -112.97                                   
REMARK 500    VAL G  27      -60.86   -121.42                                   
REMARK 500    ARG G  96      -71.77    -57.82                                   
REMARK 500    LYS G  99      -63.85   -121.47                                   
REMARK 500    TYR G 106      -70.61   -134.60                                   
REMARK 500    LEU G 163      -70.02    -96.39                                   
REMARK 500    GLU G 186      -73.22    -95.20                                   
REMARK 500    TYR G 271      -57.48   -121.06                                   
REMARK 500    ASP G 303     -168.69   -127.18                                   
REMARK 500    LEU G 323      -59.27   -126.39                                   
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 STU A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RED   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN AMPK ALPHA1 KD-AID WITH K43A              
REMARK 900 MUTATION                                                             
REMARK 900 RELATED ID: 4RER   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PHOSPHORYLATED HUMAN ALPHA1 BETA2           
REMARK 900 GAMMA1 HOLO-AMPK COMPLEX BOUND TO AMP AND CYCLODEXTRIN               
DBREF  4REW A   11   550  UNP    Q13131   AAPK1_HUMAN     20    559             
DBREF  4REW B   76   272  UNP    O43741   AAKB2_HUMAN     76    272             
DBREF  4REW G   23   326  UNP    P54619   AAKG1_HUMAN     24    327             
SEQADV 4REW SER A   12  UNP  Q13131    ARG    21 CONFLICT                       
SEQADV 4REW SER A  260  UNP  Q13131    THR   269 CONFLICT                       
SEQADV 4REW GLY A  471  UNP  Q13131    GLU   480 ENGINEERED MUTATION            
SEQADV 4REW ALA A  474  UNP  Q13131    GLU   483 ENGINEERED MUTATION            
SEQADV 4REW ALA A  476  UNP  Q13131    LYS   485 ENGINEERED MUTATION            
SEQRES   1 A  540  GLY SER VAL LYS ILE GLY HIS TYR ILE LEU GLY ASP THR          
SEQRES   2 A  540  LEU GLY VAL GLY THR PHE GLY LYS VAL LYS VAL GLY LYS          
SEQRES   3 A  540  HIS GLU LEU THR GLY HIS LYS VAL ALA VAL LYS ILE LEU          
SEQRES   4 A  540  ASN ARG GLN LYS ILE ARG SER LEU ASP VAL VAL GLY LYS          
SEQRES   5 A  540  ILE ARG ARG GLU ILE GLN ASN LEU LYS LEU PHE ARG HIS          
SEQRES   6 A  540  PRO HIS ILE ILE LYS LEU TYR GLN VAL ILE SER THR PRO          
SEQRES   7 A  540  SER ASP ILE PHE MET VAL MET GLU TYR VAL SER GLY GLY          
SEQRES   8 A  540  GLU LEU PHE ASP TYR ILE CYS LYS ASN GLY ARG LEU ASP          
SEQRES   9 A  540  GLU LYS GLU SER ARG ARG LEU PHE GLN GLN ILE LEU SER          
SEQRES  10 A  540  GLY VAL ASP TYR CYS HIS ARG HIS MET VAL VAL HIS ARG          
SEQRES  11 A  540  ASP LEU LYS PRO GLU ASN VAL LEU LEU ASP ALA HIS MET          
SEQRES  12 A  540  ASN ALA LYS ILE ALA ASP PHE GLY LEU SER ASN MET MET          
SEQRES  13 A  540  SER ASP GLY GLU PHE LEU ARG THR SER CYS GLY SER PRO          
SEQRES  14 A  540  ASN TYR ALA ALA PRO GLU VAL ILE SER GLY ARG LEU TYR          
SEQRES  15 A  540  ALA GLY PRO GLU VAL ASP ILE TRP SER SER GLY VAL ILE          
SEQRES  16 A  540  LEU TYR ALA LEU LEU CYS GLY THR LEU PRO PHE ASP ASP          
SEQRES  17 A  540  ASP HIS VAL PRO THR LEU PHE LYS LYS ILE CYS ASP GLY          
SEQRES  18 A  540  ILE PHE TYR THR PRO GLN TYR LEU ASN PRO SER VAL ILE          
SEQRES  19 A  540  SER LEU LEU LYS HIS MET LEU GLN VAL ASP PRO MET LYS          
SEQRES  20 A  540  ARG ALA SER ILE LYS ASP ILE ARG GLU HIS GLU TRP PHE          
SEQRES  21 A  540  LYS GLN ASP LEU PRO LYS TYR LEU PHE PRO GLU ASP PRO          
SEQRES  22 A  540  SER TYR SER SER THR MET ILE ASP ASP GLU ALA LEU LYS          
SEQRES  23 A  540  GLU VAL CYS GLU LYS PHE GLU CYS SER GLU GLU GLU VAL          
SEQRES  24 A  540  LEU SER CYS LEU TYR ASN ARG ASN HIS GLN ASP PRO LEU          
SEQRES  25 A  540  ALA VAL ALA TYR HIS LEU ILE ILE ASP ASN ARG ARG ILE          
SEQRES  26 A  540  MET ASN GLU ALA LYS ASP PHE TYR LEU ALA THR SER PRO          
SEQRES  27 A  540  PRO ASP SER PHE LEU ASP ASP HIS HIS LEU THR ARG PRO          
SEQRES  28 A  540  HIS PRO GLU ARG VAL PRO PHE LEU VAL ALA GLU THR PRO          
SEQRES  29 A  540  ARG ALA ARG HIS THR LEU ASP GLU LEU ASN PRO GLN LYS          
SEQRES  30 A  540  SER LYS HIS GLN GLY VAL ARG LYS ALA LYS TRP HIS LEU          
SEQRES  31 A  540  GLY ILE ARG SER GLN SER ARG PRO ASN ASP ILE MET ALA          
SEQRES  32 A  540  GLU VAL CYS ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP          
SEQRES  33 A  540  LYS VAL VAL ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS          
SEQRES  34 A  540  ASN PRO VAL THR SER THR TYR SER LYS MET SER LEU GLN          
SEQRES  35 A  540  LEU TYR GLN VAL ASP SER ARG THR TYR LEU LEU ASP PHE          
SEQRES  36 A  540  ARG SER ILE ASP ASP GLY ILE THR ALA ALA ALA SER GLY          
SEQRES  37 A  540  THR ALA THR PRO GLN ARG SER GLY SER VAL SER ASN TYR          
SEQRES  38 A  540  ARG SER CYS GLN ARG SER ASP SER ASP ALA GLU ALA GLN          
SEQRES  39 A  540  GLY LYS SER SER GLU VAL SER LEU THR SER SER VAL THR          
SEQRES  40 A  540  SER LEU ASP SER SER PRO VAL ASP LEU THR PRO ARG PRO          
SEQRES  41 A  540  GLY SER HIS THR ILE GLU PHE PHE GLU MET CYS ALA ASN          
SEQRES  42 A  540  LEU ILE LYS ILE LEU ALA GLN                                  
SEQRES   1 B  197  ALA ARG PRO THR VAL ILE ARG TRP SER GLU GLY GLY LYS          
SEQRES   2 B  197  GLU VAL PHE ILE SER GLY SER PHE ASN ASN TRP SER THR          
SEQRES   3 B  197  LYS ILE PRO LEU ILE LYS SER HIS ASN ASP PHE VAL ALA          
SEQRES   4 B  197  ILE LEU ASP LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE          
SEQRES   5 B  197  PHE VAL ASP GLY GLN TRP VAL HIS ASP PRO SER GLU PRO          
SEQRES   6 B  197  VAL VAL THR SER GLN LEU GLY THR ILE ASN ASN LEU ILE          
SEQRES   7 B  197  HIS VAL LYS LYS SER ASP PHE GLU VAL PHE ASP ALA LEU          
SEQRES   8 B  197  LYS LEU ASP SER MET GLU SER SER GLU THR SER CYS ARG          
SEQRES   9 B  197  ASP LEU SER SER SER PRO PRO GLY PRO TYR GLY GLN GLU          
SEQRES  10 B  197  MET TYR ALA PHE ARG SER GLU GLU ARG PHE LYS SER PRO          
SEQRES  11 B  197  PRO ILE LEU PRO PRO HIS LEU LEU GLN VAL ILE LEU ASN          
SEQRES  12 B  197  LYS ASP THR ASN ILE SER CYS ASP PRO ALA LEU LEU PRO          
SEQRES  13 B  197  GLU PRO ASN HIS VAL MET LEU ASN HIS LEU TYR ALA LEU          
SEQRES  14 B  197  SER ILE LYS ASP SER VAL MET VAL LEU SER ALA THR HIS          
SEQRES  15 B  197  ARG TYR LYS LYS LYS TYR VAL THR THR LEU LEU TYR LYS          
SEQRES  16 B  197  PRO ILE                                                      
SEQRES   1 G  304  SER ASN ASN SER VAL TYR THR SER PHE MET LYS SER HIS          
SEQRES   2 G  304  ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS LEU VAL          
SEQRES   3 G  304  VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA PHE PHE          
SEQRES   4 G  304  ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO LEU TRP          
SEQRES   5 G  304  ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU THR ILE          
SEQRES   6 G  304  THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR LYS SER          
SEQRES   7 G  304  ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS LYS ILE          
SEQRES   8 G  304  GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER PHE LYS          
SEQRES   9 G  304  PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU PHE ASP          
SEQRES  10 G  304  ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS ARG LEU          
SEQRES  11 G  304  PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU TYR ILE          
SEQRES  12 G  304  LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS LEU PHE          
SEQRES  13 G  304  ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER LYS SER          
SEQRES  14 G  304  LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN ILE ALA          
SEQRES  15 G  304  MET VAL ARG THR THR THR PRO VAL TYR VAL ALA LEU GLY          
SEQRES  16 G  304  ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO VAL VAL          
SEQRES  17 G  304  ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER LYS PHE          
SEQRES  18 G  304  ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR ASN ASN          
SEQRES  19 G  304  LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS ARG SER          
SEQRES  20 G  304  HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU HIS GLU          
SEQRES  21 G  304  THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU ALA GLU          
SEQRES  22 G  304  VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP VAL VAL          
SEQRES  23 G  304  LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN ALA LEU          
SEQRES  24 G  304  VAL LEU THR GLY GLY                                          
HET    STU  A 601      35                                                       
HET    AMP  G 401      23                                                       
HET    AMP  G 402      23                                                       
HET    AMP  G 403      23                                                       
HETNAM     STU STAUROSPORINE                                                    
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5  AMP    3(C10 H14 N5 O7 P)                                           
HELIX    1   1 ARG A   51  LEU A   57  1                                   7    
HELIX    2   2 GLY A   61  PHE A   73  1                                  13    
HELIX    3   3 GLU A  102  GLY A  111  1                                  10    
HELIX    4   4 ASP A  114  HIS A  135  1                                  22    
HELIX    5   5 GLY A  194  GLY A  212  1                                  19    
HELIX    6   6 PRO A  222  ASP A  230  1                                   9    
HELIX    7   7 ASN A  240  LEU A  251  1                                  12    
HELIX    8   8 SER A  260  HIS A  267  1                                   8    
HELIX    9   9 HIS A  267  GLN A  272  1                                   6    
HELIX   10  10 ASP A  331  LYS A  340  1                                  10    
HELIX   11  11 ARG A  365  ALA A  371  1                                   7    
HELIX   12  12 SER A  406  ILE A  419  1                                  14    
HELIX   13  13 SER A  532  GLN A  550  1                                  19    
HELIX   14  14 PRO B  209  GLN B  214  5                                   6    
HELIX   15  15 VAL G   27  SER G   34  1                                   8    
HELIX   16  16 ARG G   36  LEU G   40  5                                   5    
HELIX   17  17 GLN G   55  GLY G   67  1                                  13    
HELIX   18  18 ILE G   87  TYR G   97  1                                  11    
HELIX   19  19 TYR G  106  HIS G  111  1                                   6    
HELIX   20  20 LYS G  112  LEU G  121  1                                  10    
HELIX   21  21 SER G  136  ASN G  147  1                                  12    
HELIX   22  22 THR G  167  ILE G  179  1                                  13    
HELIX   23  23 SER G  191  GLN G  196  1                                   6    
HELIX   24  24 PRO G  211  HIS G  222  1                                  12    
HELIX   25  25 PHE G  243  VAL G  245  5                                   3    
HELIX   26  26 ILE G  246  GLU G  251  1                                   6    
HELIX   27  27 SER G  260  LEU G  265  1                                   6    
HELIX   28  28 GLN G  266  ARG G  268  5                                   3    
HELIX   29  29 THR G  283  GLU G  295  1                                  13    
HELIX   30  30 LEU G  314  ALA G  320  1                                   7    
SHEET    1   A 4 LYS A  14  ILE A  15  0                                        
SHEET    2   A 4 TYR A  18  ILE A  19 -1  O  TYR A  18   N  ILE A  15           
SHEET    3   A 4 VAL A  32  HIS A  37 -1  O  LYS A  36   N  ILE A  19           
SHEET    4   A 4 THR A  23  GLY A  25 -1  N  LEU A  24   O  VAL A  32           
SHEET    1   B 6 LYS A  14  ILE A  15  0                                        
SHEET    2   B 6 TYR A  18  ILE A  19 -1  O  TYR A  18   N  ILE A  15           
SHEET    3   B 6 VAL A  32  HIS A  37 -1  O  LYS A  36   N  ILE A  19           
SHEET    4   B 6 LYS A  43  ASN A  50 -1  O  VAL A  44   N  GLY A  35           
SHEET    5   B 6 ASP A  90  GLU A  96 -1  O  MET A  95   N  ALA A  45           
SHEET    6   B 6 LEU A  81  GLN A  83 -1  N  GLN A  83   O  VAL A  94           
SHEET    1   C 2 VAL A 137  VAL A 138  0                                        
SHEET    2   C 2 ASN A 164  MET A 165 -1  O  ASN A 164   N  VAL A 138           
SHEET    1   D 2 VAL A 147  LEU A 148  0                                        
SHEET    2   D 2 LYS A 156  ILE A 157 -1  O  LYS A 156   N  LEU A 148           
SHEET    1   E 5 ILE A 402  ARG A 403  0                                        
SHEET    2   E 5 TYR A 461  ARG A 466 -1  O  TYR A 461   N  ARG A 403           
SHEET    3   E 5 SER A 450  GLN A 455 -1  N  TYR A 454   O  LEU A 462           
SHEET    4   E 5 TYR A 433  LYS A 439 -1  N  LEU A 434   O  LEU A 451           
SHEET    5   E 5 TYR A 424  TRP A 426 -1  N  TRP A 426   O  ARG A 435           
SHEET    1   F 5 ILE A 402  ARG A 403  0                                        
SHEET    2   F 5 TYR A 461  ARG A 466 -1  O  TYR A 461   N  ARG A 403           
SHEET    3   F 5 SER A 450  GLN A 455 -1  N  TYR A 454   O  LEU A 462           
SHEET    4   F 5 TYR A 433  LYS A 439 -1  N  LEU A 434   O  LEU A 451           
SHEET    5   F 5 TYR A 446  LYS A 448 -1  O  SER A 447   N  ARG A 438           
SHEET    1   G 6 LEU B 241  LEU B 244  0                                        
SHEET    2   G 6 VAL B 250  ARG B 258 -1  O  SER B 254   N  TYR B 242           
SHEET    3   G 6 TYR B 263  PRO B 271 -1  O  VAL B 264   N  HIS B 257           
SHEET    4   G 6 SER G  44  ASP G  51  1  O  VAL G  49   N  LEU B 267           
SHEET    5   G 6 ALA G  70  ASP G  75  1  O  TRP G  74   N  PHE G  50           
SHEET    6   G 6 SER G  80  THR G  86 -1  O  GLY G  83   N  LEU G  73           
SHEET    1   H 2 LEU G 152  ILE G 155  0                                        
SHEET    2   H 2 THR G 162  LEU G 166 -1  O  LEU G 163   N  VAL G 154           
SHEET    1   I 3 VAL G 206  ARG G 207  0                                        
SHEET    2   I 3 ALA G 226  VAL G 230  1  O  VAL G 230   N  VAL G 206           
SHEET    3   I 3 VAL G 236  SER G 241 -1  O  TYR G 240   N  LEU G 227           
SHEET    1   J 3 LYS G 277  TYR G 279  0                                        
SHEET    2   J 3 ARG G 298  VAL G 302  1  O  VAL G 302   N  CYS G 278           
SHEET    3   J 3 GLY G 310  SER G 313 -1  O  VAL G 312   N  LEU G 299           
CISPEP   1 VAL A  221    PRO A  222          0        -6.63                     
CISPEP   2 ALA B  195    PHE B  196          0        -2.94                     
CISPEP   3 SER B  204    PRO B  205          0         1.22                     
SITE     1 AC1 13 LEU A  24  GLY A  25  GLY A  27  ALA A  45                    
SITE     2 AC1 13 MET A  95  GLU A  96  TYR A  97  VAL A  98                    
SITE     3 AC1 13 GLU A 102  GLU A 145  ASN A 146  LEU A 148                    
SITE     4 AC1 13 ASP A 159                                                     
SITE     1 AC2 10 MET G  84  THR G  86  THR G  88  ASP G  89                    
SITE     2 AC2 10 TYR G 120  LEU G 128  VAL G 129  ILE G 149                    
SITE     3 AC2 10 HIS G 150  ARG G 151                                          
SITE     1 AC3 12 PRO A 363  ARG G  69  LYS G 169  ILE G 239                    
SITE     2 AC3 12 SER G 241  PHE G 243  ASP G 244  ARG G 268                    
SITE     3 AC3 12 LEU G 276  VAL G 296  HIS G 297  ARG G 298                    
SITE     1 AC4 12 HIS G 150  THR G 199  ASN G 202  ALA G 204                    
SITE     2 AC4 12 VAL G 224  SER G 225  ALA G 226  HIS G 297                    
SITE     3 AC4 12 ILE G 311  SER G 313  SER G 315  ASP G 316                    
CRYST1  126.900  126.900  188.794  90.00  90.00 120.00 P 32 2 1      6          
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      0.007880  0.004550  0.000000        0.00000                         
SCALE2      0.000000  0.009099  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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