GenomeNet

Database: PDB
Entry: 4CFH
LinkDB: 4CFH
Original site: 4CFH 
HEADER    TRANSFERASE                             18-NOV-13   4CFH              
TITLE     STRUCTURE OF AN ACTIVE FORM OF MAMMALIAN AMPK                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 13-481;                                           
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1;                                       
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: PROTEASE RECOGNITION SITES WERE ENGINEERED INTO THE   
COMPND   9 ALPHA SUBUNIT AT BOTH ENDS OF A LARGE FLEXIBLE LOOP IN THE C-TERMINAL
COMPND  10 REGION (RESIDUES 470 TO 524), RESIDUES 471 TO 523 WERE REMOVED FROM  
COMPND  11 THE PROTEIN, RESIDUES 523 TO 548 ARE GIVEN AS CHAIN C;               
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: RESIDUES 187-272;                                          
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND  19 CHAIN: C;                                                            
COMPND  20 FRAGMENT: RESIDUES 535-559;                                          
COMPND  21 SYNONYM: AMPK SUBUNIT ALPHA-1;                                       
COMPND  22 EC: 2.7.11.1;                                                        
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 OTHER_DETAILS: PROTEASE RECOGNITION SITES WERE ENGINEERED INTO THE   
COMPND  25 SUBUNIT ALPHA AT BOTH ENDS OF A LARGE FLEXIBLE LOOP IN THE C-TERMINAL
COMPND  26 REGION (RESIDUES 470 AND 524), RESIDUES 471 TO 523 WERE REMOVED FROM 
COMPND  27 THE PROTEIN, RESIDUES 2 TO 470 ARE GIVEN AS CHAIN A;                 
COMPND  28 MOL_ID: 4;                                                           
COMPND  29 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  30 CHAIN: E;                                                            
COMPND  31 SYNONYM: AMPK SUBUNIT ALPHA-1, AMPK GAMMA1, AMPK SUBUNIT GAMMA-1,    
COMPND  32 AMPKG;                                                               
COMPND  33 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;                                        
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  21 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  22 ORGANISM_TAXID: 10116;                                               
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, TRANSFERASE PHOSPHORYLATION, ACTIVE FORM, NUCLEOTIDE-    
KEYWDS   2 BINDING, STAUROSPORINE-BINDING, SERINE/THREONINE-PROTEIN KINASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,M.J.SANDERS,E.UNDERWOOD,R.HEATH,F.MAYER,D.CARMENA,C.JING,      
AUTHOR   2 P.A.WALKER,J.F.ECCLESTON,L.F.HAIRE,P.SAIU,S.A.HOWELL,R.AASLAND,      
AUTHOR   3 S.R.MARTIN,D.CARLING,S.J.GAMBLIN                                     
REVDAT   3   08-MAY-19 4CFH    1       REMARK LINK                              
REVDAT   2   08-JAN-14 4CFH    1       REMARK                                   
REVDAT   1   25-DEC-13 4CFH    0                                                
SPRSDE     25-DEC-13 4CFH      2Y94                                             
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   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.XIAO,M.J.SANDERS,D.CARMENA,N.J.BRIGHT,L.F.HAIRE,           
REMARK   1  AUTH 2 E.UNDERWOOD,B.R.PATEL,R.B.HEATH,P.A.WALKER,S.HALLEN,         
REMARK   1  AUTH 3 F.GIORDANETTO,S.R.MARTIN,D.CARLING,S.J.GAMBLIN               
REMARK   1  TITL   STRUCTURAL BASIS OF AMPK REGULATION BY SMALL MOLECULE        
REMARK   1  TITL 2 ACTIVATORS.                                                  
REMARK   1  REF    NAT.COMMUN.                   V.   4  3017 2013              
REMARK   1  REFN                   ESSN 2041-1723                               
REMARK   1  PMID   24352254                                                     
REMARK   1  DOI    10.1038/NCOMMS4017                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 19619                          
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) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 989                             
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 29.5333 -  6.1817    0.85     2601   132  0.2094 0.2439        
REMARK   3     2  6.1817 -  4.9139    0.93     2679   134  0.2348 0.2903        
REMARK   3     3  4.9139 -  4.2949    0.93     2637   154  0.2104 0.2440        
REMARK   3     4  4.2949 -  3.9032    0.94     2679   131  0.2311 0.2708        
REMARK   3     5  3.9032 -  3.6239    0.95     2669   140  0.2662 0.2823        
REMARK   3     6  3.6239 -  3.4106    0.96     2682   152  0.2893 0.2967        
REMARK   3     7  3.4106 -  3.2400    0.96     2683   146  0.3412 0.3568        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4CFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058999.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18662                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE, PHASER                                         
REMARK 200 STARTING MODEL: PDB ENTRIES 2V8Q AND 2H6D                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY THE HANGING       
REMARK 280  DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 8% ISOPROPANOL       
REMARK 280  AND 5% MPD AS PRECIPITANT IN 0.1M TRIS AT PH 7.5 AT 18 DEGREES.,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.94800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       66.95850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       66.95850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.47400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       66.95850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       66.95850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      106.42200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       66.95850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.95850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.47400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       66.95850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.95850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      106.42200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.94800            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     TYR A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     MET A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     ASP A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     GLU A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     GLU A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     CYS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PHE A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     CYS A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     CYS A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     TYR A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     ASP A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     TPO A   377                                                      
REMARK 465     LEU A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     LEU A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     LYS A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     LEU A   471                                                      
REMARK 465     GLU A   472                                                      
REMARK 465     VAL A   473                                                      
REMARK 465     LEU A   474                                                      
REMARK 465     MET 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     TYR B   194                                                      
REMARK 465     ALA B   195                                                      
REMARK 465     PHE B   196                                                      
REMARK 465     ARG B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLU B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     ARG B   201                                                      
REMARK 465     PHE B   202                                                      
REMARK 465     ILE B   272                                                      
REMARK 465     PHE C   522                                                      
REMARK 465     GLN C   523                                                      
REMARK 465     VAL C   524                                                      
REMARK 465     ALA C   525                                                      
REMARK 465     PRO C   526                                                      
REMARK 465     ARG C   527                                                      
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     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     VAL A 322    CG1  CG2                                            
REMARK 470     TYR A 324    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A 325    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 326    CG   CD1  CD2                                       
REMARK 470     ILE A 327    CG1  CG2  CD1                                       
REMARK 470     ILE A 328    CG1  CG2  CD1                                       
REMARK 470     ASP A 329    CG   OD1  OD2                                       
REMARK 470     ASN A 330    CG   OD1  ND2                                       
REMARK 470     ARG A 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 332    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 333    CG1  CG2  CD1                                       
REMARK 470     MET A 334    CG   SD   CE                                        
REMARK 470     ASN A 335    CG   OD1  ND2                                       
REMARK 470     GLU A 336    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 338    CG   CD   CE   NZ                                   
REMARK 470     ASP A 339    CG   OD1  OD2                                       
REMARK 470     LYS E  99    CG   CD   CE   NZ                                   
REMARK 470     PHE E 182    CG   CD1  CD2  CE1  CE2  CZ                         
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  27      -31.27   -172.35                                   
REMARK 500    CYS A 106      -65.90     58.89                                   
REMARK 500    ASN A 108      175.83     59.55                                   
REMARK 500    ARG A 110     -143.57     51.76                                   
REMARK 500    HIS A 150       31.08    -94.07                                   
REMARK 500    MET A 151       51.49     39.08                                   
REMARK 500    ALA A 156      -79.88   -117.21                                   
REMARK 500    ARG A 171     -122.51     66.12                                   
REMARK 500    TPO A 172      -57.66     65.90                                   
REMARK 500    SER A 173       86.06     60.99                                   
REMARK 500    TYR A 179       -5.25     62.96                                   
REMARK 500    GLN A 235     -103.76     51.25                                   
REMARK 500    PHE A 277      159.40     68.29                                   
REMARK 500    VAL A 322       50.52   -115.01                                   
REMARK 500    ALA A 337       74.88   -104.24                                   
REMARK 500    ARG A 363       40.81   -140.60                                   
REMARK 500    ARG A 373       50.79   -142.86                                   
REMARK 500    PRO A 439       30.25    -76.28                                   
REMARK 500    VAL A 440      -54.71   -135.35                                   
REMARK 500    VAL A 454      -65.10   -101.83                                   
REMARK 500    ARG A 457       28.16   -152.71                                   
REMARK 500    ASN B 239      -19.10     71.46                                   
REMARK 500    ASP B 248      -97.58     56.78                                   
REMARK 500    SER B 249       18.04   -154.70                                   
REMARK 500    LYS B 260     -102.06     52.02                                   
REMARK 500    SER E  26       82.69     99.98                                   
REMARK 500    VAL E  27      -40.17   -156.55                                   
REMARK 500    SER E  44      108.69   -160.14                                   
REMARK 500    TYR E  97       31.55    -97.69                                   
REMARK 500    HIS E 111      119.05   -160.99                                   
REMARK 500    SER E 124       30.77   -166.38                                   
REMARK 500    SER E 159      -37.53     64.18                                   
REMARK 500    PHE E 178       40.58    -99.35                                   
REMARK 500    PRO E 183       42.22    -88.92                                   
REMARK 500    SER E 269     -123.67     52.80                                   
REMARK 500    TYR E 271       58.34   -100.19                                   
REMARK 500    PHE E 272       -9.31   -145.61                                   
REMARK 500    GLU E 273        3.42     55.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E 1325                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E 1326                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STU A 1550                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CFE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FULL LENGTH HUMAN AMPK IN COMPLEX WITH A SMALL          
REMARK 900 MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE ( 991)                
REMARK 900 RELATED ID: 4CFF   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FULL LENGTH HUMAN AMPK IN COMPLEX WITH A SMALL          
REMARK 900 MOLECULE ACTIVATOR, A THIENOPYRIDONE DERIVATIVE ( A-769662)          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 U40819 IN PUBMED. THE 19 RESIDUES (MSHHHHHHSSGLEVLFQGP)AT            
REMARK 999 THE N-TERMINAL ARE EXPRESSION TAG. RESIDUES 471 TO 523 ARE           
REMARK 999 REMOVED TO FAVOUR CRYSTALLIZATION, THE 6 RESIDUES (LEVLFQ)           
REMARK 999 ARE EXPRESSION TAG AT THIS SITE.                                     
REMARK 999 M AT THE N-TERMINAL IS EXPRESSION TAG.                               
DBREF  4CFH A    2   470  UNP    P54645   AAPK1_RAT       13    481             
DBREF  4CFH C  524   548  UNP    P54645   AAPK1_RAT      535    559             
DBREF  4CFH B  187   272  UNP    O43741   AAKB2_HUMAN    187    272             
DBREF  4CFH E    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4CFH MET A  -18  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH SER A  -17  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -16  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -15  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -14  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -13  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -12  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH HIS A  -11  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH SER A  -10  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH SER A   -9  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH GLY A   -8  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH LEU A   -7  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH GLU A   -6  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH VAL A   -5  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH LEU A   -4  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH PHE A   -3  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH GLN A   -2  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH GLY A   -1  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH PRO A    0  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH MET A    1  UNP  P54645              EXPRESSION TAG                 
SEQADV 4CFH LEU A  471  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH GLU A  472  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH VAL A  473  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH LEU A  474  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH PHE C  522  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH GLN C  523  UNP  P54645              SEE REMARK 999                 
SEQADV 4CFH MET B  186  UNP  O43741              EXPRESSION TAG                 
SEQRES   1 A  493  MET SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU          
SEQRES   2 A  493  VAL LEU PHE GLN GLY PRO MET ALA GLU LYS GLN LYS HIS          
SEQRES   3 A  493  ASP GLY ARG VAL LYS ILE GLY HIS TYR ILE LEU GLY ASP          
SEQRES   4 A  493  THR LEU GLY VAL GLY THR PHE GLY LYS VAL LYS VAL GLY          
SEQRES   5 A  493  LYS HIS GLU LEU THR GLY HIS LYS VAL ALA VAL LYS ILE          
SEQRES   6 A  493  LEU ASN ARG GLN LYS ILE ARG SER LEU ASP VAL VAL GLY          
SEQRES   7 A  493  LYS ILE ARG ARG GLU ILE GLN ASN LEU LYS LEU PHE ARG          
SEQRES   8 A  493  HIS PRO HIS ILE ILE LYS LEU TYR GLN VAL ILE SER THR          
SEQRES   9 A  493  PRO SER ASP ILE PHE MET VAL MET GLU TYR VAL SER GLY          
SEQRES  10 A  493  GLY GLU LEU PHE ASP TYR ILE CYS LYS ASN GLY ARG LEU          
SEQRES  11 A  493  ASP GLU LYS GLU SER ARG ARG LEU PHE GLN GLN ILE LEU          
SEQRES  12 A  493  SER GLY VAL ASP TYR CYS HIS ARG HIS MET VAL VAL HIS          
SEQRES  13 A  493  ARG ASP LEU LYS PRO GLU ASN VAL LEU LEU ASP ALA HIS          
SEQRES  14 A  493  MET ASN ALA LYS ILE ALA ASP PHE GLY LEU SER ASN MET          
SEQRES  15 A  493  MET SER ASP GLY GLU PHE LEU ARG TPO SER CYS GLY SER          
SEQRES  16 A  493  PRO ASN TYR ALA ALA PRO GLU VAL ILE SER GLY ARG LEU          
SEQRES  17 A  493  TYR ALA GLY PRO GLU VAL ASP ILE TRP SER SER GLY VAL          
SEQRES  18 A  493  ILE LEU TYR ALA LEU LEU CYS GLY THR LEU PRO PHE ASP          
SEQRES  19 A  493  ASP ASP HIS VAL PRO THR LEU PHE LYS LYS ILE CYS ASP          
SEQRES  20 A  493  GLY ILE PHE TYR THR PRO GLN TYR LEU ASN PRO SER VAL          
SEQRES  21 A  493  ILE SER LEU LEU LYS HIS MET LEU GLN VAL ASP PRO MET          
SEQRES  22 A  493  LYS ARG ALA THR ILE LYS ASP ILE ARG GLU HIS GLU TRP          
SEQRES  23 A  493  PHE LYS GLN ASP LEU PRO LYS TYR LEU PHE PRO GLU ASP          
SEQRES  24 A  493  PRO SER TYR SER SER THR MET ILE ASP ASP GLU ALA LEU          
SEQRES  25 A  493  LYS GLU VAL CYS GLU LYS PHE GLU CYS SER GLU GLU GLU          
SEQRES  26 A  493  VAL LEU SER CYS LEU TYR ASN ARG ASN HIS GLN ASP PRO          
SEQRES  27 A  493  LEU ALA VAL ALA TYR HIS LEU ILE ILE ASP ASN ARG ARG          
SEQRES  28 A  493  ILE MET ASN GLU ALA LYS ASP PHE TYR LEU ALA THR SER          
SEQRES  29 A  493  PRO PRO ASP SER PHE LEU ASP ASP HIS HIS LEU THR ARG          
SEQRES  30 A  493  PRO HIS PRO GLU ARG VAL PRO PHE LEU VAL ALA GLU THR          
SEQRES  31 A  493  PRO ARG ALA ARG HIS TPO LEU ASP GLU LEU ASN PRO GLN          
SEQRES  32 A  493  LYS SER LYS HIS GLN GLY VAL ARG LYS ALA LYS TRP HIS          
SEQRES  33 A  493  LEU GLY ILE ARG SER GLN SER ARG PRO ASN ASP ILE MET          
SEQRES  34 A  493  ALA GLU VAL CYS ARG ALA ILE LYS GLN LEU ASP TYR GLU          
SEQRES  35 A  493  TRP LYS VAL VAL ASN PRO TYR TYR LEU ARG VAL ARG ARG          
SEQRES  36 A  493  LYS ASN PRO VAL THR SER THR PHE SER LYS MET SER LEU          
SEQRES  37 A  493  GLN LEU TYR GLN VAL ASP SER ARG THR TYR LEU LEU ASP          
SEQRES  38 A  493  PHE ARG SER ILE ASP ASP GLU ILE LEU GLU VAL LEU              
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 C   27  PHE GLN VAL ALA PRO ARG PRO GLY SER HIS THR ILE GLU          
SEQRES   2 C   27  PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA          
SEQRES   3 C   27  GLN                                                          
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                                          
MODRES 4CFH TPO A  172  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 172      11                                                       
HET    STU  A1550      35                                                       
HET    AMP  E1325      23                                                       
HET    AMP  E1326      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     STU STAUROSPORINE                                                    
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   5  STU    C28 H26 N4 O3                                                
FORMUL   6  AMP    2(C10 H14 N5 O7 P)                                           
HELIX    1   1 ARG A   49  ARG A   53  1                                   5    
HELIX    2   2 VAL A   57  LEU A   70  1                                  14    
HELIX    3   3 ASP A  112  HIS A  133  1                                  22    
HELIX    4   4 ALA A  181  SER A  186  1                                   6    
HELIX    5   5 GLY A  192  GLY A  210  1                                  19    
HELIX    6   6 HIS A  218  ASP A  228  1                                  11    
HELIX    7   7 ASN A  238  LEU A  249  1                                  12    
HELIX    8   8 THR A  258  GLU A  264  1                                   7    
HELIX    9   9 HIS A  265  GLN A  270  1                                   6    
HELIX   10  10 ALA A  323  ALA A  337  1                                  15    
HELIX   11  11 LYS A  338  TYR A  341  5                                   4    
HELIX   12  12 HIS A  360  ARG A  363  5                                   4    
HELIX   13  13 VAL A  364  THR A  371  1                                   8    
HELIX   14  14 ARG A  405  GLN A  419  1                                  15    
HELIX   15  15 PRO B  209  GLN B  214  5                                   6    
HELIX   16  16 ASN B  234  LEU B  238  5                                   5    
HELIX   17  17 SER C  530  ALA C  547  1                                  18    
HELIX   18  18 VAL E   27  HIS E   35  1                                   9    
HELIX   19  19 CYS E   37  LEU E   40  5                                   4    
HELIX   20  20 GLN E   55  GLY E   67  1                                  13    
HELIX   21  21 THR E   86  TYR E   97  1                                  12    
HELIX   22  22 ILE E  105  GLU E  110  1                                   6    
HELIX   23  23 LYS E  112  ARG E  117  1                                   6    
HELIX   24  24 SER E  136  LYS E  148  1                                  13    
HELIX   25  25 THR E  167  PHE E  178  1                                  12    
HELIX   26  26 GLU E  186  LYS E  190  5                                   5    
HELIX   27  27 SER E  191  GLN E  196  1                                   6    
HELIX   28  28 PRO E  211  HIS E  222  1                                  12    
HELIX   29  29 PHE E  243  VAL E  245  5                                   3    
HELIX   30  30 ILE E  246  GLU E  251  1                                   6    
HELIX   31  31 SER E  260  LEU E  265  1                                   6    
HELIX   32  32 THR E  283  ALA E  294  1                                  12    
HELIX   33  33 LEU E  314  LEU E  323  1                                  10    
SHEET    1  AA 6 LYS A  12  ILE A  13  0                                        
SHEET    2  AA 6 TYR A  16  GLY A  23 -1  O  TYR A  16   N  ILE A  13           
SHEET    3  AA 6 VAL A  30  HIS A  35 -1  O  VAL A  30   N  LEU A  22           
SHEET    4  AA 6 LYS A  41  ASN A  48 -1  O  VAL A  42   N  GLY A  33           
SHEET    5  AA 6 ASP A  88  GLU A  94 -1  O  ILE A  89   N  LEU A  47           
SHEET    6  AA 6 LEU A  79  SER A  84 -1  N  TYR A  80   O  VAL A  92           
SHEET    1  AB 2 VAL A 135  VAL A 136  0                                        
SHEET    2  AB 2 ASN A 162  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1  AC 2 VAL A 145  LEU A 147  0                                        
SHEET    2  AC 2 ALA A 153  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1  AD 7 HIS A 397  LEU A 398  0                                        
SHEET    2  AD 7 TYR B 242  ALA B 243 -1  O  ALA B 243   N  HIS A 397           
SHEET    3  AD 7 MET B 251  TYR B 259 -1  O  SER B 254   N  TYR B 242           
SHEET    4  AD 7 LYS B 262  LYS B 270 -1  O  LYS B 262   N  TYR B 259           
SHEET    5  AD 7 SER E  44  ASP E  51  1  O  SER E  45   N  THR B 265           
SHEET    6  AD 7 ALA E  71  ASP E  75  1  O  PRO E  72   N  PHE E  50           
SHEET    7  AD 7 SER E  80  LEU E  85 -1  O  SER E  80   N  ASP E  75           
SHEET    1  AE 5 ILE A 400  SER A 402  0                                        
SHEET    2  AE 5 TYR A 459  ILE A 466 -1  O  TYR A 459   N  SER A 402           
SHEET    3  AE 5 PHE A 444  GLN A 453 -1  O  LYS A 446   N  ILE A 466           
SHEET    4  AE 5 TYR A 431  LYS A 437 -1  O  LEU A 432   N  LEU A 449           
SHEET    5  AE 5 VAL A 426  ASN A 428 -1  N  VAL A 427   O  TYR A 431           
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           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.34  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.33  
CISPEP   1 GLU A  279    ASP A  280          0         0.41                     
CISPEP   2 SER E  100    ALA E  101          0        -3.28                     
SITE     1 AC1 12 ARG E  69  LYS E 169  ILE E 239  SER E 241                    
SITE     2 AC1 12 PHE E 243  ASP E 244  ARG E 268  VAL E 275                    
SITE     3 AC1 12 LEU E 276  VAL E 296  HIS E 297  ARG E 298                    
SITE     1 AC2 12 HIS E 150  THR E 199  ILE E 203  ALA E 204                    
SITE     2 AC2 12 VAL E 224  SER E 225  ALA E 226  HIS E 297                    
SITE     3 AC2 12 ILE E 311  SER E 313  SER E 315  ASP E 316                    
SITE     1 AC3 16 LEU A  22  GLY A  23  VAL A  24  GLY A  25                    
SITE     2 AC3 16 ALA A  43  LYS A  45  MET A  93  GLU A  94                    
SITE     3 AC3 16 TYR A  95  VAL A  96  GLY A  99  GLU A 100                    
SITE     4 AC3 16 GLU A 143  ASN A 144  LEU A 146  ASP A 157                    
CRYST1  133.917  133.917  141.896  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007467  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007047        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system