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Database: PDB
Entry: 2V9J
LinkDB: 2V9J
Original site: 2V9J 
HEADER    TRANSFERASE                             23-AUG-07   2V9J              
TITLE     CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN             
TITLE    2 AMPK IN COMPLEXES WITH MG.ATP-AMP                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC                  
COMPND   3  SUBUNIT ALPHA-1;                                                    
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: RESIDUES 396-548;                                          
COMPND   6 SYNONYM: AMPK ALPHA-1 CHAIN, AMP-ACTIVATED PROTEIN KINASE;           
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RESIDUES 187-272;                                          
COMPND  13 SYNONYM: AMPK BETA-2 CHAIN, AMP-ACTIVATED PROTEIN KINASE;            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  17 CHAIN: E;                                                            
COMPND  18 SYNONYM: AMPK GAMMA-1 CHAIN, AMPKG, AMP-ACTIVATED PROTEIN            
COMPND  19  KINASE;                                                             
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: 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: RAT;                                                
SOURCE  16 ORGANISM_TAXID: 10116;                                               
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATP-BINDING, POLYMORPHISM, METAL-BINDING,                             
KEYWDS   2 SERINE/THREONINE-PROTEIN KINASE, KINASE, MAGNESIUM, CBS              
KEYWDS   3 DOMAIN, TRANSFERASE, STEROL BIOSYNTHESIS, STEROID                    
KEYWDS   4 BIOSYNTHESIS, FATTY ACID BIOSYNTHESIS, CHOLESTEROL                   
KEYWDS   5 BIOSYNTHESIS, LIPID SYNTHESIS, PHOSPHORYLATION,                      
KEYWDS   6 NUCLEOTIDE-BINDING                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,P.A.WALKER,           
AUTHOR   2 L.HAIRE,J.F.ECCLESTON,C.T.DAVIS,S.R.MARTIN,D.CARLING,                
AUTHOR   3 S.J.GAMBLIN                                                          
REVDAT   3   24-FEB-09 2V9J    1       VERSN                                    
REVDAT   2   02-OCT-07 2V9J    1       JRNL                                     
REVDAT   1   25-SEP-07 2V9J    0                                                
JRNL        AUTH   B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,             
JRNL        AUTH 2 P.A.WALKER,L.HAIRE,J.F.ECCLESTON,C.T.DAVIS,                  
JRNL        AUTH 3 S.R.MARTIN,D.CARLING,S.J.GAMBLIN                             
JRNL        TITL   STRUCTURAL BASIS FOR AMP BINDING TO MAMMALIAN AMP-           
JRNL        TITL 2 ACTIVATED PROTEIN KINASE                                     
JRNL        REF    NATURE                        V. 449   496 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17851531                                                     
JRNL        DOI    10.1038/NATURE06161                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25861                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3885                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. THE FIRST FOUR RESIDUES (GSMA) OF THE             
REMARK   3  SEQUENCE OF CHAIN A ARE GENERATED FROM THE POST HIS-TAG             
REMARK   3  CLEAVAGE THE FIRST RESIDUES (M) OF THE SEQUENCE OF CHAIN B IS       
REMARK   3  GENERATED BY THE WAY IT WAS CLONED INTO THE VECTOR                  
REMARK   4                                                                      
REMARK   4 2V9J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33573.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : MULTIWIRE                          
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25861                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.53                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 6.0                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2OOX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 61.83                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.39500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.53450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.34250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.53450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.39500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.34250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 7220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   392                                                      
REMARK 465     ILE A   470                                                      
REMARK 465     THR A   471                                                      
REMARK 465     GLU A   472                                                      
REMARK 465     ALA A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     THR A   477                                                      
REMARK 465     ALA A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     ARG A   482                                                      
REMARK 465     SER A   483                                                      
REMARK 465     GLY A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     ILE A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     ASN A   488                                                      
REMARK 465     TYR A   489                                                      
REMARK 465     ARG A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     CYS A   492                                                      
REMARK 465     GLN A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     ASP A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     ASP A   498                                                      
REMARK 465     ALA A   499                                                      
REMARK 465     GLU A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     LYS A   504                                                      
REMARK 465     PRO A   505                                                      
REMARK 465     SER A   506                                                      
REMARK 465     GLU A   507                                                      
REMARK 465     VAL A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     LEU A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     VAL A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     ASP A   518                                                      
REMARK 465     SER A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     VAL A   522                                                      
REMARK 465     ASP A   523                                                      
REMARK 465     MET B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     CYS B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     PRO B   227                                                      
REMARK 465     ALA B   228                                                      
REMARK 465     LEU B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     PRO B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     GLU E     7                                                      
REMARK 465     SER E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     PRO E    10                                                      
REMARK 465     ALA E    11                                                      
REMARK 465     PRO E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     ASN E    14                                                      
REMARK 465     GLU E    15                                                      
REMARK 465     HIS E    16                                                      
REMARK 465     SER E    17                                                      
REMARK 465     GLN E    18                                                      
REMARK 465     GLU E    19                                                      
REMARK 465     THR E    20                                                      
REMARK 465     PRO E    21                                                      
REMARK 465     GLU E    22                                                      
REMARK 465     GLU E   327                                                      
REMARK 465     LYS E   328                                                      
REMARK 465     LYS E   329                                                      
REMARK 465     PRO E   330                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A 394      -74.75    -80.38                                   
REMARK 500    ARG A 527      177.80     56.69                                   
REMARK 500    SER A 530      114.94   -161.95                                   
REMARK 500    LEU A 546      -12.22   -147.00                                   
REMARK 500    GLU B 199      168.99     59.71                                   
REMARK 500    GLU B 200     -149.54     43.49                                   
REMARK 500    ARG B 201      -46.61     51.07                                   
REMARK 500    LYS B 203      -72.55    -70.65                                   
REMARK 500    LEU B 208      -89.42    -65.47                                   
REMARK 500    PRO B 209       90.03    -47.93                                   
REMARK 500    HIS B 211       17.69   -158.70                                   
REMARK 500    ASN B 218       57.12   -118.35                                   
REMARK 500    LYS B 219      -76.50    -63.01                                   
REMARK 500    ASP B 220      -15.63     62.25                                   
REMARK 500    THR B 221       43.86     77.95                                   
REMARK 500    HIS B 235      -90.42    -81.28                                   
REMARK 500    ASN B 239       -3.30     74.38                                   
REMARK 500    LYS B 260     -107.03     48.09                                   
REMARK 500    SER E  25      -42.57     90.24                                   
REMARK 500    SER E  26      141.28     67.64                                   
REMARK 500    LEU E 121       32.85    -69.34                                   
REMARK 500    GLN E 122     -112.48    -34.28                                   
REMARK 500    TYR E 164      153.29    174.72                                   
REMARK 500    GLU E 181      136.20    143.69                                   
REMARK 500    THR E 208      -49.08    -22.22                                   
REMARK 500    ARG E 223       78.00     51.21                                   
REMARK 500    LYS E 252       31.58    -90.51                                   
REMARK 500    THR E 253      -58.68   -129.64                                   
REMARK 500    TYR E 254      -21.71     84.88                                   
REMARK 500    ASN E 256       42.03    -79.87                                   
REMARK 500    HIS E 270      161.71     78.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  208     PRO B  209                 -149.24                    
REMARK 500 PHE E  182     PRO E  183                  133.45                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE E 182        20.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1330  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E1327   O2B                                                    
REMARK 620 2 HOH E2074   O    98.3                                              
REMARK 620 3 ATP E1327   O1G  97.4 134.2                                        
REMARK 620 4 HOH E2077   O   163.2  94.2  81.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1331  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E1328   O1G                                                    
REMARK 620 2 HOH E2078   O    74.6                                              
REMARK 620 3 ATP E1328   O2B 100.0 147.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1330                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1331                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2V92   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT                        
REMARK 900  OF MAMMALIAN AMPK IN COMPLEXES WITH ATP-                            
REMARK 900  AMP                                                                 
REMARK 900 RELATED ID: 2V8Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT                        
REMARK 900  OF MAMMALIAN AMPK IN COMPLEXES WITH AMP                             
REMARK 900 RELATED ID: 2F15   RELATED DB: PDB                                   
REMARK 900  GLYCOGEN-BINDING DOMAIN OF THE AMP-ACTIVATED                        
REMARK 900   PROTEIN KINASEBETA2 SUBUNIT                                        
DBREF  2V9J A  392   395  PDB    2V9J     2V9J           392    395             
DBREF  2V9J A  396   548  UNP    P54645   AAPK1_RAT      396    548             
DBREF  2V9J B  186   186  PDB    2V9J     2V9J           186    186             
DBREF  2V9J B  187   272  UNP    O43741   AAKB2_HUMAN    187    272             
DBREF  2V9J E    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQRES   1 A  157  GLY SER MET ALA TRP HIS LEU GLY ILE ARG SER GLN SER          
SEQRES   2 A  157  ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA ILE          
SEQRES   3 A  157  LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO TYR          
SEQRES   4 A  157  TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER THR          
SEQRES   5 A  157  PHE SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP SER          
SEQRES   6 A  157  ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP GLU          
SEQRES   7 A  157  ILE THR GLU ALA LYS SER GLY THR ALA THR PRO GLN ARG          
SEQRES   8 A  157  SER GLY SER ILE SER ASN TYR ARG SER CYS GLN ARG SER          
SEQRES   9 A  157  ASP SER ASP ALA GLU ALA GLN GLY LYS PRO SER GLU VAL          
SEQRES  10 A  157  SER LEU THR SER SER VAL THR SER LEU ASP SER SER PRO          
SEQRES  11 A  157  VAL ASP VAL ALA PRO ARG PRO GLY SER HIS THR ILE GLU          
SEQRES  12 A  157  PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA          
SEQRES  13 A  157  GLN                                                          
SEQRES   1 B   87  MET GLY PRO TYR GLY GLN GLU MET TYR ALA PHE ARG SER          
SEQRES   2 B   87  GLU GLU ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS          
SEQRES   3 B   87  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR ASN ILE SER          
SEQRES   4 B   87  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES   5 B   87  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP SER VAL          
SEQRES   6 B   87  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES   7 B   87  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 E  330  MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU          
SEQRES   2 E  330  ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER          
SEQRES   3 E  330  VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP          
SEQRES   4 E  330  LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR          
SEQRES   5 E  330  SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR          
SEQRES   6 E  330  ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS          
SEQRES   7 E  330  GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE          
SEQRES   8 E  330  ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN          
SEQRES   9 E  330  ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG          
SEQRES  10 E  330  GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS          
SEQRES  11 E  330  ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER          
SEQRES  12 E  330  LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP          
SEQRES  13 E  330  PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS          
SEQRES  14 E  330  ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE          
SEQRES  15 E  330  PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU          
SEQRES  16 E  330  GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR          
SEQRES  17 E  330  THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN          
SEQRES  18 E  330  HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY          
SEQRES  19 E  330  ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN          
SEQRES  20 E  330  LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER          
SEQRES  21 E  330  VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU          
SEQRES  22 E  330  GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA          
SEQRES  23 E  330  ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU          
SEQRES  24 E  330  VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL          
SEQRES  25 E  330  SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY          
SEQRES  26 E  330  GLY GLU LYS LYS PRO                                          
HET    ATP  E1327      31                                                       
HET    ATP  E1328      31                                                       
HET    AMP  E1329      23                                                       
HET     MG  E1330       1                                                       
HET     MG  E1331       1                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   4  AMP    C10 H14 N5 O7 P                                              
FORMUL   5  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *142(H2 O1)                                                   
HELIX    1   1 ARG A  405  LEU A  420  1                                  16    
HELIX    2   2 SER A  530  ILE A  545  1                                  16    
HELIX    3   3 SER E   26  SER E   34  1                                   9    
HELIX    4   4 CYS E   37  ILE E   41  5                                   5    
HELIX    5   5 GLN E   55  GLY E   67  1                                  13    
HELIX    6   6 ILE E   87  VAL E  103  1                                  17    
HELIX    7   7 GLU E  107  HIS E  111  5                                   5    
HELIX    8   8 LYS E  112  LEU E  121  1                                  10    
HELIX    9   9 SER E  136  LYS E  148  1                                  13    
HELIX   10  10 THR E  167  THR E  180  1                                  14    
HELIX   11  11 PRO E  185  LYS E  190  5                                   6    
HELIX   12  12 SER E  191  GLN E  196  1                                   6    
HELIX   13  13 PRO E  211  ARG E  223  1                                  13    
HELIX   14  14 PHE E  243  ALA E  250  5                                   8    
HELIX   15  15 SER E  260  HIS E  267  1                                   8    
HELIX   16  16 THR E  283  GLU E  295  1                                  13    
HELIX   17  17 LEU E  314  LEU E  323  1                                  10    
SHEET    1  BA 8 VAL B 215  LEU B 217  0                                        
SHEET    2  BA 8 ALA A 395  LEU A 398 -1  O  TRP A 396   N  ILE B 216           
SHEET    3  BA 8 TYR B 242  LYS B 247 -1  O  ALA B 243   N  HIS A 397           
SHEET    4  BA 8 VAL B 250  TYR B 259 -1  O  VAL B 250   N  LYS B 247           
SHEET    5  BA 8 LYS B 262  PRO B 271 -1  O  LYS B 262   N  TYR B 259           
SHEET    6  BA 8 SER E  44  ASP E  51  1  O  SER E  45   N  THR B 265           
SHEET    7  BA 8 ALA E  70  ASP E  75  1  O  PRO E  72   N  PHE E  50           
SHEET    8  BA 8 SER E  80  THR E  86 -1  O  SER E  80   N  ASP E  75           
SHEET    1  AA 5 ILE A 400  SER A 402  0                                        
SHEET    2  AA 5 TYR A 459  ILE A 466 -1  O  TYR A 459   N  SER A 402           
SHEET    3  AA 5 PHE A 444  GLN A 453 -1  O  LYS A 446   N  ILE A 466           
SHEET    4  AA 5 TYR A 431  LYS A 437 -1  O  LEU A 432   N  LEU A 449           
SHEET    5  AA 5 GLU A 423  ASN A 428 -1  O  GLU A 423   N  ARG A 435           
SHEET    1  EA 2 LEU E 152  ILE E 155  0                                        
SHEET    2  EA 2 THR E 162  LEU E 166 -1  N  LEU E 163   O  VAL E 154           
SHEET    1  EB 3 VAL E 206  ARG E 207  0                                        
SHEET    2  EB 3 ALA E 226  VAL E 230  1  O  PRO E 228   N  VAL E 206           
SHEET    3  EB 3 VAL E 236  SER E 241 -1  N  VAL E 237   O  VAL E 229           
SHEET    1  EC 3 LYS E 277  TYR E 279  0                                        
SHEET    2  EC 3 ARG E 298  VAL E 302  1  O  VAL E 300   N  CYS E 278           
SHEET    3  EC 3 VAL E 308  SER E 313 -1  N  LYS E 309   O  VAL E 301           
LINK        MG    MG E1330                 O2B ATP E1327     1555   1555  2.08  
LINK        MG    MG E1330                 O   HOH E2074     1555   1555  1.97  
LINK        MG    MG E1330                 O1G ATP E1327     1555   1555  2.07  
LINK        MG    MG E1330                 O   HOH E2077     1555   1555  2.13  
LINK        MG    MG E1331                 O   HOH E2078     1555   1555  2.09  
LINK        MG    MG E1331                 O2B ATP E1328     1555   1555  2.09  
LINK        MG    MG E1331                 O1G ATP E1328     1555   1555  2.08  
SITE     1 AC1 21 ARG E  69  ARG E 151  LYS E 169  ILE E 239                    
SITE     2 AC1 21 SER E 241  PHE E 243  ASP E 244  ARG E 268                    
SITE     3 AC1 21 PHE E 272  VAL E 275  LEU E 276  VAL E 296                    
SITE     4 AC1 21 HIS E 297  ARG E 298  LEU E 314   MG E1330                    
SITE     5 AC1 21 HOH E2074  HOH E2075  HOH E2076  HOH E2077                    
SITE     6 AC1 21 HOH E2078                                                     
SITE     1 AC2 17 MET E  84  THR E  86  ILE E  87  THR E  88                    
SITE     2 AC2 17 ASP E  89  PRO E 127  LEU E 128  VAL E 129                    
SITE     3 AC2 17 ILE E 149  HIS E 150  ARG E 151  PRO E 153                    
SITE     4 AC2 17 SER E 225  LYS E 242   MG E1331  HOH E2078                    
SITE     5 AC2 17 HOH E2079                                                     
SITE     1 AC3 15 ARG A 457  HIS E 150  THR E 199  ILE E 203                    
SITE     2 AC3 15 ALA E 204  VAL E 224  SER E 225  ALA E 226                    
SITE     3 AC3 15 HIS E 297  ILE E 311  SER E 313  SER E 315                    
SITE     4 AC3 15 ASP E 316  HOH E2079  HOH E2080                               
SITE     1 AC4  4 LYS E 169  ATP E1327  HOH E2074  HOH E2077                    
SITE     1 AC5  3 ILE E  87  ATP E1328  HOH E2078                               
CRYST1   48.790  120.685  127.069  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020496  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008286  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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