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Database: PDB
Entry: 4RER
LinkDB: 4RER
Original site: 4RER 
HEADER    TRANSFERASE                             23-SEP-14   4RER              
TITLE     CRYSTAL STRUCTURE OF THE PHOSPHORYLATED HUMAN ALPHA1 BETA2 GAMMA1     
TITLE    2 HOLO-AMPK COMPLEX BOUND TO AMP AND CYCLODEXTRIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HUMAN AMPK ALPHA1 SUBUNIT [G11-Q550];                      
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1, ACETYL-COA CARBOXYLASE KINASE, ACACA  
COMPND   6 KINASE, HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE, HMGCR KINASE,    
COMPND   7 TAU-PROTEIN KINASE PRKAA1;                                           
COMPND   8 EC: 2.7.11.1, 2.7.11.27, 2.7.11.31, 2.7.11.26;                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: HUMAN AMPK BETA2 SUBUNIT [A76-I272];                       
COMPND  15 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  19 CHAIN: G;                                                            
COMPND  20 FRAGMENT: HUMAN AMPK GAMMA1 SUBUNIT [S24-G327];                      
COMPND  21 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AMPK1, HUMAN HOLO-AMPK ALPHA1 SUBUNIT, PRKAA1;                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HUMAN HOLO-AMPK BETA2 SUBUNIT, PRKAB2;                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: HUMAN HOLO-AMPK GAMMA1 SUBUNIT, PRKAG1;                        
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    HUMAN ALPHA1 BETA2 GAMMA1 HOLO-AMPK COMPLEX, SERINE/THREONINE PROTEIN 
KEYWDS   2 KINASE, AXIN, CAMKKBETA, LKB1, GLYCOGEN, PHOSPHORYLATION,            
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.E.ZHOU,J.KE,X.LI,L.WANG,X.GU,P.W.DE WAAL,M.H.E.TAN,D.WANG,D.WU,     
AUTHOR   2 H.E.XU,K.MELCHER                                                     
REVDAT   3   11-MAR-15 4RER    1       AUTHOR                                   
REVDAT   2   14-JAN-15 4RER    1       JRNL                                     
REVDAT   1   10-DEC-14 4RER    0                                                
JRNL        AUTH   X.LI,L.WANG,X.E.ZHOU,J.KE,P.W.DE WAAL,X.GU,M.H.TAN,D.WANG,   
JRNL        AUTH 2 D.WU,H.E.XU,K.MELCHER                                        
JRNL        TITL   STRUCTURAL BASIS OF AMPK REGULATION BY ADENINE NUCLEOTIDES   
JRNL        TITL 2 AND GLYCOGEN.                                                
JRNL        REF    CELL RES.                     V.  25    50 2015              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   25412657                                                     
JRNL        DOI    10.1038/CR.2014.150                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM-LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16566                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1213                            
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 39.6586 -  8.3942    1.00     1810   159  0.1812 0.2279        
REMARK   3     2  8.3942 -  6.6731    1.00     1728   168  0.2219 0.2266        
REMARK   3     3  6.6731 -  5.8326    1.00     1733   120  0.2291 0.2291        
REMARK   3     4  5.8326 -  5.3006    1.00     1683   156  0.2224 0.2535        
REMARK   3     5  5.3006 -  4.9215    1.00     1726   109  0.2225 0.2653        
REMARK   3     6  4.9215 -  4.6318    1.00     1706   117  0.2257 0.2919        
REMARK   3     7  4.6318 -  4.4001    1.00     1705   130  0.2532 0.3375        
REMARK   3     8  4.4001 -  4.2088    1.00     1707   111  0.2896 0.3320        
REMARK   3     9  4.2088 -  4.0469    0.93     1555   143  0.3169 0.3535        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.550            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           8005                                  
REMARK   3   ANGLE     :  0.964          10885                                  
REMARK   3   CHIRALITY :  0.040           1226                                  
REMARK   3   PLANARITY :  0.006           1337                                  
REMARK   3   DIHEDRAL  : 17.872           2982                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  59.3918 -41.5710  17.4551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5056 T22:   1.3797                                     
REMARK   3      T33:   1.4497 T12:  -0.1368                                     
REMARK   3      T13:   0.0322 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4620 L22:   1.7250                                     
REMARK   3      L33:   2.3653 L12:  -1.8943                                     
REMARK   3      L13:   0.5936 L23:  -0.2680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:   0.0704 S13:  -0.2423                       
REMARK   3      S21:   0.1674 S22:   0.0523 S23:   0.1015                       
REMARK   3      S31:   0.1874 S32:  -0.2247 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B and resid 78:167                               
REMARK   3    ORIGIN FOR THE GROUP (A):  39.5702 -44.0271 -23.5219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0111 T22:   2.6888                                     
REMARK   3      T33:   2.5007 T12:  -0.0710                                     
REMARK   3      T13:  -0.0437 T23:  -0.3303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1301 L22:   1.0847                                     
REMARK   3      L33:   0.3992 L12:  -0.3970                                     
REMARK   3      L13:   0.0243 L23:  -0.2226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1977 S12:   1.2238 S13:  -0.2751                       
REMARK   3      S21:  -0.5660 S22:   0.1161 S23:  -0.2330                       
REMARK   3      S31:   0.4100 S32:  -0.4952 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain B and resid 182:272                              
REMARK   3    ORIGIN FOR THE GROUP (A):  75.0015 -53.5780  20.5358              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7248 T22:   1.5968                                     
REMARK   3      T33:   1.4856 T12:  -0.0020                                     
REMARK   3      T13:  -0.0020 T23:  -0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4998 L22:   3.0879                                     
REMARK   3      L33:   0.6707 L12:   0.2949                                     
REMARK   3      L13:  -0.8278 L23:  -0.8643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0677 S12:   0.1735 S13:   0.2273                       
REMARK   3      S21:  -0.7988 S22:  -0.0272 S23:  -0.3635                       
REMARK   3      S31:   0.3259 S32:   0.1178 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain G                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  69.7181 -66.4984  50.3439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3380 T22:   1.0504                                     
REMARK   3      T33:   1.4390 T12:  -0.0501                                     
REMARK   3      T13:   0.0413 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9978 L22:   1.8646                                     
REMARK   3      L33:   4.7935 L12:  -0.1449                                     
REMARK   3      L13:   0.5101 L23:  -0.6097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1475 S12:  -0.1842 S13:  -0.1991                       
REMARK   3      S21:  -0.0741 S22:   0.1152 S23:   0.2525                       
REMARK   3      S31:   0.4192 S32:  -0.3697 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4RER COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087254.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16621                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 13.100                             
REMARK 200  R MERGE                    (I) : 0.18600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2Y94                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000,0.1 M HEPES, PH7.8, 10%     
REMARK 280  2-PROPANOL (V/V) AND 0.19 MM 7-CYCLOHEXYL-1-HEPTYL-D-MALTOSIDE,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      130.26133            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       65.13067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       65.13067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      130.26133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE HETEROTRIMERIC SERINE/THREONINE PROTEIN KINASE           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 47460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     MET A   289                                                      
REMARK 465     ILE A   290                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     ASN A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     GLN A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     THR A   473                                                      
REMARK 465     ALA A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     ALA A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     GLY A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 465     ALA A   480                                                      
REMARK 465     THR A   481                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     GLN A   483                                                      
REMARK 465     ARG A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     GLY A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     VAL A   488                                                      
REMARK 465     SER A   489                                                      
REMARK 465     ASN A   490                                                      
REMARK 465     TYR A   491                                                      
REMARK 465     ARG A   492                                                      
REMARK 465     SER A   493                                                      
REMARK 465     CYS A   494                                                      
REMARK 465     GLN A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     ASP A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     ASP A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     LYS A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     VAL A   510                                                      
REMARK 465     SER A   511                                                      
REMARK 465     LEU A   512                                                      
REMARK 465     THR A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     SER A   515                                                      
REMARK 465     VAL A   516                                                      
REMARK 465     THR A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     LEU A   519                                                      
REMARK 465     ASP A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     SER A   522                                                      
REMARK 465     PRO A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     ASP A   525                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     ARG B    77                                                      
REMARK 465     LEU B   168                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     SER B   170                                                      
REMARK 465     MET B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     CYS B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     ASP B   180                                                      
REMARK 465     LEU B   181                                                      
REMARK 465     SER G    24                                                      
REMARK 465     THR G   325                                                      
REMARK 465     GLY G   326                                                      
REMARK 465     GLY G   327                                                      
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     THR G 287    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  39      -69.53    -95.02                                   
REMARK 500    ALA A 158      -74.44   -104.41                                   
REMARK 500    LEU A 210      -62.33   -122.57                                   
REMARK 500    TYR A 285      -68.25   -107.48                                   
REMARK 500    ASP A 292     -169.28   -162.85                                   
REMARK 500    SER A 305      -10.79     74.12                                   
REMARK 500    ASP A 423        3.99     89.31                                   
REMARK 500    VAL A 429      -62.67    -94.77                                   
REMARK 500    PRO A 530       53.09    -95.56                                   
REMARK 500    VAL B 162      -57.55   -122.61                                   
REMARK 500    PRO B 186       85.11    -64.55                                   
REMARK 500    MET B 193       -3.69     82.06                                   
REMARK 500    ALA B 195      165.55    179.62                                   
REMARK 500    PHE B 196      -69.86   -134.94                                   
REMARK 500    VAL G  28      -58.80   -121.58                                   
REMARK 500    LYS G 100      -62.18   -122.64                                   
REMARK 500    GLN G 105      -78.06   -117.60                                   
REMARK 500    GLU G 187      -75.06   -129.60                                   
REMARK 500    ALA G 202      -72.46    -82.21                                   
REMARK 500    TYR G 272      -54.82   -126.91                                   
REMARK 500    ASP G 304     -168.31   -125.21                                   
REMARK 500    LYS G 310      -55.45   -120.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STU A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP G 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RED   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN AMPK ALPHA1 KD-AID WITH K43A              
REMARK 900 MUTATION                                                             
REMARK 900 RELATED ID: 4REW   RELATED DB: PDB                                   
DBREF  4RER A   11   550  UNP    Q13131   AAPK1_HUMAN     20    559             
DBREF  4RER B   76   272  UNP    O43741   AAKB2_HUMAN     76    272             
DBREF  4RER G   24   327  UNP    P54619   AAKG1_HUMAN     24    327             
SEQADV 4RER SER A   12  UNP  Q13131    ARG    21 CONFLICT                       
SEQADV 4RER SER A  260  UNP  Q13131    THR   269 CONFLICT                       
SEQADV 4RER GLY A  471  UNP  Q13131    GLU   480 ENGINEERED MUTATION            
SEQADV 4RER ALA A  474  UNP  Q13131    GLU   483 ENGINEERED MUTATION            
SEQADV 4RER ALA A  476  UNP  Q13131    LYS   485 ENGINEERED MUTATION            
SEQRES   1 A  540  GLY SER VAL LYS ILE GLY HIS TYR ILE LEU GLY ASP THR          
SEQRES   2 A  540  LEU GLY VAL GLY THR PHE GLY LYS VAL LYS VAL GLY LYS          
SEQRES   3 A  540  HIS GLU LEU THR GLY HIS LYS VAL ALA VAL LYS ILE LEU          
SEQRES   4 A  540  ASN ARG GLN LYS ILE ARG SER LEU ASP VAL VAL GLY LYS          
SEQRES   5 A  540  ILE ARG ARG GLU ILE GLN ASN LEU LYS LEU PHE ARG HIS          
SEQRES   6 A  540  PRO HIS ILE ILE LYS LEU TYR GLN VAL ILE SER THR PRO          
SEQRES   7 A  540  SER ASP ILE PHE MET VAL MET GLU TYR VAL SER GLY GLY          
SEQRES   8 A  540  GLU LEU PHE ASP TYR ILE CYS LYS ASN GLY ARG LEU ASP          
SEQRES   9 A  540  GLU LYS GLU SER ARG ARG LEU PHE GLN GLN ILE LEU SER          
SEQRES  10 A  540  GLY VAL ASP TYR CYS HIS ARG HIS MET VAL VAL HIS ARG          
SEQRES  11 A  540  ASP LEU LYS PRO GLU ASN VAL LEU LEU ASP ALA HIS MET          
SEQRES  12 A  540  ASN ALA LYS ILE ALA ASP PHE GLY LEU SER ASN MET MET          
SEQRES  13 A  540  SER ASP GLY GLU PHE LEU ARG TPO SER CYS GLY SER PRO          
SEQRES  14 A  540  ASN TYR ALA ALA PRO GLU VAL ILE SER GLY ARG LEU TYR          
SEQRES  15 A  540  ALA GLY PRO GLU VAL ASP ILE TRP SER SER GLY VAL ILE          
SEQRES  16 A  540  LEU TYR ALA LEU LEU CYS GLY THR LEU PRO PHE ASP ASP          
SEQRES  17 A  540  ASP HIS VAL PRO THR LEU PHE LYS LYS ILE CYS ASP GLY          
SEQRES  18 A  540  ILE PHE TYR THR PRO GLN TYR LEU ASN PRO SER VAL ILE          
SEQRES  19 A  540  SER LEU LEU LYS HIS MET LEU GLN VAL ASP PRO MET LYS          
SEQRES  20 A  540  ARG ALA SER ILE LYS ASP ILE ARG GLU HIS GLU TRP PHE          
SEQRES  21 A  540  LYS GLN ASP LEU PRO LYS TYR LEU PHE PRO GLU ASP PRO          
SEQRES  22 A  540  SER TYR SER SER THR MET ILE ASP ASP GLU ALA LEU LYS          
SEQRES  23 A  540  GLU VAL CYS GLU LYS PHE GLU CYS SER GLU GLU GLU VAL          
SEQRES  24 A  540  LEU SER CYS LEU TYR ASN ARG ASN HIS GLN ASP PRO LEU          
SEQRES  25 A  540  ALA VAL ALA TYR HIS LEU ILE ILE ASP ASN ARG ARG ILE          
SEQRES  26 A  540  MET ASN GLU ALA LYS ASP PHE TYR LEU ALA THR SER PRO          
SEQRES  27 A  540  PRO ASP SER PHE LEU ASP ASP HIS HIS LEU THR ARG PRO          
SEQRES  28 A  540  HIS PRO GLU ARG VAL PRO PHE LEU VAL ALA GLU THR PRO          
SEQRES  29 A  540  ARG ALA ARG HIS THR LEU ASP GLU LEU ASN PRO GLN LYS          
SEQRES  30 A  540  SER LYS HIS GLN GLY VAL ARG LYS ALA LYS TRP HIS LEU          
SEQRES  31 A  540  GLY ILE ARG SER GLN SER ARG PRO ASN ASP ILE MET ALA          
SEQRES  32 A  540  GLU VAL CYS ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP          
SEQRES  33 A  540  LYS VAL VAL ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS          
SEQRES  34 A  540  ASN PRO VAL THR SER THR TYR SER LYS MET SER LEU GLN          
SEQRES  35 A  540  LEU TYR GLN VAL ASP SER ARG THR TYR LEU LEU ASP PHE          
SEQRES  36 A  540  ARG SER ILE ASP ASP GLY ILE THR ALA ALA ALA SER GLY          
SEQRES  37 A  540  THR ALA THR PRO GLN ARG SER GLY SER VAL SER ASN TYR          
SEQRES  38 A  540  ARG SER CYS GLN ARG SER ASP SER ASP ALA GLU ALA GLN          
SEQRES  39 A  540  GLY LYS SER SER GLU VAL SER LEU THR SER SER VAL THR          
SEQRES  40 A  540  SER LEU ASP SER SER PRO VAL ASP LEU THR PRO ARG PRO          
SEQRES  41 A  540  GLY SER HIS THR ILE GLU PHE PHE GLU MET CYS ALA ASN          
SEQRES  42 A  540  LEU ILE LYS ILE LEU ALA GLN                                  
SEQRES   1 B  197  ALA ARG PRO THR VAL ILE ARG TRP SER GLU GLY GLY LYS          
SEQRES   2 B  197  GLU VAL PHE ILE SER GLY SER PHE ASN ASN TRP SER THR          
SEQRES   3 B  197  LYS ILE PRO LEU ILE LYS SEP HIS ASN ASP PHE VAL ALA          
SEQRES   4 B  197  ILE LEU ASP LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE          
SEQRES   5 B  197  PHE VAL ASP GLY GLN TRP VAL HIS ASP PRO SER GLU PRO          
SEQRES   6 B  197  VAL VAL THR SER GLN LEU GLY THR ILE ASN ASN LEU ILE          
SEQRES   7 B  197  HIS VAL LYS LYS SER ASP PHE GLU VAL PHE ASP ALA LEU          
SEQRES   8 B  197  LYS LEU ASP SER MET GLU SER SER GLU THR SER CYS ARG          
SEQRES   9 B  197  ASP LEU SER SER SER PRO PRO GLY PRO TYR GLY GLN GLU          
SEQRES  10 B  197  MET TYR ALA PHE ARG SER GLU GLU ARG PHE LYS SER PRO          
SEQRES  11 B  197  PRO ILE LEU PRO PRO HIS LEU LEU GLN VAL ILE LEU ASN          
SEQRES  12 B  197  LYS ASP THR ASN ILE SER CYS ASP PRO ALA LEU LEU PRO          
SEQRES  13 B  197  GLU PRO ASN HIS VAL MET LEU ASN HIS LEU TYR ALA LEU          
SEQRES  14 B  197  SER ILE LYS ASP SER VAL MET VAL LEU SER ALA THR HIS          
SEQRES  15 B  197  ARG TYR LYS LYS LYS TYR VAL THR THR LEU LEU TYR LYS          
SEQRES  16 B  197  PRO ILE                                                      
SEQRES   1 G  304  SER ASN ASN SER VAL TYR THR SER PHE MET LYS SER HIS          
SEQRES   2 G  304  ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS LEU VAL          
SEQRES   3 G  304  VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA PHE PHE          
SEQRES   4 G  304  ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO LEU TRP          
SEQRES   5 G  304  ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU THR ILE          
SEQRES   6 G  304  THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR LYS SER          
SEQRES   7 G  304  ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS LYS ILE          
SEQRES   8 G  304  GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER PHE LYS          
SEQRES   9 G  304  PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU PHE ASP          
SEQRES  10 G  304  ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS ARG LEU          
SEQRES  11 G  304  PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU TYR ILE          
SEQRES  12 G  304  LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS LEU PHE          
SEQRES  13 G  304  ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER LYS SER          
SEQRES  14 G  304  LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN ILE ALA          
SEQRES  15 G  304  MET VAL ARG THR THR THR PRO VAL TYR VAL ALA LEU GLY          
SEQRES  16 G  304  ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO VAL VAL          
SEQRES  17 G  304  ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER LYS PHE          
SEQRES  18 G  304  ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR ASN ASN          
SEQRES  19 G  304  LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS ARG SER          
SEQRES  20 G  304  HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU HIS GLU          
SEQRES  21 G  304  THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU ALA GLU          
SEQRES  22 G  304  VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP VAL VAL          
SEQRES  23 G  304  LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN ALA LEU          
SEQRES  24 G  304  VAL LEU THR GLY GLY                                          
MODRES 4RER TPO A  174  THR  PHOSPHOTHREONINE                                   
MODRES 4RER SEP B  108  SER  PHOSPHOSERINE                                      
HET    TPO  A 174      11                                                       
HET    SEP  B 108      10                                                       
HET    STU  A 601      35                                                       
HET    EPE  A 602      15                                                       
HET    BCD  B 301      77                                                       
HET    AMP  G 401      23                                                       
HET    AMP  G 402      23                                                       
HET    AMP  G 403      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     STU STAUROSPORINE                                                    
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     BCD BETA-CYCLODEXTRIN                                                
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     EPE HEPES                                                            
HETSYN     BCD CYCLO-HEPTA-AMYLOSE                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5  EPE    C8 H18 N2 O4 S                                               
FORMUL   6  BCD    C42 H70 O35                                                  
FORMUL   7  AMP    3(C10 H14 N5 O7 P)                                           
HELIX    1   1 ARG A   51  LEU A   57  1                                   7    
HELIX    2   2 VAL A   59  LEU A   72  1                                  14    
HELIX    3   3 LEU A  103  GLY A  111  1                                   9    
HELIX    4   4 ASP A  114  HIS A  135  1                                  22    
HELIX    5   5 GLY A  194  LEU A  209  1                                  16    
HELIX    6   6 PRO A  222  ASP A  230  1                                   9    
HELIX    7   7 ASN A  240  LEU A  251  1                                  12    
HELIX    8   8 SER A  260  GLU A  266  1                                   7    
HELIX    9   9 HIS A  267  GLN A  272  1                                   6    
HELIX   10  10 ASP A  292  LYS A  296  5                                   5    
HELIX   11  11 GLU A  297  PHE A  302  1                                   6    
HELIX   12  12 VAL A  309  ASN A  315  1                                   7    
HELIX   13  13 TYR A  326  GLU A  338  1                                  13    
HELIX   14  14 HIS A  362  GLU A  364  5                                   3    
HELIX   15  15 ARG A  365  THR A  373  1                                   9    
HELIX   16  16 ARG A  407  LEU A  422  1                                  16    
HELIX   17  17 SER A  532  GLN A  550  1                                  19    
HELIX   18  18 PRO B  209  GLN B  214  1                                   6    
HELIX   19  19 ASN B  234  LEU B  238  5                                   5    
HELIX   20  20 VAL G   28  SER G   35  1                                   8    
HELIX   21  21 ARG G   37  ILE G   42  5                                   6    
HELIX   22  22 GLN G   56  GLY G   68  1                                  13    
HELIX   23  23 ILE G   88  TYR G   98  1                                  11    
HELIX   24  24 ILE G  106  GLU G  111  1                                   6    
HELIX   25  25 LYS G  113  LEU G  122  1                                  10    
HELIX   26  26 SER G  137  ASN G  148  1                                  12    
HELIX   27  27 THR G  168  ILE G  180  1                                  13    
HELIX   28  28 SER G  192  GLN G  197  1                                   6    
HELIX   29  29 PRO G  212  HIS G  223  1                                  12    
HELIX   30  30 VAL G  246  GLU G  252  1                                   7    
HELIX   31  31 SER G  261  LEU G  266  1                                   6    
HELIX   32  32 GLN G  267  ARG G  269  5                                   3    
HELIX   33  33 THR G  284  GLU G  296  1                                  13    
HELIX   34  34 LEU G  315  LEU G  324  1                                  10    
SHEET    1   A 6 LYS A  14  ILE A  15  0                                        
SHEET    2   A 6 TYR A  18  GLY A  25 -1  O  TYR A  18   N  ILE A  15           
SHEET    3   A 6 VAL A  32  HIS A  37 -1  O  VAL A  34   N  GLY A  21           
SHEET    4   A 6 LYS A  43  ASN A  50 -1  O  VAL A  44   N  GLY A  35           
SHEET    5   A 6 ASP A  90  GLU A  96 -1  O  ILE A  91   N  LEU A  49           
SHEET    6   A 6 LEU A  81  GLN A  83 -1  N  GLN A  83   O  VAL A  94           
SHEET    1   B 3 GLY A 101  GLU A 102  0                                        
SHEET    2   B 3 VAL A 147  LEU A 149 -1  O  LEU A 149   N  GLY A 101           
SHEET    3   B 3 LYS A 156  ILE A 157 -1  O  LYS A 156   N  LEU A 148           
SHEET    1   C 2 VAL A 137  VAL A 138  0                                        
SHEET    2   C 2 ASN A 164  MET A 165 -1  O  ASN A 164   N  VAL A 138           
SHEET    1   D 5 ILE A 402  SER A 404  0                                        
SHEET    2   D 5 THR A 460  ARG A 466 -1  O  LEU A 463   N  ILE A 402           
SHEET    3   D 5 TYR A 446  ASP A 457 -1  N  TYR A 454   O  LEU A 462           
SHEET    4   D 5 TYR A 433  LYS A 439 -1  N  VAL A 436   O  MET A 449           
SHEET    5   D 5 GLU A 425  ASN A 430 -1  N  LYS A 427   O  ARG A 435           
SHEET    1   E 3 THR B  79  ILE B  81  0                                        
SHEET    2   E 3 PHE B 112  LEU B 116 -1  O  LEU B 116   N  THR B  79           
SHEET    3   E 3 ILE B 106  LYS B 107 -1  N  ILE B 106   O  VAL B 113           
SHEET    1   F 4 ILE B 103  PRO B 104  0                                        
SHEET    2   F 4 VAL B  90  ILE B  92 -1  N  ILE B  92   O  ILE B 103           
SHEET    3   F 4 PHE B 127  VAL B 129 -1  O  PHE B 128   N  PHE B  91           
SHEET    4   F 4 GLN B 132  VAL B 134 -1  O  VAL B 134   N  PHE B 127           
SHEET    1   G 3 GLN B 124  TYR B 125  0                                        
SHEET    2   G 3 ILE B 149  LEU B 152 -1  O  ASN B 151   N  TYR B 125           
SHEET    3   G 3 VAL B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1   H 6 LEU B 241  LEU B 244  0                                        
SHEET    2   H 6 VAL B 250  ARG B 258 -1  O  SER B 254   N  TYR B 242           
SHEET    3   H 6 TYR B 263  PRO B 271 -1  O  LYS B 270   N  MET B 251           
SHEET    4   H 6 SER G  45  ASP G  52  1  O  LEU G  48   N  LEU B 267           
SHEET    5   H 6 ALA G  71  ASP G  76  1  O  TRP G  75   N  PHE G  51           
SHEET    6   H 6 SER G  81  THR G  87 -1  O  GLY G  84   N  LEU G  74           
SHEET    1   I 2 LEU G 153  ILE G 156  0                                        
SHEET    2   I 2 THR G 163  LEU G 167 -1  O  TYR G 165   N  VAL G 155           
SHEET    1   J 3 VAL G 207  ARG G 208  0                                        
SHEET    2   J 3 ALA G 227  VAL G 231  1  O  VAL G 231   N  VAL G 207           
SHEET    3   J 3 VAL G 237  SER G 242 -1  O  TYR G 241   N  LEU G 228           
SHEET    1   K 3 LYS G 278  TYR G 280  0                                        
SHEET    2   K 3 ARG G 299  VAL G 303  1  O  VAL G 303   N  CYS G 279           
SHEET    3   K 3 VAL G 309  SER G 314 -1  O  VAL G 313   N  LEU G 300           
LINK         C   ARG A 173                 N   TPO A 174     1555   1555  1.34  
LINK         C   TPO A 174                 N   SER A 175     1555   1555  1.33  
LINK         C   LYS B 107                 N   SEP B 108     1555   1555  1.33  
LINK         C   SEP B 108                 N   HIS B 109     1555   1555  1.33  
CISPEP   1 VAL A  221    PRO A  222          0         1.72                     
SITE     1 AC1 11 LEU A  24  GLY A  25  GLY A  27  ALA A  45                    
SITE     2 AC1 11 GLU A  96  TYR A  97  VAL A  98  GLU A 102                    
SITE     3 AC1 11 GLU A 145  ASN A 146  LEU A 148                               
SITE     1 AC2  5 LYS A  14  GLY A  16  THR A  87  PRO B  78                    
SITE     2 AC2  5 VAL B  80                                                     
SITE     1 AC3 12 ILE A 232  PHE A 233  TYR A 234  THR A 235                    
SITE     2 AC3 12 PHE B  96  TRP B  99  PRO B 119  LYS B 126                    
SITE     3 AC3 12 GLN B 145  LEU B 146  THR B 148  ASN B 150                    
SITE     1 AC4 10 THR G  87  THR G  89  ASP G  90  TYR G 121                    
SITE     2 AC4 10 PRO G 128  LEU G 129  VAL G 130  ILE G 150                    
SITE     3 AC4 10 HIS G 151  ARG G 152                                          
SITE     1 AC5 12 ARG G  70  LYS G 170  ILE G 240  SER G 242                    
SITE     2 AC5 12 PHE G 244  ASP G 245  ARG G 269  GLY G 275                    
SITE     3 AC5 12 LEU G 277  VAL G 297  HIS G 298  ARG G 299                    
SITE     1 AC6 13 HIS G 151  THR G 200  ASN G 203  ALA G 205                    
SITE     2 AC6 13 ARG G 224  VAL G 225  SER G 226  ALA G 227                    
SITE     3 AC6 13 HIS G 298  ILE G 312  SER G 314  SER G 316                    
SITE     4 AC6 13 ASP G 317                                                     
CRYST1  132.566  132.566  195.392  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007543  0.004355  0.000000        0.00000                         
SCALE2      0.000000  0.008710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005118        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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