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Database: PDB
Entry: 5T5T
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HEADER    TRANSFERASE                             31-AUG-16   5T5T              
TITLE     AMPK BOUND TO ALLOSTERIC ACTIVATOR                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-1,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE,TAU-  
COMPND   6 PROTEIN KINASE PRKAA1;                                               
COMPND   7 EC: 2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26;                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: AMPKB,5'-AMP-ACTIVATED PROTEIN KINASE 40 KDA SUBUNIT;       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: AMPKG;                                                      
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: PRKAA1, AMPK1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: RAT;                                                
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 GENE: PRKAB1;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  17 ORGANISM_COMMON: RAT;                                                
SOURCE  18 ORGANISM_TAXID: 10116;                                               
SOURCE  19 GENE: PRKAG1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AMPK, KINASE, ALLOSTERY, ACTIVATOR, TRANSFERASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.CALABRESE,R.G.KURUMBAIL                                           
REVDAT   2   26-APR-17 5T5T    1       JRNL                                     
REVDAT   1   29-MAR-17 5T5T    0                                                
JRNL        AUTH   C.T.SALATTO,R.A.MILLER,K.O.CAMERON,E.COKORINOS,A.REYES,      
JRNL        AUTH 2 J.WARD,M.F.CALABRESE,R.G.KURUMBAIL,F.RAJAMOHAN,              
JRNL        AUTH 3 A.S.KALGUTKAR,D.A.TESS,A.SHAVNYA,N.E.GENUNG,D.J.EDMONDS,     
JRNL        AUTH 4 A.JATKAR,B.S.MACIEJEWSKI,M.AMARO,H.GANDHOK,M.MONETTI,        
JRNL        AUTH 5 K.CIALDEA,E.BOLLINGER,J.M.KREEGER,T.M.COSKRAN,A.C.OPSAHL,    
JRNL        AUTH 6 G.G.BOUCHER,M.J.BIRNBAUM,P.DASILVA-JARDINE,T.ROLPH           
JRNL        TITL   SELECTIVE ACTIVATION OF AMPK BETA 1-CONTAINING ISOFORMS      
JRNL        TITL 2 IMPROVES KIDNEY FUNCTION IN A RAT MODEL OF DIABETIC          
JRNL        TITL 3 NEPHROPATHY.                                                 
JRNL        REF    J. PHARMACOL. EXP. THER.      V. 361   303 2017              
JRNL        REFN                   ESSN 1521-0103                               
JRNL        PMID   28289077                                                     
JRNL        DOI    10.1124/JPET.116.237925                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.11.7                                    
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25312                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.212                          
REMARK   3   R VALUE            (WORKING SET)  : 0.211                          
REMARK   3   FREE R VALUE                      : 0.231                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.920                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1246                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.46                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.60                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.32                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2757                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2645                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2450                   
REMARK   3   BIN FREE R VALUE                        : 0.3050                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.06                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 112                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6177                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 145                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 93.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 125.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.53630                                            
REMARK   3    B22 (A**2) : -10.53630                                            
REMARK   3    B33 (A**2) : 21.07260                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.460               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.397               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.399               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6476   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8890   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2043   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 113    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1064   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6476   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 895    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7344   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.96                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.59                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   29.7622  -76.2037  -16.2853           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2835 T22:   -0.3714                                    
REMARK   3     T33:   -0.6721 T12:    0.0632                                    
REMARK   3     T13:   -0.0549 T23:   -0.2364                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8558 L22:    1.7174                                    
REMARK   3     L33:    3.5360 L12:    0.0674                                    
REMARK   3     L13:   -0.3204 L23:    1.3098                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0048 S12:    0.0945 S13:    0.0467                     
REMARK   3     S21:   -0.1476 S22:   -0.2334 S23:    0.2132                     
REMARK   3     S31:   -0.7134 S32:   -0.8470 S33:    0.2286                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   35.8744  -68.2562  -31.0944           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1263 T22:   -0.1463                                    
REMARK   3     T33:   -0.3592 T12:    0.1724                                    
REMARK   3     T13:    0.0369 T23:   -0.2300                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2723 L22:    0.2225                                    
REMARK   3     L33:    5.8247 L12:   -1.1187                                    
REMARK   3     L13:   -3.5000 L23:    1.9245                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1466 S12:    0.3477 S13:    0.1089                     
REMARK   3     S21:   -0.1675 S22:   -0.0039 S23:    0.2563                     
REMARK   3     S31:   -0.7079 S32:   -0.6586 S33:    0.1506                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   22.9957  -41.1912   16.3785           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1831 T22:    0.5148                                    
REMARK   3     T33:    0.2222 T12:    0.3847                                    
REMARK   3     T13:    0.0265 T23:   -0.4066                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.2262 L22:    5.7443                                    
REMARK   3     L33:    3.9353 L12:   -3.3862                                    
REMARK   3     L13:   -1.5849 L23:    3.8380                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1860 S12:   -0.5823 S13:    0.8207                     
REMARK   3     S21:   -0.3235 S22:    0.8352 S23:   -0.7324                     
REMARK   3     S31:   -0.3747 S32:    0.7751 S33:   -0.6492                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5T5T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223770.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25312                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.00                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, PHASER                                        
REMARK 200 STARTING MODEL: 4QFG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRISODIUM CITRATE, 500 MM         
REMARK 280  AMMONIUM SULFATE, 900 MM LITHIUM SULFATE, AND 4% GLYCEROL, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      134.45333            
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      268.90667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      201.68000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      336.13333            
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       67.22667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      134.45333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      268.90667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      336.13333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      201.68000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       67.22667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -127.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 27980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 69280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -263.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 350   BIOMT1   2  0.500000 -0.866025  0.000000      -62.52000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000     -108.28782            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -67.22667            
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    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     TYR A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     MET A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     ASP A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     GLU A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     GLU A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     CYS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PHE A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     CYS A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     CYS A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     TYR A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     ASP A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     VAL A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     TYR A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     ILE A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     ASN A   330                                                      
REMARK 465     ARG A   331                                                      
REMARK 465     ARG A   332                                                      
REMARK 465     ILE A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     ALA A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     PHE A   340                                                      
REMARK 465     TYR A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     ALA A   343                                                      
REMARK 465     THR A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     PRO A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     ASP A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     LEU A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     ARG A   358                                                      
REMARK 465     PRO A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     ARG A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     PHE A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     VAL A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     THR A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     ARG A   373                                                      
REMARK 465     ALA A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     LEU A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     LEU A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     LYS A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     GLY A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     GLY A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     ALA A   525                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     MET B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     PRO B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     TYR B   187                                                      
REMARK 465     HIS B   188                                                      
REMARK 465     GLN B   189                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     PRO B   191                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     ILE B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     PRO B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     GLY B   220                                                      
REMARK 465     ILE B   221                                                      
REMARK 465     SER B   222                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ASN C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     SER C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     TYR C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     THR C   324                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     PRO C   330                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     LYS A  60    CG   CD   CE   NZ                                   
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     LEU A  70    CG   CD1  CD2                                       
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     GLU A 115    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     LYS A 225    CG   CD   CE   NZ                                   
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     GLU A 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     LYS A 395    CG   CD   CE   NZ                                   
REMARK 470     ARG A 401    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 402    OG                                                  
REMARK 470     ARG A 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 407    CG   OD1  ND2                                       
REMARK 470     ASP A 408    CG   OD1  OD2                                       
REMARK 470     MET A 410    CG   SD   CE                                        
REMARK 470     ARG A 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 418    CG   CD   CE   NZ                                   
REMARK 470     GLN A 419    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 420    CG   CD1  CD2                                       
REMARK 470     TYR A 422    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     ARG A 435    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 437    CG   CD   CE   NZ                                   
REMARK 470     PHE A 444    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 446    CG   CD   CE   NZ                                   
REMARK 470     ARG A 457    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 460    CG   CD1  CD2                                       
REMARK 470     GLU A 469    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 527    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 537    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 542    CG   CD1  CD2                                       
REMARK 470     LYS A 544    CG   CD   CE   NZ                                   
REMARK 470     LEU A 546    CG   CD1  CD2                                       
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  90    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 110    CG   OD1  ND2                                       
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     PHE B 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     SER B 170    OG                                                  
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     CYS B 173    SG                                                  
REMARK 470     LYS B 217    CG   CD   CE   NZ                                   
REMARK 470     CYS B 223    CB   SG                                             
REMARK 470     ASP B 224    CG   OD1  OD2                                       
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     MET B 249    CG   SD   CE                                        
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     LYS B 268    CG   CD   CE   NZ                                   
REMARK 470     LYS C  33    CG   CD   CE   NZ                                   
REMARK 470     ARG C  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C  40    CG   CD1  CD2                                       
REMARK 470     LYS C  77    CG   CD   CE   NZ                                   
REMARK 470     LYS C  78    CG   CD   CE   NZ                                   
REMARK 470     LYS C  99    CG   CD   CE   NZ                                   
REMARK 470     GLN C 104    CG   CD   OE1  NE2                                  
REMARK 470     TYR C 106    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 112    CG   CD   CE   NZ                                   
REMARK 470     GLU C 114    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 118    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 121    CG   CD1  CD2                                       
REMARK 470     GLN C 122    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 123    CG   OD1  OD2                                       
REMARK 470     SER C 124    OG                                                  
REMARK 470     PHE C 125    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 126    CG   CD   CE   NZ                                   
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 169    CG   CD   CE   NZ                                   
REMARK 470     LEU C 172    CG   CD1  CD2                                       
REMARK 470     LYS C 173    CG   CD   CE   NZ                                   
REMARK 470     LYS C 176    CG   CD   CE   NZ                                   
REMARK 470     PHE C 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE C 179    CG1  CG2  CD1                                       
REMARK 470     GLU C 181    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 182    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 184    CG   CD   CE   NZ                                   
REMARK 470     MET C 188    CG   SD   CE                                        
REMARK 470     SER C 189    OG                                                  
REMARK 470     LYS C 190    CG   CD   CE   NZ                                   
REMARK 470     GLU C 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 194    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 195    CG   CD1  CD2                                       
REMARK 470     GLN C 196    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 197    CG1  CG2  CD1                                       
REMARK 470     ARG C 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 209    OG1  CG2                                            
REMARK 470     ARG C 223    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 231    CG   OD1  OD2                                       
REMARK 470     GLU C 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 233    CG   CD   CE   NZ                                   
REMARK 470     ARG C 235    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 246    CG1  CG2  CD1                                       
REMARK 470     LYS C 263    CG   CD   CE   NZ                                   
REMARK 470     GLN C 266    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 273    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 276    CG   CD1  CD2                                       
REMARK 470     LYS C 277    CG   CD   CE   NZ                                   
REMARK 470     LEU C 280    CG   CD1  CD2                                       
REMARK 470     GLU C 282    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 285    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 293    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 304    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 305    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP C 306    CG   OD1  OD2                                       
REMARK 470     VAL C 307    CG1  CG2                                            
REMARK 470     VAL C 308    CG1  CG2                                            
REMARK 470     LYS C 309    CG   CD   CE   NZ                                   
REMARK 470     LEU C 318    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  56       49.02    -81.82                                   
REMARK 500    ARG A  72       78.70   -165.61                                   
REMARK 500    ASP A 157       84.70     62.59                                   
REMARK 500    LEU A 249       54.72    -98.25                                   
REMARK 500    PRO A 278     -156.68    -82.88                                   
REMARK 500    ASP A 421       75.45     55.01                                   
REMARK 500    VAL A 440      -69.97   -104.80                                   
REMARK 500    PRO A 528     -136.60    -86.19                                   
REMARK 500    SER A 530      105.42   -170.00                                   
REMARK 500    ASP B 108      -84.48    -89.75                                   
REMARK 500    HIS B 109      -70.27    -94.52                                   
REMARK 500    ALA B 114      116.84   -163.27                                   
REMARK 500    GLU B 120      108.93    -53.07                                   
REMARK 500    LYS B 258     -111.56     56.72                                   
REMARK 500    THR C  43      -39.97    -38.45                                   
REMARK 500    PRO C 185     -169.02    -77.32                                   
REMARK 500    GLN C 196       81.68     55.91                                   
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 CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 75O B 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404                 
DBREF  5T5T A    0   548  UNP    P54645   AAPK1_RAT       11    559             
DBREF  5T5T B   68   270  UNP    P80386   AAKB1_RAT       68    270             
DBREF  5T5T C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 5T5T GLY A   -1  UNP  P54645              EXPRESSION TAG                 
SEQADV 5T5T     A       UNP  P54645    ILE   481 DELETION                       
SEQADV 5T5T     A       UNP  P54645    THR   482 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLU   483 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ALA   484 DELETION                       
SEQADV 5T5T     A       UNP  P54645    LYS   485 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   486 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLY   487 DELETION                       
SEQADV 5T5T     A       UNP  P54645    THR   488 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ALA   489 DELETION                       
SEQADV 5T5T     A       UNP  P54645    THR   490 DELETION                       
SEQADV 5T5T     A       UNP  P54645    PRO   491 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLN   492 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ARG   493 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   494 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLY   495 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   496 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ILE   497 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   498 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ASN   499 DELETION                       
SEQADV 5T5T     A       UNP  P54645    TYR   500 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ARG   501 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   502 DELETION                       
SEQADV 5T5T     A       UNP  P54645    CYS   503 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLN   504 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ARG   505 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   506 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ASP   507 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   508 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ASP   509 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ALA   510 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLU   511 DELETION                       
SEQADV 5T5T     A       UNP  P54645    ALA   512 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLN   513 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLY   514 DELETION                       
SEQADV 5T5T     A       UNP  P54645    LYS   515 DELETION                       
SEQADV 5T5T     A       UNP  P54645    PRO   516 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   517 DELETION                       
SEQADV 5T5T     A       UNP  P54645    GLU   518 DELETION                       
SEQADV 5T5T     A       UNP  P54645    VAL   519 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   520 DELETION                       
SEQADV 5T5T     A       UNP  P54645    LEU   521 DELETION                       
SEQADV 5T5T     A       UNP  P54645    THR   522 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   523 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   524 DELETION                       
SEQADV 5T5T     A       UNP  P54645    VAL   525 DELETION                       
SEQADV 5T5T     A       UNP  P54645    THR   526 DELETION                       
SEQADV 5T5T     A       UNP  P54645    SER   527 DELETION                       
SEQADV 5T5T ALA A  517  UNP  P54645    LEU   528 LINKER                         
SEQADV 5T5T SER A  518  UNP  P54645    ASP   529 LINKER                         
SEQADV 5T5T GLY A  519  UNP  P54645    SER   530 LINKER                         
SEQADV 5T5T GLY A  520  UNP  P54645    SER   531 LINKER                         
SEQADV 5T5T GLY A  522  UNP  P54645    VAL   533 LINKER                         
SEQADV 5T5T GLY A  523  UNP  P54645    ASP   534 LINKER                         
SEQADV 5T5T SER A  524  UNP  P54645    VAL   535 LINKER                         
SEQADV 5T5T MET B   67  UNP  P80386              INITIATING METHIONINE          
SEQADV 5T5T ASP B  108  UNP  P80386    SER   108 ENGINEERED MUTATION            
SEQADV 5T5T HIS B  109  UNP  P80386    GLN   109 ENGINEERED MUTATION            
SEQRES   1 A  503  GLY ALA THR ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL          
SEQRES   2 A  503  LYS ILE GLY HIS TYR ILE LEU GLY ASP THR LEU GLY VAL          
SEQRES   3 A  503  GLY THR PHE GLY LYS VAL LYS VAL GLY LYS HIS GLU LEU          
SEQRES   4 A  503  THR GLY HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN          
SEQRES   5 A  503  LYS ILE ARG SER LEU ASP VAL VAL GLY LYS ILE ARG ARG          
SEQRES   6 A  503  GLU ILE GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE          
SEQRES   7 A  503  ILE LYS LEU TYR GLN VAL ILE SER THR PRO SER ASP ILE          
SEQRES   8 A  503  PHE MET VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  503  ASP TYR ILE CYS LYS ASN GLY ARG LEU ASP GLU LYS GLU          
SEQRES  10 A  503  SER ARG ARG LEU PHE GLN GLN ILE LEU SER GLY VAL ASP          
SEQRES  11 A  503  TYR CYS HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS          
SEQRES  12 A  503  PRO GLU ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS          
SEQRES  13 A  503  ILE ALA ASP PHE GLY LEU SER ASN MET MET SER ASP GLY          
SEQRES  14 A  503  GLU PHE LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA          
SEQRES  15 A  503  ALA PRO GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO          
SEQRES  16 A  503  GLU VAL ASP ILE TRP SER SER GLY VAL ILE LEU TYR ALA          
SEQRES  17 A  503  LEU LEU CYS GLY THR LEU PRO PHE ASP ASP ASP HIS VAL          
SEQRES  18 A  503  PRO THR LEU PHE LYS LYS ILE CYS ASP GLY ILE PHE TYR          
SEQRES  19 A  503  THR PRO GLN TYR LEU ASN PRO SER VAL ILE SER LEU LEU          
SEQRES  20 A  503  LYS HIS MET LEU GLN VAL ASP PRO MET LYS ARG ALA THR          
SEQRES  21 A  503  ILE LYS ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN ASP          
SEQRES  22 A  503  LEU PRO LYS TYR LEU PHE PRO GLU ASP PRO SER TYR SER          
SEQRES  23 A  503  SER THR MET ILE ASP ASP GLU ALA LEU LYS GLU VAL CYS          
SEQRES  24 A  503  GLU LYS PHE GLU CYS SER GLU GLU GLU VAL LEU SER CYS          
SEQRES  25 A  503  LEU TYR ASN ARG ASN HIS GLN ASP PRO LEU ALA VAL ALA          
SEQRES  26 A  503  TYR HIS LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLU          
SEQRES  27 A  503  ALA LYS ASP PHE TYR LEU ALA THR SER PRO PRO ASP SER          
SEQRES  28 A  503  PHE LEU ASP ASP HIS HIS LEU THR ARG PRO HIS PRO GLU          
SEQRES  29 A  503  ARG VAL PRO PHE LEU VAL ALA GLU THR PRO ARG ALA ARG          
SEQRES  30 A  503  HIS THR LEU ASP GLU LEU ASN PRO GLN LYS SER LYS HIS          
SEQRES  31 A  503  GLN GLY VAL ARG LYS ALA LYS TRP HIS LEU GLY ILE ARG          
SEQRES  32 A  503  SER GLN SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS          
SEQRES  33 A  503  ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL          
SEQRES  34 A  503  ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL          
SEQRES  35 A  503  THR SER THR PHE SER LYS MET SER LEU GLN LEU TYR GLN          
SEQRES  36 A  503  VAL ASP SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE          
SEQRES  37 A  503  ASP ASP GLU ALA SER GLY GLY PRO GLY GLY SER ALA PRO          
SEQRES  38 A  503  ARG PRO GLY SER HIS THR ILE GLU PHE PHE GLU MET CYS          
SEQRES  39 A  503  ALA ASN LEU ILE LYS ILE LEU ALA GLN                          
SEQRES   1 B  204  MET GLU VAL ASN GLU LYS ALA PRO ALA GLN ALA ARG PRO          
SEQRES   2 B  204  THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL TYR          
SEQRES   3 B  204  LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO LEU          
SEQRES   4 B  204  THR ARG ASP HIS ASN ASN PHE VAL ALA ILE LEU ASP LEU          
SEQRES   5 B  204  PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP GLY          
SEQRES   6 B  204  GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR SER          
SEQRES   7 B  204  GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS LYS          
SEQRES   8 B  204  THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP SER          
SEQRES   9 B  204  GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER PRO          
SEQRES  10 B  204  PRO GLY PRO TYR HIS GLN GLU PRO TYR ILE SER LYS PRO          
SEQRES  11 B  204  GLU GLU ARG PHE LYS ALA PRO PRO ILE LEU PRO PRO HIS          
SEQRES  12 B  204  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER          
SEQRES  13 B  204  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES  14 B  204  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL          
SEQRES  15 B  204  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES  16 B  204  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 C  330  MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU          
SEQRES   2 C  330  ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER          
SEQRES   3 C  330  VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP          
SEQRES   4 C  330  LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR          
SEQRES   5 C  330  SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR          
SEQRES   6 C  330  ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS          
SEQRES   7 C  330  GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE          
SEQRES   8 C  330  ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN          
SEQRES   9 C  330  ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG          
SEQRES  10 C  330  GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS          
SEQRES  11 C  330  ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER          
SEQRES  12 C  330  LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP          
SEQRES  13 C  330  PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS          
SEQRES  14 C  330  ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE          
SEQRES  15 C  330  PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU          
SEQRES  16 C  330  GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR          
SEQRES  17 C  330  THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN          
SEQRES  18 C  330  HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY          
SEQRES  19 C  330  ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN          
SEQRES  20 C  330  LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER          
SEQRES  21 C  330  VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU          
SEQRES  22 C  330  GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA          
SEQRES  23 C  330  ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU          
SEQRES  24 C  330  VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL          
SEQRES  25 C  330  SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY          
SEQRES  26 C  330  GLY GLU LYS LYS PRO                                          
MODRES 5T5T TPO A  172  THR  MODIFIED RESIDUE                                   
HET    TPO  A 172      11                                                       
HET    STU  A 601      35                                                       
HET     CL  A 602       1                                                       
HET     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET    SO4  A 605       5                                                       
HET    75O  B4000      24                                                       
HET    AMP  C 401      23                                                       
HET    AMP  C 402      23                                                       
HET    ADP  C 403      27                                                       
HET    SO4  C 404       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     STU STAUROSPORINE                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     75O 6-CHLORO-5-[6-(DIMETHYLAMINO)-2-METHOXYPYRIDIN-3-YL]-            
HETNAM   2 75O  1H-INDOLE-3-CARBOXYLIC ACID                                     
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   8  SO4    2(O4 S 2-)                                                   
FORMUL   9  75O    C17 H16 CL N3 O3                                             
FORMUL  10  AMP    2(C10 H14 N5 O7 P)                                           
FORMUL  12  ADP    C10 H15 N5 O10 P2                                            
HELIX    1 AA1 GLN A   50  LEU A   55  1                                   6    
HELIX    2 AA2 VAL A   57  PHE A   71  1                                  15    
HELIX    3 AA3 LEU A  101  ASN A  108  1                                   8    
HELIX    4 AA4 ASP A  112  ARG A  132  1                                  21    
HELIX    5 AA5 ALA A  181  SER A  186  1                                   6    
HELIX    6 AA6 GLY A  192  GLY A  210  1                                  19    
HELIX    7 AA7 HIS A  218  ASP A  228  1                                  11    
HELIX    8 AA8 ASN A  238  LEU A  249  1                                  12    
HELIX    9 AA9 THR A  258  HIS A  265  1                                   8    
HELIX   10 AB1 HIS A  265  GLN A  270  1                                   6    
HELIX   11 AB2 PRO A  273  PHE A  277  5                                   5    
HELIX   12 AB3 ARG A  405  LYS A  418  1                                  14    
HELIX   13 AB4 SER A  530  ILE A  545  1                                  16    
HELIX   14 AB5 PHE B   97  ASN B   99  5                                   3    
HELIX   15 AB6 LYS B  156  PHE B  160  5                                   5    
HELIX   16 AB7 GLU B  161  CYS B  173  1                                  13    
HELIX   17 AB8 PRO B  207  GLN B  212  5                                   6    
HELIX   18 AB9 ASN B  232  LEU B  236  5                                   5    
HELIX   19 AC1 VAL C   27  LYS C   33  1                                   7    
HELIX   20 AC2 ARG C   36  ILE C   41  5                                   6    
HELIX   21 AC3 GLN C   55  GLY C   67  1                                  13    
HELIX   22 AC4 THR C   86  TYR C   98  1                                  13    
HELIX   23 AC5 ILE C  105  GLU C  110  1                                   6    
HELIX   24 AC6 LYS C  112  LEU C  121  1                                  10    
HELIX   25 AC7 SER C  136  ASN C  147  1                                  12    
HELIX   26 AC8 HIS C  168  THR C  180  1                                  13    
HELIX   27 AC9 SER C  191  GLN C  196  1                                   6    
HELIX   28 AD1 PRO C  211  ARG C  223  1                                  13    
HELIX   29 AD2 VAL C  245  GLU C  251  1                                   7    
HELIX   30 AD3 SER C  260  LEU C  265  1                                   6    
HELIX   31 AD4 GLN C  266  ARG C  268  5                                   3    
HELIX   32 AD5 THR C  283  GLU C  295  1                                  13    
HELIX   33 AD6 LEU C  314  LEU C  321  1                                   8    
SHEET    1 AA1 6 LYS A  12  ILE A  13  0                                        
SHEET    2 AA1 6 TYR A  16  VAL A  24 -1  O  TYR A  16   N  ILE A  13           
SHEET    3 AA1 6 LYS A  29  HIS A  35 -1  O  LYS A  34   N  ILE A  17           
SHEET    4 AA1 6 LYS A  41  ASN A  48 -1  O  VAL A  44   N  LYS A  31           
SHEET    5 AA1 6 ASP A  88  GLU A  94 -1  O  ILE A  89   N  LEU A  47           
SHEET    6 AA1 6 LEU A  79  SER A  84 -1  N  ILE A  83   O  PHE A  90           
SHEET    1 AA2 3 GLY A  99  GLU A 100  0                                        
SHEET    2 AA2 3 VAL A 145  LEU A 147 -1  O  LEU A 147   N  GLY A  99           
SHEET    3 AA2 3 ALA A 153  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1 AA3 2 VAL A 135  VAL A 136  0                                        
SHEET    2 AA3 2 ASN A 162  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1 AA4 7 TRP A 396  LEU A 398  0                                        
SHEET    2 AA4 7 TYR B 240  LYS B 245 -1  O  ALA B 241   N  HIS A 397           
SHEET    3 AA4 7 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    4 AA4 7 LYS B 260  PRO B 269 -1  O  VAL B 262   N  HIS B 255           
SHEET    5 AA4 7 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 265           
SHEET    6 AA4 7 ALA C  71  TRP C  74  1  O  TRP C  74   N  PHE C  50           
SHEET    7 AA4 7 PHE C  81  LEU C  85 -1  O  GLY C  83   N  LEU C  73           
SHEET    1 AA5 4 GLU A 423  VAL A 426  0                                        
SHEET    2 AA5 4 TYR A 431  LYS A 437 -1  O  ARG A 435   N  GLU A 423           
SHEET    3 AA5 4 PHE A 444  GLN A 453 -1  O  LEU A 449   N  LEU A 432           
SHEET    4 AA5 4 TYR A 459  ILE A 466 -1  O  LEU A 460   N  TYR A 452           
SHEET    1 AA6 3 ARG B  78  TRP B  84  0                                        
SHEET    2 AA6 3 PHE B 112  LEU B 118 -1  O  PHE B 112   N  TRP B  84           
SHEET    3 AA6 3 THR B 106  ARG B 107 -1  N  THR B 106   O  VAL B 113           
SHEET    1 AA7 4 LEU B 103  PRO B 104  0                                        
SHEET    2 AA7 4 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA7 4 GLY B 121  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4 AA7 4 GLN B 132  THR B 134 -1  O  THR B 134   N  PHE B 127           
SHEET    1 AA8 5 LEU B 103  PRO B 104  0                                        
SHEET    2 AA8 5 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA8 5 GLY B 121  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4 AA8 5 VAL B 149  VAL B 155 -1  O  ASN B 151   N  TYR B 125           
SHEET    5 AA8 5 ILE B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1 AA9 2 ARG C 151  ILE C 155  0                                        
SHEET    2 AA9 2 THR C 162  THR C 167 -1  O  LEU C 163   N  VAL C 154           
SHEET    1 AB1 3 VAL C 206  ARG C 207  0                                        
SHEET    2 AB1 3 ALA C 226  VAL C 230  1  O  VAL C 230   N  VAL C 206           
SHEET    3 AB1 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1 AB2 3 LYS C 277  CYS C 278  0                                        
SHEET    2 AB2 3 ARG C 298  VAL C 302  1  O  VAL C 300   N  CYS C 278           
SHEET    3 AB2 3 VAL C 308  SER C 313 -1  O  LYS C 309   N  VAL C 301           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.35  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.34  
SITE     1 AC1 16 LEU A  22  GLY A  23  VAL A  24  GLY A  25                    
SITE     2 AC1 16 VAL A  30  ALA A  43  MET A  93  GLU A  94                    
SITE     3 AC1 16 TYR A  95  VAL A  96  GLY A  99  GLU A 100                    
SITE     4 AC1 16 GLU A 143  ASN A 144  LEU A 146  ASP A 157                    
SITE     1 AC2  2 SER A  97  ALA A 149                                          
SITE     1 AC3  1 GLY A 210                                                     
SITE     1 AC4  2 GLY A  23  VAL A  24                                          
SITE     1 AC5  2 LYS A  34  LYS A  41                                          
SITE     1 AC6 12 LEU A  18  GLY A  19  LYS A  29  LYS A  31                    
SITE     2 AC6 12 ILE A  46  ASP A  88  VAL B  81  ARG B  83                    
SITE     3 AC6 12 ASP B 108  ASN B 111  VAL B 113  ILE B 115                    
SITE     1 AC7 12 HIS C 150  THR C 199  ILE C 203  ALA C 204                    
SITE     2 AC7 12 VAL C 224  SER C 225  ALA C 226  HIS C 297                    
SITE     3 AC7 12 ILE C 311  SER C 313  SER C 315  ASP C 316                    
SITE     1 AC8 11 ARG C  69  ILE C 239  SER C 241  PHE C 243                    
SITE     2 AC8 11 ASP C 244  ARG C 268  LEU C 276  VAL C 296                    
SITE     3 AC8 11 HIS C 297  ARG C 298  VAL C 300                               
SITE     1 AC9 11 ARG C  69  MET C  84  THR C  86  THR C  88                    
SITE     2 AC9 11 ASP C  89  TYR C 120  LEU C 128  VAL C 129                    
SITE     3 AC9 11 ILE C 149  HIS C 150  ARG C 151                               
SITE     1 AD1  2 ARG C 151  THR C 167                                          
CRYST1  125.040  125.040  403.360  90.00  90.00 120.00 P 61 2 2     12          
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      0.007997  0.004617  0.000000        0.00000                         
SCALE2      0.000000  0.009235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002479        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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