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Database: PDB
Entry: 4QFS
LinkDB: 4QFS
Original site: 4QFS 
HEADER    SIGNALING PROTEIN/INHIBITOR/ACTIVATOR   21-MAY-14   4QFS              
TITLE     STRUCTURE OF AMPK IN COMPLEX WITH BR2-A769662CORE ACTIVATOR AND       
TITLE    2 STAUROSPORINE INHIBITOR                                              
CAVEAT     4QFS    CHIRALITY ERROR ON C7 AND C8 CENTERS OF STU LIGAND           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: AMPK ALPHA 1;                                              
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-1;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: AMPK BETA 1;                                               
COMPND  15 SYNONYM: AMPK SUBUNIT BETA-1, AMPKB, 5'-AMP-ACTIVATED PROTEIN KINASE 
COMPND  16 40 KDA SUBUNIT;                                                      
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MUTATION: YES;                                                       
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  21 CHAIN: C;                                                            
COMPND  22 FRAGMENT: AMPK GAMMA 1;                                              
COMPND  23 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: AMPK1, PRKAA1;                                                 
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: BROWN RAT,RAT,RATS;                                 
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: BROWN RAT,RAT,RATS;                                 
SOURCE  18 ORGANISM_TAXID: 10116;                                               
SOURCE  19 GENE: PRKAG1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CBM, KINASE, AMPK, SIGNALING PROTEIN-INHIBITOR-ACTIVATOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.CALABRESE,R.G.KURUMBAIL                                           
REVDAT   5   22-NOV-17 4QFS    1       REMARK                                   
REVDAT   4   16-AUG-17 4QFS    1       SOURCE REMARK                            
REVDAT   3   20-AUG-14 4QFS    1       JRNL                                     
REVDAT   2   13-AUG-14 4QFS    1       JRNL                                     
REVDAT   1   06-AUG-14 4QFS    0                                                
JRNL        AUTH   M.F.CALABRESE,F.RAJAMOHAN,M.S.HARRIS,N.L.CASPERS,R.MAGYAR,   
JRNL        AUTH 2 J.M.WITHKA,H.WANG,K.A.BORZILLERI,P.V.SAHASRABUDHE,L.R.HOTH,  
JRNL        AUTH 3 K.F.GEOGHEGAN,S.HAN,J.BROWN,T.A.SUBASHI,A.R.REYES,           
JRNL        AUTH 4 R.K.FRISBIE,J.WARD,R.A.MILLER,J.A.LANDRO,A.T.LONDREGAN,      
JRNL        AUTH 5 P.A.CARPINO,S.CABRAL,A.C.SMITH,E.L.CONN,K.O.CAMERON,X.QIU,   
JRNL        AUTH 6 R.G.KURUMBAIL                                                
JRNL        TITL   STRUCTURAL BASIS FOR AMPK ACTIVATION: NATURAL AND SYNTHETIC  
JRNL        TITL 2 LIGANDS REGULATE KINASE ACTIVITY FROM OPPOSITE POLES BY      
JRNL        TITL 3 DIFFERENT MOLECULAR MECHANISMS.                              
JRNL        REF    STRUCTURE                     V.  22  1161 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25066137                                                     
JRNL        DOI    10.1016/J.STR.2014.06.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.5                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 20802                          
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)  : 0.228                          
REMARK   3   R VALUE            (WORKING SET)  : 0.226                          
REMARK   3   FREE R VALUE                      : 0.269                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1047                           
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               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.55                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 90.54                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3003                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2202                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2861                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2175                   
REMARK   3   BIN FREE R VALUE                        : 0.2762                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.73                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 142                      
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            : 6008                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.69080                                             
REMARK   3    B22 (A**2) : -6.69080                                             
REMARK   3    B33 (A**2) : 13.38150                                             
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) : 0.828               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.894                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6265   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8583   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2020   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 122    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 947    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6265   ; 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   : 851    ; 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   : 7429   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.27                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
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):   28.7835  -75.4714  -16.0284           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1345 T22:   -0.1273                                    
REMARK   3     T33:   -0.2735 T12:    0.0644                                    
REMARK   3     T13:   -0.0058 T23:   -0.1024                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2989 L22:    1.5869                                    
REMARK   3     L33:    2.6095 L12:   -0.1707                                    
REMARK   3     L13:   -0.1758 L23:    0.6955                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0940 S12:    0.0451 S13:    0.0482                     
REMARK   3     S21:   -0.1051 S22:   -0.0878 S23:    0.1831                     
REMARK   3     S31:   -0.6876 S32:   -0.2900 S33:   -0.0063                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   35.0754  -67.5099  -30.9143           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3153 T22:   -0.0178                                    
REMARK   3     T33:   -0.0670 T12:    0.0057                                    
REMARK   3     T13:    0.0537 T23:   -0.1102                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6386 L22:   -0.1891                                    
REMARK   3     L33:    2.9340 L12:   -0.5964                                    
REMARK   3     L13:   -1.5712 L23:    0.8657                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0198 S12:    0.0504 S13:    0.2396                     
REMARK   3     S21:   -0.1276 S22:    0.0685 S23:    0.2578                     
REMARK   3     S31:   -0.5928 S32:   -0.2492 S33:   -0.0882                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   21.7018  -40.7227   16.5192           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0289 T22:    0.3431                                    
REMARK   3     T33:    0.2127 T12:    0.1407                                    
REMARK   3     T13:    0.1913 T23:   -0.5257                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5050 L22:    4.2381                                    
REMARK   3     L33:    3.6816 L12:   -3.1369                                    
REMARK   3     L13:   -0.0882 L23:    4.5419                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1196 S12:   -0.7564 S13:    0.6686                     
REMARK   3     S21:   -0.3574 S22:    1.4672 S23:   -0.8916                     
REMARK   3     S31:   -0.2282 S32:    0.7063 S33:   -1.3476                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085999.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20989                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 750 MM AMMONIUM SULFATE, 500 MM          
REMARK 280  LITHIUM SULFATE, 100 MM TRI-SODIUM CITRATE, 1% ETHYLENE GLYCOL,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
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      133.88000            
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      267.76000            
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      200.82000            
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      334.70000            
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       66.94000            
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      133.88000            
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      267.76000            
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      334.70000            
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      200.82000            
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       66.94000            
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: 10910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 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: 25170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -302.0 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      -61.94000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000     -107.28323            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -66.94000            
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     PRO A   278                                                      
REMARK 465     GLU A   279                                                      
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   394                                                      
REMARK 465     GLU A   516                                                      
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     ARG A   527                                                      
REMARK 465     PRO A   528                                                      
REMARK 465     GLY A   529                                                      
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     ALA B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     LYS B   172                                                      
REMARK 465     CYS B   173                                                      
REMARK 465     SER B   174                                                      
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    26                                                      
REMARK 465     VAL C    27                                                      
REMARK 465     GLU C   181                                                      
REMARK 465     PHE C   182                                                      
REMARK 465     PRO C   183                                                      
REMARK 465     LYS C   184                                                      
REMARK 465     PRO C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     PHE C   187                                                      
REMARK 465     MET C   188                                                      
REMARK 465     SER C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     ILE C   197                                                      
REMARK 465     GLY C   198                                                      
REMARK 465     THR C   199                                                      
REMARK 465     TYR C   200                                                      
REMARK 465     ALA C   201                                                      
REMARK 465     ASN C   202                                                      
REMARK 465     SER C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     TYR C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     GLU C   273                                                      
REMARK 465     GLY C   274                                                      
REMARK 465     VAL C   275                                                      
REMARK 465     VAL C   301                                                      
REMARK 465     VAL C   302                                                      
REMARK 465     ASP C   303                                                      
REMARK 465     GLU C   304                                                      
REMARK 465     HIS C   305                                                      
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     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     LYS A 395    CG   CD   CE   NZ                                   
REMARK 470     ARG A 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 418    CG   CD   CE   NZ                                   
REMARK 470     LEU A 420    CG   CD1  CD2                                       
REMARK 470     ASP A 421    CG   OD1  OD2                                       
REMARK 470     TYR A 422    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     ARG A 433    CG   CD   NE   CZ   NH1  NH2                        
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     TYR A 459    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 468    CG   OD1  OD2                                       
REMARK 470     LYS A 544    CG   CD   CE   NZ                                   
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 201    CG   CD   CE   NZ                                   
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     ASP B 246    CG   OD1  OD2                                       
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     THR C  30    OG1  CG2                                            
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     ARG C  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  99    CG   CD   CE   NZ                                   
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     ARG C 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     LEU C 152    CG   CD1  CD2                                       
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 165    CG1  CG2  CD1                                       
REMARK 470     LEU C 166    CG   CD1  CD2                                       
REMARK 470     LYS C 169    CG   CD   CE   NZ                                   
REMARK 470     ARG C 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 172    CG   CD1  CD2                                       
REMARK 470     LYS C 173    CG   CD   CE   NZ                                   
REMARK 470     PHE C 174    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU C 175    CG   CD1  CD2                                       
REMARK 470     LYS C 176    CG   CD   CE   NZ                                   
REMARK 470     LEU C 177    CG   CD1  CD2                                       
REMARK 470     PHE C 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER C 191    OG                                                  
REMARK 470     LEU C 192    CG   CD1  CD2                                       
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     ARG C 207    CG   CD   NE   CZ   NH1  NH2                        
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     LYS C 263    CG   CD   CE   NZ                                   
REMARK 470     LEU C 276    CG   CD1  CD2                                       
REMARK 470     LYS C 277    CG   CD   CE   NZ                                   
REMARK 470     LEU C 284    CG   CD1  CD2                                       
REMARK 470     GLU C 285    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 287    CG1  CG2  CD1                                       
REMARK 470     ARG C 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 293    CG   CD   OE1  OE2                                  
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     ILE C 311    CG1  CG2  CD1                                       
REMARK 470     VAL C 312    CG1  CG2                                            
REMARK 470     LEU C 318    CG   CD1  CD2                                       
REMARK 470     GLN C 319    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  14   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    HIS A 137       87.64    -68.10                                   
REMARK 500    ASP A 139       34.75     90.30                                   
REMARK 500    TPO A 172      112.99    -32.19                                   
REMARK 500    LEU A 249       53.11    -96.35                                   
REMARK 500    ASP A 271        5.25     55.68                                   
REMARK 500    SER A 404      172.66    -59.80                                   
REMARK 500    ALA A 416      -36.65   -133.48                                   
REMARK 500    VAL A 427      -77.50    -80.21                                   
REMARK 500    VAL A 440      -70.58    -85.49                                   
REMARK 500    VAL A 454      -64.78   -106.60                                   
REMARK 500    TRP B 100       27.75     46.11                                   
REMARK 500    ASP B 108      -67.89    -99.71                                   
REMARK 500    GLN B 109      -74.82   -141.08                                   
REMARK 500    SER B 170       52.69    -92.72                                   
REMARK 500    ILE B 244       93.98    -62.08                                   
REMARK 500    ASP B 246       95.26     62.32                                   
REMARK 500    LYS B 258     -123.28     56.02                                   
REMARK 500    SER C  34      -70.77   -100.09                                   
REMARK 500    GLU C 110       20.54   -142.42                                   
REMARK 500    GLN C 122     -101.51    -75.64                                   
REMARK 500    ASP C 231     -138.07    -79.79                                   
REMARK 500    ASN C 255       39.80    -86.36                                   
REMARK 500    ASN C 256       95.73   -168.43                                   
REMARK 500    LYS C 309      -34.89   -130.06                                   
REMARK 500    LEU C 321       49.48    -93.11                                   
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 32H 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 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QFG   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN THE ABSENCE OF A SYNTHETIC ACTIVATOR                 
REMARK 900 RELATED ID: 4QFR   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN BOUND TO A RELATED SYNTHETIC ACTIVATOR                  
REMARK 900 RELATED ID: 4QFS   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ENGINEERED INSERTION ASGGPGGS                                        
DBREF  4QFS A    0   468  UNP    P54645   AAPK1_RAT       11    479             
DBREF  4QFS A  525   548  UNP    P54645   AAPK1_RAT      536    559             
DBREF  4QFS B   68   270  UNP    P80386   AAKB1_RAT       68    270             
DBREF  4QFS C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4QFS GLY A   -1  UNP  P54645              EXPRESSION TAG                 
SEQADV 4QFS ALA A  517  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS SER A  518  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS GLY A  519  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS GLY A  520  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS PRO A  521  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS GLY A  522  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS GLY A  523  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS SER A  524  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFS MET B   67  UNP  P80386              EXPRESSION TAG                 
SEQADV 4QFS ASP B  108  UNP  P80386    SER   108 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 GLN 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 4QFS TPO A  172  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 172      11                                                       
HET    STU  A 601      61                                                       
HET    32H  A 602      21                                                       
HET     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET     CL  A 605       1                                                       
HET     CL  A 606       1                                                       
HET     CL  B 301       1                                                       
HET    AMP  C 401      23                                                       
HET    SO4  C 402       5                                                       
HET    SO4  C 403       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     STU STAUROSPORINE                                                    
HETNAM     32H 2-BROMO-3-(4-BROMOPHENYL)-4-HYDROXY-6-OXO-6,7-                   
HETNAM   2 32H  DIHYDROTHIENO[2,3-B]PYRIDINE-5-CARBONITRILE                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     32H BR2-A769662CORE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5  32H    C14 H6 BR2 N2 O2 S                                           
FORMUL   6   CL    5(CL 1-)                                                     
FORMUL  11  AMP    C10 H14 N5 O7 P                                              
FORMUL  12  SO4    2(O4 S 2-)                                                   
HELIX    1   1 GLN A   50  LEU A   55  1                                   6    
HELIX    2   2 VAL A   57  LYS A   69  1                                  13    
HELIX    3   3 LEU A  101  ASN A  108  1                                   8    
HELIX    4   4 ASP A  112  ARG A  132  1                                  21    
HELIX    5   5 ASP A  157  SER A  161  5                                   5    
HELIX    6   6 ALA A  181  SER A  186  1                                   6    
HELIX    7   7 GLY A  192  GLY A  210  1                                  19    
HELIX    8   8 HIS A  218  ASP A  228  1                                  11    
HELIX    9   9 ASN A  238  LEU A  249  1                                  12    
HELIX   10  10 THR A  258  HIS A  265  1                                   8    
HELIX   11  11 HIS A  265  GLN A  270  1                                   6    
HELIX   12  12 ARG A  405  LYS A  418  1                                  14    
HELIX   13  13 GLN A  419  ASP A  421  5                                   3    
HELIX   14  14 HIS A  531  ILE A  545  1                                  15    
HELIX   15  15 PHE B   97  ASN B   99  5                                   3    
HELIX   16  16 GLU B  161  SER B  170  1                                  10    
HELIX   17  17 PRO B  207  LEU B  211  5                                   5    
HELIX   18  18 ASN B  232  LEU B  236  5                                   5    
HELIX   19  19 THR C   29  HIS C   35  1                                   7    
HELIX   20  20 ARG C   36  LEU C   40  5                                   5    
HELIX   21  21 GLN C   55  GLY C   67  1                                  13    
HELIX   22  22 ILE C   87  TYR C   98  1                                  12    
HELIX   23  23 ILE C  105  HIS C  111  1                                   7    
HELIX   24  24 LYS C  112  LEU C  121  1                                  10    
HELIX   25  25 SER C  136  ASN C  147  1                                  12    
HELIX   26  26 HIS C  168  LEU C  175  1                                   8    
HELIX   27  27 LEU C  192  GLN C  196  1                                   5    
HELIX   28  28 PRO C  211  ARG C  223  1                                  13    
HELIX   29  29 VAL C  245  GLU C  251  1                                   7    
HELIX   30  30 SER C  260  GLN C  266  1                                   7    
HELIX   31  31 THR C  283  ALA C  294  1                                  12    
HELIX   32  32 LEU C  314  LEU C  321  1                                   8    
SHEET    1   A 6 LYS A  12  ILE A  13  0                                        
SHEET    2   A 6 TYR A  16  GLY A  23 -1  O  TYR A  16   N  ILE A  13           
SHEET    3   A 6 LYS A  29  HIS A  35 -1  O  VAL A  30   N  GLY A  23           
SHEET    4   A 6 LYS A  41  ASN A  48 -1  O  VAL A  44   N  LYS A  31           
SHEET    5   A 6 ASP A  88  GLU A  94 -1  O  MET A  93   N  ALA A  43           
SHEET    6   A 6 GLN A  81  SER A  84 -1  N  ILE A  83   O  PHE A  90           
SHEET    1   B 3 GLY A  99  GLU A 100  0                                        
SHEET    2   B 3 VAL A 145  LEU A 147 -1  O  LEU A 147   N  GLY A  99           
SHEET    3   B 3 ALA A 153  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1   C 2 VAL A 135  VAL A 136  0                                        
SHEET    2   C 2 ASN A 162  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1   D 7 HIS A 397  LEU A 398  0                                        
SHEET    2   D 7 TYR B 240  LEU B 242 -1  O  ALA B 241   N  HIS A 397           
SHEET    3   D 7 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    4   D 7 LYS B 260  PRO B 269 -1  O  LEU B 266   N  LEU B 251           
SHEET    5   D 7 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 265           
SHEET    6   D 7 ALA C  70  ASP C  75  1  O  PRO C  72   N  PHE C  50           
SHEET    7   D 7 SER C  80  THR C  86 -1  O  LEU C  85   N  ALA C  71           
SHEET    1   E 4 ILE A 400  SER A 402  0                                        
SHEET    2   E 4 TYR A 459  SER A 465 -1  O  TYR A 459   N  SER A 402           
SHEET    3   E 4 SER A 445  GLN A 453 -1  N  GLN A 450   O  ASP A 462           
SHEET    4   E 4 TYR A 431  ARG A 436 -1  N  LEU A 432   O  LEU A 449           
SHEET    1   F 3 THR B  80  THR B  85  0                                        
SHEET    2   F 3 ASN B 111  LEU B 116 -1  O  ALA B 114   N  PHE B  82           
SHEET    3   F 3 THR B 106  ARG B 107 -1  N  THR B 106   O  VAL B 113           
SHEET    1   G 4 LEU B 103  PRO B 104  0                                        
SHEET    2   G 4 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3   G 4 GLU B 122  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4   G 4 GLN B 132  THR B 134 -1  O  THR B 134   N  PHE B 127           
SHEET    1   H 5 LEU B 103  PRO B 104  0                                        
SHEET    2   H 5 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3   H 5 GLU B 122  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4   H 5 VAL B 149  GLN B 154 -1  O  ASN B 151   N  TYR B 125           
SHEET    5   H 5 ILE B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1   I 2 ARG C 151  ILE C 155  0                                        
SHEET    2   I 2 THR C 162  THR C 167 -1  O  LEU C 163   N  VAL C 154           
SHEET    1   J 3 VAL C 206  ARG C 207  0                                        
SHEET    2   J 3 ALA C 226  VAL C 230  1  O  PRO C 228   N  VAL C 206           
SHEET    3   J 3 VAL C 236  SER C 241 -1  O  ASP C 238   N  VAL C 229           
SHEET    1   K 2 ARG C 298  LEU C 299  0                                        
SHEET    2   K 2 VAL C 312  SER C 313 -1  O  VAL C 312   N  LEU C 299           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.36  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.34  
SITE     1 AC1 15 LEU A  22  GLY A  23  GLY A  25  VAL A  30                    
SITE     2 AC1 15 ALA A  43  ILE A  77  GLU A  94  TYR A  95                    
SITE     3 AC1 15 VAL A  96  GLU A 100  GLU A 143  ASN A 144                    
SITE     4 AC1 15 LEU A 146  ALA A 156  ASP A 157                               
SITE     1 AC2  7 LYS A  29  ILE A  46  LYS A  51  ASP A  88                    
SITE     2 AC2  7 ARG B  83  ASP B 108  VAL B 113                               
SITE     1 AC3  1 VAL A  24                                                     
SITE     1 AC4  2 SER A  97  ALA A 149                                          
SITE     1 AC5  2 THR B  85  ASP B 136                                          
SITE     1 AC6 10 HIS C 150  ILE C 203  ALA C 204  VAL C 224                    
SITE     2 AC6 10 SER C 225  ALA C 226  HIS C 297  SER C 313                    
SITE     3 AC6 10 SER C 315  ASP C 316                                          
SITE     1 AC7  6 ARG C  69  THR C  86  THR C  88  ILE C 149                    
SITE     2 AC7  6 HIS C 150  ARG C 151                                          
SITE     1 AC8  5 ARG C  69  SER C 241  PHE C 243  HIS C 297                    
SITE     2 AC8  5 ARG C 298                                                     
CRYST1  123.880  123.880  401.640  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      0.008072  0.004661  0.000000        0.00000                         
SCALE2      0.000000  0.009321  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002490        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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