GenomeNet

Database: PDB
Entry: 6B1U
LinkDB: 6B1U
Original site: 6B1U 
HEADER    TRANSFERASE                             19-SEP-17   6B1U              
TITLE     STRUCTURE OF FULL-LENGTH HUMAN AMPK (A2B1G1) IN COMPLEX WITH A SMALL  
TITLE    2 MOLECULE ACTIVATOR SC4                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2; 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-2,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE;      
COMPND   6 EC: 2.7.11.1,2.7.11.27,2.7.11.31;                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 SYNONYM: AMPKB;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 SYNONYM: AMPKG;                                                      
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRKAA2, AMPK, AMPK2;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: PRKAB1, AMPK;                                                  
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: PRKAG1;                                                        
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PETDUET-1                                 
KEYWDS    PHOSPHORYLATED, ACTIVE, HETEROTRIMER, KINASE., TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.JOHNSON,M.C.CAMERINO, 
AUTHOR   2 S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,W.J.SMILES,R.JACOBS,       
AUTHOR   3 H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,B.E.KEMP,R.C.FOITZIK,         
AUTHOR   4 J.B.BAELL,J.S.OAKHILL                                                
REVDAT   3   04-JUL-18 6B1U    1       JRNL                                     
REVDAT   2   02-MAY-18 6B1U    1       JRNL                                     
REVDAT   1   25-APR-18 6B1U    0                                                
JRNL        AUTH   K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.VARGHESE,    
JRNL        AUTH 2 M.A.CAMERINO,S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,      
JRNL        AUTH 3 W.J.SMILES,R.JACOBS,H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,  
JRNL        AUTH 4 R.C.FOITZIK,B.E.KEMP,J.B.BAELL,J.S.OAKHILL                   
JRNL        TITL   STRUCTURAL DETERMINANTS FOR SMALL-MOLECULE ACTIVATION OF     
JRNL        TITL 2 SKELETAL MUSCLE AMPK ALPHA 2 BETA 2 GAMMA 1 BY THE GLUCOSE   
JRNL        TITL 3 IMPORTAGOG SC4.                                              
JRNL        REF    CELL CHEM BIOL                V.  25   728 2018              
JRNL        REFN                   ESSN 2451-9448                               
JRNL        PMID   29657085                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2018.03.008                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
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) : 2.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 71762                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.196                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.226                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3627                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.77                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.84                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.96                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5298                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2440                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5032                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2420                   
REMARK   3   BIN FREE R VALUE                        : 0.2720                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.02                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 266                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14537                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 171                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27170                                              
REMARK   3    B22 (A**2) : -5.67060                                             
REMARK   3    B33 (A**2) : 5.39890                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.71490                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.360               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.531               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.275               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.606               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.286               
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      : 0.932                         
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              : 15198  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 20731  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5006   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 296    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2198   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 15198  ; 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   : 2011   ; 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   : 16650  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.01                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.69                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1638   53.6043  -22.0760           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1737 T22:   -0.0116                                    
REMARK   3     T33:   -0.0671 T12:   -0.0169                                    
REMARK   3     T13:   -0.0667 T23:   -0.0158                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0323 L22:    1.2536                                    
REMARK   3     L33:    0.9188 L12:    1.1852                                    
REMARK   3     L13:   -1.1734 L23:   -0.4762                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0742 S12:    0.1153 S13:    0.0113                     
REMARK   3     S21:   -0.1098 S22:    0.0990 S23:   -0.0499                     
REMARK   3     S31:    0.1479 S32:   -0.0853 S33:   -0.0247                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    2.9734   36.0527  -19.1068           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1470 T22:   -0.2515                                    
REMARK   3     T33:   -0.2127 T12:    0.0783                                    
REMARK   3     T13:    0.0427 T23:    0.0332                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6707 L22:    2.0221                                    
REMARK   3     L33:    1.5406 L12:    1.7766                                    
REMARK   3     L13:   -1.3228 L23:   -1.5102                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2780 S12:    0.0670 S13:   -0.1584                     
REMARK   3     S21:   -0.1781 S22:    0.2020 S23:   -0.2209                     
REMARK   3     S31:    0.3995 S32:    0.0673 S33:    0.0760                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -36.1154    5.5559  -50.5487           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0904 T22:   -0.1141                                    
REMARK   3     T33:   -0.1266 T12:    0.1277                                    
REMARK   3     T13:    0.0351 T23:    0.0029                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4076 L22:    1.1306                                    
REMARK   3     L33:    1.2023 L12:   -0.8783                                    
REMARK   3     L13:    0.8234 L23:   -0.5532                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2029 S12:   -0.3201 S13:    0.0379                     
REMARK   3     S21:    0.2589 S22:    0.2689 S23:    0.0889                     
REMARK   3     S31:   -0.2754 S32:   -0.2480 S33:   -0.0660                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -34.8630   24.6059  -52.6795           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0636 T22:   -0.2007                                    
REMARK   3     T33:   -0.1942 T12:    0.0873                                    
REMARK   3     T13:   -0.1075 T23:   -0.0678                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8071 L22:    2.1942                                    
REMARK   3     L33:    0.9592 L12:   -1.1598                                    
REMARK   3     L13:    0.6164 L23:   -1.5810                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1648 S12:   -0.2110 S13:    0.0736                     
REMARK   3     S21:    0.3741 S22:    0.2248 S23:   -0.0418                     
REMARK   3     S31:   -0.2679 S32:    0.0441 S33:   -0.0600                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   35.8697   77.7248  -33.4083           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2072 T22:   -0.1790                                    
REMARK   3     T33:   -0.1363 T12:    0.0362                                    
REMARK   3     T13:   -0.0136 T23:   -0.0110                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9472 L22:    1.8718                                    
REMARK   3     L33:    2.3645 L12:    0.8196                                    
REMARK   3     L13:   -1.4911 L23:   -0.4521                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0865 S12:   -0.1654 S13:    0.1831                     
REMARK   3     S21:    0.0767 S22:    0.0083 S23:   -0.1221                     
REMARK   3     S31:   -0.3387 S32:    0.2502 S33:   -0.0949                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.2804  -15.8287  -35.7343           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1915 T22:   -0.0943                                    
REMARK   3     T33:   -0.1697 T12:    0.0807                                    
REMARK   3     T13:   -0.0516 T23:   -0.0083                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5864 L22:    1.0325                                    
REMARK   3     L33:    3.1044 L12:   -0.4696                                    
REMARK   3     L13:    0.8453 L23:   -0.2472                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1048 S12:   -0.2329 S13:   -0.0896                     
REMARK   3     S21:    0.0465 S22:    0.1302 S23:   -0.1829                     
REMARK   3     S31:    0.1216 S32:    0.3543 S33:   -0.0254                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6B1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230128.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71788                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 4ZHX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.1 M MGCL2, 1.0%           
REMARK 280  GLUCOSE, 0.001% COCAMIDOPROPYL BETAINE AND 0.1 M IMIDAZOLE., PH     
REMARK 280  6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       66.94850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 15930 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 16340 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     PRO 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     GLU A   301                                                      
REMARK 465     CYS A   302                                                      
REMARK 465     THR A   303                                                      
REMARK 465     SER A   313                                                      
REMARK 465     GLY A   314                                                      
REMARK 465     ASP A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     GLY A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     PHE A   351                                                      
REMARK 465     MET A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     SER A   355                                                      
REMARK 465     ALA A   356                                                      
REMARK 465     MET A   357                                                      
REMARK 465     HIS A   358                                                      
REMARK 465     ILE A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     ALA A   374A                                                     
REMARK 465     ASP A   374B                                                     
REMARK 465     SER A   374C                                                     
REMARK 465     PRO A   374D                                                     
REMARK 465     LYS A   374E                                                     
REMARK 465     ALA A   374F                                                     
REMARK 465     ARG A   374G                                                     
REMARK 465     CYS A   374H                                                     
REMARK 465     PRO A   374I                                                     
REMARK 465     LEU A   374J                                                     
REMARK 465     ASP A   374K                                                     
REMARK 465     ALA A   374L                                                     
REMARK 465     LEU A   374M                                                     
REMARK 465     ASN A   374N                                                     
REMARK 465     THR A   374O                                                     
REMARK 465     THR A   374P                                                     
REMARK 465     LYS A   374Q                                                     
REMARK 465     PRO A   374R                                                     
REMARK 465     LYS A   374S                                                     
REMARK 465     SER A   374T                                                     
REMARK 465     LEU A   374U                                                     
REMARK 465     ALA A   374V                                                     
REMARK 465     VAL A   374W                                                     
REMARK 465     GLU A   469                                                      
REMARK 465     VAL A   470                                                      
REMARK 465     VAL A   471                                                      
REMARK 465     GLU A   472                                                      
REMARK 465     GLN A   473                                                      
REMARK 465     ARG A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     ARG A   482                                                      
REMARK 465     SER A   483                                                      
REMARK 465     CYS A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     ALA A   486                                                      
REMARK 465     ALA A   487                                                      
REMARK 465     GLY A   488                                                      
REMARK 465     LEU A   489                                                      
REMARK 465     HIS A   490                                                      
REMARK 465     ARG A   491                                                      
REMARK 465     PRO A   492                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     SER A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     PHE A   496                                                      
REMARK 465     ASP A   497                                                      
REMARK 465     SER A   498                                                      
REMARK 465     THR A   499                                                      
REMARK 465     THR A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     SER A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     LEU A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     LEU A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     GLY A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     THR A   518                                                      
REMARK 465     LEU A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     VAL A   522                                                      
REMARK 465     SER A   523                                                      
REMARK 465     ALA A   545                                                      
REMARK 465     ARG A   546                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     THR B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     ARG B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     THR B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     ASP B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     ILE B    36                                                      
REMARK 465     LEU B    37                                                      
REMARK 465     MET B    38                                                      
REMARK 465     ASP B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     PRO B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     PHE B    47                                                      
REMARK 465     HIS B    48                                                      
REMARK 465     SER B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     ILE B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     LYS B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     PHE B    60                                                      
REMARK 465     LEU B    61                                                      
REMARK 465     ALA B    62                                                      
REMARK 465     TRP B    63                                                      
REMARK 465     GLN B    64                                                      
REMARK 465     HIS B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     LEU B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ASP 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     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     MET C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     GLN C    -1                                                      
REMARK 465     ASP C     0                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     LYS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     PRO C   347                                                      
REMARK 465     SER C   348                                                      
REMARK 465     GLY C   349                                                      
REMARK 465     SER C   350                                                      
REMARK 465     PHE C   351                                                      
REMARK 465     MET C   352                                                      
REMARK 465     ASP C   353                                                      
REMARK 465     ASP C   354                                                      
REMARK 465     SER C   355                                                      
REMARK 465     ALA C   356                                                      
REMARK 465     SER C   376A                                                     
REMARK 465     PRO C   376B                                                     
REMARK 465     LYS C   376C                                                     
REMARK 465     ALA C   376D                                                     
REMARK 465     ARG C   376E                                                     
REMARK 465     CYS C   376F                                                     
REMARK 465     PRO C   376G                                                     
REMARK 465     LEU C   376H                                                     
REMARK 465     ASP C   376I                                                     
REMARK 465     ALA C   376J                                                     
REMARK 465     LEU C   376K                                                     
REMARK 465     ASN C   376L                                                     
REMARK 465     THR C   376M                                                     
REMARK 465     THR C   376N                                                     
REMARK 465     LYS C   376O                                                     
REMARK 465     PRO C   376P                                                     
REMARK 465     LYS C   376Q                                                     
REMARK 465     SER C   376R                                                     
REMARK 465     LEU C   376S                                                     
REMARK 465     GLU C   469                                                      
REMARK 465     VAL C   470                                                      
REMARK 465     VAL C   471                                                      
REMARK 465     GLU C   472                                                      
REMARK 465     GLN C   473                                                      
REMARK 465     ARG C   474                                                      
REMARK 465     SER C   475                                                      
REMARK 465     GLY C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     SER C   478                                                      
REMARK 465     THR C   479                                                      
REMARK 465     PRO C   480                                                      
REMARK 465     GLN C   481                                                      
REMARK 465     ARG C   482                                                      
REMARK 465     SER C   483                                                      
REMARK 465     CYS C   484                                                      
REMARK 465     SER C   485                                                      
REMARK 465     ALA C   486                                                      
REMARK 465     ALA C   487                                                      
REMARK 465     GLY C   488                                                      
REMARK 465     LEU C   489                                                      
REMARK 465     HIS C   490                                                      
REMARK 465     ARG C   491                                                      
REMARK 465     PRO C   492                                                      
REMARK 465     ARG C   493                                                      
REMARK 465     SER C   494                                                      
REMARK 465     SER C   495                                                      
REMARK 465     PHE C   496                                                      
REMARK 465     ASP C   497                                                      
REMARK 465     SER C   498                                                      
REMARK 465     THR C   499                                                      
REMARK 465     THR C   500                                                      
REMARK 465     ALA C   501                                                      
REMARK 465     GLU C   502                                                      
REMARK 465     SER C   503                                                      
REMARK 465     HIS C   504                                                      
REMARK 465     SER C   505                                                      
REMARK 465     LEU C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     GLY C   508                                                      
REMARK 465     SER C   509                                                      
REMARK 465     LEU C   510                                                      
REMARK 465     THR C   511                                                      
REMARK 465     GLY C   512                                                      
REMARK 465     SER C   513                                                      
REMARK 465     LEU C   514                                                      
REMARK 465     THR C   515                                                      
REMARK 465     GLY C   516                                                      
REMARK 465     SER C   517                                                      
REMARK 465     THR C   518                                                      
REMARK 465     LEU C   519                                                      
REMARK 465     SER C   520                                                      
REMARK 465     SER C   521                                                      
REMARK 465     VAL C   522                                                      
REMARK 465     SER C   523                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     ARG D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     GLU D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     HIS D    14                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     HIS D    17                                                      
REMARK 465     LYS D    18                                                      
REMARK 465     THR D    19                                                      
REMARK 465     PRO D    20                                                      
REMARK 465     ARG D    21                                                      
REMARK 465     ARG D    22                                                      
REMARK 465     ASP D    23                                                      
REMARK 465     SER D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     THR D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     ASP D    30                                                      
REMARK 465     GLY D    31                                                      
REMARK 465     ASP D    32                                                      
REMARK 465     ARG D    33                                                      
REMARK 465     PRO D    34                                                      
REMARK 465     LYS D    35                                                      
REMARK 465     ILE D    36                                                      
REMARK 465     LEU D    37                                                      
REMARK 465     MET D    38                                                      
REMARK 465     ASP D    39                                                      
REMARK 465     SER D    40                                                      
REMARK 465     PRO D    41                                                      
REMARK 465     GLU D    42                                                      
REMARK 465     ASP D    43                                                      
REMARK 465     ALA D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     PHE D    47                                                      
REMARK 465     HIS D    48                                                      
REMARK 465     SER D    49                                                      
REMARK 465     GLU D    50                                                      
REMARK 465     GLU D    51                                                      
REMARK 465     ILE D    52                                                      
REMARK 465     LYS D    53                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     PRO D    55                                                      
REMARK 465     GLU D    56                                                      
REMARK 465     LYS D    57                                                      
REMARK 465     GLU D    58                                                      
REMARK 465     GLU D    59                                                      
REMARK 465     PHE D    60                                                      
REMARK 465     LEU D    61                                                      
REMARK 465     ALA D    62                                                      
REMARK 465     TRP D    63                                                      
REMARK 465     GLN D    64                                                      
REMARK 465     HIS D    65                                                      
REMARK 465     ASP D    66                                                      
REMARK 465     LEU D    67                                                      
REMARK 465     GLU D    68                                                      
REMARK 465     VAL D    69                                                      
REMARK 465     ASN D    70                                                      
REMARK 465     ASP D    71                                                      
REMARK 465     LYS D    72                                                      
REMARK 465     ALA D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     ALA D    75                                                      
REMARK 465     SER D   180                                                      
REMARK 465     SER D   181                                                      
REMARK 465     SER D   182                                                      
REMARK 465     PRO D   183                                                      
REMARK 465     PRO D   184                                                      
REMARK 465     GLY D   185                                                      
REMARK 465     LYS D   195                                                      
REMARK 465     PRO D   196                                                      
REMARK 465     GLU D   197                                                      
REMARK 465     GLU D   198                                                      
REMARK 465     ARG D   199                                                      
REMARK 465     PHE D   200                                                      
REMARK 465     ILE D   270                                                      
REMARK 465     MET E    -4                                                      
REMARK 465     ALA E    -3                                                      
REMARK 465     ASP E    -2                                                      
REMARK 465     LEU E    -1                                                      
REMARK 465     ASN E     0                                                      
REMARK 465     TRP E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     ILE E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     SER E     7                                                      
REMARK 465     ASP E     8                                                      
REMARK 465     SER E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     PRO E    11                                                      
REMARK 465     ALA E    12                                                      
REMARK 465     VAL E    13                                                      
REMARK 465     GLU E    14                                                      
REMARK 465     ASN E    15                                                      
REMARK 465     GLU E    16                                                      
REMARK 465     HIS E    17                                                      
REMARK 465     PRO E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     GLU E    20                                                      
REMARK 465     THR E    21                                                      
REMARK 465     PRO E    22                                                      
REMARK 465     GLU E    23                                                      
REMARK 465     SER E    24                                                      
REMARK 465     ASN E    25                                                      
REMARK 465     ASP E   124                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLY E   327                                                      
REMARK 465     GLU E   328                                                      
REMARK 465     LYS E   329                                                      
REMARK 465     LYS E   330                                                      
REMARK 465     PRO E   331                                                      
REMARK 465     MET F    -4                                                      
REMARK 465     ALA F    -3                                                      
REMARK 465     ASP F    -2                                                      
REMARK 465     LEU F    -1                                                      
REMARK 465     ASN F     0                                                      
REMARK 465     TRP F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     THR F     3                                                      
REMARK 465     VAL F     4                                                      
REMARK 465     ILE F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     SER F     7                                                      
REMARK 465     ASP F     8                                                      
REMARK 465     SER F     9                                                      
REMARK 465     SER F    10                                                      
REMARK 465     PRO F    11                                                      
REMARK 465     ALA F    12                                                      
REMARK 465     VAL F    13                                                      
REMARK 465     GLU F    14                                                      
REMARK 465     ASN F    15                                                      
REMARK 465     GLU F    16                                                      
REMARK 465     HIS F    17                                                      
REMARK 465     PRO F    18                                                      
REMARK 465     GLN F    19                                                      
REMARK 465     GLU F    20                                                      
REMARK 465     THR F    21                                                      
REMARK 465     PRO F    22                                                      
REMARK 465     GLU F    23                                                      
REMARK 465     SER F    24                                                      
REMARK 465     ASP F   124                                                      
REMARK 465     THR F   325                                                      
REMARK 465     GLY F   326                                                      
REMARK 465     GLY F   327                                                      
REMARK 465     GLU F   328                                                      
REMARK 465     LYS F   329                                                      
REMARK 465     LYS F   330                                                      
REMARK 465     PRO F   331                                                      
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     ASP A   8    CG   OD1  OD2                                       
REMARK 470     LYS A  12    CD   CE   NZ                                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     LYS A  60    CE   NZ                                             
REMARK 470     LYS A  62    CD   CE   NZ                                        
REMARK 470     ARG A  72    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 112    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 217    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 224    CE   NZ                                             
REMARK 470     ARG A 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     GLU A 291    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     LYS A 299    CD   CE   NZ                                        
REMARK 470     PHE A 300    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 304    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 309    CG   OD1  ND2                                       
REMARK 470     GLN A 317    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 318    CG   OD1  OD2                                       
REMARK 470     GLN A 319    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 320    CG   CD1  CD2                                       
REMARK 470     ARG A 332    CZ   NH1  NH2                                       
REMARK 470     LEU A 363    CG   CD1  CD2                                       
REMARK 470     LYS A 364    CG   CD   CE   NZ                                   
REMARK 470     LYS A 392    CG   CD   CE   NZ                                   
REMARK 470     LYS A 393    CG   CD   CE   NZ                                   
REMARK 470     LYS A 405    CE   NZ                                             
REMARK 470     TYR A 407    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 418    CG   CD   CE   NZ                                   
REMARK 470     VAL A 426    CG1  CG2                                            
REMARK 470     LYS A 437    CE   NZ                                             
REMARK 470     ARG A 457    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 468    CG   OD1  OD2                                       
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  89    CG   CD   CE   NZ                                   
REMARK 470     ASN B  99    CG   OD1  ND2                                       
REMARK 470     LYS B 102    CE   NZ                                             
REMARK 470     ASP B 117    CG   OD1  OD2                                       
REMARK 470     GLU B 122    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     MET B 167    SD   CE                                             
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 190    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 195    CG   CD   CE   NZ                                   
REMARK 470     GLU B 197    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 198    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 200    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 245    CE   NZ                                             
REMARK 470     LYS B 259    CD   CE   NZ                                        
REMARK 470     ILE B 270    CG1  CG2  CD1                                       
REMARK 470     ARG C  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  12    CE   NZ                                             
REMARK 470     LYS C  51    CD   CE   NZ                                        
REMARK 470     LYS C  60    CE   NZ                                             
REMARK 470     LYS C  62    CE   NZ                                             
REMARK 470     ARG C  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 217    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 219    CG1  CG2                                            
REMARK 470     LYS C 224    CG   CD   CE   NZ                                   
REMARK 470     LYS C 225    CG   CD   CE   NZ                                   
REMARK 470     LYS C 260    CG   CD   CE   NZ                                   
REMARK 470     ASP C 290    CG   OD1  OD2                                       
REMARK 470     GLN C 317    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 318    CG   OD1  OD2                                       
REMARK 470     GLN C 319    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 320    CG   CD1  CD2                                       
REMARK 470     MET C 357    CG   SD   CE                                        
REMARK 470     HIS C 358    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE C 359    CG1  CG2  CD1                                       
REMARK 470     LEU C 363    CG   CD1  CD2                                       
REMARK 470     LYS C 364    CG   CD   CE   NZ                                   
REMARK 470     LYS C 392    CG   CD   CE   NZ                                   
REMARK 470     LYS C 393    CG   CD   CE   NZ                                   
REMARK 470     LYS C 405    CG   CD   CE   NZ                                   
REMARK 470     GLU C 412    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 418    CG   CD   CE   NZ                                   
REMARK 470     LYS C 437    CG   CD   CE   NZ                                   
REMARK 470     ARG C 457    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 467    CG   OD1  OD2                                       
REMARK 470     LEU C 540    CG   CD1  CD2                                       
REMARK 470     LEU C 544    CG   CD1  CD2                                       
REMARK 470     ARG C 546    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  89    CG   CD   CE   NZ                                   
REMARK 470     GLU D 120    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 156    CE   NZ                                             
REMARK 470     LYS D 157    CG   CD   CE   NZ                                   
REMARK 470     LYS D 172    CD   CE   NZ                                        
REMARK 470     LEU D 179    CG   CD1  CD2                                       
REMARK 470     GLU D 190    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 217    CG   CD   CE   NZ                                   
REMARK 470     LYS D 245    CD   CE   NZ                                        
REMARK 470     LYS D 258    NZ                                                  
REMARK 470     ASN E  26    CG   OD1  ND2                                       
REMARK 470     LEU E 122    CG   CD1  CD2                                       
REMARK 470     GLN E 123    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 127    CE   NZ                                             
REMARK 470     GLU E 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 177    CD   CE   NZ                                        
REMARK 470     GLU E 187    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 195    CD   OE1  OE2                                       
REMARK 470     GLN E 197    CG   CD   OE1  NE2                                  
REMARK 470     ARG E 208    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E 222    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 233    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 234    CG   CD   CE   NZ                                   
REMARK 470     ARG E 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 264    CE   NZ                                             
REMARK 470     HIS E 271    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU E 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 278    CG   CD   CE   NZ                                   
REMARK 470     GLU E 294    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 310    CG   CD   CE   NZ                                   
REMARK 470     LEU E 324    CG   CD1  CD2                                       
REMARK 470     ASN F  25    CG   OD1  ND2                                       
REMARK 470     ASN F  26    CG   OD1  ND2                                       
REMARK 470     TYR F 107    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU F 111    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 119    CG   CD   OE1  OE2                                  
REMARK 470     SER F 125    OG                                                  
REMARK 470     LYS F 127    CD   CE   NZ                                        
REMARK 470     GLU F 187    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 194    CG   CD   OE1  OE2                                  
REMARK 470     GLN F 197    CG   CD   OE1  NE2                                  
REMARK 470     LEU F 228    CG   CD1  CD2                                       
REMARK 470     GLU F 233    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 264    CG   CD   CE   NZ                                   
REMARK 470     SER F 270    OG                                                  
REMARK 470     HIS F 271    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS F 278    CG   CD   CE   NZ                                   
REMARK 470     ASN F 306    CG   OD1  ND2                                       
REMARK 470     LYS F 310    CG   CD   CE   NZ                                   
REMARK 470     VAL F 323    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HIS C   358     N    VAL E   309     1445     2.01            
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    ASP A 139       45.73   -146.35                                   
REMARK 500    ALA A 156      -55.38   -129.47                                   
REMARK 500    TPO A 172      122.37    -33.22                                   
REMARK 500    LEU A 249       42.02   -100.73                                   
REMARK 500    GLU A 279      -11.41     85.96                                   
REMARK 500    LYS A 393       72.20     58.65                                   
REMARK 500    SEP B 108     -117.29    -93.47                                   
REMARK 500    ASN B 237      -10.50     73.44                                   
REMARK 500    LYS B 258     -116.00     60.29                                   
REMARK 500    ASP C 139       39.98   -143.33                                   
REMARK 500    ALA C 156      -50.46   -133.95                                   
REMARK 500    CYS C 174     -130.04     59.85                                   
REMARK 500    GLU C 279       -0.89     75.80                                   
REMARK 500    ALA C 337       56.37   -115.92                                   
REMARK 500    SER C 344     -157.10    -86.26                                   
REMARK 500    ASP C 455     -133.63     54.26                                   
REMARK 500    SEP D 108     -111.67    -94.22                                   
REMARK 500    ILE D 221      -33.98    -37.97                                   
REMARK 500    ASN D 237       -4.45     71.84                                   
REMARK 500    LYS D 258     -123.10     56.50                                   
REMARK 500    VAL E 323      -65.84   -107.05                                   
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 CG7 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue STU C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CG7 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP F 402                 
DBREF  6B1U A    2   546  UNP    P54646   AAPK2_HUMAN      2    552             
DBREF  6B1U B    1   270  UNP    Q9Y478   AAKB1_HUMAN      1    270             
DBREF  6B1U C    2   546  UNP    P54646   AAPK2_HUMAN      2    552             
DBREF  6B1U D    1   270  UNP    Q9Y478   AAKB1_HUMAN      1    270             
DBREF  6B1U E    2   331  UNP    P54619   AAKG1_HUMAN      2    331             
DBREF  6B1U F    2   331  UNP    P54619   AAKG1_HUMAN      2    331             
SEQADV 6B1U MET A  -12  UNP  P54646              INITIATING METHIONINE          
SEQADV 6B1U GLY A  -11  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER A  -10  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER A   -9  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -8  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -7  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -6  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -5  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -4  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS A   -3  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER A   -2  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U GLN A   -1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U ASP A    0  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U PRO A    1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U GLY A  271  UNP  P54646    ASP   271 CONFLICT                       
SEQADV 6B1U MET C  -12  UNP  P54646              INITIATING METHIONINE          
SEQADV 6B1U GLY C  -11  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER C  -10  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER C   -9  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -8  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -7  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -6  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -5  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -4  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U HIS C   -3  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U SER C   -2  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U GLN C   -1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U ASP C    0  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U PRO C    1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B1U GLY C  271  UNP  P54646    ASP   271 CONFLICT                       
SEQADV 6B1U MET E   -4  UNP  P54619              INITIATING METHIONINE          
SEQADV 6B1U ALA E   -3  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U ASP E   -2  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U LEU E   -1  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U ASN E    0  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U TRP E    1  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U MET F   -4  UNP  P54619              INITIATING METHIONINE          
SEQADV 6B1U ALA F   -3  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U ASP F   -2  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U LEU F   -1  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U ASN F    0  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B1U TRP F    1  UNP  P54619              EXPRESSION TAG                 
SEQRES   1 A  565  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  565  PRO ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL LYS ILE          
SEQRES   3 A  565  GLY HIS TYR VAL LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   4 A  565  PHE GLY LYS VAL LYS ILE GLY GLU HIS GLN LEU THR GLY          
SEQRES   5 A  565  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   6 A  565  ARG SER LEU ASP VAL VAL GLY LYS ILE LYS ARG GLU ILE          
SEQRES   7 A  565  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   8 A  565  LEU TYR GLN VAL ILE SER THR PRO THR ASP PHE PHE MET          
SEQRES   9 A  565  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 A  565  ILE CYS LYS HIS GLY ARG VAL GLU GLU MET GLU ALA ARG          
SEQRES  11 A  565  ARG LEU PHE GLN GLN ILE LEU SER ALA VAL ASP TYR CYS          
SEQRES  12 A  565  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 A  565  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  14 A  565  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  15 A  565  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  16 A  565  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  17 A  565  ASP ILE TRP SER CYS GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  18 A  565  CYS GLY THR LEU PRO PHE ASP ASP GLU HIS VAL PRO THR          
SEQRES  19 A  565  LEU PHE LYS LYS ILE ARG GLY GLY VAL PHE TYR ILE PRO          
SEQRES  20 A  565  GLU TYR LEU ASN ARG SER VAL ALA THR LEU LEU MET HIS          
SEQRES  21 A  565  MET LEU GLN VAL ASP PRO LEU LYS ARG ALA THR ILE LYS          
SEQRES  22 A  565  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN GLY LEU PRO          
SEQRES  23 A  565  SER TYR LEU PHE PRO GLU ASP PRO SER TYR ASP ALA ASN          
SEQRES  24 A  565  VAL ILE ASP ASP GLU ALA VAL LYS GLU VAL CYS GLU LYS          
SEQRES  25 A  565  PHE GLU CYS THR GLU SER GLU VAL MET ASN SER LEU TYR          
SEQRES  26 A  565  SER GLY ASP PRO GLN ASP GLN LEU ALA VAL ALA TYR HIS          
SEQRES  27 A  565  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLN ALA SER          
SEQRES  28 A  565  GLU PHE TYR LEU ALA SER SER PRO PRO SER GLY SER PHE          
SEQRES  29 A  565  MET ASP ASP SER ALA MET HIS ILE PRO PRO GLY LEU LYS          
SEQRES  30 A  565  PRO HIS PRO GLU ARG MET PRO PRO LEU ILE ALA ASP SER          
SEQRES  31 A  565  PRO LYS ALA ARG CYS PRO LEU ASP ALA LEU ASN THR THR          
SEQRES  32 A  565  LYS PRO LYS SER LEU ALA VAL LYS LYS ALA LYS TRP HIS          
SEQRES  33 A  565  LEU GLY ILE ARG SER GLN SER LYS PRO TYR ASP ILE MET          
SEQRES  34 A  565  ALA GLU VAL TYR ARG ALA MET LYS GLN LEU ASP PHE GLU          
SEQRES  35 A  565  TRP LYS VAL VAL ASN ALA TYR HIS LEU ARG VAL ARG ARG          
SEQRES  36 A  565  LYS ASN PRO VAL THR GLY ASN TYR VAL LYS MET SER LEU          
SEQRES  37 A  565  GLN LEU TYR LEU VAL ASP ASN ARG SER TYR LEU LEU ASP          
SEQRES  38 A  565  PHE LYS SER ILE ASP ASP GLU VAL VAL GLU GLN ARG SER          
SEQRES  39 A  565  GLY SER SER THR PRO GLN ARG SER CYS SER ALA ALA GLY          
SEQRES  40 A  565  LEU HIS ARG PRO ARG SER SER PHE ASP SER THR THR ALA          
SEQRES  41 A  565  GLU SER HIS SER LEU SER GLY SER LEU THR GLY SER LEU          
SEQRES  42 A  565  THR GLY SER THR LEU SER SER VAL SER PRO ARG LEU GLY          
SEQRES  43 A  565  SER HIS THR MET ASP PHE PHE GLU MET CYS ALA SER LEU          
SEQRES  44 A  565  ILE THR THR LEU ALA ARG                                      
SEQRES   1 B  270  MET GLY ASN THR SER SER GLU ARG ALA ALA LEU GLU ARG          
SEQRES   2 B  270  HIS GLY GLY HIS LYS THR PRO ARG ARG ASP SER SER GLY          
SEQRES   3 B  270  GLY THR LYS ASP GLY ASP ARG PRO LYS ILE LEU MET ASP          
SEQRES   4 B  270  SER PRO GLU ASP ALA ASP LEU PHE HIS SER GLU GLU ILE          
SEQRES   5 B  270  LYS ALA PRO GLU LYS GLU GLU PHE LEU ALA TRP GLN HIS          
SEQRES   6 B  270  ASP LEU GLU VAL ASN ASP LYS ALA PRO ALA GLN ALA ARG          
SEQRES   7 B  270  PRO THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL          
SEQRES   8 B  270  TYR LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO          
SEQRES   9 B  270  LEU THR ARG SEP HIS ASN ASN PHE VAL ALA ILE LEU ASP          
SEQRES  10 B  270  LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP          
SEQRES  11 B  270  GLY GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR          
SEQRES  12 B  270  SER GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS          
SEQRES  13 B  270  LYS THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP          
SEQRES  14 B  270  SER GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER          
SEQRES  15 B  270  PRO PRO GLY PRO TYR HIS GLN GLU PRO TYR VAL CYS LYS          
SEQRES  16 B  270  PRO GLU GLU ARG PHE ARG ALA PRO PRO ILE LEU PRO PRO          
SEQRES  17 B  270  HIS LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE          
SEQRES  18 B  270  SER CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL          
SEQRES  19 B  270  MET LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY          
SEQRES  20 B  270  VAL MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS          
SEQRES  21 B  270  TYR VAL THR THR LEU LEU TYR LYS PRO ILE                      
SEQRES   1 C  565  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 C  565  PRO ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL LYS ILE          
SEQRES   3 C  565  GLY HIS TYR VAL LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   4 C  565  PHE GLY LYS VAL LYS ILE GLY GLU HIS GLN LEU THR GLY          
SEQRES   5 C  565  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   6 C  565  ARG SER LEU ASP VAL VAL GLY LYS ILE LYS ARG GLU ILE          
SEQRES   7 C  565  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   8 C  565  LEU TYR GLN VAL ILE SER THR PRO THR ASP PHE PHE MET          
SEQRES   9 C  565  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 C  565  ILE CYS LYS HIS GLY ARG VAL GLU GLU MET GLU ALA ARG          
SEQRES  11 C  565  ARG LEU PHE GLN GLN ILE LEU SER ALA VAL ASP TYR CYS          
SEQRES  12 C  565  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 C  565  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  14 C  565  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  15 C  565  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  16 C  565  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  17 C  565  ASP ILE TRP SER CYS GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  18 C  565  CYS GLY THR LEU PRO PHE ASP ASP GLU HIS VAL PRO THR          
SEQRES  19 C  565  LEU PHE LYS LYS ILE ARG GLY GLY VAL PHE TYR ILE PRO          
SEQRES  20 C  565  GLU TYR LEU ASN ARG SER VAL ALA THR LEU LEU MET HIS          
SEQRES  21 C  565  MET LEU GLN VAL ASP PRO LEU LYS ARG ALA THR ILE LYS          
SEQRES  22 C  565  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN GLY LEU PRO          
SEQRES  23 C  565  SER TYR LEU PHE PRO GLU ASP PRO SER TYR ASP ALA ASN          
SEQRES  24 C  565  VAL ILE ASP ASP GLU ALA VAL LYS GLU VAL CYS GLU LYS          
SEQRES  25 C  565  PHE GLU CYS THR GLU SER GLU VAL MET ASN SER LEU TYR          
SEQRES  26 C  565  SER GLY ASP PRO GLN ASP GLN LEU ALA VAL ALA TYR HIS          
SEQRES  27 C  565  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLN ALA SER          
SEQRES  28 C  565  GLU PHE TYR LEU ALA SER SER PRO PRO SER GLY SER PHE          
SEQRES  29 C  565  MET ASP ASP SER ALA MET HIS ILE PRO PRO GLY LEU LYS          
SEQRES  30 C  565  PRO HIS PRO GLU ARG MET PRO PRO LEU ILE ALA ASP SER          
SEQRES  31 C  565  PRO LYS ALA ARG CYS PRO LEU ASP ALA LEU ASN THR THR          
SEQRES  32 C  565  LYS PRO LYS SER LEU ALA VAL LYS LYS ALA LYS TRP HIS          
SEQRES  33 C  565  LEU GLY ILE ARG SER GLN SER LYS PRO TYR ASP ILE MET          
SEQRES  34 C  565  ALA GLU VAL TYR ARG ALA MET LYS GLN LEU ASP PHE GLU          
SEQRES  35 C  565  TRP LYS VAL VAL ASN ALA TYR HIS LEU ARG VAL ARG ARG          
SEQRES  36 C  565  LYS ASN PRO VAL THR GLY ASN TYR VAL LYS MET SER LEU          
SEQRES  37 C  565  GLN LEU TYR LEU VAL ASP ASN ARG SER TYR LEU LEU ASP          
SEQRES  38 C  565  PHE LYS SER ILE ASP ASP GLU VAL VAL GLU GLN ARG SER          
SEQRES  39 C  565  GLY SER SER THR PRO GLN ARG SER CYS SER ALA ALA GLY          
SEQRES  40 C  565  LEU HIS ARG PRO ARG SER SER PHE ASP SER THR THR ALA          
SEQRES  41 C  565  GLU SER HIS SER LEU SER GLY SER LEU THR GLY SER LEU          
SEQRES  42 C  565  THR GLY SER THR LEU SER SER VAL SER PRO ARG LEU GLY          
SEQRES  43 C  565  SER HIS THR MET ASP PHE PHE GLU MET CYS ALA SER LEU          
SEQRES  44 C  565  ILE THR THR LEU ALA ARG                                      
SEQRES   1 D  270  MET GLY ASN THR SER SER GLU ARG ALA ALA LEU GLU ARG          
SEQRES   2 D  270  HIS GLY GLY HIS LYS THR PRO ARG ARG ASP SER SER GLY          
SEQRES   3 D  270  GLY THR LYS ASP GLY ASP ARG PRO LYS ILE LEU MET ASP          
SEQRES   4 D  270  SER PRO GLU ASP ALA ASP LEU PHE HIS SER GLU GLU ILE          
SEQRES   5 D  270  LYS ALA PRO GLU LYS GLU GLU PHE LEU ALA TRP GLN HIS          
SEQRES   6 D  270  ASP LEU GLU VAL ASN ASP LYS ALA PRO ALA GLN ALA ARG          
SEQRES   7 D  270  PRO THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL          
SEQRES   8 D  270  TYR LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO          
SEQRES   9 D  270  LEU THR ARG SEP HIS ASN ASN PHE VAL ALA ILE LEU ASP          
SEQRES  10 D  270  LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP          
SEQRES  11 D  270  GLY GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR          
SEQRES  12 D  270  SER GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS          
SEQRES  13 D  270  LYS THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP          
SEQRES  14 D  270  SER GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER          
SEQRES  15 D  270  PRO PRO GLY PRO TYR HIS GLN GLU PRO TYR VAL CYS LYS          
SEQRES  16 D  270  PRO GLU GLU ARG PHE ARG ALA PRO PRO ILE LEU PRO PRO          
SEQRES  17 D  270  HIS LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE          
SEQRES  18 D  270  SER CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL          
SEQRES  19 D  270  MET LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY          
SEQRES  20 D  270  VAL MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS          
SEQRES  21 D  270  TYR VAL THR THR LEU LEU TYR LYS PRO ILE                      
SEQRES   1 E  336  MET ALA ASP LEU ASN TRP GLU THR VAL ILE SER SER ASP          
SEQRES   2 E  336  SER SER PRO ALA VAL GLU ASN GLU HIS PRO GLN GLU THR          
SEQRES   3 E  336  PRO GLU SER ASN ASN SER VAL TYR THR SER PHE MET LYS          
SEQRES   4 E  336  SER HIS ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS          
SEQRES   5 E  336  LEU VAL VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA          
SEQRES   6 E  336  PHE PHE ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO          
SEQRES   7 E  336  LEU TRP ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU          
SEQRES   8 E  336  THR ILE THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR          
SEQRES   9 E  336  LYS SER ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS          
SEQRES  10 E  336  LYS ILE GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER          
SEQRES  11 E  336  PHE LYS PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU          
SEQRES  12 E  336  PHE ASP ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS          
SEQRES  13 E  336  ARG LEU PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU          
SEQRES  14 E  336  TYR ILE LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS          
SEQRES  15 E  336  LEU PHE ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER          
SEQRES  16 E  336  LYS SER LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN          
SEQRES  17 E  336  ILE ALA MET VAL ARG THR THR THR PRO VAL TYR VAL ALA          
SEQRES  18 E  336  LEU GLY ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO          
SEQRES  19 E  336  VAL VAL ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER          
SEQRES  20 E  336  LYS PHE ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR          
SEQRES  21 E  336  ASN ASN LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS          
SEQRES  22 E  336  ARG SER HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU          
SEQRES  23 E  336  HIS GLU THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU          
SEQRES  24 E  336  ALA GLU VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP          
SEQRES  25 E  336  VAL VAL LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN          
SEQRES  26 E  336  ALA LEU VAL LEU THR GLY GLY GLU LYS LYS PRO                  
SEQRES   1 F  336  MET ALA ASP LEU ASN TRP GLU THR VAL ILE SER SER ASP          
SEQRES   2 F  336  SER SER PRO ALA VAL GLU ASN GLU HIS PRO GLN GLU THR          
SEQRES   3 F  336  PRO GLU SER ASN ASN SER VAL TYR THR SER PHE MET LYS          
SEQRES   4 F  336  SER HIS ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS          
SEQRES   5 F  336  LEU VAL VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA          
SEQRES   6 F  336  PHE PHE ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO          
SEQRES   7 F  336  LEU TRP ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU          
SEQRES   8 F  336  THR ILE THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR          
SEQRES   9 F  336  LYS SER ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS          
SEQRES  10 F  336  LYS ILE GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER          
SEQRES  11 F  336  PHE LYS PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU          
SEQRES  12 F  336  PHE ASP ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS          
SEQRES  13 F  336  ARG LEU PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU          
SEQRES  14 F  336  TYR ILE LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS          
SEQRES  15 F  336  LEU PHE ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER          
SEQRES  16 F  336  LYS SER LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN          
SEQRES  17 F  336  ILE ALA MET VAL ARG THR THR THR PRO VAL TYR VAL ALA          
SEQRES  18 F  336  LEU GLY ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO          
SEQRES  19 F  336  VAL VAL ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER          
SEQRES  20 F  336  LYS PHE ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR          
SEQRES  21 F  336  ASN ASN LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS          
SEQRES  22 F  336  ARG SER HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU          
SEQRES  23 F  336  HIS GLU THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU          
SEQRES  24 F  336  ALA GLU VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP          
SEQRES  25 F  336  VAL VAL LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN          
SEQRES  26 F  336  ALA LEU VAL LEU THR GLY GLY GLU LYS LYS PRO                  
MODRES 6B1U TPO A  172  THR  MODIFIED RESIDUE                                   
MODRES 6B1U SEP B  108  SER  MODIFIED RESIDUE                                   
MODRES 6B1U TPO C  172  THR  MODIFIED RESIDUE                                   
MODRES 6B1U SEP D  108  SER  MODIFIED RESIDUE                                   
HET    TPO  A 172      11                                                       
HET    SEP  B 108      10                                                       
HET    TPO  C 172      11                                                       
HET    SEP  D 108      10                                                       
HET    STU  A 601      35                                                       
HET    CG7  A 602      68                                                       
HET    STU  C 601      35                                                       
HET    CG7  C 602      34                                                       
HET    IMD  C 603       5                                                       
HET    AMP  E 401      23                                                       
HET    AMP  E 402      23                                                       
HET    AMP  F 401      23                                                       
HET    AMP  F 402      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     STU STAUROSPORINE                                                    
HETNAM     CG7 5-{[6-CHLORO-5-(2'-HYDROXY[1,1'-BIPHENYL]-4-YL)-1H-              
HETNAM   2 CG7  IMIDAZO[4,5-B]PYRIDIN-2-YL]OXY}-2-METHYLBENZOIC ACID            
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   2  SEP    2(C3 H8 N O6 P)                                              
FORMUL   7  STU    2(C28 H26 N4 O3)                                             
FORMUL   8  CG7    2(C26 H18 CL N3 O4)                                          
FORMUL  11  IMD    C3 H5 N2 1+                                                  
FORMUL  12  AMP    4(C10 H14 N5 O7 P)                                           
FORMUL  16  HOH   *171(H2 O)                                                    
HELIX    1 AA1 ARG A   49  ASP A   56  1                                   8    
HELIX    2 AA2 VAL A   57  PHE A   71  1                                  15    
HELIX    3 AA3 LEU A  101  GLY A  109  1                                   9    
HELIX    4 AA4 GLU A  112  HIS A  133  1                                  22    
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  GLY A  229  1                                  12    
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 SER A  282  VAL A  287  1                                   6    
HELIX   12 AB3 ASP A  289  PHE A  300  1                                  12    
HELIX   13 AB4 VAL A  307  TYR A  312  1                                   6    
HELIX   14 AB5 ASP A  318  ALA A  337  1                                  20    
HELIX   15 AB6 ALA A  337  LEU A  342  1                                   6    
HELIX   16 AB7 LYS A  405  LEU A  420  1                                  16    
HELIX   17 AB8 SER A  528  LEU A  544  1                                  17    
HELIX   18 AB9 PHE B   97  ASN B   99  5                                   3    
HELIX   19 AC1 LYS B  156  PHE B  160  5                                   5    
HELIX   20 AC2 GLU B  161  ASP B  175  1                                  15    
HELIX   21 AC3 PRO B  207  GLN B  212  5                                   6    
HELIX   22 AC4 ASN B  232  LEU B  236  5                                   5    
HELIX   23 AC5 ARG C   49  ASP C   56  1                                   8    
HELIX   24 AC6 VAL C   57  PHE C   71  1                                  15    
HELIX   25 AC7 GLU C  100  HIS C  108  1                                   9    
HELIX   26 AC8 GLU C  112  HIS C  133  1                                  22    
HELIX   27 AC9 ALA C  181  SER C  186  1                                   6    
HELIX   28 AD1 GLY C  192  GLY C  210  1                                  19    
HELIX   29 AD2 HIS C  218  GLY C  229  1                                  12    
HELIX   30 AD3 ASN C  238  LEU C  249  1                                  12    
HELIX   31 AD4 THR C  258  HIS C  265  1                                   8    
HELIX   32 AD5 HIS C  265  GLN C  270  1                                   6    
HELIX   33 AD6 SER C  282  VAL C  287  1                                   6    
HELIX   34 AD7 ASP C  289  GLU C  301  1                                  13    
HELIX   35 AD8 THR C  303  SER C  313  1                                  11    
HELIX   36 AD9 ASP C  318  GLN C  336  1                                  19    
HELIX   37 AE1 ALA C  337  LEU C  342  1                                   6    
HELIX   38 AE2 LYS C  405  LEU C  420  1                                  16    
HELIX   39 AE3 SER C  528  ARG C  546  1                                  19    
HELIX   40 AE4 PHE D   97  ASN D   99  5                                   3    
HELIX   41 AE5 LYS D  156  PHE D  160  5                                   5    
HELIX   42 AE6 GLU D  161  LEU D  179  1                                  19    
HELIX   43 AE7 PRO D  207  GLN D  212  5                                   6    
HELIX   44 AE8 VAL D  213  LYS D  217  5                                   5    
HELIX   45 AE9 ASN D  232  LEU D  236  5                                   5    
HELIX   46 AF1 SER E   27  HIS E   36  1                                  10    
HELIX   47 AF2 ARG E   37  ILE E   42  5                                   6    
HELIX   48 AF3 GLN E   56  ASN E   67  1                                  12    
HELIX   49 AF4 THR E   87  TYR E   99  1                                  13    
HELIX   50 AF5 ILE E  106  HIS E  112  1                                   7    
HELIX   51 AF6 LYS E  113  GLN E  123  1                                  11    
HELIX   52 AF7 SER E  137  ASN E  148  1                                  12    
HELIX   53 AF8 HIS E  169  PHE E  179  1                                  11    
HELIX   54 AF9 ILE E  180  PHE E  183  5                                   4    
HELIX   55 AG1 SER E  192  GLN E  197  1                                   6    
HELIX   56 AG2 PRO E  212  ARG E  224  1                                  13    
HELIX   57 AG3 PHE E  244  VAL E  246  5                                   3    
HELIX   58 AG4 ILE E  247  GLU E  252  1                                   6    
HELIX   59 AG5 SER E  261  LEU E  266  1                                   6    
HELIX   60 AG6 GLN E  267  SER E  270  5                                   4    
HELIX   61 AG7 THR E  284  GLU E  296  1                                  13    
HELIX   62 AG8 LEU E  315  VAL E  323  1                                   9    
HELIX   63 AG9 SER F   27  HIS F   36  1                                  10    
HELIX   64 AH1 ARG F   37  ILE F   42  5                                   6    
HELIX   65 AH2 GLN F   56  GLY F   68  1                                  13    
HELIX   66 AH3 THR F   87  TYR F   99  1                                  13    
HELIX   67 AH4 ILE F  106  HIS F  112  1                                   7    
HELIX   68 AH5 LYS F  113  LEU F  122  1                                  10    
HELIX   69 AH6 SER F  137  ASN F  148  1                                  12    
HELIX   70 AH7 THR F  168  PHE F  179  1                                  12    
HELIX   71 AH8 ILE F  180  PHE F  183  5                                   4    
HELIX   72 AH9 PRO F  186  LYS F  191  5                                   6    
HELIX   73 AI1 SER F  192  GLN F  197  1                                   6    
HELIX   74 AI2 PRO F  212  ARG F  224  1                                  13    
HELIX   75 AI3 PHE F  244  VAL F  246  5                                   3    
HELIX   76 AI4 ILE F  247  GLU F  252  1                                   6    
HELIX   77 AI5 SER F  261  LEU F  266  1                                   6    
HELIX   78 AI6 GLN F  267  SER F  270  5                                   4    
HELIX   79 AI7 THR F  284  GLU F  296  1                                  13    
HELIX   80 AI8 LEU F  315  LEU F  324  1                                  10    
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  ILE A  32   N  GLY A  19           
SHEET    4 AA1 6 LYS A  41  ASN A  48 -1  O  ILE A  46   N  LYS A  29           
SHEET    5 AA1 6 ASP A  88  GLU A  94 -1  O  MET A  93   N  ALA A  43           
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 HIS A 397  LEU A 398  0                                        
SHEET    2 AA4 7 TYR B 240  ALA B 241 -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  LYS B 260   N  TYR B 257           
SHEET    5 AA4 7 SER E  45  ASP E  52  1  O  LEU E  48   N  LEU B 265           
SHEET    6 AA4 7 ALA E  72  ASP E  76  1  O  TRP E  75   N  PHE E  51           
SHEET    7 AA4 7 SER E  81  LEU E  86 -1  O  GLY E  84   N  LEU E  74           
SHEET    1 AA5 5 ILE A 400  SER A 402  0                                        
SHEET    2 AA5 5 TYR A 459  SER A 465 -1  O  LEU A 461   N  ILE A 400           
SHEET    3 AA5 5 TYR A 444  LEU A 453 -1  N  GLN A 450   O  ASP A 462           
SHEET    4 AA5 5 HIS A 431  LYS A 437 -1  N  LEU A 432   O  LEU A 449           
SHEET    5 AA5 5 GLU A 423  ASN A 428 -1  N  GLU A 423   O  ARG A 435           
SHEET    1 AA6 3 PRO B  79  TRP B  84  0                                        
SHEET    2 AA6 3 PHE B 112  ASP B 117 -1  O  LEU B 116   N  THR B  80           
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  LYS B 126   N  SER B  94           
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  LYS B 126   N  SER B  94           
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 6 LYS C  12  ILE C  13  0                                        
SHEET    2 AA9 6 TYR C  16  VAL C  24 -1  O  TYR C  16   N  ILE C  13           
SHEET    3 AA9 6 LYS C  29  HIS C  35 -1  O  GLU C  34   N  VAL C  17           
SHEET    4 AA9 6 LYS C  41  ASN C  48 -1  O  VAL C  44   N  LYS C  31           
SHEET    5 AA9 6 ASP C  88  GLU C  94 -1  O  MET C  91   N  LYS C  45           
SHEET    6 AA9 6 LEU C  79  SER C  84 -1  N  ILE C  83   O  PHE C  90           
SHEET    1 AB1 2 VAL C 135  VAL C 136  0                                        
SHEET    2 AB1 2 ASN C 162  MET C 163 -1  O  ASN C 162   N  VAL C 136           
SHEET    1 AB2 2 VAL C 145  LEU C 147  0                                        
SHEET    2 AB2 2 ALA C 153  ILE C 155 -1  O  LYS C 154   N  LEU C 146           
SHEET    1 AB3 7 HIS C 397  LEU C 398  0                                        
SHEET    2 AB3 7 TYR D 240  ALA D 241 -1  O  ALA D 241   N  HIS C 397           
SHEET    3 AB3 7 MET D 249  TYR D 257 -1  O  SER D 252   N  TYR D 240           
SHEET    4 AB3 7 LYS D 260  LYS D 268 -1  O  LYS D 260   N  TYR D 257           
SHEET    5 AB3 7 SER F  45  ASP F  52  1  O  SER F  46   N  THR D 263           
SHEET    6 AB3 7 ALA F  72  ASP F  76  1  O  TRP F  75   N  PHE F  51           
SHEET    7 AB3 7 SER F  81  LEU F  86 -1  O  GLY F  84   N  LEU F  74           
SHEET    1 AB4 5 ILE C 400  SER C 402  0                                        
SHEET    2 AB4 5 SER C 458  SER C 465 -1  O  TYR C 459   N  SER C 402           
SHEET    3 AB4 5 TYR C 444  VAL C 454 -1  N  SER C 448   O  LYS C 464           
SHEET    4 AB4 5 HIS C 431  LYS C 437 -1  N  VAL C 434   O  MET C 447           
SHEET    5 AB4 5 GLU C 423  VAL C 426 -1  N  LYS C 425   O  ARG C 433           
SHEET    1 AB5 3 PRO D  79  TRP D  84  0                                        
SHEET    2 AB5 3 PHE D 112  ASP D 117 -1  O  PHE D 112   N  TRP D  84           
SHEET    3 AB5 3 THR D 106  ARG D 107 -1  N  THR D 106   O  VAL D 113           
SHEET    1 AB6 4 LEU D 103  PRO D 104  0                                        
SHEET    2 AB6 4 VAL D  91  GLY D  95 -1  N  LEU D  93   O  LEU D 103           
SHEET    3 AB6 4 GLY D 121  VAL D 129 -1  O  LYS D 126   N  SER D  94           
SHEET    4 AB6 4 GLN D 132  THR D 134 -1  O  THR D 134   N  PHE D 127           
SHEET    1 AB7 5 LEU D 103  PRO D 104  0                                        
SHEET    2 AB7 5 VAL D  91  GLY D  95 -1  N  LEU D  93   O  LEU D 103           
SHEET    3 AB7 5 GLY D 121  VAL D 129 -1  O  LYS D 126   N  SER D  94           
SHEET    4 AB7 5 VAL D 149  VAL D 155 -1  O  ASN D 151   N  TYR D 125           
SHEET    5 AB7 5 ILE D 141  THR D 143 -1  N  VAL D 142   O  ASN D 150           
SHEET    1 AB8 2 ARG E 152  ILE E 156  0                                        
SHEET    2 AB8 2 THR E 163  THR E 168 -1  O  TYR E 165   N  VAL E 155           
SHEET    1 AB9 3 VAL E 207  ARG E 208  0                                        
SHEET    2 AB9 3 ALA E 227  VAL E 231  1  O  PRO E 229   N  VAL E 207           
SHEET    3 AB9 3 VAL E 237  SER E 242 -1  O  TYR E 241   N  LEU E 228           
SHEET    1 AC1 3 LYS E 278  TYR E 280  0                                        
SHEET    2 AC1 3 ARG E 299  VAL E 303  1  O  VAL E 301   N  CYS E 279           
SHEET    3 AC1 3 VAL E 309  SER E 314 -1  O  VAL E 313   N  LEU E 300           
SHEET    1 AC2 2 LEU F 153  ILE F 156  0                                        
SHEET    2 AC2 2 THR F 163  LEU F 167 -1  O  LEU F 164   N  VAL F 155           
SHEET    1 AC3 3 VAL F 207  ARG F 208  0                                        
SHEET    2 AC3 3 ALA F 227  VAL F 231  1  O  VAL F 231   N  VAL F 207           
SHEET    3 AC3 3 VAL F 237  SER F 242 -1  O  TYR F 241   N  LEU F 228           
SHEET    1 AC4 3 LYS F 278  CYS F 279  0                                        
SHEET    2 AC4 3 ARG F 299  VAL F 303  1  O  VAL F 303   N  CYS F 279           
SHEET    3 AC4 3 VAL F 309  SER F 314 -1  O  LYS F 310   N  VAL F 302           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.35  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.35  
LINK         C   ARG B 107                 N   SEP B 108     1555   1555  1.35  
LINK         C   SEP B 108                 N   HIS B 109     1555   1555  1.34  
LINK         C   ARG C 171                 N   TPO C 172     1555   1555  1.32  
LINK         C   TPO C 172                 N   SER C 173     1555   1555  1.33  
LINK         C   ARG D 107                 N   SEP D 108     1555   1555  1.32  
LINK         C   SEP D 108                 N   HIS D 109     1555   1555  1.32  
SITE     1 AC1 15 LEU A  22  GLY A  23  VAL A  24  GLY A  25                    
SITE     2 AC1 15 VAL A  30  ALA A  43  LYS A  45  GLU A  94                    
SITE     3 AC1 15 TYR A  95  VAL A  96  GLY A  99  GLU A 100                    
SITE     4 AC1 15 GLU A 143  LEU A 146  ASP A 157                               
SITE     1 AC2 11 VAL A  11  LEU A  18  GLY A  19  LYS A  29                    
SITE     2 AC2 11 LYS A  31  ILE A  46  ASN A  48  ASP A  88                    
SITE     3 AC2 11 ARG B  83  SEP B 108  VAL B 113                               
SITE     1 AC3 14 LEU C  22  GLY C  23  VAL C  24  GLY C  25                    
SITE     2 AC3 14 VAL C  30  ALA C  43  GLU C  94  TYR C  95                    
SITE     3 AC3 14 VAL C  96  GLU C 100  GLU C 143  ASN C 144                    
SITE     4 AC3 14 LEU C 146  ASP C 157                                          
SITE     1 AC4 10 LEU C  18  GLY C  19  LYS C  29  LYS C  31                    
SITE     2 AC4 10 ILE C  46  ASN C  48  ASP C  88  ARG D  83                    
SITE     3 AC4 10 SEP D 108  VAL D 113                                          
SITE     1 AC5  4 PHE C  27  GLY C  28  ASN C  48  LYS C  51                    
SITE     1 AC6 15 PRO A 367  ARG E  70  LYS E 170  ILE E 240                    
SITE     2 AC6 15 SER E 242  PHE E 244  ASP E 245  ARG E 269                    
SITE     3 AC6 15 GLY E 275  VAL E 276  LEU E 277  VAL E 297                    
SITE     4 AC6 15 HIS E 298  ARG E 299  HOH E 523                               
SITE     1 AC7 13 HIS E 151  THR E 200  ILE E 204  ALA E 205                    
SITE     2 AC7 13 VAL E 225  SER E 226  ALA E 227  HIS E 298                    
SITE     3 AC7 13 ILE E 312  SER E 314  SER E 316  ASP E 317                    
SITE     4 AC7 13 HOH E 517                                                     
SITE     1 AC8 13 PRO C 367  ARG F  70  LYS F 170  ILE F 240                    
SITE     2 AC8 13 SER F 242  PHE F 244  ASP F 245  ARG F 269                    
SITE     3 AC8 13 GLY F 275  LEU F 277  VAL F 297  HIS F 298                    
SITE     4 AC8 13 ARG F 299                                                     
SITE     1 AC9 12 HIS F 151  THR F 200  ILE F 204  ALA F 205                    
SITE     2 AC9 12 VAL F 225  SER F 226  ALA F 227  HIS F 298                    
SITE     3 AC9 12 ILE F 312  SER F 314  SER F 316  ASP F 317                    
CRYST1   75.827  133.897  141.725  90.00  92.74  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013188  0.000000  0.000631        0.00000                         
SCALE2      0.000000  0.007468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007064        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system