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Database: PDB
Entry: 5WXN
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HEADER    PROTEIN BINDING/TRANSFERASE             08-JAN-17   5WXN              
TITLE     STRUCTURE OF THE LKB1 AND 14-3-3 COMPLEX                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN ZETA/DELTA;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1,KCIP-1;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SERINE/THREONINE-PROTEIN KINASE STK11;                     
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 331-343;                                      
COMPND  10 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: YWHAZ;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST17;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    KINASE, TUMOR SUPPRESSOR, PROTEIN COMPLEX, PROTEIN BINDING-           
KEYWDS   2 TRANSFERASE COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DING,Z.B.SHI                                                        
REVDAT   1   19-APR-17 5WXN    0                                                
JRNL        AUTH   Y.LU,S.DING,R.ZHOU,J.WU                                      
JRNL        TITL   STRUCTURE OF THE COMPLEX OF PHOSPHORYLATED LIVER KINASE B1   
JRNL        TITL 2 AND 14-3-3 ZETA                                              
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  73   196 2017              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   28368277                                                     
JRNL        DOI    10.1107/S2053230X17003521                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15587                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1559                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.5685 -  6.5103    0.98     1354   149  0.1859 0.2025        
REMARK   3     2  6.5103 -  5.1699    1.00     1299   145  0.2109 0.2473        
REMARK   3     3  5.1699 -  4.5171    1.00     1288   142  0.1500 0.2235        
REMARK   3     4  4.5171 -  4.1044    1.00     1276   143  0.1560 0.2521        
REMARK   3     5  4.1044 -  3.8104    1.00     1273   142  0.1687 0.2299        
REMARK   3     6  3.8104 -  3.5859    1.00     1277   142  0.1926 0.2644        
REMARK   3     7  3.5859 -  3.4063    0.99     1244   139  0.2228 0.3306        
REMARK   3     8  3.4063 -  3.2581    1.00     1258   139  0.2350 0.3192        
REMARK   3     9  3.2581 -  3.1327    1.00     1254   140  0.2362 0.3315        
REMARK   3    10  3.1327 -  3.0246    1.00     1253   139  0.2829 0.3800        
REMARK   3    11  3.0246 -  2.9301    1.00     1252   139  0.3208 0.3975        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           3697                                  
REMARK   3   ANGLE     :  1.239           5020                                  
REMARK   3   CHIRALITY :  0.066            584                                  
REMARK   3   PLANARITY :  0.008            649                                  
REMARK   3   DIHEDRAL  :  6.878           3017                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 1 THROUGH 37 )                      
REMARK   3    ORIGIN FOR THE GROUP (A):  69.8213  96.2012 -14.0374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8110 T22:   0.9716                                     
REMARK   3      T33:   0.5679 T12:  -0.1803                                     
REMARK   3      T13:   0.1463 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0876 L22:   3.6364                                     
REMARK   3      L33:   5.5612 L12:  -4.8158                                     
REMARK   3      L13:   3.8071 L23:  -2.0687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5784 S12:   0.2064 S13:   0.4978                       
REMARK   3      S21:  -1.0963 S22:  -0.3988 S23:  -0.5482                       
REMARK   3      S31:  -0.1412 S32:   0.6389 S33:  -0.1566                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 38 THROUGH 103 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1927  91.2207   4.5511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6033 T22:   0.7233                                     
REMARK   3      T33:   0.4201 T12:   0.1111                                     
REMARK   3      T13:   0.0113 T23:  -0.0990                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6053 L22:   2.8330                                     
REMARK   3      L33:   6.0598 L12:   1.7381                                     
REMARK   3      L13:   2.4842 L23:   0.4063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3101 S12:  -0.1715 S13:   0.1603                       
REMARK   3      S21:  -0.1023 S22:  -0.2264 S23:   0.0869                       
REMARK   3      S31:  -0.8436 S32:  -0.3267 S33:   0.5091                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 104 THROUGH 159 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  48.9876  89.9798  -9.6709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5292 T22:   0.8011                                     
REMARK   3      T33:   0.5187 T12:   0.1039                                     
REMARK   3      T13:  -0.0633 T23:   0.0890                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5592 L22:   6.4331                                     
REMARK   3      L33:   7.4845 L12:   1.6101                                     
REMARK   3      L13:   3.4631 L23:   0.5054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5048 S12:  -0.0295 S13:   0.2653                       
REMARK   3      S21:  -0.5217 S22:   0.1474 S23:   0.6667                       
REMARK   3      S31:  -1.2572 S32:  -1.3196 S33:   0.2990                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 160 THROUGH 230 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6783  73.4574 -11.0719              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4062 T22:   0.7362                                     
REMARK   3      T33:   0.4337 T12:   0.0030                                     
REMARK   3      T13:  -0.0359 T23:  -0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8448 L22:   8.4775                                     
REMARK   3      L33:   6.6916 L12:  -1.9620                                     
REMARK   3      L13:   0.3849 L23:   1.8028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0216 S12:   0.7134 S13:  -0.4286                       
REMARK   3      S21:  -0.5974 S22:  -0.2710 S23:   0.6314                       
REMARK   3      S31:  -0.2487 S32:  -0.5516 S33:   0.2431                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 1 THROUGH 111 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  82.6669  93.4696   8.5290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5508 T22:   0.6765                                     
REMARK   3      T33:   0.5741 T12:  -0.1111                                     
REMARK   3      T13:   0.0437 T23:  -0.1358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5590 L22:   2.1530                                     
REMARK   3      L33:   4.4688 L12:  -0.3389                                     
REMARK   3      L13:   0.3354 L23:  -0.1457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1847 S12:   0.2433 S13:   0.3858                       
REMARK   3      S21:  -0.0327 S22:   0.1321 S23:  -0.4330                       
REMARK   3      S31:  -0.4462 S32:   0.3171 S33:  -0.0204                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 112 THROUGH 230 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  97.4100  80.5571  12.2014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4231 T22:   0.8781                                     
REMARK   3      T33:   0.7555 T12:  -0.0833                                     
REMARK   3      T13:   0.0526 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2112 L22:   6.9855                                     
REMARK   3      L33:   3.0490 L12:   0.0515                                     
REMARK   3      L13:   2.5373 L23:   0.8423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1322 S12:  -0.4026 S13:   0.2798                       
REMARK   3      S21:   0.1978 S22:  -0.0140 S23:  -0.8704                       
REMARK   3      S31:   0.0224 S32:   0.4713 S33:   0.1193                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 332 THROUGH 341 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8254  79.2209  -6.5364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6103 T22:   0.8957                                     
REMARK   3      T33:   0.7734 T12:  -0.0900                                     
REMARK   3      T13:   0.0133 T23:   0.0683                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1733 L22:   9.9110                                     
REMARK   3      L33:   2.7332 L12:  -0.2426                                     
REMARK   3      L13:   1.8911 L23:   3.8300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0047 S12:   0.0113 S13:   0.0836                       
REMARK   3      S21:  -0.3471 S22:   0.0701 S23:  -1.0719                       
REMARK   3      S31:  -1.7921 S32:   2.2574 S33:  -0.2704                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 332 THROUGH 341 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  88.4725  79.6046   8.6240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7358 T22:   0.8494                                     
REMARK   3      T33:   1.2867 T12:   0.1892                                     
REMARK   3      T13:   0.0238 T23:  -0.1629                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4283 L22:   6.3366                                     
REMARK   3      L33:   4.4148 L12:   3.3149                                     
REMARK   3      L13:  -2.6632 L23:  -5.3100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0712 S12:   0.2646 S13:  -0.0450                       
REMARK   3      S21:   0.9319 S22:   1.7561 S23:   1.4368                       
REMARK   3      S31:  -0.2243 S32:  -0.9481 S33:  -2.0481                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15953                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.93700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.780                              
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: 4ZDR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M AMMONIUM CHLORIDE, 18% PEG3350,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.38550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.36900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.69100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.36900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.38550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.69100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     TYR A   -19                                                      
REMARK 465     TYR A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ASP A   231                                                      
REMARK 465     THR A   232                                                      
REMARK 465     GLN A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ASP A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     GLY A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     TYR B   -19                                                      
REMARK 465     TYR B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLU B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     LYS B    -4                                                      
REMARK 465     LYS B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     ASP B   231                                                      
REMARK 465     THR B   232                                                      
REMARK 465     GLN B   233                                                      
REMARK 465     GLY B   234                                                      
REMARK 465     ASP B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     ALA B   239                                                      
REMARK 465     GLY B   240                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     GLY B   242                                                      
REMARK 465     GLY B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     ASN B   245                                                      
REMARK 465     ARG C   331                                                      
REMARK 465     GLU C   342                                                      
REMARK 465     ASP C   343                                                      
REMARK 465     ARG D   331                                                      
REMARK 465     GLU D   342                                                      
REMARK 465     ASP D   343                                                      
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     LEU A   0    CG   CD1  CD2                                       
REMARK 470     LYS A   3    CD   CE   NZ                                        
REMARK 470     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     GLN A   8    CG   CD   OE1  NE2                                  
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     LYS A  11    CG   CD   CE   NZ                                   
REMARK 470     LEU A  12    CG   CD1  CD2                                       
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CE   NZ                                             
REMARK 470     GLN A  77    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  85    CD   CE   NZ                                        
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     ASP A 137    CG   OD1  OD2                                       
REMARK 470     LYS A 139    CG   CD   CE   NZ                                   
REMARK 470     GLN A 147    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 157    CD   CE   NZ                                        
REMARK 470     LYS A 158    NZ                                                  
REMARK 470     GLU A 159    OE1  OE2                                            
REMARK 470     GLU A 186    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 187    CE   NZ                                             
REMARK 470     GLU A 202    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 204    CG   OD1  OD2                                       
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 209    OE1  OE2                                            
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     GLU B   5    CG   CD   OE1  OE2                                  
REMARK 470     LYS B   9    CG   CD   CE   NZ                                   
REMARK 470     GLU B  35    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  40    CD   OE1  OE2                                       
REMARK 470     GLN B  67    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  68    CE   NZ                                             
REMARK 470     GLU B  70    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    CG   CD   CE   NZ                                   
REMARK 470     GLN B  77    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  85    CG   CD   CE   NZ                                   
REMARK 470     GLU B 102    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 113    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     LYS B 138    CE   NZ                                             
REMARK 470     LYS B 139    CG   CD   CE   NZ                                   
REMARK 470     GLN B 147    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     LYS B 158    CD   CE   NZ                                        
REMARK 470     GLU B 159    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 180    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     GLU B 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 208    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 209    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 211    CE1  CE2  CZ   OH                                   
REMARK 470     LYS B 212    CG   CD   CE   NZ                                   
REMARK 470     LEU B 216    CG   CD1  CD2                                       
REMARK 470     SER B 230    OG                                                  
REMARK 470     TRP C 332    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 332    CZ3  CH2                                            
REMARK 470     TRP D 332    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 332    CZ3  CH2                                            
REMARK 470     LEU D 341    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 107   C   -  N   -  CD  ANGL. DEV. = -26.2 DEGREES          
REMARK 500    LYS B  49   CD  -  CE  -  NZ  ANGL. DEV. = -14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  34     -106.86      7.27                                   
REMARK 500    GLU A  35      115.09    118.97                                   
REMARK 500    SER A  37      174.88    -59.98                                   
REMARK 500    PHE A 104      -48.46   -131.23                                   
REMARK 500    ASN A 108      -97.08    -87.95                                   
REMARK 500    ALA A 109       71.74     46.39                                   
REMARK 500    ASP A 136      -59.60    -26.44                                   
REMARK 500    GLU B  31        6.49    -68.44                                   
REMARK 500    SER B  37      172.90    -59.10                                   
REMARK 500    ALA B 134     -145.08   -134.54                                   
REMARK 500    SER B 184       78.06   -110.44                                   
REMARK 500    VAL C 338       59.84   -112.93                                   
REMARK 500    PRO C 339      108.29    -45.75                                   
REMARK 500    VAL D 337     -153.48   -130.70                                   
REMARK 500    VAL D 338       74.16   -174.05                                   
REMARK 500    PRO D 339      -49.83      9.99                                   
REMARK 500    TYR D 340       88.60     59.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL C  338     PRO C  339                 -138.25                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 309        DISTANCE =  7.18 ANGSTROMS                       
DBREF  5WXN A    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  5WXN B    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  5WXN C  331   343  UNP    Q15831   STK11_HUMAN    331    343             
DBREF  5WXN D  331   343  UNP    Q15831   STK11_HUMAN    331    343             
SEQADV 5WXN MET A  -21  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER A  -20  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR A  -19  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR A  -18  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -17  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -16  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -15  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -14  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -13  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS A  -12  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU A  -11  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN GLU A  -10  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER A   -9  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN THR A   -8  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER A   -7  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU A   -6  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR A   -5  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LYS A   -4  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LYS A   -3  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN ALA A   -2  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN GLY A   -1  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU A    0  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN MET B  -21  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER B  -20  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR B  -19  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR B  -18  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -17  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -16  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -15  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -14  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -13  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN HIS B  -12  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU B  -11  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN GLU B  -10  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER B   -9  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN THR B   -8  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN SER B   -7  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU B   -6  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN TYR B   -5  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LYS B   -4  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LYS B   -3  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN ALA B   -2  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN GLY B   -1  UNP  P63104              EXPRESSION TAG                 
SEQADV 5WXN LEU B    0  UNP  P63104              EXPRESSION TAG                 
SEQRES   1 A  267  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 A  267  THR SER LEU TYR LYS LYS ALA GLY LEU MET ASP LYS ASN          
SEQRES   3 A  267  GLU LEU VAL GLN LYS ALA LYS LEU ALA GLU GLN ALA GLU          
SEQRES   4 A  267  ARG TYR ASP ASP MET ALA ALA CYS MET LYS SER VAL THR          
SEQRES   5 A  267  GLU GLN GLY ALA GLU LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   6 A  267  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   7 A  267  SER SER TRP ARG VAL VAL SER SER ILE GLU GLN LYS THR          
SEQRES   8 A  267  GLU GLY ALA GLU LYS LYS GLN GLN MET ALA ARG GLU TYR          
SEQRES   9 A  267  ARG GLU LYS ILE GLU THR GLU LEU ARG ASP ILE CYS ASN          
SEQRES  10 A  267  ASP VAL LEU SER LEU LEU GLU LYS PHE LEU ILE PRO ASN          
SEQRES  11 A  267  ALA SER GLN ALA GLU SER LYS VAL PHE TYR LEU LYS MET          
SEQRES  12 A  267  LYS GLY ASP TYR TYR ARG TYR LEU ALA GLU VAL ALA ALA          
SEQRES  13 A  267  GLY ASP ASP LYS LYS GLY ILE VAL ASP GLN SER GLN GLN          
SEQRES  14 A  267  ALA TYR GLN GLU ALA PHE GLU ILE SER LYS LYS GLU MET          
SEQRES  15 A  267  GLN PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN          
SEQRES  16 A  267  PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO GLU          
SEQRES  17 A  267  LYS ALA CYS SER LEU ALA LYS THR ALA PHE ASP GLU ALA          
SEQRES  18 A  267  ILE ALA GLU LEU ASP THR LEU SER GLU GLU SER TYR LYS          
SEQRES  19 A  267  ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU          
SEQRES  20 A  267  THR LEU TRP THR SER ASP THR GLN GLY ASP GLU ALA GLU          
SEQRES  21 A  267  ALA GLY GLU GLY GLY GLU ASN                                  
SEQRES   1 B  267  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 B  267  THR SER LEU TYR LYS LYS ALA GLY LEU MET ASP LYS ASN          
SEQRES   3 B  267  GLU LEU VAL GLN LYS ALA LYS LEU ALA GLU GLN ALA GLU          
SEQRES   4 B  267  ARG TYR ASP ASP MET ALA ALA CYS MET LYS SER VAL THR          
SEQRES   5 B  267  GLU GLN GLY ALA GLU LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   6 B  267  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   7 B  267  SER SER TRP ARG VAL VAL SER SER ILE GLU GLN LYS THR          
SEQRES   8 B  267  GLU GLY ALA GLU LYS LYS GLN GLN MET ALA ARG GLU TYR          
SEQRES   9 B  267  ARG GLU LYS ILE GLU THR GLU LEU ARG ASP ILE CYS ASN          
SEQRES  10 B  267  ASP VAL LEU SER LEU LEU GLU LYS PHE LEU ILE PRO ASN          
SEQRES  11 B  267  ALA SER GLN ALA GLU SER LYS VAL PHE TYR LEU LYS MET          
SEQRES  12 B  267  LYS GLY ASP TYR TYR ARG TYR LEU ALA GLU VAL ALA ALA          
SEQRES  13 B  267  GLY ASP ASP LYS LYS GLY ILE VAL ASP GLN SER GLN GLN          
SEQRES  14 B  267  ALA TYR GLN GLU ALA PHE GLU ILE SER LYS LYS GLU MET          
SEQRES  15 B  267  GLN PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN          
SEQRES  16 B  267  PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO GLU          
SEQRES  17 B  267  LYS ALA CYS SER LEU ALA LYS THR ALA PHE ASP GLU ALA          
SEQRES  18 B  267  ILE ALA GLU LEU ASP THR LEU SER GLU GLU SER TYR LYS          
SEQRES  19 B  267  ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU          
SEQRES  20 B  267  THR LEU TRP THR SER ASP THR GLN GLY ASP GLU ALA GLU          
SEQRES  21 B  267  ALA GLY GLU GLY GLY GLU ASN                                  
SEQRES   1 C   13  ARG TRP ARG SER MET TPO VAL VAL PRO TYR LEU GLU ASP          
SEQRES   1 D   13  ARG TRP ARG SER MET TPO VAL VAL PRO TYR LEU GLU ASP          
MODRES 5WXN TPO C  336  THR  MODIFIED RESIDUE                                   
MODRES 5WXN TPO D  336  THR  MODIFIED RESIDUE                                   
HET    TPO  C 336      11                                                       
HET    TPO  D 336      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   3  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  HOH   *18(H2 O)                                                     
HELIX    1 AA1 ASP A    2  ALA A   16  1                                  15    
HELIX    2 AA2 ARG A   18  GLU A   31  1                                  14    
HELIX    3 AA3 SER A   37  THR A   69  1                                  33    
HELIX    4 AA4 ALA A   72  PHE A  104  1                                  33    
HELIX    5 AA5 GLN A  111  ALA A  133  1                                  23    
HELIX    6 AA6 ALA A  134  ASP A  136  5                                   3    
HELIX    7 AA7 ASP A  137  MET A  160  1                                  24    
HELIX    8 AA8 HIS A  164  LEU A  182  1                                  19    
HELIX    9 AA9 SER A  184  GLU A  202  1                                  19    
HELIX   10 AB1 LEU A  203  LEU A  206  5                                   4    
HELIX   11 AB2 SER A  210  THR A  229  1                                  20    
HELIX   12 AB3 ASP B    2  ALA B   16  1                                  15    
HELIX   13 AB4 ARG B   18  GLU B   31  1                                  14    
HELIX   14 AB5 SER B   37  THR B   69  1                                  33    
HELIX   15 AB6 ALA B   72  PHE B  104  1                                  33    
HELIX   16 AB7 GLN B  111  GLU B  131  1                                  21    
HELIX   17 AB8 ASP B  137  MET B  160  1                                  24    
HELIX   18 AB9 HIS B  164  ILE B  181  1                                  18    
HELIX   19 AC1 SER B  184  ALA B  201  1                                  18    
HELIX   20 AC2 GLU B  202  LEU B  206  5                                   5    
HELIX   21 AC3 SER B  210  THR B  229  1                                  20    
LINK         C   MET C 335                 N   TPO C 336     1555   1555  1.34  
LINK         C   TPO C 336                 N   VAL C 337     1555   1555  1.33  
LINK         C   MET D 335                 N   TPO D 336     1555   1555  1.33  
LINK         C   TPO D 336                 N   VAL D 337     1555   1555  1.33  
CRYST1   72.771   85.382  112.738  90.00  90.00  90.00 P 21 21 21    8          
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      0.013742  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system