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Database: PDB
Entry: 5JR7
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Original site: 5JR7 
HEADER    TRANSFERASE/CAMP BINDING PROTEIN        05-MAY-16   5JR7              
TITLE     CRYSTAL STRUCTURE OF AN ACRDYS HETERODIMER [RIA(92-365):C] OF PKA     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY      
COMPND   9 SUBUNIT;                                                             
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 92-366;                                       
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: BOVINE;                                             
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 GENE: PRKAR1A;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    PKA SIGNALING, RIA SUBUNIT, DISEASE MUTATIONS, DYSFUNCTIONAL ACRDYS   
KEYWDS   2 MUTANT, TRANSFERASE-CAMP BINDING PROTEIN COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.G.H.BRUYSTENS,J.WU,S.S.TAYLOR                                       
REVDAT   3   25-DEC-19 5JR7    1       REMARK                                   
REVDAT   2   27-SEP-17 5JR7    1       REMARK                                   
REVDAT   1   15-MAR-17 5JR7    0                                                
JRNL        AUTH   J.G.BRUYSTENS,J.WU,A.FORTEZZO,J.DEL RIO,C.NIELSEN,           
JRNL        AUTH 2 D.K.BLUMENTHAL,R.ROCK,E.STEFAN,S.S.TAYLOR                    
JRNL        TITL   STRUCTURE OF A PKA RI ALPHA RECURRENT ACRODYSOSTOSIS MUTANT  
JRNL        TITL 2 EXPLAINS DEFECTIVE CAMP-DEPENDENT ACTIVATION.                
JRNL        REF    J. MOL. BIOL.                 V. 428  4890 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27825928                                                     
JRNL        DOI    10.1016/J.JMB.2016.10.033                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7_650                                       
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15043                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.269                           
REMARK   3   R VALUE            (WORKING SET) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 765                             
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 49.1104 -  6.0846    0.99     2902   164  0.2182 0.2558        
REMARK   3     2  6.0846 -  4.8309    0.99     2890   165  0.2729 0.3065        
REMARK   3     3  4.8309 -  4.2206    0.97     2841   159  0.2472 0.3636        
REMARK   3     4  4.2206 -  3.8349    0.95     2814   132  0.3044 0.3902        
REMARK   3     5  3.8349 -  3.5601    0.97     2831   145  0.3668 0.4017        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 74.42                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.580            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.870           
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) : -2.77090                                             
REMARK   3    B22 (A**2) : 9.79920                                              
REMARK   3    B33 (A**2) : -7.02830                                             
REMARK   3    B12 (A**2) : 0.19230                                              
REMARK   3    B13 (A**2) : -5.50600                                             
REMARK   3    B23 (A**2) : -8.11560                                             
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           9971                                  
REMARK   3   ANGLE     :  1.738          13489                                  
REMARK   3   CHIRALITY :  0.126           1452                                  
REMARK   3   PLANARITY :  0.007           1728                                  
REMARK   3   DIHEDRAL  : 18.060           3690                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 13:42)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9034 -27.6877   7.3914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0376 T22:   0.7090                                     
REMARK   3      T33:   0.7414 T12:   0.3876                                     
REMARK   3      T13:  -0.5277 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4474 L22:   1.0834                                     
REMARK   3      L33:   0.1717 L12:   0.6758                                     
REMARK   3      L13:   0.2791 L23:   0.4273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1312 S12:   0.1517 S13:   0.0424                       
REMARK   3      S21:  -0.2797 S22:  -0.0996 S23:   1.0231                       
REMARK   3      S31:  -0.7287 S32:   0.2020 S33:  -0.2464                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 43:160)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5287 -34.0081  22.8319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1526 T22:   0.1565                                     
REMARK   3      T33:   0.1094 T12:  -0.2077                                     
REMARK   3      T13:  -0.0679 T23:  -0.0660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8913 L22:   2.1089                                     
REMARK   3      L33:   1.5391 L12:   0.2773                                     
REMARK   3      L13:  -0.5017 L23:  -1.2796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2159 S12:   0.3762 S13:   0.0412                       
REMARK   3      S21:   0.1167 S22:   0.6353 S23:   1.1316                       
REMARK   3      S31:  -0.4117 S32:  -0.7722 S33:   1.2926                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 161:272)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1035 -29.2162  24.2045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0262 T22:   0.0763                                     
REMARK   3      T33:   0.2784 T12:   0.0590                                     
REMARK   3      T13:  -0.0221 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6014 L22:   0.5674                                     
REMARK   3      L33:   0.4822 L12:  -0.1732                                     
REMARK   3      L13:  -0.2607 L23:  -0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4420 S12:   0.4585 S13:   0.0280                       
REMARK   3      S21:   0.0860 S22:   0.2258 S23:   0.1113                       
REMARK   3      S31:  -0.0362 S32:   0.0110 S33:  -0.6903                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 273:316)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8355 -36.8915  11.6878              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2958 T22:   0.4997                                     
REMARK   3      T33:  -0.1383 T12:  -0.0460                                     
REMARK   3      T13:   0.0342 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5038 L22:   0.1653                                     
REMARK   3      L33:   0.3782 L12:  -0.2816                                     
REMARK   3      L13:  -0.1362 L23:   0.1241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2068 S12:   0.5073 S13:   0.2140                       
REMARK   3      S21:  -0.3566 S22:  -0.1880 S23:  -0.0173                       
REMARK   3      S31:  -0.0624 S32:  -0.0368 S33:   0.0436                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 317:350)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1268 -32.0910  30.4277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5101 T22:   1.0478                                     
REMARK   3      T33:   0.8655 T12:   0.3463                                     
REMARK   3      T13:  -0.0606 T23:  -0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8419 L22:   0.4270                                     
REMARK   3      L33:   0.6821 L12:   0.3994                                     
REMARK   3      L13:  -0.1475 L23:  -0.3658                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:   0.5949 S13:   0.7383                       
REMARK   3      S21:  -0.2215 S22:  -0.1008 S23:   0.4572                       
REMARK   3      S31:  -0.4587 S32:  -0.6267 S33:  -0.3561                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 92:119)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0362  -9.9505  31.1525              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1015 T22:   0.2225                                     
REMARK   3      T33:   0.7415 T12:   0.4872                                     
REMARK   3      T13:  -0.2105 T23:   0.1389                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3378 L22:   0.9895                                     
REMARK   3      L33:   0.8094 L12:  -0.0093                                     
REMARK   3      L13:   0.0073 L23:   0.5829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0755 S12:  -0.1233 S13:   0.1177                       
REMARK   3      S21:   0.5675 S22:   0.2795 S23:   0.0963                       
REMARK   3      S31:   0.2427 S32:  -0.2493 S33:  -0.3918                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 120:151)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6984  -4.0625  35.8501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4690 T22:   0.2896                                     
REMARK   3      T33:   0.9319 T12:  -0.0776                                     
REMARK   3      T13:   0.0565 T23:  -0.1855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0346 L22:   0.0087                                     
REMARK   3      L33:   0.2104 L12:  -0.0146                                     
REMARK   3      L13:   0.0533 L23:  -0.0189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1677 S12:   0.3230 S13:  -0.1030                       
REMARK   3      S21:   0.0297 S22:   0.2109 S23:  -0.2583                       
REMARK   3      S31:   0.3606 S32:   0.5006 S33:  -0.0099                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 152:198)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2745 -11.4575  51.5686              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7642 T22:   0.3564                                     
REMARK   3      T33:   0.0778 T12:   0.2687                                     
REMARK   3      T13:  -0.3005 T23:   0.4760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7246 L22:   0.0936                                     
REMARK   3      L33:   0.4487 L12:   0.1483                                     
REMARK   3      L13:  -0.2065 L23:  -0.1825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1104 S12:  -0.4721 S13:  -0.2561                       
REMARK   3      S21:   0.2042 S22:  -0.0602 S23:  -0.0402                       
REMARK   3      S31:  -0.1240 S32:   0.0212 S33:  -0.4670                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 199:211)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9886 -16.3603  40.2100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1529 T22:   0.1308                                     
REMARK   3      T33:   0.4867 T12:   0.2179                                     
REMARK   3      T13:   0.0633 T23:  -0.0974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0540 L22:   0.0642                                     
REMARK   3      L33:   0.0300 L12:  -0.0428                                     
REMARK   3      L13:  -0.0184 L23:  -0.0079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0237 S12:  -0.1027 S13:  -0.0137                       
REMARK   3      S21:   0.0266 S22:   0.0273 S23:   0.0633                       
REMARK   3      S31:   0.0527 S32:   0.0536 S33:  -0.0418                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 212:225)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3038  -6.0799  51.3862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3689 T22:   0.5323                                     
REMARK   3      T33:   0.3883 T12:   0.2775                                     
REMARK   3      T13:   0.2823 T23:  -0.1069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0691 L22:   0.0799                                     
REMARK   3      L33:   0.2341 L12:  -0.0263                                     
REMARK   3      L13:  -0.0765 L23:   0.1268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0008 S12:  -0.1313 S13:  -0.0782                       
REMARK   3      S21:   0.3274 S22:   0.1999 S23:  -0.0759                       
REMARK   3      S31:   0.1930 S32:   0.1663 S33:   0.1465                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 226:251)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0830  -4.0966  19.2413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7085 T22:  -0.5967                                     
REMARK   3      T33:   0.3093 T12:  -0.0907                                     
REMARK   3      T13:  -0.0126 T23:  -0.2759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2014 L22:   0.2749                                     
REMARK   3      L33:   0.3243 L12:  -0.1194                                     
REMARK   3      L13:  -0.0011 L23:   0.2542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2733 S12:  -0.0505 S13:   0.1383                       
REMARK   3      S21:   0.2806 S22:  -0.1526 S23:   0.3860                       
REMARK   3      S31:   0.1285 S32:  -0.0981 S33:  -1.0262                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 252:302)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8508  -4.7476  11.1379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1157 T22:   0.2259                                     
REMARK   3      T33:   0.6225 T12:  -0.2348                                     
REMARK   3      T13:  -0.1448 T23:   0.0357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4575 L22:   0.5720                                     
REMARK   3      L33:   0.2726 L12:  -0.0706                                     
REMARK   3      L13:  -0.3192 L23:   0.0325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0768 S12:   0.2949 S13:   0.1851                       
REMARK   3      S21:  -0.0167 S22:  -0.0342 S23:   0.2377                       
REMARK   3      S31:  -0.0264 S32:  -0.4242 S33:   0.0877                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 303:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  64.9295   3.5707   6.1012              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1608 T22:   0.7767                                     
REMARK   3      T33:   0.9995 T12:  -0.3473                                     
REMARK   3      T13:   0.2759 T23:   0.2593                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0113 L22:   0.0008                                     
REMARK   3      L33:   0.0476 L12:   0.0012                                     
REMARK   3      L13:   0.0236 L23:   0.0036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0407 S12:   0.0240 S13:   0.0580                       
REMARK   3      S21:  -0.0038 S22:  -0.0386 S23:  -0.0301                       
REMARK   3      S31:  -0.0828 S32:   0.0829 S33:  -0.0829                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 311:358)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  45.5217  -4.7372   8.9958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3541 T22:   0.5496                                     
REMARK   3      T33:   0.1466 T12:  -0.2225                                     
REMARK   3      T13:   0.1300 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6708 L22:   0.6493                                     
REMARK   3      L33:   0.9160 L12:   0.3402                                     
REMARK   3      L13:   0.2295 L23:  -0.3261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0962 S12:  -0.2577 S13:  -0.0732                       
REMARK   3      S21:  -0.2652 S22:  -0.0601 S23:  -0.1814                       
REMARK   3      S31:   0.1331 S32:   0.4839 S33:  -1.4128                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 13:42)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0725 -26.0599  52.3278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3016 T22:   0.7978                                     
REMARK   3      T33:   0.9180 T12:   0.1446                                     
REMARK   3      T13:   0.3949 T23:   0.3763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2029 L22:   0.6467                                     
REMARK   3      L33:   0.1262 L12:   0.2299                                     
REMARK   3      L13:   0.0046 L23:   0.2221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1441 S12:  -0.0546 S13:  -0.5064                       
REMARK   3      S21:  -0.1000 S22:  -0.2291 S23:  -0.9723                       
REMARK   3      S31:   0.6411 S32:   0.0796 S33:   0.0410                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 43:160)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8039 -26.2273  69.2516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3634 T22:   0.3603                                     
REMARK   3      T33:   0.4111 T12:  -0.0378                                     
REMARK   3      T13:   0.3609 T23:   0.1764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3565 L22:   0.4343                                     
REMARK   3      L33:   0.5294 L12:  -0.1023                                     
REMARK   3      L13:   0.1862 L23:   0.2355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2595 S12:   0.4534 S13:  -0.1161                       
REMARK   3      S21:  -0.4964 S22:  -0.0446 S23:  -0.9369                       
REMARK   3      S31:   0.4608 S32:   1.2138 S33:   0.0695                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 161:272)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7009 -31.2328  68.7736              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3038 T22:  -0.4725                                     
REMARK   3      T33:   0.0854 T12:  -0.1126                                     
REMARK   3      T13:   0.1061 T23:   0.3638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4904 L22:   0.6809                                     
REMARK   3      L33:   0.8564 L12:  -0.1813                                     
REMARK   3      L13:   0.5313 L23:  -0.6067                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3847 S12:   0.3933 S13:   0.4649                       
REMARK   3      S21:  -0.6786 S22:  -0.4617 S23:   0.2584                       
REMARK   3      S31:   0.4585 S32:   0.6875 S33:  -0.1212                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 273:316)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5619 -19.3045  60.3148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4706 T22:   0.2756                                     
REMARK   3      T33:  -0.2357 T12:   0.0167                                     
REMARK   3      T13:   0.1742 T23:   0.1878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2138 L22:   0.5275                                     
REMARK   3      L33:   0.4143 L12:  -0.0689                                     
REMARK   3      L13:  -0.1707 L23:  -0.2919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2464 S12:   0.3547 S13:   0.0242                       
REMARK   3      S21:  -0.2967 S22:  -0.2993 S23:  -0.1963                       
REMARK   3      S31:   0.1690 S32:  -0.0510 S33:  -0.3981                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 317:350)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6622 -30.8973  75.2235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8131 T22:   1.2597                                     
REMARK   3      T33:   1.2533 T12:   0.0175                                     
REMARK   3      T13:   0.2052 T23:  -0.1690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1103 L22:  -0.0003                                     
REMARK   3      L33:   0.0590 L12:  -0.0073                                     
REMARK   3      L13:  -0.0476 L23:   0.0132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:   0.0017 S13:  -0.1359                       
REMARK   3      S21:  -0.6384 S22:  -0.1243 S23:  -0.9014                       
REMARK   3      S31:   0.1613 S32:  -0.2430 S33:  -0.0037                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 92:119)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9216 -51.6885  67.2419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4534 T22:   0.4151                                     
REMARK   3      T33:   0.6518 T12:   0.0455                                     
REMARK   3      T13:   0.2527 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3855 L22:   0.0568                                     
REMARK   3      L33:   0.4643 L12:   0.0785                                     
REMARK   3      L13:   0.2319 L23:  -0.0748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1422 S12:   0.1788 S13:  -0.4129                       
REMARK   3      S21:  -0.1256 S22:   0.0406 S23:  -0.0228                       
REMARK   3      S31:   0.1971 S32:   0.4637 S33:   0.0593                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 120:151)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2913 -58.9977  69.7545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2759 T22:   0.8218                                     
REMARK   3      T33:   1.1448 T12:   0.0962                                     
REMARK   3      T13:   0.2090 T23:  -0.0823                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0757 L22:   0.2743                                     
REMARK   3      L33:   0.0892 L12:   0.1176                                     
REMARK   3      L13:  -0.0491 L23:  -0.1474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0474 S12:  -0.1827 S13:  -0.5330                       
REMARK   3      S21:   0.2183 S22:  -0.0967 S23:  -0.0915                       
REMARK   3      S31:   0.6178 S32:  -0.4990 S33:  -0.0044                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 152:198)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7361 -58.7629  86.5012              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5200 T22:  -0.0034                                     
REMARK   3      T33:   0.7855 T12:   0.4938                                     
REMARK   3      T13:  -0.0744 T23:   0.1826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6582 L22:   0.8522                                     
REMARK   3      L33:   0.3846 L12:  -0.0062                                     
REMARK   3      L13:  -0.0030 L23:  -0.5737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1026 S12:  -0.4010 S13:  -0.1866                       
REMARK   3      S21:   0.5234 S22:   0.0736 S23:  -0.2939                       
REMARK   3      S31:  -0.2353 S32:  -0.0881 S33:   0.2567                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 199:211)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4692 -49.5119  78.0923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3104 T22:   0.5678                                     
REMARK   3      T33:   0.4447 T12:   0.3908                                     
REMARK   3      T13:  -0.3396 T23:  -0.1080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0776 L22:   0.0811                                     
REMARK   3      L33:   0.1485 L12:  -0.0487                                     
REMARK   3      L13:  -0.0968 L23:   0.0247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1084 S12:  -0.0073 S13:   0.0061                       
REMARK   3      S21:  -0.0214 S22:  -0.0571 S23:   0.0310                       
REMARK   3      S31:   0.0780 S32:  -0.0765 S33:  -0.0486                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 212:225)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8314 -63.6345  84.2824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7787 T22:   0.2670                                     
REMARK   3      T33:   1.0625 T12:   0.5668                                     
REMARK   3      T13:  -0.1184 T23:   0.4093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3238 L22:   0.6652                                     
REMARK   3      L33:   0.1663 L12:  -0.1674                                     
REMARK   3      L13:  -0.0420 L23:  -0.0975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:  -0.1049 S13:   0.0099                       
REMARK   3      S21:   0.1410 S22:  -0.0628 S23:  -0.0309                       
REMARK   3      S31:   0.1020 S32:   0.0311 S33:  -0.3011                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 226:251)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1773 -52.1762  53.9812              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4692 T22:   0.2263                                     
REMARK   3      T33:   0.5235 T12:   0.1280                                     
REMARK   3      T13:   0.0335 T23:  -0.3791                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5847 L22:   0.3444                                     
REMARK   3      L33:   0.4428 L12:  -0.1916                                     
REMARK   3      L13:  -0.0265 L23:   0.1281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:  -0.2375 S13:   0.0683                       
REMARK   3      S21:   0.5561 S22:   0.2239 S23:  -0.6055                       
REMARK   3      S31:   0.2783 S32:   0.2427 S33:   0.3173                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 252:302)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2017 -48.1234  46.8507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5886 T22:   0.3193                                     
REMARK   3      T33:   0.4421 T12:   0.0916                                     
REMARK   3      T13:  -0.0495 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0485 L22:   0.2298                                     
REMARK   3      L33:   0.5981 L12:  -0.0897                                     
REMARK   3      L13:   0.0456 L23:   0.0789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1815 S12:   0.0468 S13:  -0.1278                       
REMARK   3      S21:  -0.1224 S22:  -0.0445 S23:   0.1295                       
REMARK   3      S31:   0.6995 S32:  -0.6096 S33:  -0.0037                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 303:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1071 -54.2059  40.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7312 T22:   1.0771                                     
REMARK   3      T33:   1.3378 T12:  -0.2532                                     
REMARK   3      T13:   0.2094 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1486 L22:   0.0752                                     
REMARK   3      L33:   0.1234 L12:   0.1057                                     
REMARK   3      L13:  -0.1366 L23:  -0.0971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0389 S12:  -0.0825 S13:  -0.1101                       
REMARK   3      S21:   0.0513 S22:  -0.0335 S23:  -0.0267                       
REMARK   3      S31:   0.0340 S32:   0.0375 S33:  -0.0211                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 311:357)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9429 -47.3138  45.0507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4718 T22:  -0.2608                                     
REMARK   3      T33:   0.1622 T12:   0.1987                                     
REMARK   3      T13:   0.0147 T23:   0.2047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3756 L22:   0.3594                                     
REMARK   3      L33:   0.6654 L12:   0.0903                                     
REMARK   3      L13:   0.1230 L23:   0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0836 S12:  -0.0400 S13:  -0.4041                       
REMARK   3      S21:   0.0075 S22:   0.3668 S23:   0.1258                       
REMARK   3      S31:   0.2889 S32:  -0.3776 S33:   0.3005                       
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 5JR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221098.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15767                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.15500                            
REMARK 200  R SYM                      (I) : 0.10700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
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: 2QCS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THERE ARE TWO MOLECULES PER ASYMMETRICAL UNIT                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE AND 20% PEG     
REMARK 280  3350 WITH THE PROTEIN AT A FINAL CONCENTRATION OF 5 MG/ML IN A      
REMARK 280  1.6 UL DROP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     GLY B    91                                                      
REMARK 465     PRO B   359                                                      
REMARK 465     CYS B   360                                                      
REMARK 465     SER B   361                                                      
REMARK 465     ASP B   362                                                      
REMARK 465     ILE B   363                                                      
REMARK 465     LEU B   364                                                      
REMARK 465     LYS B   365                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     GLN C    12                                                      
REMARK 465     GLY D    91                                                      
REMARK 465     GLY D   358                                                      
REMARK 465     PRO D   359                                                      
REMARK 465     CYS D   360                                                      
REMARK 465     SER D   361                                                      
REMARK 465     ASP D   362                                                      
REMARK 465     ILE D   363                                                      
REMARK 465     LEU D   364                                                      
REMARK 465     LYS D   365                                                      
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     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  16    CD   CE   NZ                                        
REMARK 470     LYS A  21    CE   NZ                                             
REMARK 470     LYS A  28    CD   CE   NZ                                        
REMARK 470     GLU A  31    CD   OE1  OE2                                       
REMARK 470     LYS A  81    CD   CE   NZ                                        
REMARK 470     ARG A  93    CZ   NH1  NH2                                       
REMARK 470     LYS A 105    CD   CE   NZ                                        
REMARK 470     LYS A 192    CE   NZ                                             
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 256    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 309    CE   NZ                                             
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLU B 101    OE1                                                 
REMARK 470     LYS B 114    CD   CE   NZ                                        
REMARK 470     LYS B 121    CD   CE   NZ                                        
REMARK 470     LYS B 128    CE   NZ                                             
REMARK 470     GLN B 177    CD   OE1  NE2                                       
REMARK 470     GLU B 270    OE2                                                 
REMARK 470     LYS B 279    CE   NZ                                             
REMARK 470     ARG B 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 304    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 305    OG                                                  
REMARK 470     GLU B 306    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 307    CB   CG   OD1  ND2                                  
REMARK 470     ARG B 333    NH1  NH2                                            
REMARK 470     GLU C  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  16    CD   CE   NZ                                        
REMARK 470     LYS C  21    CE   NZ                                             
REMARK 470     LYS C  28    CD   CE   NZ                                        
REMARK 470     GLU C  31    CD   OE1  OE2                                       
REMARK 470     LYS C  81    CD   CE   NZ                                        
REMARK 470     ARG C  93    CZ   NH1  NH2                                       
REMARK 470     LYS C 105    CD   CE   NZ                                        
REMARK 470     LYS C 192    CE   NZ                                             
REMARK 470     LYS C 254    CG   CD   CE   NZ                                   
REMARK 470     ARG C 256    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C 309    CE   NZ                                             
REMARK 470     LYS C 317    CG   CD   CE   NZ                                   
REMARK 470     PHE C 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 319    CG   CD   CE   NZ                                   
REMARK 470     GLU C 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 345    CG   CD   CE   NZ                                   
REMARK 470     GLU D 101    OE1  OE2                                            
REMARK 470     GLU D 106    CD   OE1  OE2                                       
REMARK 470     LYS D 114    CD   CE   NZ                                        
REMARK 470     LYS D 121    CD   CE   NZ                                        
REMARK 470     LYS D 128    CE   NZ                                             
REMARK 470     GLN D 177    CD   OE1  NE2                                       
REMARK 470     GLU D 270    CD   OE1  OE2                                       
REMARK 470     LYS D 279    CE   NZ                                             
REMARK 470     ARG D 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 304    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 305    OG                                                  
REMARK 470     GLU D 306    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 307    CB   CG   OD1  ND2                                  
REMARK 470     ARG D 333    NH1  NH2                                            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     PHE A  318   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLU B  245   CD                                                  
REMARK 480     GLU D  245   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP D   181     CZ3  TRP D   188              1.99            
REMARK 500   OD1  ASP A   112     OH   TYR A   117              2.03            
REMARK 500   O    PHE A    43     NH1  ARG A    45              2.05            
REMARK 500   O    SER B   249     OE2  GLU B   255              2.06            
REMARK 500   O    TPO A   197     OH   TYR A   215              2.10            
REMARK 500   O    GLN A    39     OE1  GLN A    42              2.11            
REMARK 500   O    HIS C    87     N    ASN C    90              2.11            
REMARK 500   OD1  ASP D   181     CH2  TRP D   188              2.12            
REMARK 500   OD2  ASP A   328     NH2  ARG B    92              2.13            
REMARK 500   O    THR B   264     OD1  ASP B   267              2.15            
REMARK 500   ND2  ASN C    90     O    ALA C   188              2.16            
REMARK 500   O    SER B   305     OE1  GLU B   308              2.16            
REMARK 500   OE1  GLU D   275     OE1  GLN D   278              2.16            
REMARK 500   O    SER B   305     OE2  GLU B   308              2.17            
REMARK 500   NZ   LYS A   111     CD1  PHE A   350              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A 111   CE    LYS A 111   NZ     -0.175                       
REMARK 500    ARG B 333   NE    ARG B 333   CZ      0.164                       
REMARK 500    TRP C  30   CB    TRP C  30   CG     -0.114                       
REMARK 500    ASP D 181   CB    ASP D 181   CG     -0.190                       
REMARK 500    TRP D 188   CZ3   TRP D 188   CH2    -0.113                       
REMARK 500    ARG D 333   NE    ARG D 333   CZ      0.162                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LEU A  27   CB  -  CG  -  CD1 ANGL. DEV. = -29.6 DEGREES          
REMARK 500    LYS A 111   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    LEU A 116   CB  -  CG  -  CD1 ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG B  92   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    LEU B 126   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG B 333   CD  -  NE  -  CZ  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LYS C  61   CD  -  CE  -  NZ  ANGL. DEV. = -41.5 DEGREES          
REMARK 500    LEU C 167   CB  -  CG  -  CD2 ANGL. DEV. = -17.4 DEGREES          
REMARK 500    LEU C 227   CB  -  CG  -  CD1 ANGL. DEV. = -22.3 DEGREES          
REMARK 500    ASP D 181   CB  -  CG  -  OD1 ANGL. DEV. = -21.3 DEGREES          
REMARK 500    ASP D 181   CB  -  CG  -  OD2 ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ARG D 333   CD  -  NE  -  CZ  ANGL. DEV. = -10.8 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    THR A  32       79.23   -117.50                                   
REMARK 500    ILE A  46      -81.57   -104.12                                   
REMARK 500    SEP A 139      142.26    -39.07                                   
REMARK 500    ASP A 184       76.68     64.37                                   
REMARK 500    ASN A 216     -169.79   -129.91                                   
REMARK 500    LEU A 273       46.24    -82.71                                   
REMARK 500    ASN B 185       42.68     39.44                                   
REMARK 500    ASN B 186       -2.34     72.21                                   
REMARK 500    SER B 256        0.39    -62.77                                   
REMARK 500    ASP B 276      123.56    -39.82                                   
REMARK 500    ASN B 307       65.41   -101.08                                   
REMARK 500    GLU B 308      -90.63   -138.11                                   
REMARK 500    SER B 319      -17.94     87.21                                   
REMARK 500    LYS C  28      -75.04    -59.20                                   
REMARK 500    ILE C  46      -76.98   -115.78                                   
REMARK 500    PHE C 100      137.30   -177.70                                   
REMARK 500    PHE C 110     -178.30    174.17                                   
REMARK 500    ASP C 112     -168.78   -165.65                                   
REMARK 500    ARG C 165      -21.93     72.48                                   
REMARK 500    LYS C 168      150.34    175.82                                   
REMARK 500    ASP C 184       86.07     54.89                                   
REMARK 500    TRP C 196      -63.20   -133.88                                   
REMARK 500    TPO C 197      127.65    -23.24                                   
REMARK 500    SER C 212       -0.29     68.16                                   
REMARK 500    ASN C 216     -169.08   -126.29                                   
REMARK 500    TYR C 229      -73.65    -50.37                                   
REMARK 500    LYS C 266      -72.32    -58.64                                   
REMARK 500    CYS C 343       70.89     63.57                                   
REMARK 500    GLU C 346      -60.61    -90.40                                   
REMARK 500    GLU D 106       -7.48    -54.36                                   
REMARK 500    PHE D 136      -57.23   -126.65                                   
REMARK 500    ASN D 142      -71.28    -51.41                                   
REMARK 500    ALA D 150       -7.33    -58.85                                   
REMARK 500    ASN D 186       -6.58     66.03                                   
REMARK 500    ALA D 189      -74.32    -91.87                                   
REMARK 500    SER D 197      177.78    174.03                                   
REMARK 500    PHE D 198      172.44    179.22                                   
REMARK 500    SER D 252      -72.02    -72.80                                   
REMARK 500    ARG D 304      -76.70   -101.06                                   
REMARK 500    GLU D 308     -159.11   -133.69                                   
REMARK 500    SER D 319      -10.26     78.78                                   
REMARK 500    PRO D 332     -177.29    -60.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA B 189         13.71                                           
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 ADP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 400                 
DBREF  5JR7 A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  5JR7 B   91   365  UNP    P00514   KAP0_BOVIN      92    366             
DBREF  5JR7 C    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  5JR7 D   91   365  UNP    P00514   KAP0_BOVIN      92    366             
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B  275  GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR          
SEQRES   2 B  275  THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE          
SEQRES   3 B  275  PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA          
SEQRES   4 B  275  ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN          
SEQRES   5 B  275  GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER          
SEQRES   6 B  275  PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU          
SEQRES   7 B  275  GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP          
SEQRES   8 B  275  VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU          
SEQRES   9 B  275  GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR          
SEQRES  10 B  275  PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS          
SEQRES  11 B  275  LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU          
SEQRES  12 B  275  MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU GLU          
SEQRES  13 B  275  PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP LYS          
SEQRES  14 B  275  TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO VAL          
SEQRES  15 B  275  GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY GLU          
SEQRES  16 B  275  PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER ALA          
SEQRES  17 B  275  ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE VAL          
SEQRES  18 B  275  GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY GLU          
SEQRES  19 B  275  ILE ALA LEU LEU MET ASN ARG PRO ARG ALA ALA THR VAL          
SEQRES  20 B  275  VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP ARG          
SEQRES  21 B  275  PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP ILE          
SEQRES  22 B  275  LEU LYS                                                      
SEQRES   1 C  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 C  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 C  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 C  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 C  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 C  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 C  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 C  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 C  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 C  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 C  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 C  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 C  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 C  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 C  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 C  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 C  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 C  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 C  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 C  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 C  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 C  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 C  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 C  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 C  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 C  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 C  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 D  275  GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR          
SEQRES   2 D  275  THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE          
SEQRES   3 D  275  PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA          
SEQRES   4 D  275  ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN          
SEQRES   5 D  275  GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER          
SEQRES   6 D  275  PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU          
SEQRES   7 D  275  GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP          
SEQRES   8 D  275  VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU          
SEQRES   9 D  275  GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR          
SEQRES  10 D  275  PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS          
SEQRES  11 D  275  LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU          
SEQRES  12 D  275  MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU GLU          
SEQRES  13 D  275  PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP LYS          
SEQRES  14 D  275  TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO VAL          
SEQRES  15 D  275  GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY GLU          
SEQRES  16 D  275  PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER ALA          
SEQRES  17 D  275  ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE VAL          
SEQRES  18 D  275  GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY GLU          
SEQRES  19 D  275  ILE ALA LEU LEU MET ASN ARG PRO ARG ALA ALA THR VAL          
SEQRES  20 D  275  VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP ARG          
SEQRES  21 D  275  PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP ILE          
SEQRES  22 D  275  LEU LYS                                                      
MODRES 5JR7 SEP A  139  SER  MODIFIED RESIDUE                                   
MODRES 5JR7 TPO A  197  THR  MODIFIED RESIDUE                                   
MODRES 5JR7 SEP A  338  SER  MODIFIED RESIDUE                                   
MODRES 5JR7 SEP C  139  SER  MODIFIED RESIDUE                                   
MODRES 5JR7 TPO C  197  THR  MODIFIED RESIDUE                                   
MODRES 5JR7 SEP C  338  SER  MODIFIED RESIDUE                                   
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    SEP  C 139      10                                                       
HET    TPO  C 197      11                                                       
HET    SEP  C 338      10                                                       
HET    ADP  A 400      27                                                       
HET    ADP  C 400      27                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    4(C3 H8 N O6 P)                                              
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  ADP    2(C10 H15 N5 O10 P2)                                         
HELIX    1 AA1 GLU A   13  THR A   32  1                                  20    
HELIX    2 AA2 GLN A   39  ASP A   41  5                                   3    
HELIX    3 AA3 LYS A   76  LEU A   82  1                                   7    
HELIX    4 AA4 GLN A   84  VAL A   98  1                                  15    
HELIX    5 AA5 GLU A  127  GLY A  136  1                                  10    
HELIX    6 AA6 SEP A  139  LEU A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  201  LEU A  205  5                                   5    
HELIX    9 AA9 ALA A  206  LEU A  211  1                                   6    
HELIX   10 AB1 ALA A  218  GLY A  234  1                                  17    
HELIX   11 AB2 GLN A  242  GLY A  253  1                                  12    
HELIX   12 AB3 SER A  262  LEU A  273  1                                  12    
HELIX   13 AB4 VAL A  288  ASN A  293  1                                   6    
HELIX   14 AB5 HIS A  294  ALA A  298  5                                   5    
HELIX   15 AB6 ASP A  301  GLN A  307  1                                   7    
HELIX   16 AB7 THR B  104  TYR B  111  1                                   8    
HELIX   17 AB8 ASP B  119  GLU B  131  1                                  13    
HELIX   18 AB9 ASN B  133  HIS B  138  1                                   6    
HELIX   19 AC1 ASP B  140  MET B  151  1                                  12    
HELIX   20 AC2 GLY B  199  ILE B  204  5                                   6    
HELIX   21 AC3 ARG B  226  LYS B  250  1                                  25    
HELIX   22 AC4 VAL B  251  GLU B  255  5                                   5    
HELIX   23 AC5 ASP B  258  LEU B  269  1                                  12    
HELIX   24 AC6 GLU B  324  MET B  329  1                                   6    
HELIX   25 AC7 ARG B  350  LEU B  357  1                                   8    
HELIX   26 AC8 VAL C   15  THR C   32  1                                  18    
HELIX   27 AC9 GLN C   39  PHE C   43  5                                   5    
HELIX   28 AD1 LYS C   76  LEU C   82  1                                   7    
HELIX   29 AD2 GLN C   84  GLN C   96  1                                  13    
HELIX   30 AD3 GLU C  127  GLY C  136  1                                  10    
HELIX   31 AD4 SEP C  139  LEU C  160  1                                  22    
HELIX   32 AD5 LYS C  168  GLU C  170  5                                   3    
HELIX   33 AD6 THR C  201  LEU C  205  5                                   5    
HELIX   34 AD7 ALA C  206  LEU C  211  1                                   6    
HELIX   35 AD8 ALA C  218  GLY C  234  1                                  17    
HELIX   36 AD9 GLN C  242  VAL C  251  1                                  10    
HELIX   37 AE1 SER C  262  LEU C  273  1                                  12    
HELIX   38 AE2 VAL C  288  ASN C  293  1                                   6    
HELIX   39 AE3 HIS C  294  ALA C  298  5                                   5    
HELIX   40 AE4 ASP C  301  GLN C  307  1                                   7    
HELIX   41 AE5 THR D  104  ALA D  109  1                                   6    
HELIX   42 AE6 ASP D  119  ALA D  124  1                                   6    
HELIX   43 AE7 ALA D  124  GLU D  131  1                                   8    
HELIX   44 AE8 ASN D  133  HIS D  138  1                                   6    
HELIX   45 AE9 ASP D  140  MET D  151  1                                  12    
HELIX   46 AF1 GLU D  200  TYR D  205  1                                   6    
HELIX   47 AF2 ARG D  226  VAL D  251  1                                  26    
HELIX   48 AF3 ASP D  258  ASP D  267  1                                  10    
HELIX   49 AF4 GLU D  324  MET D  329  1                                   6    
HELIX   50 AF5 ASP D  349  LEU D  357  1                                   9    
SHEET    1 AA1 5 PHE A  43  THR A  51  0                                        
SHEET    2 AA1 5 GLY A  55  HIS A  62 -1  O  VAL A  57   N  GLY A  50           
SHEET    3 AA1 5 ASN A  67  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4 AA1 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5 AA1 5 LEU A 106  LYS A 111 -1  N  GLU A 107   O  VAL A 119           
SHEET    1 AA2 2 LEU A 162  ILE A 163  0                                        
SHEET    2 AA2 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1 AA3 2 LEU A 172  ILE A 174  0                                        
SHEET    2 AA3 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1 AA4 2 CYS A 199  GLY A 200  0                                        
SHEET    2 AA4 2 ILE B  98  SER B  99 -1  O  ILE B  98   N  GLY A 200           
SHEET    1 AA5 4 PHE B 152  PHE B 156  0                                        
SHEET    2 AA5 4 VAL B 219  ASP B 225 -1  O  GLY B 223   N  PHE B 152           
SHEET    3 AA5 4 ASN B 171  GLN B 177 -1  N  VAL B 174   O  TRP B 222           
SHEET    4 AA5 4 SER B 197  PHE B 198 -1  O  PHE B 198   N  TYR B 173           
SHEET    1 AA6 4 THR B 161  ILE B 163  0                                        
SHEET    2 AA6 4 THR B 212  ALA B 215 -1  O  VAL B 213   N  VAL B 162           
SHEET    3 AA6 4 MET B 180  VAL B 184 -1  N  ASP B 181   O  LYS B 214           
SHEET    4 AA6 4 GLU B 187  VAL B 192 -1  O  GLU B 187   N  VAL B 184           
SHEET    1 AA7 4 GLU B 270  PHE B 274  0                                        
SHEET    2 AA7 4 THR B 336  ASP B 349 -1  O  LEU B 343   N  PHE B 274           
SHEET    3 AA7 4 GLU B 289  GLN B 302 -1  N  LEU B 301   O  THR B 336           
SHEET    4 AA7 4 VAL B 311  LEU B 316 -1  O  LEU B 316   N  ALA B 298           
SHEET    1 AA8 4 LYS B 279  VAL B 281  0                                        
SHEET    2 AA8 4 THR B 336  ASP B 349 -1  O  VAL B 337   N  VAL B 281           
SHEET    3 AA8 4 GLU B 289  GLN B 302 -1  N  LEU B 301   O  THR B 336           
SHEET    4 AA8 4 TYR B 321  PHE B 322 -1  O  PHE B 322   N  PHE B 291           
SHEET    1 AA9 2 PRO B 286  GLY B 287  0                                        
SHEET    2 AA9 2 ARG B 331  PRO B 332 -1  O  ARG B 331   N  GLY B 287           
SHEET    1 AB1 5 LYS C  47  THR C  51  0                                        
SHEET    2 AB1 5 ARG C  56  HIS C  62 -1  O  LEU C  59   N  LYS C  47           
SHEET    3 AB1 5 ASN C  67  ASP C  75 -1  O  ILE C  73   N  ARG C  56           
SHEET    4 AB1 5 ASN C 115  GLU C 121 -1  O  MET C 118   N  LYS C  72           
SHEET    5 AB1 5 LEU C 106  PHE C 110 -1  N  PHE C 110   O  TYR C 117           
SHEET    1 AB2 2 LEU C 162  ILE C 163  0                                        
SHEET    2 AB2 2 LYS C 189  ARG C 190 -1  O  LYS C 189   N  ILE C 163           
SHEET    1 AB3 2 LEU C 172  ILE C 174  0                                        
SHEET    2 AB3 2 ILE C 180  VAL C 182 -1  O  GLN C 181   N  LEU C 173           
SHEET    1 AB4 2 CYS C 199  GLY C 200  0                                        
SHEET    2 AB4 2 ILE D  98  SER D  99 -1  O  ILE D  98   N  GLY C 200           
SHEET    1 AB5 3 VAL D 154  PHE D 156  0                                        
SHEET    2 AB5 3 VAL D 219  ASP D 225 -1  O  LEU D 221   N  VAL D 154           
SHEET    3 AB5 3 ASN D 171  ILE D 175 -1  N  VAL D 174   O  TRP D 222           
SHEET    1 AB6 4 GLU D 160  ILE D 163  0                                        
SHEET    2 AB6 4 THR D 212  ALA D 215 -1  O  ALA D 215   N  GLU D 160           
SHEET    3 AB6 4 MET D 180  VAL D 184 -1  N  ASP D 181   O  LYS D 214           
SHEET    4 AB6 4 GLU D 187  VAL D 192 -1  O  ALA D 189   N  VAL D 182           
SHEET    1 AB7 4 GLU D 270  PHE D 274  0                                        
SHEET    2 AB7 4 THR D 336  LYS D 347 -1  O  CYS D 345   N  VAL D 272           
SHEET    3 AB7 4 PHE D 291  ARG D 303 -1  N  LEU D 301   O  THR D 336           
SHEET    4 AB7 4 PHE D 310  LEU D 316 -1  O  LEU D 316   N  ALA D 298           
SHEET    1 AB8 4 GLU D 270  PHE D 274  0                                        
SHEET    2 AB8 4 THR D 336  LYS D 347 -1  O  CYS D 345   N  VAL D 272           
SHEET    3 AB8 4 PHE D 291  ARG D 303 -1  N  LEU D 301   O  THR D 336           
SHEET    4 AB8 4 TYR D 321  PHE D 322 -1  O  PHE D 322   N  PHE D 291           
SHEET    1 AB9 2 PRO D 286  GLY D 287  0                                        
SHEET    2 AB9 2 ARG D 331  PRO D 332 -1  O  ARG D 331   N  GLY D 287           
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.33  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.34  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.32  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.32  
LINK         C   PHE C 138                 N   SEP C 139     1555   1555  1.33  
LINK         C   SEP C 139                 N   GLU C 140     1555   1555  1.33  
LINK         C   TRP C 196                 N   TPO C 197     1555   1555  1.33  
LINK         C   TPO C 197                 N   LEU C 198     1555   1555  1.33  
LINK         C   VAL C 337                 N   SEP C 338     1555   1555  1.33  
LINK         C   SEP C 338                 N   ILE C 339     1555   1555  1.33  
SITE     1 AC1 16 GLY A  50  GLY A  52  GLY A  55  VAL A  57                    
SITE     2 AC1 16 ALA A  70  LYS A  72  MET A 120  GLU A 121                    
SITE     3 AC1 16 VAL A 123  GLU A 127  GLU A 170  ASN A 171                    
SITE     4 AC1 16 LEU A 173  THR A 183  ASP A 184  PHE A 327                    
SITE     1 AC2 13 GLY C  50  GLY C  52  GLY C  55  VAL C  57                    
SITE     2 AC2 13 ALA C  70  LYS C  72  GLU C 121  VAL C 123                    
SITE     3 AC2 13 GLU C 127  GLU C 170  LEU C 173  THR C 183                    
SITE     4 AC2 13 ASP C 184                                                     
CRYST1   60.146   66.790   87.932 101.76  89.37 105.27 P 1           2          
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      0.016626  0.004539  0.000781        0.00000                         
SCALE2      0.000000  0.015520  0.003306        0.00000                         
SCALE3      0.000000  0.000000  0.011628        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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