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Database: PDB
Entry: 5UQ1
LinkDB: 5UQ1
Original site: 5UQ1 
HEADER    TRANSFERASE/CELL CYCLE                  06-FEB-17   5UQ1              
TITLE     CRYSTAL STRUCTURE OF HUMAN CDK2-SPY1 COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SPEEDY PROTEIN A;                                          
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 61-213;                                       
COMPND  11 SYNONYM: RAPID INDUCER OF G2/M PROGRESSION IN OOCYTES A,HSPY/RINGO A,
COMPND  12 SPEEDY-1,SPY1;                                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SPDYA, SPDY1, SPY1;                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOTRANSFERASE, PROTEIN KINASE, CELL CYCLE REGULATION,            
KEYWDS   2 TRANSFERASE-CELL CYCLE COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.MCGRATH,S.M.TRIPATHI,S.M.RUBIN                                    
REVDAT   3   09-AUG-17 5UQ1    1       JRNL                                     
REVDAT   2   19-JUL-17 5UQ1    1       JRNL                                     
REVDAT   1   05-JUL-17 5UQ1    0                                                
JRNL        AUTH   D.A.MCGRATH,B.A.FIFIELD,A.H.MARCEAU,S.TRIPATHI,L.A.PORTER,   
JRNL        AUTH 2 S.M.RUBIN                                                    
JRNL        TITL   STRUCTURAL BASIS OF DIVERGENT CYCLIN-DEPENDENT KINASE        
JRNL        TITL 2 ACTIVATION BY SPY1/RINGO PROTEINS.                           
JRNL        REF    EMBO J.                       V.  36  2251 2017              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   28666995                                                     
JRNL        DOI    10.15252/EMBJ.201796905                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17621                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 865                             
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 46.1155 -  5.8125    0.99     3139   157  0.1871 0.2178        
REMARK   3     2  5.8125 -  4.6150    1.00     2967   152  0.1935 0.2521        
REMARK   3     3  4.6150 -  4.0320    1.00     2915   175  0.1765 0.2339        
REMARK   3     4  4.0320 -  3.6635    1.00     2896   147  0.2140 0.2809        
REMARK   3     5  3.6635 -  3.4010    0.87     2506   140  0.2497 0.3482        
REMARK   3     6  3.4010 -  3.2005    0.80     2333    94  0.3015 0.3881        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           7095                                  
REMARK   3   ANGLE     :  1.049           9618                                  
REMARK   3   CHIRALITY :  0.044           1070                                  
REMARK   3   PLANARITY :  0.006           1213                                  
REMARK   3   DIHEDRAL  : 14.241           2604                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4755   3.5406  19.1117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5690 T22:   0.2858                                     
REMARK   3      T33:   0.3307 T12:   0.0010                                     
REMARK   3      T13:   0.0337 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0092 L22:   0.0101                                     
REMARK   3      L33:   0.0103 L12:  -0.0016                                     
REMARK   3      L13:   0.0077 L23:   0.0081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0722 S12:  -0.0937 S13:  -0.0820                       
REMARK   3      S21:   0.1274 S22:  -0.0990 S23:  -0.0824                       
REMARK   3      S31:  -0.1241 S32:  -0.0264 S33:  -0.0009                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 140 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2338   3.8461  18.3202              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1993 T22:  -0.0370                                     
REMARK   3      T33:   0.0577 T12:  -0.2867                                     
REMARK   3      T13:  -0.1350 T23:  -0.1073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0478 L22:   0.0213                                     
REMARK   3      L33:   0.0191 L12:   0.0297                                     
REMARK   3      L13:  -0.0000 L23:  -0.0141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1053 S12:   0.1904 S13:  -0.0150                       
REMARK   3      S21:  -0.1246 S22:   0.0830 S23:   0.0022                       
REMARK   3      S31:   0.0393 S32:  -0.0385 S33:  -0.2040                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3948   7.6017  35.3124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2366 T22:   0.1747                                     
REMARK   3      T33:   0.1145 T12:  -0.2142                                     
REMARK   3      T13:   0.0261 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0062 L22:   0.1693                                     
REMARK   3      L33:   0.0419 L12:   0.0049                                     
REMARK   3      L13:   0.0033 L23:   0.0802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:  -0.0438 S13:  -0.1148                       
REMARK   3      S21:   0.2098 S22:  -0.0458 S23:  -0.0875                       
REMARK   3      S31:   0.0535 S32:  -0.0045 S33:   0.0952                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 296 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7317  16.2656  30.8527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2732 T22:   0.0727                                     
REMARK   3      T33:   0.2855 T12:  -0.2523                                     
REMARK   3      T13:   0.0775 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0338 L22:   0.0344                                     
REMARK   3      L33:   0.0418 L12:  -0.0246                                     
REMARK   3      L13:  -0.0076 L23:  -0.0236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1142 S12:  -0.1111 S13:   0.2207                       
REMARK   3      S21:   0.1304 S22:  -0.0282 S23:   0.3524                       
REMARK   3      S31:  -0.1390 S32:  -0.0465 S33:   0.1004                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 80 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6062 -22.6410  45.9649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5969 T22:   0.6632                                     
REMARK   3      T33:   0.6092 T12:  -0.1865                                     
REMARK   3      T13:  -0.0403 T23:   0.1380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0273 L22:   0.0229                                     
REMARK   3      L33:   0.0201 L12:   0.0022                                     
REMARK   3      L13:  -0.0145 L23:  -0.0173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0813 S12:   0.0623 S13:  -0.0669                       
REMARK   3      S21:  -0.0592 S22:  -0.0137 S23:   0.0610                       
REMARK   3      S31:   0.1119 S32:  -0.0463 S33:  -0.0009                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 97 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2598  -6.3524  52.3803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2879 T22:   0.4264                                     
REMARK   3      T33:   0.2383 T12:  -0.0820                                     
REMARK   3      T13:  -0.0619 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0021 L22:   0.0008                                     
REMARK   3      L33:   0.0014 L12:  -0.0023                                     
REMARK   3      L13:  -0.0004 L23:  -0.0013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0222 S12:   0.0200 S13:   0.0408                       
REMARK   3      S21:  -0.0387 S22:   0.0263 S23:   0.0600                       
REMARK   3      S31:  -0.0237 S32:  -0.0565 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 98 THROUGH 134 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3249 -13.0501  39.4039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2870 T22:   0.1947                                     
REMARK   3      T33:   0.3899 T12:  -0.1191                                     
REMARK   3      T13:   0.0062 T23:   0.1308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0616 L22:   0.0162                                     
REMARK   3      L33:   0.1953 L12:   0.0253                                     
REMARK   3      L13:   0.1064 L23:   0.0545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1742 S12:  -0.0389 S13:  -0.1963                       
REMARK   3      S21:  -0.0059 S22:   0.1487 S23:  -0.0220                       
REMARK   3      S31:  -0.0042 S32:  -0.0919 S33:   0.0401                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 200 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8692  -7.1627  41.2381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2979 T22:   0.4489                                     
REMARK   3      T33:   0.3971 T12:  -0.1220                                     
REMARK   3      T13:  -0.0057 T23:   0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0456 L22:   0.0750                                     
REMARK   3      L33:   0.1014 L12:  -0.0419                                     
REMARK   3      L13:  -0.0564 L23:   0.0807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0675 S12:  -0.2306 S13:  -0.0478                       
REMARK   3      S21:  -0.1466 S22:   0.1549 S23:  -0.0059                       
REMARK   3      S31:   0.0933 S32:   0.0344 S33:   0.0246                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 158 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9623  34.2400  15.5398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4150 T22:   0.0461                                     
REMARK   3      T33:   0.2221 T12:  -0.2093                                     
REMARK   3      T13:  -0.0211 T23:   0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2522 L22:   0.1509                                     
REMARK   3      L33:   0.1329 L12:   0.1375                                     
REMARK   3      L13:   0.0755 L23:   0.0315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2242 S12:   0.1321 S13:   0.1382                       
REMARK   3      S21:   0.0424 S22:  -0.0068 S23:   0.0205                       
REMARK   3      S31:   0.0767 S32:  -0.0042 S33:  -0.4417                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 159 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7234  27.9713  31.5471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5688 T22:   0.5103                                     
REMARK   3      T33:   0.3469 T12:  -0.1098                                     
REMARK   3      T13:   0.0508 T23:   0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0022 L22:   0.0015                                     
REMARK   3      L33:  -0.0000 L12:   0.0009                                     
REMARK   3      L13:  -0.0014 L23:  -0.0011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:   0.0502 S13:  -0.0549                       
REMARK   3      S21:  -0.0022 S22:  -0.0154 S23:  -0.0331                       
REMARK   3      S31:   0.0212 S32:  -0.0058 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 182 THROUGH 289 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8151  22.6164  24.0910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3554 T22:   0.3525                                     
REMARK   3      T33:   0.4359 T12:  -0.0336                                     
REMARK   3      T13:  -0.0046 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0559 L22:   0.0424                                     
REMARK   3      L33:   0.0264 L12:  -0.0376                                     
REMARK   3      L13:   0.0290 L23:   0.0026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1139 S12:   0.0620 S13:   0.1515                       
REMARK   3      S21:   0.0100 S22:  -0.1781 S23:  -0.3463                       
REMARK   3      S31:   0.0929 S32:   0.0688 S33:   0.0003                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 63 THROUGH 71 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0648  65.2555  28.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6904 T22:   0.3702                                     
REMARK   3      T33:   0.7081 T12:  -0.2579                                     
REMARK   3      T13:  -0.1200 T23:   0.0946                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0297 L22:   0.0609                                     
REMARK   3      L33:   0.0791 L12:  -0.0426                                     
REMARK   3      L13:  -0.0493 L23:   0.0701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0246 S12:  -0.0076 S13:   0.0747                       
REMARK   3      S21:   0.0385 S22:   0.0157 S23:   0.0035                       
REMARK   3      S31:  -0.0883 S32:  -0.0211 S33:  -0.0059                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 72 THROUGH 119 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3327  56.3925  39.4702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3900 T22:   0.2040                                     
REMARK   3      T33:   0.3843 T12:  -0.1390                                     
REMARK   3      T13:   0.0158 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0307 L22:   0.0378                                     
REMARK   3      L33:   0.0239 L12:  -0.0053                                     
REMARK   3      L13:   0.0009 L23:   0.0251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0289 S12:  -0.0378 S13:   0.0289                       
REMARK   3      S21:   0.2070 S22:   0.0330 S23:  -0.0282                       
REMARK   3      S31:   0.0894 S32:  -0.0635 S33:  -0.0205                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8414  45.0880  38.2540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3300 T22:   0.0953                                     
REMARK   3      T33:   0.1735 T12:  -0.2313                                     
REMARK   3      T13:   0.0855 T23:   0.0657                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1493 L22:   0.0772                                     
REMARK   3      L33:   0.1419 L12:  -0.0729                                     
REMARK   3      L13:   0.0042 L23:  -0.0687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0578 S12:  -0.0550 S13:  -0.1228                       
REMARK   3      S21:   0.0370 S22:   0.0436 S23:   0.0679                       
REMARK   3      S31:  -0.0226 S32:   0.0076 S33:   0.1763                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 171 THROUGH 185 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9059  53.0588  26.7431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4032 T22:   0.3525                                     
REMARK   3      T33:   0.3062 T12:  -0.1806                                     
REMARK   3      T13:   0.0175 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0115 L22:   0.0432                                     
REMARK   3      L33:   0.0365 L12:   0.0056                                     
REMARK   3      L13:  -0.0201 L23:   0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0909 S12:   0.0506 S13:  -0.0177                       
REMARK   3      S21:   0.0275 S22:  -0.0545 S23:   0.0357                       
REMARK   3      S31:  -0.0565 S32:   0.0152 S33:  -0.0202                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 186 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0273  57.7682  42.0928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5379 T22:   0.4776                                     
REMARK   3      T33:   0.4673 T12:  -0.1773                                     
REMARK   3      T13:   0.0887 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0034 L22:   0.0003                                     
REMARK   3      L33:   0.0027 L12:   0.0012                                     
REMARK   3      L13:  -0.0026 L23:  -0.0032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0149 S12:   0.0162 S13:   0.0392                       
REMARK   3      S21:   0.0682 S22:  -0.0092 S23:  -0.0676                       
REMARK   3      S31:   0.0633 S32:   0.0663 S33:   0.0001                       
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 5UQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226012.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17634                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.111                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LITHIUM CHLORIDE, 12% PEG 6000, AND   
REMARK 280  0.1M MES PH 6.2, HARVESTED AND FLASH FROZEN IN THE SAME SOLUTION    
REMARK 280  WITH 20% PEG 200., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.59700            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      217.19400            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      217.19400            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.59700            
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: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     MET B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     PHE B    60                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     CYS B    63                                                      
REMARK 465     LEU B    64                                                      
REMARK 465     VAL B    65                                                      
REMARK 465     ILE B    66                                                      
REMARK 465     VAL B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     SER B   204                                                      
REMARK 465     GLY B   205                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     VAL B   207                                                      
REMARK 465     ARG B   208                                                      
REMARK 465     ASN B   209                                                      
REMARK 465     TYR B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     GLU C    -1                                                      
REMARK 465     PHE C     0                                                      
REMARK 465     THR C   290                                                      
REMARK 465     LYS C   291                                                      
REMARK 465     PRO C   292                                                      
REMARK 465     VAL C   293                                                      
REMARK 465     PRO C   294                                                      
REMARK 465     HIS C   295                                                      
REMARK 465     LEU C   296                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLY D    54                                                      
REMARK 465     ALA D    55                                                      
REMARK 465     MET D    56                                                      
REMARK 465     ASP D    57                                                      
REMARK 465     PRO D    58                                                      
REMARK 465     GLU D    59                                                      
REMARK 465     PHE D    60                                                      
REMARK 465     GLY D    61                                                      
REMARK 465     PRO D    62                                                      
REMARK 465     HIS D   202                                                      
REMARK 465     HIS D   203                                                      
REMARK 465     SER D   204                                                      
REMARK 465     GLY D   205                                                      
REMARK 465     ALA D   206                                                      
REMARK 465     VAL D   207                                                      
REMARK 465     ARG D   208                                                      
REMARK 465     ASN D   209                                                      
REMARK 465     TYR D   210                                                      
REMARK 465     ASN D   211                                                      
REMARK 465     ARG D   212                                                      
REMARK 465     ASP D   213                                                      
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  28    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     ASP B  81    CG   OD1  OD2                                       
REMARK 470     GLN B  84    CG   CD   OE1  NE2                                  
REMARK 470     TRP B  88    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  88    CZ3  CH2                                            
REMARK 470     GLU C   2    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 125    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR C 179    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 250    CG   CD   CE   NZ                                   
REMARK 470     ASP D  81    CG   OD1  OD2                                       
REMARK 470     TRP D  88    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D  88    CZ3  CH2                                            
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   OE1  GLU D   135     NH2  ARG D   199              2.09            
REMARK 500   O    SER A   181     N    ALA A   183              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   CYS B    91     SG   CYS D    92     6655     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 127       74.76    176.07                                   
REMARK 500    LEU A 128       59.11   -105.40                                   
REMARK 500    ASN A 136     -163.38   -113.71                                   
REMARK 500    ASP A 145       68.28     61.82                                   
REMARK 500    PHE A 146       36.80    -90.54                                   
REMARK 500    VAL A 156       54.18     29.32                                   
REMARK 500    VAL A 163      -41.16   -138.16                                   
REMARK 500    TYR A 179       82.90     60.73                                   
REMARK 500    THR A 182      -46.20     21.86                                   
REMARK 500    PRO A 284       10.00    -61.20                                   
REMARK 500    ASP C 127       68.71    169.17                                   
REMARK 500    LEU C 128       61.67   -100.78                                   
REMARK 500    ASN C 136     -162.44   -115.21                                   
REMARK 500    VAL C 156       53.71     28.04                                   
REMARK 500    VAL C 163     -123.49   -139.61                                   
REMARK 500    LEU C 166      -96.86     16.70                                   
REMARK 500    TRP C 167      -25.42    -22.19                                   
REMARK 500    SER C 181     -131.72   -151.39                                   
REMARK 500    PRO C 284       60.13    -64.10                                   
REMARK 500    GLN D  67      166.82    175.43                                   
REMARK 500    ARG D  68     -138.07   -127.28                                   
REMARK 500    GLN D  69       48.94    -71.85                                   
REMARK 500    HIS D 118       49.63    -80.70                                   
REMARK 500    ARG D 197       58.72    -95.38                                   
REMARK 500    SER D 200       55.92    -96.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A  247     PHE A  248                 -148.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UQ2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UQ3   RELATED DB: PDB                                   
DBREF  5UQ1 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5UQ1 B   61   213  UNP    Q5MJ70   SPDYA_HUMAN     61    213             
DBREF  5UQ1 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5UQ1 D   61   213  UNP    Q5MJ70   SPDYA_HUMAN     61    213             
SEQADV 5UQ1 GLY A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 GLU A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 PHE A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 GLY B   54  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 ALA B   55  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 MET B   56  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 ASP B   57  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 PRO B   58  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 GLU B   59  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 PHE B   60  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 GLY C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 GLU C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 PHE C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ1 GLY D   54  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 ALA D   55  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 MET D   56  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 ASP D   57  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 PRO D   58  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 GLU D   59  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ1 PHE D   60  UNP  Q5MJ70              EXPRESSION TAG                 
SEQRES   1 A  301  GLY GLU PHE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 A  301  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 A  301  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 A  301  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 A  301  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 A  301  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 A  301  LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS          
SEQRES   8 A  301  LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 A  301  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 A  301  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 A  301  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 A  301  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 A  301  VAL PRO VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU          
SEQRES  14 A  301  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 A  301  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 A  301  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 A  301  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 A  301  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 A  301  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 A  301  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 A  301  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 A  301  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 A  301  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 A  301  ARG LEU                                                      
SEQRES   1 B  160  GLY ALA MET ASP PRO GLU PHE GLY PRO CYS LEU VAL ILE          
SEQRES   2 B  160  GLN ARG GLN ASP MET THR ALA PHE PHE LYS LEU PHE ASP          
SEQRES   3 B  160  ASP ASP LEU ILE GLN ASP PHE LEU TRP MET ASP CYS CYS          
SEQRES   4 B  160  CYS LYS ILE ALA ASP LYS TYR LEU LEU ALA MET THR PHE          
SEQRES   5 B  160  VAL TYR PHE LYS ARG ALA LYS PHE THR ILE SER GLU HIS          
SEQRES   6 B  160  THR ARG ILE ASN PHE PHE ILE ALA LEU TYR LEU ALA ASN          
SEQRES   7 B  160  THR VAL GLU GLU ASP GLU GLU GLU THR LYS TYR GLU ILE          
SEQRES   8 B  160  PHE PRO TRP ALA LEU GLY LYS ASN TRP ARG LYS LEU PHE          
SEQRES   9 B  160  PRO ASN PHE LEU LYS LEU ARG ASP GLN LEU TRP ASP ARG          
SEQRES  10 B  160  ILE ASP TYR ARG ALA ILE VAL SER ARG ARG CYS CYS GLU          
SEQRES  11 B  160  GLU VAL MET ALA ILE ALA PRO THR HIS TYR ILE TRP GLN          
SEQRES  12 B  160  ARG GLU ARG SER VAL HIS HIS SER GLY ALA VAL ARG ASN          
SEQRES  13 B  160  TYR ASN ARG ASP                                              
SEQRES   1 C  301  GLY GLU PHE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 C  301  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 C  301  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 C  301  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 C  301  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 C  301  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 C  301  LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS          
SEQRES   8 C  301  LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 C  301  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 C  301  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 C  301  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 C  301  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 C  301  VAL PRO VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU          
SEQRES  14 C  301  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 C  301  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 C  301  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 C  301  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 C  301  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 C  301  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 C  301  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 C  301  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 C  301  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 C  301  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 C  301  ARG LEU                                                      
SEQRES   1 D  160  GLY ALA MET ASP PRO GLU PHE GLY PRO CYS LEU VAL ILE          
SEQRES   2 D  160  GLN ARG GLN ASP MET THR ALA PHE PHE LYS LEU PHE ASP          
SEQRES   3 D  160  ASP ASP LEU ILE GLN ASP PHE LEU TRP MET ASP CYS CYS          
SEQRES   4 D  160  CYS LYS ILE ALA ASP LYS TYR LEU LEU ALA MET THR PHE          
SEQRES   5 D  160  VAL TYR PHE LYS ARG ALA LYS PHE THR ILE SER GLU HIS          
SEQRES   6 D  160  THR ARG ILE ASN PHE PHE ILE ALA LEU TYR LEU ALA ASN          
SEQRES   7 D  160  THR VAL GLU GLU ASP GLU GLU GLU THR LYS TYR GLU ILE          
SEQRES   8 D  160  PHE PRO TRP ALA LEU GLY LYS ASN TRP ARG LYS LEU PHE          
SEQRES   9 D  160  PRO ASN PHE LEU LYS LEU ARG ASP GLN LEU TRP ASP ARG          
SEQRES  10 D  160  ILE ASP TYR ARG ALA ILE VAL SER ARG ARG CYS CYS GLU          
SEQRES  11 D  160  GLU VAL MET ALA ILE ALA PRO THR HIS TYR ILE TRP GLN          
SEQRES  12 D  160  ARG GLU ARG SER VAL HIS HIS SER GLY ALA VAL ARG ASN          
SEQRES  13 D  160  TYR ASN ARG ASP                                              
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  THR A  198  1                                  17    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  258  LEU A  267  1                                  10    
HELIX   12 AB3 SER A  276  LEU A  281  1                                   6    
HELIX   13 AB4 MET B   71  LYS B   76  1                                   6    
HELIX   14 AB5 LEU B   77  ASP B   79  5                                   3    
HELIX   15 AB6 ASP B   80  ASP B   90  1                                  11    
HELIX   16 AB7 ASP B   97  ALA B  111  1                                  15    
HELIX   17 AB8 THR B  114  HIS B  118  5                                   5    
HELIX   18 AB9 THR B  119  GLU B  135  1                                  17    
HELIX   19 AC1 GLU B  139  TYR B  142  5                                   4    
HELIX   20 AC2 GLU B  143  GLY B  150  1                                   8    
HELIX   21 AC3 ASN B  152  LYS B  155  5                                   4    
HELIX   22 AC4 LEU B  156  ILE B  171  1                                  16    
HELIX   23 AC5 SER B  178  MET B  186  1                                   9    
HELIX   24 AC6 HIS B  192  ARG B  197  5                                   6    
HELIX   25 AC7 PRO C   45  LYS C   56  1                                  12    
HELIX   26 AC8 LEU C   87  SER C   94  1                                   8    
HELIX   27 AC9 PRO C  100  HIS C  121  1                                  22    
HELIX   28 AD1 LYS C  129  GLN C  131  5                                   3    
HELIX   29 AD2 THR C  165  ARG C  169  5                                   5    
HELIX   30 AD3 ALA C  170  LEU C  175  1                                   6    
HELIX   31 AD4 THR C  182  THR C  198  1                                  17    
HELIX   32 AD5 SER C  207  GLY C  220  1                                  14    
HELIX   33 AD6 GLY C  229  MET C  233  5                                   5    
HELIX   34 AD7 ASP C  258  LEU C  267  1                                  10    
HELIX   35 AD8 SER C  276  ALA C  282  1                                   7    
HELIX   36 AD9 MET D   71  LYS D   76  1                                   6    
HELIX   37 AE1 LEU D   77  ASP D   79  5                                   3    
HELIX   38 AE2 ASP D   80  ASP D   90  1                                  11    
HELIX   39 AE3 ASP D   97  ALA D  111  1                                  15    
HELIX   40 AE4 THR D  114  HIS D  118  5                                   5    
HELIX   41 AE5 THR D  119  GLU D  135  1                                  17    
HELIX   42 AE6 GLU D  139  TYR D  142  5                                   4    
HELIX   43 AE7 GLU D  143  GLY D  150  1                                   8    
HELIX   44 AE8 ASN D  152  LYS D  155  5                                   4    
HELIX   45 AE9 LEU D  156  ILE D  171  1                                  16    
HELIX   46 AF1 SER D  178  MET D  186  1                                   9    
HELIX   47 AF2 HIS D  192  ARG D  197  5                                   6    
SHEET    1 AA1 5 GLU A   8  GLU A  12  0                                        
SHEET    2 AA1 5 GLY A  16  ALA A  21 -1  O  LYS A  20   N  GLU A   8           
SHEET    3 AA1 5 VAL A  30  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LEU A  76  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLU C  12  0                                        
SHEET    2 AA4 5 GLY C  16  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3 AA4 5 VAL C  29  ILE C  35 -1  O  LYS C  34   N  VAL C  17           
SHEET    4 AA4 5 LEU C  76  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  ASP C  68   O  VAL C  79           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
SSBOND   1 CYS B   91    CYS D   92                          1555   6655  2.05  
CRYST1   75.359   75.359  325.791  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013270  0.007661  0.000000        0.00000                         
SCALE2      0.000000  0.015323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003069        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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