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Database: PDB
Entry: 4EK2
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HEADER    TRANSFERASE                             09-APR-12   4EK2              
TITLE     THE STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE (NDK) FROM BURKHOLDERIA
TITLE    2 THAILANDENSIS BOUND TO DEOXYADENOSINE MONOPHOSPHATE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NDK, NDP KINASE, NUCLEOSIDE-2-P KINASE;                     
COMPND   5 EC: 2.7.4.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA THAILANDENSIS;                     
SOURCE   3 ORGANISM_TAXID: 271848;                                              
SOURCE   4 STRAIN: E264 / ATCC 700388 / DSM 13276 / CIP 106301;                 
SOURCE   5 GENE: NDK, BTH_I2231;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID,    
KEYWDS   2 DAMP, NIAID, NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES,  
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   2   30-OCT-13 4EK2    1       JRNL                                     
REVDAT   1   09-MAY-12 4EK2    0                                                
JRNL        AUTH   L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,             
JRNL        AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,  
JRNL        AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,  
JRNL        AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,    
JRNL        AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL, 
JRNL        AUTH 6 W.C.VAN VOORHIS                                              
JRNL        TITL   COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE   
JRNL        TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.                            
JRNL        REF    PLOS ONE                      V.   8 53851 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23382856                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0053851                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25383                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1295                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1504                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2162                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 275                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : 0.49000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.165         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.791         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2285 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1546 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3099 ; 1.332 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3756 ; 0.923 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   294 ; 5.729 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;32.722 ;23.611       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   375 ;14.022 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.641 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   346 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2584 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   484 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1431 ; 0.615 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   571 ; 0.159 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2293 ; 1.103 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   854 ; 1.885 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   799 ; 3.149 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A    45                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2148  24.2287  -5.2175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0318 T22:   0.0415                                     
REMARK   3      T33:   0.0299 T12:  -0.0012                                     
REMARK   3      T13:   0.0100 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6470 L22:   0.6818                                     
REMARK   3      L33:   0.6444 L12:   0.1689                                     
REMARK   3      L13:   0.0786 L23:  -0.2678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0367 S12:   0.1394 S13:  -0.1117                       
REMARK   3      S21:  -0.0646 S22:   0.0398 S23:   0.0290                       
REMARK   3      S31:   0.0174 S32:  -0.0495 S33:  -0.0031                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    46        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5639   7.2396  -1.3805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1676 T22:   0.0307                                     
REMARK   3      T33:   0.2802 T12:   0.0011                                     
REMARK   3      T13:   0.0648 T23:  -0.0803                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6279 L22:   3.2572                                     
REMARK   3      L33:   2.9684 L12:   0.5362                                     
REMARK   3      L13:   1.2334 L23:  -0.4976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0192 S12:   0.4131 S13:  -0.8634                       
REMARK   3      S21:  -0.4572 S22:  -0.0452 S23:  -0.2445                       
REMARK   3      S31:   0.4023 S32:   0.1392 S33:   0.0644                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    71        A    94                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3990  21.2666 -11.1139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0679 T22:   0.0696                                     
REMARK   3      T33:   0.0375 T12:  -0.0041                                     
REMARK   3      T13:   0.0091 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5571 L22:   1.0086                                     
REMARK   3      L33:   1.9352 L12:   0.0698                                     
REMARK   3      L13:   0.8701 L23:   0.0098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0332 S12:   0.3190 S13:  -0.2364                       
REMARK   3      S21:  -0.1861 S22:   0.0323 S23:  -0.0039                       
REMARK   3      S31:   0.1496 S32:  -0.0950 S33:  -0.0654                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    95        A   141                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4796  18.6421  -7.4939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0342 T22:   0.0623                                     
REMARK   3      T33:   0.0393 T12:   0.0028                                     
REMARK   3      T13:   0.0002 T23:  -0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8692 L22:   1.0748                                     
REMARK   3      L33:   0.9838 L12:   0.4498                                     
REMARK   3      L13:  -0.1262 L23:   0.1222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0430 S12:   0.2931 S13:  -0.2610                       
REMARK   3      S21:  -0.0351 S22:   0.0712 S23:  -0.1083                       
REMARK   3      S31:   0.0928 S32:  -0.0434 S33:  -0.0282                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    48                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4563  36.4748   3.3840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0400 T22:   0.0212                                     
REMARK   3      T33:   0.0358 T12:   0.0053                                     
REMARK   3      T13:   0.0103 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0627 L22:   0.6971                                     
REMARK   3      L33:   0.9478 L12:   0.0199                                     
REMARK   3      L13:  -0.1697 L23:  -0.0082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0200 S12:  -0.0118 S13:   0.0411                       
REMARK   3      S21:   0.0395 S22:   0.0284 S23:   0.0359                       
REMARK   3      S31:  -0.0820 S32:  -0.0277 S33:  -0.0485                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    49        B    67                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9232  47.7022  12.6425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2449 T22:   0.0908                                     
REMARK   3      T33:   0.0393 T12:   0.0213                                     
REMARK   3      T13:   0.0949 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5888 L22:   7.5986                                     
REMARK   3      L33:   5.4398 L12:   0.4269                                     
REMARK   3      L13:   1.7394 L23:   1.8586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2047 S12:  -0.2293 S13:   0.1411                       
REMARK   3      S21:  -0.0817 S22:  -0.1107 S23:   0.2349                       
REMARK   3      S31:  -0.5989 S32:  -0.2252 S33:  -0.0940                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    68        B    93                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4724  41.0119   6.0962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0690 T22:   0.0298                                     
REMARK   3      T33:   0.0311 T12:   0.0013                                     
REMARK   3      T13:   0.0231 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0983 L22:   1.4745                                     
REMARK   3      L33:   0.3274 L12:  -0.5632                                     
REMARK   3      L13:   0.3145 L23:  -0.1361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0586 S12:  -0.1022 S13:   0.0724                       
REMARK   3      S21:   0.0805 S22:   0.0142 S23:  -0.1152                       
REMARK   3      S31:  -0.1102 S32:   0.0036 S33:  -0.0728                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    94        B   141                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8641  40.8520   7.1162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0334 T22:   0.0195                                     
REMARK   3      T33:   0.0536 T12:  -0.0051                                     
REMARK   3      T13:   0.0275 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7919 L22:   1.4335                                     
REMARK   3      L33:   1.3596 L12:  -0.0441                                     
REMARK   3      L13:  -0.2357 L23:  -0.2720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0829 S12:  -0.0229 S13:   0.1214                       
REMARK   3      S21:   0.0626 S22:  -0.0161 S23:   0.0443                       
REMARK   3      S31:  -0.1788 S32:  -0.0079 S33:  -0.0668                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  U VALUES      : WITH TLS ADDED                                      
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   4                                                                      
REMARK   4 4EK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071716.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25415                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.553                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.2100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.950                              
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: PDB ENTRY 4DUT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BUTHA.00438.A.A1 PS01186 AT 42.64 MG/    
REMARK 280  ML IN 1.5 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, PH 7.0, 10    
REMARK 280  MM DAMP, CRYOPROTECTANT: 15% ETHYLENE GLYCOL, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.21500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       22.60750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       67.82250            
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        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.21500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       67.82250            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       22.60750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 389  LIES ON A SPECIAL POSITION.                          
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    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
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     SER A   0    OG                                                  
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LEU A  84    CG   CD1  CD2                                       
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     LYS B  96    CG   CD   CE   NZ                                   
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 115      -42.12     74.30                                   
REMARK 500    ALA B 115      -44.06     76.02                                   
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 CL A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DUT   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN BOUND TO DEOXYADENOSINE MONOPHOSPHATE                   
REMARK 900 RELATED ID: SSGCID-BUTHA.00438.A   RELATED DB: TARGETTRACK           
DBREF  4EK2 A    1   141  UNP    Q2SWE7   NDK_BURTA        1    141             
DBREF  4EK2 B    1   141  UNP    Q2SWE7   NDK_BURTA        1    141             
SEQADV 4EK2 GLY A   -3  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 PRO A   -2  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 GLY A   -1  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 SER A    0  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 GLY B   -3  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 PRO B   -2  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 GLY B   -1  UNP  Q2SWE7              EXPRESSION TAG                 
SEQADV 4EK2 SER B    0  UNP  Q2SWE7              EXPRESSION TAG                 
SEQRES   1 A  145  GLY PRO GLY SER MET ALA LEU GLU ARG THR LEU SER ILE          
SEQRES   2 A  145  ILE LYS PRO ASP ALA VAL ALA LYS ASN VAL ILE GLY GLN          
SEQRES   3 A  145  ILE TYR SER ARG PHE GLU ASN ALA GLY LEU LYS ILE VAL          
SEQRES   4 A  145  ALA ALA ARG MET ALA HIS LEU SER ARG ALA ASP ALA GLU          
SEQRES   5 A  145  LYS PHE TYR ALA VAL HIS ALA GLU ARG PRO PHE PHE LYS          
SEQRES   6 A  145  ASP LEU VAL GLU PHE MET ILE SER GLY PRO VAL MET ILE          
SEQRES   7 A  145  GLN VAL LEU GLU GLY GLU ASP ALA ILE LEU LYS ASN ARG          
SEQRES   8 A  145  ASP LEU MET GLY ALA THR ASP PRO LYS LYS ALA GLU LYS          
SEQRES   9 A  145  GLY THR ILE ARG ALA ASP PHE ALA ASP SER ILE ASP ALA          
SEQRES  10 A  145  ASN ALA VAL HIS GLY SER ASP ALA PRO GLU THR ALA ARG          
SEQRES  11 A  145  VAL GLU ILE ALA PHE PHE PHE PRO GLU MET ASN VAL TYR          
SEQRES  12 A  145  SER ARG                                                      
SEQRES   1 B  145  GLY PRO GLY SER MET ALA LEU GLU ARG THR LEU SER ILE          
SEQRES   2 B  145  ILE LYS PRO ASP ALA VAL ALA LYS ASN VAL ILE GLY GLN          
SEQRES   3 B  145  ILE TYR SER ARG PHE GLU ASN ALA GLY LEU LYS ILE VAL          
SEQRES   4 B  145  ALA ALA ARG MET ALA HIS LEU SER ARG ALA ASP ALA GLU          
SEQRES   5 B  145  LYS PHE TYR ALA VAL HIS ALA GLU ARG PRO PHE PHE LYS          
SEQRES   6 B  145  ASP LEU VAL GLU PHE MET ILE SER GLY PRO VAL MET ILE          
SEQRES   7 B  145  GLN VAL LEU GLU GLY GLU ASP ALA ILE LEU LYS ASN ARG          
SEQRES   8 B  145  ASP LEU MET GLY ALA THR ASP PRO LYS LYS ALA GLU LYS          
SEQRES   9 B  145  GLY THR ILE ARG ALA ASP PHE ALA ASP SER ILE ASP ALA          
SEQRES  10 B  145  ASN ALA VAL HIS GLY SER ASP ALA PRO GLU THR ALA ARG          
SEQRES  11 B  145  VAL GLU ILE ALA PHE PHE PHE PRO GLU MET ASN VAL TYR          
SEQRES  12 B  145  SER ARG                                                      
HET     CL  A 201       1                                                       
HET    DMS  A 202       4                                                       
HET     DA  A 203      22                                                       
HET     CL  B 201       1                                                       
HET    EDO  B 202       4                                                       
HET    DMS  B 203       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      DA 2'-DEOXYADENOSINE-5'-MONOPHOSPHATE                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  DMS    2(C2 H6 O S)                                                 
FORMUL   5   DA    C10 H14 N5 O6 P                                              
FORMUL   7  EDO    C2 H6 O2                                                     
FORMUL   9  HOH   *275(H2 O)                                                    
HELIX    1   1 LYS A   11  LYS A   17  1                                   7    
HELIX    2   2 VAL A   19  ALA A   30  1                                  12    
HELIX    3   3 SER A   43  TYR A   51  1                                   9    
HELIX    4   4 ALA A   52  ALA A   55  5                                   4    
HELIX    5   5 PHE A   59  ILE A   68  1                                  10    
HELIX    6   6 ASP A   81  GLY A   91  1                                  11    
HELIX    7   7 THR A  102  ALA A  108  1                                   7    
HELIX    8   8 ALA A  121  PHE A  133  1                                  13    
HELIX    9   9 PRO A  134  VAL A  138  5                                   5    
HELIX   10  10 LYS B   11  LYS B   17  1                                   7    
HELIX   11  11 VAL B   19  ALA B   30  1                                  12    
HELIX   12  12 SER B   43  TYR B   51  1                                   9    
HELIX   13  13 ALA B   52  ALA B   55  5                                   4    
HELIX   14  14 PHE B   59  ILE B   68  1                                  10    
HELIX   15  15 ASP B   81  GLY B   91  1                                  11    
HELIX   16  16 THR B  102  ALA B  108  1                                   7    
HELIX   17  17 ALA B  121  PHE B  133  1                                  13    
HELIX   18  18 PRO B  134  VAL B  138  5                                   5    
SHEET    1   A 4 LYS A  33  ALA A  40  0                                        
SHEET    2   A 4 VAL A  72  GLU A  80 -1  O  VAL A  72   N  ALA A  40           
SHEET    3   A 4 LEU A   3  ILE A  10 -1  N  ILE A  10   O  MET A  73           
SHEET    4   A 4 VAL A 116  GLY A 118 -1  O  HIS A 117   N  ILE A   9           
SHEET    1   B 4 LYS B  33  ALA B  40  0                                        
SHEET    2   B 4 VAL B  72  GLU B  78 -1  O  ILE B  74   N  ARG B  38           
SHEET    3   B 4 ARG B   5  ILE B  10 -1  N  ILE B  10   O  MET B  73           
SHEET    4   B 4 VAL B 116  GLY B 118 -1  O  HIS B 117   N  ILE B   9           
SITE     1 AC1  3 LYS A  11  TYR A  51  HIS A 117                               
SITE     1 AC2  8 GLU A   4  ARG A   5  PRO A 122  ALA A 125                    
SITE     2 AC2  8 ARG A 126  ILE A 129   DA A 203  HOH A 430                    
SITE     1 AC3 11 ALA A   2  LEU A   3  DMS A 202  HOH A 349                    
SITE     2 AC3 11 HOH A 429  HOH A 430  PHE B  59  LEU B  63                    
SITE     3 AC3 11 THR B  93  ASP B 112  HOH B 399                               
SITE     1 AC4  3 LYS B  11  TYR B  51  HIS B 117                               
SITE     1 AC5  5 PHE B  50  TYR B  51  VAL B  53  HIS B  54                    
SITE     2 AC5  5 GLU B 128                                                     
SITE     1 AC6  4 GLU B   4  ARG B   5  PRO B 122  ARG B 126                    
CRYST1   90.680   90.680   90.430  90.00  90.00  90.00 P 41 2 2     16          
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      0.011028  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011028  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011058        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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