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Database: PDB
Entry: 2C49
LinkDB: 2C49
Original site: 2C49 
HEADER    TRANSFERASE                             17-OCT-05   2C49              
TITLE     CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE KINASE -
TITLE    2 AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUGAR KINASE MJ0406;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NUCLEOSIDE KINASE;                                          
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOCOCCUS JANNASCHII;                       
SOURCE   3 ORGANISM_TAXID: 2190;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET17B;                                   
SOURCE   8 OTHER_DETAILS: METHANOCALDOCOCCUS JANNASCHII                         
KEYWDS    TRANSFERASE, NUCLEOSIDE KINASE, HYPERTHERMOPHILE, RIBOKINASE FAMILY,  
KEYWDS   2 RIBOKINASE FOLD                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.ARNFORS,T.HANSEN,W.MEINING,P.SCHOENHEIT,R.LADENSTEIN                
REVDAT   4   24-JUL-19 2C49    1       REMARK                                   
REVDAT   3   13-JUL-11 2C49    1       VERSN                                    
REVDAT   2   24-FEB-09 2C49    1       VERSN                                    
REVDAT   1   30-AUG-06 2C49    0                                                
JRNL        AUTH   L.ARNFORS,T.HANSEN,P.SCHOENHEIT,R.LADENSTEIN,W.MEINING       
JRNL        TITL   STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE        
JRNL        TITL 2 KINASE: AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY.         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62  1085 2006              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   16929110                                                     
JRNL        DOI    10.1107/S0907444906024826                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 55509                          
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) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2955                            
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) : 1.92                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3739                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 193                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4731                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 162                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39000                                              
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.64000                                             
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): 0.181         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.167         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.803         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4982 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6777 ; 1.700 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   596 ; 7.538 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   727 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3749 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2331 ; 0.211 ; 0.200       
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):   219 ; 0.159 ; 0.200       
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):    35 ; 0.196 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.128 ; 0.200       
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):  2971 ; 0.758 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4782 ; 1.264 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2011 ; 2.072 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1988 ; 2.989 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      6       A      15      4                      
REMARK   3           1     B      6       B      15      4                      
REMARK   3           2     A     42       A      97      4                      
REMARK   3           2     B     42       B      97      4                      
REMARK   3           3     A    115       A     297      4                      
REMARK   3           3     B    115       B     297      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1924 ;  0.44 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1924 ;  1.15 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    15                          
REMARK   3    RESIDUE RANGE :   A    41        A    98                          
REMARK   3    RESIDUE RANGE :   A   114        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3506  22.8581  60.6100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0194 T22:   0.0105                                     
REMARK   3      T33:   0.0655 T12:   0.0081                                     
REMARK   3      T13:  -0.0077 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4540 L22:   1.8679                                     
REMARK   3      L33:   2.9687 L12:  -0.6070                                     
REMARK   3      L13:   0.4665 L23:   0.2769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:   0.1163 S13:   0.0207                       
REMARK   3      S21:  -0.0744 S22:  -0.0954 S23:   0.0044                       
REMARK   3      S31:  -0.0685 S32:   0.1282 S33:   0.0722                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A    40                          
REMARK   3    RESIDUE RANGE :   A    99        A   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3457  30.0739  39.1974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2009 T22:   0.1518                                     
REMARK   3      T33:   0.1783 T12:  -0.0200                                     
REMARK   3      T13:  -0.0427 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3299 L22:   3.3372                                     
REMARK   3      L33:   5.4807 L12:  -0.0792                                     
REMARK   3      L13:  -0.2342 L23:  -1.2037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0367 S12:   0.2361 S13:   0.3473                       
REMARK   3      S21:  -0.0043 S22:  -0.0586 S23:  -0.3196                       
REMARK   3      S31:  -0.5942 S32:   0.4290 S33:   0.0952                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B    15                          
REMARK   3    RESIDUE RANGE :   B    41        B    98                          
REMARK   3    RESIDUE RANGE :   B   114        B   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8280  23.9438  12.0094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0913 T22:   0.0335                                     
REMARK   3      T33:   0.0978 T12:   0.0067                                     
REMARK   3      T13:  -0.0052 T23:  -0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7338 L22:   1.8826                                     
REMARK   3      L33:   2.1245 L12:  -0.1658                                     
REMARK   3      L13:   0.3188 L23:  -0.8849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:  -0.1607 S13:   0.1099                       
REMARK   3      S21:  -0.0860 S22:   0.0569 S23:   0.1399                       
REMARK   3      S31:  -0.0371 S32:  -0.0957 S33:  -0.0529                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    16        B    40                          
REMARK   3    RESIDUE RANGE :   B    99        B   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.5180  30.8366  38.0425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2495 T22:   0.1168                                     
REMARK   3      T33:   0.1516 T12:   0.0793                                     
REMARK   3      T13:  -0.0234 T23:   0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6212 L22:   1.5116                                     
REMARK   3      L33:   6.1729 L12:   0.6396                                     
REMARK   3      L13:   0.6430 L23:   1.5639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0963 S12:   0.1594 S13:   0.3241                       
REMARK   3      S21:   0.0615 S22:  -0.0025 S23:   0.1671                       
REMARK   3      S31:  -0.5116 S32:  -0.4866 S33:   0.0988                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2C49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290026013.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8098                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 13.70                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.10 M MGCL2, 0.1 M TRIS    
REMARK 280  -HCL PH 8.5                                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.00300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.39200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.56550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.39200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.00300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.56550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ILE A   302                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B   301                                                      
REMARK 465     ILE B   302                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 202   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B  68   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B 140   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   4      -11.89   -148.75                                   
REMARK 500    ASN A  29       49.07     71.86                                   
REMARK 500    ASP A  68       58.44    -90.80                                   
REMARK 500    PHE A  69      -60.84   -142.66                                   
REMARK 500    ASN A 107       29.69     45.60                                   
REMARK 500    THR A 138     -169.98     60.63                                   
REMARK 500    ASN A 154      -70.63   -124.98                                   
REMARK 500    LYS A 238      102.66     54.78                                   
REMARK 500    LYS B   4      -31.12   -141.14                                   
REMARK 500    GLU B   6       79.76    -60.11                                   
REMARK 500    SER B  72     -150.49    -84.85                                   
REMARK 500    ALA B 137     -164.12   -112.06                                   
REMARK 500    ASN B 154      -64.81   -128.31                                   
REMARK 500    LYS B 238      124.78   -177.48                                   
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 PHE B   69     LYS B   70                  -97.70                    
REMARK 500 LYS B   70     ASN B   71                  147.32                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2046   O                                                      
REMARK 620 2 HOH A2056   O    90.5                                              
REMARK 620 3 HOH A2057   O    90.7  87.4                                        
REMARK 620 4 HOH A2066   O    88.8  88.3 175.7                                  
REMARK 620 5 HOH A2077   O    90.9 177.8  94.2  90.1                            
REMARK 620 6 HOH A2079   O   177.9  91.3  90.6  90.0  87.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2054   O                                                      
REMARK 620 2 HOH A2018   O    91.9                                              
REMARK 620 3 HOH A2019   O   177.6  89.4                                        
REMARK 620 4 HOH A2042   O    91.5  89.2  86.5                                  
REMARK 620 5 HOH A2021   O    85.1  91.4  96.8 176.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2014   O                                                      
REMARK 620 2 HOH B2082   O    90.7                                              
REMARK 620 3 HOH B2041   O    89.7 179.2                                        
REMARK 620 4 HOH B2081   O   179.8  89.5  90.1                                  
REMARK 620 5 HOH B2053   O    90.5  88.0  91.3  89.5                            
REMARK 620 6 HOH B2040   O    90.0  90.5  90.2  90.0 178.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2036   O                                                      
REMARK 620 2 HOH B2048   O    91.8                                              
REMARK 620 3 HOH B2059   O    88.5  92.1                                        
REMARK 620 4 HOH B2058   O   178.2  86.4  91.5                                  
REMARK 620 5 HOH B2078   O    91.0 177.0  87.2  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B1304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C4E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE        
REMARK 900 KINASE - AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY                 
DBREF  2C49 A    1   302  UNP    Q57849   Y406_METJA       1    302             
DBREF  2C49 B    1   302  UNP    Q57849   Y406_METJA       1    302             
SEQRES   1 A  302  MET GLY GLY LYS MET GLU LYS ILE THR CYS VAL GLY HIS          
SEQRES   2 A  302  THR ALA LEU ASP TYR ILE PHE ASN VAL GLU LYS PHE PRO          
SEQRES   3 A  302  GLU PRO ASN THR SER ILE GLN ILE PRO SER ALA ARG LYS          
SEQRES   4 A  302  TYR TYR GLY GLY ALA ALA ALA ASN THR ALA VAL GLY ILE          
SEQRES   5 A  302  LYS LYS LEU GLY VAL ASN SER GLU LEU LEU SER CYS VAL          
SEQRES   6 A  302  GLY TYR ASP PHE LYS ASN SER GLY TYR GLU ARG TYR LEU          
SEQRES   7 A  302  LYS ASN LEU ASP ILE ASN ILE SER LYS LEU TYR TYR SER          
SEQRES   8 A  302  GLU GLU GLU GLU THR PRO LYS ALA TRP ILE PHE THR ASP          
SEQRES   9 A  302  LYS ASP ASN ASN GLN ILE THR PHE PHE LEU TRP GLY ALA          
SEQRES  10 A  302  ALA LYS HIS TYR LYS GLU LEU ASN PRO PRO ASN PHE ASN          
SEQRES  11 A  302  THR GLU ILE VAL HIS ILE ALA THR GLY ASP PRO GLU PHE          
SEQRES  12 A  302  ASN LEU LYS CYS ALA LYS LYS ALA TYR GLY ASN ASN LEU          
SEQRES  13 A  302  VAL SER PHE ASP PRO GLY GLN ASP LEU PRO GLN TYR SER          
SEQRES  14 A  302  LYS GLU MET LEU LEU GLU ILE ILE GLU HIS THR ASN PHE          
SEQRES  15 A  302  LEU PHE MET ASN LYS HIS GLU PHE GLU ARG ALA SER ASN          
SEQRES  16 A  302  LEU LEU ASN PHE GLU ILE ASP ASP TYR LEU GLU ARG VAL          
SEQRES  17 A  302  ASP ALA LEU ILE VAL THR LYS GLY SER LYS GLY SER VAL          
SEQRES  18 A  302  ILE TYR THR LYS ASP LYS LYS ILE GLU ILE PRO CYS ILE          
SEQRES  19 A  302  LYS ALA GLY LYS VAL ILE ASP PRO THR GLY ALA GLY ASP          
SEQRES  20 A  302  SER TYR ARG ALA GLY PHE LEU SER ALA TYR VAL LYS GLY          
SEQRES  21 A  302  TYR ASP LEU GLU LYS CYS GLY LEU ILE GLY ALA ALA THR          
SEQRES  22 A  302  ALA SER PHE VAL VAL GLU ALA LYS GLY CYS GLN THR ASN          
SEQRES  23 A  302  LEU PRO THR TRP ASP LYS VAL VAL GLU ARG LEU GLU LYS          
SEQRES  24 A  302  HIS ARG ILE                                                  
SEQRES   1 B  302  MET GLY GLY LYS MET GLU LYS ILE THR CYS VAL GLY HIS          
SEQRES   2 B  302  THR ALA LEU ASP TYR ILE PHE ASN VAL GLU LYS PHE PRO          
SEQRES   3 B  302  GLU PRO ASN THR SER ILE GLN ILE PRO SER ALA ARG LYS          
SEQRES   4 B  302  TYR TYR GLY GLY ALA ALA ALA ASN THR ALA VAL GLY ILE          
SEQRES   5 B  302  LYS LYS LEU GLY VAL ASN SER GLU LEU LEU SER CYS VAL          
SEQRES   6 B  302  GLY TYR ASP PHE LYS ASN SER GLY TYR GLU ARG TYR LEU          
SEQRES   7 B  302  LYS ASN LEU ASP ILE ASN ILE SER LYS LEU TYR TYR SER          
SEQRES   8 B  302  GLU GLU GLU GLU THR PRO LYS ALA TRP ILE PHE THR ASP          
SEQRES   9 B  302  LYS ASP ASN ASN GLN ILE THR PHE PHE LEU TRP GLY ALA          
SEQRES  10 B  302  ALA LYS HIS TYR LYS GLU LEU ASN PRO PRO ASN PHE ASN          
SEQRES  11 B  302  THR GLU ILE VAL HIS ILE ALA THR GLY ASP PRO GLU PHE          
SEQRES  12 B  302  ASN LEU LYS CYS ALA LYS LYS ALA TYR GLY ASN ASN LEU          
SEQRES  13 B  302  VAL SER PHE ASP PRO GLY GLN ASP LEU PRO GLN TYR SER          
SEQRES  14 B  302  LYS GLU MET LEU LEU GLU ILE ILE GLU HIS THR ASN PHE          
SEQRES  15 B  302  LEU PHE MET ASN LYS HIS GLU PHE GLU ARG ALA SER ASN          
SEQRES  16 B  302  LEU LEU ASN PHE GLU ILE ASP ASP TYR LEU GLU ARG VAL          
SEQRES  17 B  302  ASP ALA LEU ILE VAL THR LYS GLY SER LYS GLY SER VAL          
SEQRES  18 B  302  ILE TYR THR LYS ASP LYS LYS ILE GLU ILE PRO CYS ILE          
SEQRES  19 B  302  LYS ALA GLY LYS VAL ILE ASP PRO THR GLY ALA GLY ASP          
SEQRES  20 B  302  SER TYR ARG ALA GLY PHE LEU SER ALA TYR VAL LYS GLY          
SEQRES  21 B  302  TYR ASP LEU GLU LYS CYS GLY LEU ILE GLY ALA ALA THR          
SEQRES  22 B  302  ALA SER PHE VAL VAL GLU ALA LYS GLY CYS GLN THR ASN          
SEQRES  23 B  302  LEU PRO THR TRP ASP LYS VAL VAL GLU ARG LEU GLU LYS          
SEQRES  24 B  302  HIS ARG ILE                                                  
HET    ADN  A1301      19                                                       
HET     MG  A1302       1                                                       
HET     MG  A1303       1                                                       
HET    ANP  A1304      31                                                       
HET    ADN  B1301      19                                                       
HET     MG  B1302       1                                                       
HET     MG  B1303       1                                                       
HET    ANP  B1304      31                                                       
HETNAM     ADN ADENOSINE                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   3  ADN    2(C10 H13 N5 O4)                                             
FORMUL   4   MG    4(MG 2+)                                                     
FORMUL   6  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL  11  HOH   *162(H2 O)                                                    
HELIX    1   1 GLY A   43  LEU A   55  1                                  13    
HELIX    2   2 SER A   72  LEU A   81  1                                  10    
HELIX    3   3 GLY A  116  LEU A  124  5                                   9    
HELIX    4   4 ASP A  140  TYR A  152  1                                  13    
HELIX    5   5 PRO A  161  TYR A  168  5                                   8    
HELIX    6   6 SER A  169  GLU A  178  1                                  10    
HELIX    7   7 ASN A  186  ASN A  198  1                                  13    
HELIX    8   8 GLU A  200  GLU A  206  1                                   7    
HELIX    9   9 GLY A  216  LYS A  218  5                                   3    
HELIX   10  10 GLY A  244  LYS A  259  1                                  16    
HELIX   11  11 ASP A  262  VAL A  278  1                                  17    
HELIX   12  12 THR A  289  HIS A  300  1                                  12    
HELIX   13  13 GLY B   43  LEU B   55  1                                  13    
HELIX   14  14 SER B   72  LEU B   81  1                                  10    
HELIX   15  15 GLY B  116  LEU B  124  5                                   9    
HELIX   16  16 ASP B  140  TYR B  152  1                                  13    
HELIX   17  17 PRO B  161  TYR B  168  5                                   8    
HELIX   18  18 SER B  169  HIS B  179  1                                  11    
HELIX   19  19 LYS B  187  ASN B  198  1                                  12    
HELIX   20  20 GLU B  200  GLU B  206  1                                   7    
HELIX   21  21 GLY B  216  LYS B  218  5                                   3    
HELIX   22  22 GLY B  244  LYS B  259  1                                  16    
HELIX   23  23 ASP B  262  VAL B  278  1                                  17    
HELIX   24  24 THR B  289  HIS B  300  1                                  12    
SHEET    1  AA 8 ASN A  58  LEU A  62  0                                        
SHEET    2  AA 8 MET A   5  VAL A  11  1  O  GLU A   6   N  ASN A  58           
SHEET    3  AA 8 THR A 131  ALA A 137  1  N  GLU A 132   O  MET A   5           
SHEET    4  AA 8 LEU A 156  ASP A 160  1  O  LEU A 156   N  VAL A 134           
SHEET    5  AA 8 PHE A 182  MET A 185  1  O  PHE A 182   N  PHE A 159           
SHEET    6  AA 8 ALA A 210  THR A 214  1  O  ALA A 210   N  LEU A 183           
SHEET    7  AA 8 SER A 220  TYR A 223 -1  O  VAL A 221   N  VAL A 213           
SHEET    8  AA 8 LYS A 228  ILE A 231 -1  O  ILE A 229   N  ILE A 222           
SHEET    1  AB 5 LYS A  39  GLY A  42  0                                        
SHEET    2  AB 5 ALA A  15  ASN A  21 -1  O  ALA A  15   N  GLY A  42           
SHEET    3  AB 5 LYS A  98  THR A 103  1  O  ALA A  99   N  TYR A  18           
SHEET    4  AB 5 GLN A 109  LEU A 114 -1  O  ILE A 110   N  PHE A 102           
SHEET    5  AB 5 SER B  31  ILE B  34  1  O  ILE B  32   N  PHE A 113           
SHEET    1  AC 5 THR A  30  ILE A  34  0                                        
SHEET    2  AC 5 GLN B 109  LEU B 114  1  O  THR B 111   N  ILE A  32           
SHEET    3  AC 5 LYS B  98  THR B 103 -1  O  LYS B  98   N  LEU B 114           
SHEET    4  AC 5 ALA B  15  ASN B  21  1  O  LEU B  16   N  ALA B  99           
SHEET    5  AC 5 ARG B  38  GLY B  42 -1  O  ARG B  38   N  ILE B  19           
SHEET    1  AD 2 CYS A  64  VAL A  65  0                                        
SHEET    2  AD 2 TYR A  89  TYR A  90  1  O  TYR A  89   N  VAL A  65           
SHEET    1  BA 8 ASN B  58  LEU B  62  0                                        
SHEET    2  BA 8 MET B   5  VAL B  11  1  O  GLU B   6   N  ASN B  58           
SHEET    3  BA 8 THR B 131  ILE B 136  1  N  GLU B 132   O  LYS B   7           
SHEET    4  BA 8 LEU B 156  PHE B 159  1  O  LEU B 156   N  VAL B 134           
SHEET    5  BA 8 PHE B 182  ASN B 186  1  O  PHE B 182   N  PHE B 159           
SHEET    6  BA 8 ALA B 210  THR B 214  1  O  ALA B 210   N  LEU B 183           
SHEET    7  BA 8 SER B 220  TYR B 223 -1  O  VAL B 221   N  VAL B 213           
SHEET    8  BA 8 LYS B 228  ILE B 231 -1  O  ILE B 229   N  ILE B 222           
SHEET    1  BB 2 CYS B  64  VAL B  65  0                                        
SHEET    2  BB 2 TYR B  89  TYR B  90  1  O  TYR B  89   N  VAL B  65           
LINK        MG    MG A1302                 O   HOH A2046     1555   1555  2.16  
LINK        MG    MG A1302                 O   HOH A2056     1555   1555  2.15  
LINK        MG    MG A1302                 O   HOH A2057     1555   1555  2.17  
LINK        MG    MG A1302                 O   HOH A2066     1555   1555  2.18  
LINK        MG    MG A1302                 O   HOH A2077     1555   1555  2.18  
LINK        MG    MG A1302                 O   HOH A2079     1555   1555  2.15  
LINK        MG    MG A1303                 O   HOH A2054     1555   1555  2.16  
LINK        MG    MG A1303                 O   HOH A2018     1555   1555  2.19  
LINK        MG    MG A1303                 O   HOH A2019     1555   1555  2.18  
LINK        MG    MG A1303                 O   HOH A2042     1555   1555  2.16  
LINK        MG    MG A1303                 O   HOH A2021     1555   1555  2.18  
LINK        MG    MG B1302                 O   HOH B2014     1555   1555  2.18  
LINK        MG    MG B1302                 O   HOH B2082     1555   1555  2.17  
LINK        MG    MG B1302                 O   HOH B2041     1555   1555  2.17  
LINK        MG    MG B1302                 O   HOH B2081     1555   1555  2.17  
LINK        MG    MG B1302                 O   HOH B2053     1555   1555  2.18  
LINK        MG    MG B1302                 O   HOH B2040     1555   1555  2.18  
LINK        MG    MG B1303                 O   HOH B2036     1555   1555  2.19  
LINK        MG    MG B1303                 O   HOH B2048     1555   1555  2.17  
LINK        MG    MG B1303                 O   HOH B2059     1555   1555  2.17  
LINK        MG    MG B1303                 O   HOH B2058     1555   1555  2.17  
LINK        MG    MG B1303                 O   HOH B2078     1555   4555  2.19  
SITE     1 AC1  6 HOH A2046  HOH A2056  HOH A2057  HOH A2066                    
SITE     2 AC1  6 HOH A2077  HOH A2079                                          
SITE     1 AC2  5 HOH A2018  HOH A2019  HOH A2021  HOH A2042                    
SITE     2 AC2  5 HOH A2054                                                     
SITE     1 AC3  6 HOH B2014  HOH B2040  HOH B2041  HOH B2053                    
SITE     2 AC3  6 HOH B2081  HOH B2082                                          
SITE     1 AC4  5 HOH B2036  HOH B2048  HOH B2058  HOH B2059                    
SITE     2 AC4  5 HOH B2078                                                     
SITE     1 AC5 16 HIS A  13  ALA A  15  ASP A  17  GLY A  42                    
SITE     2 AC5 16 GLY A  43  ASN A  47  THR A 111  PHE A 113                    
SITE     3 AC5 16 GLN A 163  ASP A 164  ASP A 247  CYS A 283                    
SITE     4 AC5 16 HOH A2077  HOH A2078  SER B  31  GLN B  33                    
SITE     1 AC6 16 GLN A 109  ASN A 186  THR A 214  GLY A 216                    
SITE     2 AC6 16 GLY A 219  CYS A 233  ILE A 234  VAL A 239                    
SITE     3 AC6 16 THR A 243  ALA A 245  GLY A 246  ALA A 274                    
SITE     4 AC6 16 HOH A2062  HOH A2072  HOH A2079  HOH A2080                    
SITE     1 AC7  7 HIS B  13  ALA B  15  ASP B  17  GLY B  42                    
SITE     2 AC7  7 GLY B  43  ALA B  44  HOH B2080                               
SITE     1 AC8 19 ASN B 186  THR B 214  LYS B 215  GLY B 216                    
SITE     2 AC8 19 GLY B 219  CYS B 233  ILE B 234  VAL B 239                    
SITE     3 AC8 19 PRO B 242  THR B 243  GLY B 244  ALA B 245                    
SITE     4 AC8 19 GLY B 246  TYR B 249  ARG B 250  ALA B 274                    
SITE     5 AC8 19 HOH B2060  HOH B2081  HOH B2082                               
CRYST1   64.006   83.131  146.784  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015624  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012029  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006813        0.00000                         
MTRIX1   1 -0.996080  0.032971  0.082070      130.16000    1                    
MTRIX2   1  0.023822  0.993640 -0.110060       -1.78790    1                    
MTRIX3   1 -0.085177 -0.107670 -0.990530       70.50800    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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