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Database: PDB
Entry: 5DJH
LinkDB: 5DJH
Original site: 5DJH 
HEADER    HYDROLASE                               02-SEP-15   5DJH              
TITLE     STRUCTURE OF M. TUBERCULOSIS CYSQ, A PAP PHOSPHATASE WITH AMP, PO4,   
TITLE    2 AND 3MG BOUND                                                        
CAVEAT     5DJH    RESIDUES A SER 117 AND A PRO 122 ARE LINKED (INTERVENING     
CAVEAT   2 5DJH    RESIDUES SNGQ ARE OMITTED).                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3'-PHOSPHOADENOSINE 5'-PHOSPHATE PHOSPHATASE;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYSQ, PAP PHOSPHATASE, 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE, 
COMPND   5 5-BISPHOSPHONUCLEOSIDE 3'(2')-PHOSPHOHYDROLASE, D-FRUCTOSE-1,6-      
COMPND   6 BISPHOSPHATE 1-PHOSPHOHYDROLASE, DPNPASE, FRUCTOSE-1,6-              
COMPND   7 BISPHOSPHATASE, FBPASE, INOSITOL-1-MONOPHOSPHATASE,IMPASE, INOSITOL- 
COMPND   8 1-PHOSPHATASE;                                                       
COMPND   9 EC: 3.1.3.7, 3.1.3.11, 3.1.3.25;                                     
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: CYSQ, MT2189;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    CYSQ, PAP PHOSPHATASE, AMP, MAGNESIUM, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.FISHER,A.I.ERICKSON                                               
REVDAT   4   27-SEP-23 5DJH    1       LINK                                     
REVDAT   3   22-NOV-17 5DJH    1       JRNL   REMARK                            
REVDAT   2   02-DEC-15 5DJH    1       JRNL                                     
REVDAT   1   11-NOV-15 5DJH    0                                                
JRNL        AUTH   A.I.ERICKSON,R.D.SARSAM,A.J.FISHER                           
JRNL        TITL   CRYSTAL STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS CYSQ, WITH  
JRNL        TITL 2 SUBSTRATE AND PRODUCTS BOUND.                                
JRNL        REF    BIOCHEMISTRY                  V.  54  6830 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26512869                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.5B01000                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.090                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42861                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2111                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.1817 -  4.4050    0.95     2637   143  0.1466 0.1548        
REMARK   3     2  4.4050 -  3.4971    0.97     2700   134  0.1177 0.1467        
REMARK   3     3  3.4971 -  3.0553    0.96     2668   151  0.1388 0.1496        
REMARK   3     4  3.0553 -  2.7760    0.97     2655   170  0.1461 0.1640        
REMARK   3     5  2.7760 -  2.5771    0.97     2680   162  0.1515 0.1679        
REMARK   3     6  2.5771 -  2.4252    0.98     2684   154  0.1540 0.1800        
REMARK   3     7  2.4252 -  2.3037    0.97     2724   152  0.1430 0.1770        
REMARK   3     8  2.3037 -  2.2035    0.98     2702   144  0.1430 0.1422        
REMARK   3     9  2.2035 -  2.1186    0.98     2748   145  0.1402 0.1625        
REMARK   3    10  2.1186 -  2.0455    0.98     2739   121  0.1337 0.1639        
REMARK   3    11  2.0455 -  1.9816    0.98     2718   155  0.1460 0.1580        
REMARK   3    12  1.9816 -  1.9249    0.98     2706   139  0.1453 0.1478        
REMARK   3    13  1.9249 -  1.8743    0.98     2698   150  0.1475 0.1572        
REMARK   3    14  1.8743 -  1.8285    0.98     2798   129  0.1481 0.1549        
REMARK   3    15  1.8285 -  1.7870    0.98     2689   152  0.1490 0.1784        
REMARK   3    16  1.7870 -  1.7489    0.98     2721   140  0.1494 0.1826        
REMARK   3    17  1.7489 -  1.7140    0.98     2731   111  0.1541 0.1586        
REMARK   3    18  1.7140 -  1.6816    0.98     2766   122  0.1563 0.1863        
REMARK   3    19  1.6816 -  1.6516    0.97     2716   110  0.1550 0.1653        
REMARK   3    20  1.6516 -  1.6236    0.98     2672   151  0.1661 0.2385        
REMARK   3    21  1.6236 -  1.5974    0.98     2770   154  0.1614 0.1875        
REMARK   3    22  1.5974 -  1.5728    0.97     2676   134  0.1760 0.2216        
REMARK   3    23  1.5728 -  1.5497    0.97     2720   143  0.1781 0.2152        
REMARK   3    24  1.5497 -  1.5279    0.97     2704   132  0.1929 0.2247        
REMARK   3    25  1.5279 -  1.5072    0.97     2673   129  0.1885 0.2398        
REMARK   3    26  1.5072 -  1.4876    0.97     2751   133  0.2143 0.2408        
REMARK   3    27  1.4876 -  1.4690    0.97     2686   143  0.2244 0.2605        
REMARK   3    28  1.4690 -  1.4513    0.96     2623   126  0.2389 0.2586        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2042                                  
REMARK   3   ANGLE     :  1.173           2804                                  
REMARK   3   CHIRALITY :  0.079            318                                  
REMARK   3   PLANARITY :  0.006            364                                  
REMARK   3   DIHEDRAL  : 11.750            747                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID -16:17)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1471  28.1759  19.8449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1461 T22:   0.3956                                     
REMARK   3      T33:   0.2789 T12:  -0.0606                                     
REMARK   3      T13:   0.0221 T23:   0.0988                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4720 L22:   0.5712                                     
REMARK   3      L33:   0.0332 L12:   0.3515                                     
REMARK   3      L13:  -0.1156 L23:  -0.1272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0938 S12:  -0.5736 S13:  -0.0273                       
REMARK   3      S21:   0.2473 S22:   0.0596 S23:   0.5227                       
REMARK   3      S31:   0.1773 S32:  -0.5967 S33:   0.0183                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 18:123)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9226  33.0536  21.5984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0654 T22:   0.0825                                     
REMARK   3      T33:   0.0669 T12:  -0.0053                                     
REMARK   3      T13:  -0.0010 T23:   0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1090 L22:   1.8966                                     
REMARK   3      L33:   0.7665 L12:   0.2818                                     
REMARK   3      L13:   0.3356 L23:   0.0686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0040 S12:  -0.0767 S13:  -0.0193                       
REMARK   3      S21:   0.0399 S22:   0.0378 S23:  -0.0738                       
REMARK   3      S31:   0.0349 S32:  -0.0227 S33:  -0.0475                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 124:164)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2539  37.8422   5.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1071 T22:   0.1113                                     
REMARK   3      T33:   0.0827 T12:  -0.0135                                     
REMARK   3      T13:  -0.0207 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6084 L22:   0.9617                                     
REMARK   3      L33:   0.9660 L12:   0.2234                                     
REMARK   3      L13:  -0.8091 L23:  -0.5963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:   0.1445 S13:   0.0060                       
REMARK   3      S21:  -0.0848 S22:   0.0583 S23:   0.0027                       
REMARK   3      S31:   0.0233 S32:  -0.1110 S33:  -0.0443                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 165:249)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9542  30.9982   3.1375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1367 T22:   0.1105                                     
REMARK   3      T33:   0.1072 T12:   0.0094                                     
REMARK   3      T13:   0.0136 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2141 L22:   0.6200                                     
REMARK   3      L33:   1.4682 L12:   0.3077                                     
REMARK   3      L13:  -0.4054 L23:  -0.6152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0105 S12:   0.0235 S13:  -0.0465                       
REMARK   3      S21:  -0.1371 S22:  -0.0354 S23:  -0.0628                       
REMARK   3      S31:   0.1324 S32:   0.0924 S33:   0.0393                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 250:267)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6470  28.4347  -9.2652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3616 T22:   0.1663                                     
REMARK   3      T33:   0.1156 T12:  -0.0078                                     
REMARK   3      T13:   0.0570 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2874 L22:   3.9574                                     
REMARK   3      L33:   5.2623 L12:  -1.1707                                     
REMARK   3      L13:  -3.8999 L23:   2.9595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1406 S12:   0.0834 S13:  -0.0953                       
REMARK   3      S21:  -0.3798 S22:   0.0539 S23:  -0.0980                       
REMARK   3      S31:   0.4116 S32:   0.0994 S33:   0.0708                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212618.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12709                            
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING I-BEAM BENT        
REMARK 200                                   SINGLE CRYSTAL, ASYMMETRIC CUT     
REMARK 200                                   4.9650 DEGREES                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE JULY 4, 2012, XDS           
REMARK 200                                   NOVEMBER 11, 2013                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42861                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.451                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.168                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.530                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.8700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.48                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.470                              
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 5DJF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM ACETATE, 0.1 M BIS       
REMARK 280  -TRIS-HCL, 35% PEG550 MME, PH 6.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 298.15K                                                 
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       20.31800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.59900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.07000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.59900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.31800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.07000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     GLY A   -20                                                      
REMARK 465     SER A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     SER A   118                                                      
REMARK 465     ASN A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLN A   121                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     ALA A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   470     O    HOH A   627              2.12            
REMARK 500   O    ARG A   116     O    HOH A   401              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  12       74.74     59.75                                   
REMARK 500    SER A 117      -45.37    166.76                                   
REMARK 500    SER A 186      132.62     78.59                                   
REMARK 500    SER A 186      136.09     73.54                                   
REMARK 500    GLN A 208      173.60    177.69                                   
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 A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  73   OE1                                                    
REMARK 620 2 ASP A  91   OD1  91.7                                              
REMARK 620 3 LEU A  93   O   169.8  86.1                                        
REMARK 620 4 PO4 A 305   O2   96.5  96.8  93.7                                  
REMARK 620 5 PO4 A 305   O3   97.6 162.6  87.1  67.6                            
REMARK 620 6 HOH A 439   O    86.0  99.8  84.6 163.1  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  73   OE2                                                    
REMARK 620 2 PO4 A 305   O4  103.7                                              
REMARK 620 3 HOH A 414   O    89.3  93.0                                        
REMARK 620 4 HOH A 466   O    91.4  89.7 177.0                                  
REMARK 620 5 HOH A 493   O    86.6 169.4  89.5  87.6                            
REMARK 620 6 HOH A 497   O   165.8  90.2  87.1  91.5  79.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  91   OD2                                                    
REMARK 620 2 ASP A  94   OD1  95.2                                              
REMARK 620 3 ASP A 212   OD1  92.3  90.9                                        
REMARK 620 4 AMP A 304   O3' 172.8  91.8  89.6                                  
REMARK 620 5 PO4 A 305   O2   91.0  99.3 169.0  85.9                            
REMARK 620 6 HOH A 442   O    98.2 163.0  78.2  75.3  91.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DJF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DJJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DJI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DJK   RELATED DB: PDB                                   
DBREF  5DJH A    2   267  UNP    P9WKJ0   CYSQ_MYCTO       2    267             
SEQADV 5DJH MET A  -21  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH GLY A  -20  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH SER A  -19  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH SER A  -18  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -17  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -16  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -15  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -14  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -13  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A  -12  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH SER A  -10  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH SER A   -9  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH GLY A   -8  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH LEU A   -7  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH VAL A   -6  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH PRO A   -5  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH ARG A   -4  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH GLY A   -3  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH SER A   -2  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH HIS A   -1  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH MET A    0  UNP  P9WKJ0              EXPRESSION TAG                 
SEQADV 5DJH VAL A    1  UNP  P9WKJ0              EXPRESSION TAG                 
SEQRES   1 A  288  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  288  LEU VAL PRO ARG GLY SER HIS MET VAL VAL SER PRO ALA          
SEQRES   3 A  288  ALA PRO ASP LEU THR ASP ASP LEU THR ASP ALA GLU LEU          
SEQRES   4 A  288  ALA ALA ASP LEU ALA ALA ASP ALA GLY LYS LEU LEU LEU          
SEQRES   5 A  288  GLN VAL ARG ALA GLU ILE GLY PHE ASP GLN PRO TRP THR          
SEQRES   6 A  288  LEU GLY GLU ALA GLY ASP ARG GLN ALA ASN SER LEU LEU          
SEQRES   7 A  288  LEU ARG ARG LEU GLN ALA GLU ARG PRO GLY ASP ALA VAL          
SEQRES   8 A  288  LEU SER GLU GLU ALA HIS ASP ASP LEU ALA ARG LEU LYS          
SEQRES   9 A  288  SER ASP ARG VAL TRP ILE ILE ASP PRO LEU ASP GLY THR          
SEQRES  10 A  288  ARG GLU PHE SER THR PRO GLY ARG ASP ASP TRP ALA VAL          
SEQRES  11 A  288  HIS ILE ALA LEU TRP ARG ARG SER SER ASN GLY GLN PRO          
SEQRES  12 A  288  GLU ILE THR ASP ALA ALA VAL ALA LEU PRO ALA ARG GLY          
SEQRES  13 A  288  ASN VAL VAL TYR ARG THR ASP THR VAL THR SER GLY ALA          
SEQRES  14 A  288  ALA PRO ALA GLY VAL PRO GLY THR LEU ARG ILE ALA VAL          
SEQRES  15 A  288  SER ALA THR ARG PRO PRO ALA VAL LEU HIS ARG ILE ARG          
SEQRES  16 A  288  GLN THR LEU ALA ILE GLN PRO VAL SER ILE GLY SER ALA          
SEQRES  17 A  288  GLY ALA LYS ALA MET ALA VAL ILE ASP GLY TYR VAL ASP          
SEQRES  18 A  288  ALA TYR LEU HIS ALA GLY GLY GLN TRP GLU TRP ASP SER          
SEQRES  19 A  288  ALA ALA PRO ALA GLY VAL MET LEU ALA ALA GLY MET HIS          
SEQRES  20 A  288  ALA SER ARG LEU ASP GLY SER PRO LEU ARG TYR ASN GLN          
SEQRES  21 A  288  LEU ASP PRO TYR LEU PRO ASP LEU LEU MET CYS ARG ALA          
SEQRES  22 A  288  GLU VAL ALA PRO ILE LEU LEU GLY ALA ILE ALA ASP ALA          
SEQRES  23 A  288  TRP ARG                                                      
HET     MG  A 301       1                                                       
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HET    AMP  A 304      23                                                       
HET    PO4  A 305       5                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2   MG    3(MG 2+)                                                     
FORMUL   5  AMP    C10 H14 N5 O7 P                                              
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *269(H2 O)                                                    
HELIX    1 AA1 THR A   14  GLY A   38  1                                  25    
HELIX    2 AA2 GLN A   41  ARG A   65  1                                  25    
HELIX    3 AA3 LEU A   79  SER A   84  5                                   6    
HELIX    4 AA4 GLY A   95  SER A  100  1                                   6    
HELIX    5 AA5 ALA A  168  ARG A  174  1                                   7    
HELIX    6 AA6 SER A  186  ASP A  196  1                                  11    
HELIX    7 AA7 TRP A  209  ALA A  223  1                                  15    
HELIX    8 AA8 VAL A  254  ALA A  265  1                                  12    
SHEET    1 AA1 5 ALA A  69  SER A  72  0                                        
SHEET    2 AA1 5 ARG A  86  ASP A  94  1  O  TRP A  88   N  LEU A  71           
SHEET    3 AA1 5 ALA A 108  ARG A 115 -1  O  ALA A 108   N  ASP A  94           
SHEET    4 AA1 5 GLU A 123  LEU A 131 -1  O  ASP A 126   N  LEU A 113           
SHEET    5 AA1 5 VAL A 137  ARG A 140 -1  O  TYR A 139   N  VAL A 129           
SHEET    1 AA2 5 ILE A 179  ILE A 184  0                                        
SHEET    2 AA2 5 LEU A 157  SER A 162  1  N  ILE A 159   O  VAL A 182           
SHEET    3 AA2 5 ALA A 201  HIS A 204  1  O  ALA A 201   N  ALA A 160           
SHEET    4 AA2 5 LEU A 247  CYS A 250 -1  O  MET A 249   N  TYR A 202           
SHEET    5 AA2 5 HIS A 226  SER A 228 -1  N  HIS A 226   O  CYS A 250           
LINK         OE1 GLU A  73                MG    MG A 301     1555   1555  1.96  
LINK         OE2 GLU A  73                MG    MG A 303     1555   1555  2.13  
LINK         OD1 ASP A  91                MG    MG A 301     1555   1555  2.08  
LINK         OD2 ASP A  91                MG    MG A 302     1555   1555  2.06  
LINK         O   LEU A  93                MG    MG A 301     1555   1555  2.06  
LINK         OD1 ASP A  94                MG    MG A 302     1555   1555  2.07  
LINK         OD1 ASP A 212                MG    MG A 302     1555   1555  1.98  
LINK        MG    MG A 301                 O2  PO4 A 305     1555   1555  2.14  
LINK        MG    MG A 301                 O3  PO4 A 305     1555   1555  2.22  
LINK        MG    MG A 301                 O   HOH A 439     1555   1555  2.06  
LINK        MG    MG A 302                 O3' AMP A 304     1555   1555  2.17  
LINK        MG    MG A 302                 O2  PO4 A 305     1555   1555  2.00  
LINK        MG    MG A 302                 O   HOH A 442     1555   1555  2.25  
LINK        MG    MG A 303                 O4  PO4 A 305     1555   1555  1.87  
LINK        MG    MG A 303                 O   HOH A 414     1555   1555  2.15  
LINK        MG    MG A 303                 O   HOH A 466     1555   1555  2.16  
LINK        MG    MG A 303                 O   HOH A 493     1555   1655  2.20  
LINK        MG    MG A 303                 O   HOH A 497     1555   1555  2.07  
CISPEP   1 SER A  117    PRO A  122          0        -6.71                     
SITE     1 AC1  6 GLU A  73  ASP A  91  LEU A  93   MG A 302                    
SITE     2 AC1  6 PO4 A 305  HOH A 439                                          
SITE     1 AC2  7 ASP A  91  ASP A  94  ASP A 212   MG A 301                    
SITE     2 AC2  7 AMP A 304  PO4 A 305  HOH A 442                               
SITE     1 AC3  6 GLU A  73  PO4 A 305  HOH A 414  HOH A 466                    
SITE     2 AC3  6 HOH A 493  HOH A 497                                          
SITE     1 AC4 23 ASP A  94  SER A 162  ARG A 165  GLY A 185                    
SITE     2 AC4 23 SER A 186  ALA A 187  LYS A 190  HIS A 204                    
SITE     3 AC4 23 GLY A 206  GLY A 207  GLN A 208  ASP A 212                    
SITE     4 AC4 23  MG A 302  PO4 A 305  HOH A 418  HOH A 419                    
SITE     5 AC4 23 HOH A 436  HOH A 442  HOH A 445  HOH A 454                    
SITE     6 AC4 23 HOH A 466  HOH A 469  HOH A 529                               
SITE     1 AC5 15 GLU A  73  ASP A  91  LEU A  93  ASP A  94                    
SITE     2 AC5 15 GLY A  95  THR A  96   MG A 301   MG A 302                    
SITE     3 AC5 15  MG A 303  AMP A 304  HOH A 414  HOH A 421                    
SITE     4 AC5 15 HOH A 442  HOH A 466  HOH A 497                               
CRYST1   40.636   58.140  101.198  90.00  90.00  90.00 P 21 21 21    4          
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      0.024609  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017200  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009882        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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