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Database: PDB
Entry: 6NHX
LinkDB: 6NHX
Original site: 6NHX 
HEADER    LIGASE                                  24-DEC-18   6NHX              
TITLE     MYCOBACTERIAL DNA LIGASE D COMPLEXED WITH ATP AND MES                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT DNA LIGASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.5.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: ERS027656_00724;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    DNA LIGASE, LIGASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHUMAN,M.UNCIULEAC,Y.GOLDGUR                                        
REVDAT   3   10-APR-19 6NHX    1       JRNL                                     
REVDAT   2   20-FEB-19 6NHX    1       JRNL                                     
REVDAT   1   13-FEB-19 6NHX    0                                                
JRNL        AUTH   M.C.UNCIULEAC,Y.GOLDGUR,S.SHUMAN                             
JRNL        TITL   STRUCTURES OF ATP-BOUND DNA LIGASE D IN A CLOSED DOMAIN      
JRNL        TITL 2 CONFORMATION REVEAL A NETWORK OF AMINO ACID AND METAL        
JRNL        TITL 3 CONTACTS TO THE ATP PHOSPHATES.                              
JRNL        REF    J. BIOL. CHEM.                V. 294  5094 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30718283                                                     
JRNL        DOI    10.1074/JBC.RA119.007445                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 56187                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.570                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2004                            
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 40.8354 -  3.3693    0.98     3950   149  0.1633 0.1534        
REMARK   3     2  3.3693 -  2.6744    0.99     3944   147  0.1836 0.1857        
REMARK   3     3  2.6744 -  2.3364    0.99     3904   141  0.1924 0.2138        
REMARK   3     4  2.3364 -  2.1228    0.99     3916   144  0.1906 0.2039        
REMARK   3     5  2.1228 -  1.9707    0.99     3879   144  0.1913 0.2218        
REMARK   3     6  1.9707 -  1.8545    0.99     3888   143  0.1982 0.2420        
REMARK   3     7  1.8545 -  1.7616    0.99     3903   145  0.2066 0.2386        
REMARK   3     8  1.7616 -  1.6849    0.99     3894   146  0.2078 0.2219        
REMARK   3     9  1.6849 -  1.6200    0.99     3877   145  0.2119 0.2134        
REMARK   3    10  1.6200 -  1.5641    0.99     3836   141  0.2112 0.2268        
REMARK   3    11  1.5641 -  1.5152    0.99     3870   145  0.2128 0.2086        
REMARK   3    12  1.5152 -  1.4719    0.99     3860   135  0.2213 0.2429        
REMARK   3    13  1.4719 -  1.4332    0.98     3790   139  0.2271 0.2384        
REMARK   3    14  1.4332 -  1.3982    0.93     3672   140  0.2408 0.2804        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.360           
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           2431                                  
REMARK   3   ANGLE     :  0.991           3306                                  
REMARK   3   CHIRALITY :  0.078            348                                  
REMARK   3   PLANARITY :  0.005            429                                  
REMARK   3   DIHEDRAL  : 11.135            892                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9678   9.4928  16.8593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1095 T22:   0.1055                                     
REMARK   3      T33:   0.1091 T12:  -0.0031                                     
REMARK   3      T13:  -0.0134 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6306 L22:   0.7063                                     
REMARK   3      L33:   0.8470 L12:  -0.3722                                     
REMARK   3      L13:  -0.4376 L23:   0.4432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0215 S12:  -0.0002 S13:   0.0086                       
REMARK   3      S21:  -0.0861 S22:  -0.0565 S23:   0.0771                       
REMARK   3      S31:  -0.0431 S32:  -0.0826 S33:   0.0353                       
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 6NHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238766.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56236                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 25% PEG 10000, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       24.84350            
REMARK 290   SMTRY3   2  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: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 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     SER A   451                                                      
REMARK 465     MET A   452                                                      
REMARK 465     GLU A   655                                                      
REMARK 465     GLY A   656                                                      
REMARK 465     ARG A   657                                                      
REMARK 465     SER A   658                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 472    CD   CE   NZ                                        
REMARK 470     ARG A 504    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 550    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 712    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 715    CD   CE   NZ                                        
REMARK 470     LYS A 721    CD   CE   NZ                                        
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  1126     O    HOH A  1174              1.78            
REMARK 500   O    HOH A  1342     O    HOH A  1470              1.84            
REMARK 500   O    HOH A  1356     O    HOH A  1428              1.88            
REMARK 500   O    HOH A  1388     O    HOH A  1399              1.91            
REMARK 500   O    HOH A  1157     O    HOH A  1407              1.91            
REMARK 500   O    HOH A  1134     O    HOH A  1362              2.00            
REMARK 500   O    HOH A  1225     O    HOH A  1418              2.01            
REMARK 500   O    HOH A  1440     O    HOH A  1453              2.01            
REMARK 500   O    HOH A  1484     O    HOH A  1487              2.03            
REMARK 500   O    HOH A  1145     O    HOH A  1266              2.08            
REMARK 500   OE1  GLN A   512     O    HOH A  1101              2.13            
REMARK 500   NH1  ARG A   567     O    HOH A  1102              2.13            
REMARK 500   O    ARG A   514     O    HOH A  1103              2.14            
REMARK 500   NH1  ARG A   548     O    HOH A  1101              2.15            
REMARK 500   O    ALA A   515     O    HOH A  1104              2.15            
REMARK 500   O    PRO A   670     O    HOH A  1105              2.19            
REMARK 500   O    HOH A  1244     O    HOH A  1467              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1402     O    HOH A  1460     2555     2.11            
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    LEU A 683      102.31     76.63                                   
REMARK 500    GLU A 685        1.39     58.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 1001                
DBREF1 6NHX A  452   755  UNP                  A0A0T9BTX3_MYCTX                 
DBREF2 6NHX A     A0A0T9BTX3                          1         308             
SEQADV 6NHX SER A  451  UNP  A0A0T9BTX           EXPRESSION TAG                 
SEQADV 6NHX MET A  481  UNP  A0A0T9BTX LYS    30 ENGINEERED MUTATION            
SEQRES   1 A  307  SER MET PHE GLU PHE ASP ASN LEU ALA PRO MET LEU ALA          
SEQRES   2 A  307  THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN TRP          
SEQRES   3 A  307  ALA PHE GLU GLY MET TRP ASP GLY TYR ARG LEU LEU VAL          
SEQRES   4 A  307  GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG SER          
SEQRES   5 A  307  GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG ALA          
SEQRES   6 A  307  LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU ASP          
SEQRES   7 A  307  GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO SER          
SEQRES   8 A  307  PHE SER GLN MET GLN ASN ARG GLY ARG ASP THR ARG VAL          
SEQRES   9 A  307  GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY ARG          
SEQRES  10 A  307  ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS LEU          
SEQRES  11 A  307  LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL PRO          
SEQRES  12 A  307  GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA CYS          
SEQRES  13 A  307  SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS ARG          
SEQRES  14 A  307  ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA SER          
SEQRES  15 A  307  TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL VAL          
SEQRES  16 A  307  ILE GLY GLY TRP ARG ALA GLY GLU GLY ARG SER GLY VAL          
SEQRES  17 A  307  GLY SER LEU LEU MET GLY ILE PRO GLY PRO GLY GLY LEU          
SEQRES  18 A  307  GLN PHE ALA GLY ARG VAL GLY THR GLY LEU SER GLU ARG          
SEQRES  19 A  307  GLU LEU ALA ASN LEU LYS GLU MET LEU ALA PRO LEU HIS          
SEQRES  20 A  307  THR ASP GLU SER PRO PHE ASP VAL PRO LEU PRO ALA ARG          
SEQRES  21 A  307  ASP ALA LYS GLY ILE THR TYR VAL LYS PRO ALA LEU VAL          
SEQRES  22 A  307  ALA GLU VAL ARG TYR SER GLU TRP THR PRO GLU GLY ARG          
SEQRES  23 A  307  LEU ARG GLN SER SER TRP ARG GLY LEU ARG PRO ASP LYS          
SEQRES  24 A  307  LYS PRO SER GLU VAL VAL ARG GLU                              
HET    ATP  A1000      31                                                       
HET    MES  A1001      12                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   2  ATP    C10 H16 N5 O13 P3                                            
FORMUL   3  MES    C6 H13 N O4 S                                                
FORMUL   4  HOH   *387(H2 O)                                                    
HELIX    1 AA1 GLU A  454  LEU A  458  5                                   5    
HELIX    2 AA2 VAL A  506  LEU A  520  5                                  15    
HELIX    3 AA3 SER A  541  ASN A  547  1                                   7    
HELIX    4 AA4 ARG A  573  ALA A  587  1                                  15    
HELIX    5 AA5 ASP A  599  GLY A  611  1                                  13    
HELIX    6 AA6 ARG A  686  ALA A  696  1                                  11    
HELIX    7 AA7 PRO A  710  LYS A  715  1                                   6    
HELIX    8 AA8 LYS A  752  VAL A  756  5                                   5    
SHEET    1 AA1 4 LEU A 462  HIS A 465  0                                        
SHEET    2 AA1 4 ARG A 629  LYS A 637  1  O  TRP A 633   N  THR A 464           
SHEET    3 AA1 4 GLY A 614  ARG A 619 -1  N  ALA A 617   O  VAL A 634           
SHEET    4 AA1 4 TRP A 476  GLY A 480 -1  N  ALA A 477   O  LYS A 618           
SHEET    1 AA2 5 ALA A 495  SER A 500  0                                        
SHEET    2 AA2 5 TYR A 485  ASP A 492 -1  N  GLU A 490   O  ARG A 497           
SHEET    3 AA2 5 HIS A 524  VAL A 532 -1  O  ALA A 531   N  TYR A 485           
SHEET    4 AA2 5 GLU A 555  LEU A 564 -1  O  PHE A 559   N  ASP A 528           
SHEET    5 AA2 5 ARG A 567  ALA A 568 -1  O  ARG A 567   N  LEU A 564           
SHEET    1 AA3 5 GLY A 672  GLY A 680  0                                        
SHEET    2 AA3 5 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3 AA3 5 ASN A 640  ARG A 650 -1  N  VAL A 645   O  GLY A 666           
SHEET    4 AA3 5 THR A 718  VAL A 720 -1  O  THR A 718   N  TRP A 649           
SHEET    5 AA3 5 HIS A 699  THR A 700 -1  N  THR A 700   O  TYR A 719           
SHEET    1 AA4 5 GLY A 672  GLY A 680  0                                        
SHEET    2 AA4 5 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3 AA4 5 ASN A 640  ARG A 650 -1  N  VAL A 645   O  GLY A 666           
SHEET    4 AA4 5 VAL A 725  TYR A 730 -1  O  ALA A 726   N  VAL A 644           
SHEET    5 AA4 5 SER A 743  LEU A 747 -1  O  GLY A 746   N  GLU A 727           
SITE     1 AC1 23 GLU A 479  GLY A 480  MET A 481  TRP A 482                    
SITE     2 AC1 23 ARG A 486  ARG A 501  GLU A 530  PHE A 559                    
SITE     3 AC1 23 ILE A 616  LYS A 618  ARG A 629  TRP A 633                    
SITE     4 AC1 23 LYS A 635  LYS A 637  ARG A 745  ARG A 748                    
SITE     5 AC1 23 MES A1001  HOH A1159  HOH A1245  HOH A1275                    
SITE     6 AC1 23 HOH A1309  HOH A1319  HOH A1343                               
SITE     1 AC2 11 ASP A 483  GLY A 484  TYR A 485  ARG A 486                    
SITE     2 AC2 11 ARG A 501  GLU A 530  PHE A 542  ARG A 745                    
SITE     3 AC2 11 ATP A1000  HOH A1245  HOH A1309                               
CRYST1   41.089   49.687   73.522  90.00 103.18  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024337  0.000000  0.005700        0.00000                         
SCALE2      0.000000  0.020126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013969        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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