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Database: PDB
Entry: 4BGA
LinkDB: 4BGA
Original site: 4BGA 
HEADER    TRANSFERASE                             24-MAR-13   4BGA              
TITLE     NUCLEOTIDE-BOUND OPEN FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM     
TITLE    2 METHANOPYRUS KANDLERI                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PREDICTED MOLECULAR CHAPERONE DISTANTLY RELATED TO HSP70-F 
COMPND   3 OLD METALLOPROTEASES;                                                
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: RESIDUES 37-358;                                           
COMPND   6 SYNONYM: PUTATIVE SUGAR KINASE MK0840;                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOPYRUS KANDLERI;                          
SOURCE   3 ORGANISM_TAXID: 190192;                                              
SOURCE   4 STRAIN: AV19;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28A;                                    
SOURCE  10 OTHER_DETAILS: DSM6324                                               
KEYWDS    TRANSFERASE, ASKHA SUPERFAMILY, PHOSPHOTRANSFER, PSEUDOMUREIN         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SCHACHERL,U.BAUMANN                                                 
REVDAT   4   20-DEC-23 4BGA    1       HETSYN                                   
REVDAT   3   29-JUL-20 4BGA    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       FORMUL LINK   SITE   ATOM                
REVDAT   2   18-DEC-13 4BGA    1       JRNL                                     
REVDAT   1   27-NOV-13 4BGA    0                                                
JRNL        AUTH   M.SCHACHERL,S.M.WALTERSPERGER,U.BAUMANN                      
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE RIBONUCLEASE H-LIKE TYPE  
JRNL        TITL 2 ASKHA SUPERFAMILY KINASE MK0840 FROM METHANOPYRUS KANDLERI   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69  2440 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   24311585                                                     
JRNL        DOI    10.1107/S0907444913022683                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 43757                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2188                            
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 73.5972 -  6.5501    1.00     2660   140  0.1654 0.1946        
REMARK   3     2  6.5501 -  5.1995    1.00     2622   138  0.1567 0.2065        
REMARK   3     3  5.1995 -  4.5423    1.00     2617   138  0.1202 0.1513        
REMARK   3     4  4.5423 -  4.1271    1.00     2595   137  0.1153 0.1551        
REMARK   3     5  4.1271 -  3.8313    1.00     2600   137  0.1326 0.1653        
REMARK   3     6  3.8313 -  3.6054    1.00     2602   137  0.1423 0.2056        
REMARK   3     7  3.6054 -  3.4248    1.00     2602   137  0.1517 0.2235        
REMARK   3     8  3.4248 -  3.2757    1.00     2585   136  0.1606 0.1963        
REMARK   3     9  3.2757 -  3.1496    1.00     2592   136  0.1762 0.2406        
REMARK   3    10  3.1496 -  3.0410    1.00     2592   136  0.1822 0.2889        
REMARK   3    11  3.0410 -  2.9459    1.00     2569   136  0.1903 0.2511        
REMARK   3    12  2.9459 -  2.8617    1.00     2590   136  0.1784 0.2774        
REMARK   3    13  2.8617 -  2.7863    1.00     2589   136  0.1842 0.2335        
REMARK   3    14  2.7863 -  2.7183    1.00     2567   135  0.1772 0.2887        
REMARK   3    15  2.7183 -  2.6565    1.00     2605   137  0.1780 0.2466        
REMARK   3    16  2.6565 -  2.6000    1.00     2582   136  0.1773 0.2496        
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.44                          
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          10011                                  
REMARK   3   ANGLE     :  1.181          13642                                  
REMARK   3   CHIRALITY :  0.065           1561                                  
REMARK   3   PLANARITY :  0.005           1799                                  
REMARK   3   DIHEDRAL  : 20.379           3816                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FIRST 36 AMINO ACIDS OF THE PROTEIN ARE   
REMARK   3  MISSING.GSH OVERHANG FROM THROMBIN-DIGESTED 6X-HIS TAG.             
REMARK   4                                                                      
REMARK   4 4BGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290047194.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.69                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.980                              
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 4BG8 CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXED WITH 5 MM ADP, 10 MM MACL2,        
REMARK 280  CRYSTALLIZED IN 0.2 M POTASSIUM SODIUM TARTRATE AND 20% PEG 3350,   
REMARK 280  PH 7.5                                                              
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       55.83500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     ARG A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     GLY A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     THR A   358                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     GLY B   351                                                      
REMARK 465     THR B   352                                                      
REMARK 465     GLY B   353                                                      
REMARK 465     ARG B   354                                                      
REMARK 465     GLY B   355                                                      
REMARK 465     GLY B   356                                                      
REMARK 465     LYS B   357                                                      
REMARK 465     THR B   358                                                      
REMARK 465     GLY C    34                                                      
REMARK 465     SER C    35                                                      
REMARK 465     HIS C    36                                                      
REMARK 465     GLY D    34                                                      
REMARK 465     SER D    35                                                      
REMARK 465     HIS D    36                                                      
REMARK 465     GLY D   351                                                      
REMARK 465     THR D   352                                                      
REMARK 465     GLY D   353                                                      
REMARK 465     ARG D   354                                                      
REMARK 465     GLY D   355                                                      
REMARK 465     GLY D   356                                                      
REMARK 465     LYS D   357                                                      
REMARK 465     THR D   358                                                      
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   OE2  GLU A    62     NH1  ARG C   101              2.12            
REMARK 500   NH2  ARG A   179     OE1  GLU A   341              2.15            
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    PHE A 320       79.56   -112.65                                   
REMARK 500    SER B  75      149.83   -171.23                                   
REMARK 500    ASP C 261       36.72    -89.06                                   
REMARK 500    PHE C 320       73.83   -119.49                                   
REMARK 500    SER D  75      145.49   -170.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2027        DISTANCE =  6.69 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 SUCROSE (SUC): CRYOPROTECTANT                                        
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                               K A1351   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 114   OD2                                                    
REMARK 620 2 ASP A 138   O   103.9                                              
REMARK 620 3 GLY A 141   O   165.4  67.1                                        
REMARK 620 4 PRO A 143   O    82.9  83.6  84.6                                  
REMARK 620 5 ASP A 144   OD1  96.0 147.3  87.5  73.3                            
REMARK 620 6 ASP A 144   OD2  71.7 173.9 118.1  99.8  38.7                      
REMARK 620 7 HOH A2014   O    82.8  86.6 107.4 160.2 121.8  88.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1352   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 138   OD2                                                    
REMARK 620 2 ALA A 142   O    85.6                                              
REMARK 620 3 PHE A 182   O    91.8  88.9                                        
REMARK 620 4 GLY A 183   O    93.8 165.3  76.4                                  
REMARK 620 5 ALA A 185   O   173.7  90.7  93.3  91.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1351   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 114   OD2                                                    
REMARK 620 2 ASP B 138   O   104.2                                              
REMARK 620 3 GLY B 141   O   164.2  72.7                                        
REMARK 620 4 PRO B 143   O    82.7  84.5  81.6                                  
REMARK 620 5 ASP B 144   OD2  70.4 174.0 113.3  97.2                            
REMARK 620 6 HOH B2019   O    98.4  81.4  96.4 165.6  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1352   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 138   OD2                                                    
REMARK 620 2 ALA B 142   O    88.1                                              
REMARK 620 3 PHE B 182   O    93.5  88.5                                        
REMARK 620 4 GLY B 183   O    90.0 166.5  78.3                                  
REMARK 620 5 ALA B 185   O   171.9  90.6  94.5  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1354  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B1355   O2A                                                    
REMARK 620 2 ADP B1355   O1B  65.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1359   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 114   OD2                                                    
REMARK 620 2 ASP C 138   O   103.8                                              
REMARK 620 3 GLY C 141   O   151.9  70.3                                        
REMARK 620 4 PRO C 143   O    77.3  80.7  74.6                                  
REMARK 620 5 ASP C 144   OD2  70.4 169.5 110.5  89.5                            
REMARK 620 6 HOH C2016   O   106.5  93.8 101.4 174.0  96.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1360   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 138   OD2                                                    
REMARK 620 2 ALA C 142   O    92.8                                              
REMARK 620 3 PHE C 182   O    91.3  90.7                                        
REMARK 620 4 GLY C 183   O    89.8 169.0  78.5                                  
REMARK 620 5 ALA C 185   O   172.8  89.9  95.3  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D1352   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 114   OD2                                                    
REMARK 620 2 ASP D 138   O    99.5                                              
REMARK 620 3 GLY D 141   O   163.5  65.0                                        
REMARK 620 4 PRO D 143   O    88.1  86.7  85.4                                  
REMARK 620 5 ASP D 144   OD2  76.5 169.1 119.8 103.2                            
REMARK 620 6 ASP D 144   OD1 102.4 151.6  90.8  76.3  38.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D1351   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 138   OD2                                                    
REMARK 620 2 ALA D 142   O    88.6                                              
REMARK 620 3 PHE D 182   O    92.3  91.8                                        
REMARK 620 4 GLY D 183   O    93.8 168.8  77.2                                  
REMARK 620 5 ALA D 185   O   171.0  87.7  96.1  91.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1355  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP D1356   O1B                                                    
REMARK 620 2 ADP D1356   O2A  67.4                                              
REMARK 620 N                    1                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BG8   RELATED DB: PDB                                   
REMARK 900 APO FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM METHANOPYRUS         
REMARK 900 KANDLERI (MONOCLINIC SPACE GROUP)                                    
REMARK 900 RELATED ID: 4BG9   RELATED DB: PDB                                   
REMARK 900 APO FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM METHANOPYRUS         
REMARK 900 KANDLERI (ORTHORHOMBIC SPACE GROUP)                                  
REMARK 900 RELATED ID: 4BGB   RELATED DB: PDB                                   
REMARK 900 NUCLEOTIDE-BOUND CLOSED FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM  
REMARK 900 METHANOPYRUS KANDLERI                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 TRUNCATED CONSTRUCT LACKING THE FIRST 36 AMINO ACIDS                 
DBREF  4BGA A   37   358  UNP    Q8TX37   Q8TX37_METKA    37    358             
DBREF  4BGA B   37   358  UNP    Q8TX37   Q8TX37_METKA    37    358             
DBREF  4BGA C   37   358  UNP    Q8TX37   Q8TX37_METKA    37    358             
DBREF  4BGA D   37   358  UNP    Q8TX37   Q8TX37_METKA    37    358             
SEQADV 4BGA GLY A   34  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA SER A   35  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA HIS A   36  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA GLY B   34  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA SER B   35  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA HIS B   36  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA GLY C   34  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA SER C   35  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA HIS C   36  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA GLY D   34  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA SER D   35  UNP  Q8TX37              EXPRESSION TAG                 
SEQADV 4BGA HIS D   36  UNP  Q8TX37              EXPRESSION TAG                 
SEQRES   1 A  325  GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY          
SEQRES   2 A  325  ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY          
SEQRES   3 A  325  ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY          
SEQRES   4 A  325  LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG          
SEQRES   5 A  325  ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG          
SEQRES   6 A  325  VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR          
SEQRES   7 A  325  ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE          
SEQRES   8 A  325  HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY          
SEQRES   9 A  325  ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA          
SEQRES  10 A  325  PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS          
SEQRES  11 A  325  VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG          
SEQRES  12 A  325  ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL          
SEQRES  13 A  325  GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU          
SEQRES  14 A  325  GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU          
SEQRES  15 A  325  GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER          
SEQRES  16 A  325  VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG          
SEQRES  17 A  325  GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL          
SEQRES  18 A  325  LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU          
SEQRES  19 A  325  ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR          
SEQRES  20 A  325  ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU          
SEQRES  21 A  325  VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS          
SEQRES  22 A  325  ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE          
SEQRES  23 A  325  PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU          
SEQRES  24 A  325  LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA          
SEQRES  25 A  325  LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR          
SEQRES   1 B  325  GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY          
SEQRES   2 B  325  ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY          
SEQRES   3 B  325  ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY          
SEQRES   4 B  325  LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG          
SEQRES   5 B  325  ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG          
SEQRES   6 B  325  VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR          
SEQRES   7 B  325  ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE          
SEQRES   8 B  325  HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY          
SEQRES   9 B  325  ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA          
SEQRES  10 B  325  PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS          
SEQRES  11 B  325  VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG          
SEQRES  12 B  325  ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL          
SEQRES  13 B  325  GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU          
SEQRES  14 B  325  GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU          
SEQRES  15 B  325  GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER          
SEQRES  16 B  325  VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG          
SEQRES  17 B  325  GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL          
SEQRES  18 B  325  LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU          
SEQRES  19 B  325  ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR          
SEQRES  20 B  325  ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU          
SEQRES  21 B  325  VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS          
SEQRES  22 B  325  ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE          
SEQRES  23 B  325  PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU          
SEQRES  24 B  325  LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA          
SEQRES  25 B  325  LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR          
SEQRES   1 C  325  GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY          
SEQRES   2 C  325  ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY          
SEQRES   3 C  325  ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY          
SEQRES   4 C  325  LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG          
SEQRES   5 C  325  ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG          
SEQRES   6 C  325  VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR          
SEQRES   7 C  325  ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE          
SEQRES   8 C  325  HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY          
SEQRES   9 C  325  ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA          
SEQRES  10 C  325  PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS          
SEQRES  11 C  325  VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG          
SEQRES  12 C  325  ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL          
SEQRES  13 C  325  GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU          
SEQRES  14 C  325  GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU          
SEQRES  15 C  325  GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER          
SEQRES  16 C  325  VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG          
SEQRES  17 C  325  GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL          
SEQRES  18 C  325  LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU          
SEQRES  19 C  325  ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR          
SEQRES  20 C  325  ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU          
SEQRES  21 C  325  VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS          
SEQRES  22 C  325  ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE          
SEQRES  23 C  325  PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU          
SEQRES  24 C  325  LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA          
SEQRES  25 C  325  LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR          
SEQRES   1 D  325  GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY          
SEQRES   2 D  325  ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY          
SEQRES   3 D  325  ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY          
SEQRES   4 D  325  LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG          
SEQRES   5 D  325  ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG          
SEQRES   6 D  325  VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR          
SEQRES   7 D  325  ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE          
SEQRES   8 D  325  HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY          
SEQRES   9 D  325  ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA          
SEQRES  10 D  325  PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS          
SEQRES  11 D  325  VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG          
SEQRES  12 D  325  ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL          
SEQRES  13 D  325  GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU          
SEQRES  14 D  325  GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU          
SEQRES  15 D  325  GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER          
SEQRES  16 D  325  VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG          
SEQRES  17 D  325  GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL          
SEQRES  18 D  325  LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU          
SEQRES  19 D  325  ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR          
SEQRES  20 D  325  ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU          
SEQRES  21 D  325  VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS          
SEQRES  22 D  325  ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE          
SEQRES  23 D  325  PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU          
SEQRES  24 D  325  LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA          
SEQRES  25 D  325  LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR          
HET    GLC  E   1      11                                                       
HET    FRU  E   2      12                                                       
HET    GLC  F   1      11                                                       
HET    FRU  F   2      12                                                       
HET      K  A1351       1                                                       
HET      K  A1352       1                                                       
HET    BGC  A1353      12                                                       
HET    ADP  A1354      27                                                       
HET      K  B1351       1                                                       
HET      K  B1352       1                                                       
HET    BGC  B1353      12                                                       
HET     MG  B1354       1                                                       
HET    ADP  B1355      27                                                       
HET      K  C1359       1                                                       
HET      K  C1360       1                                                       
HET    BGC  C1361      12                                                       
HET     MG  C1363       1                                                       
HET    ADP  C1364      27                                                       
HET      K  D1351       1                                                       
HET      K  D1352       1                                                       
HET    BGC  D1353      12                                                       
HET     MG  D1355       1                                                       
HET    ADP  D1356      27                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
HETNAM       K POTASSIUM ION                                                    
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                              
HETSYN     FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE                            
HETSYN     BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                               
FORMUL   5  GLC    2(C6 H12 O6)                                                 
FORMUL   5  FRU    2(C6 H12 O6)                                                 
FORMUL   7    K    8(K 1+)                                                      
FORMUL   9  BGC    4(C6 H12 O6)                                                 
FORMUL  10  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL  14   MG    3(MG 2+)                                                     
FORMUL  26  HOH   *222(H2 O)                                                    
HELIX    1   1 THR A   79  GLU A   90  1                                  12    
HELIX    2   2 GLU A   90  ASN A  103  1                                  14    
HELIX    3   3 VAL A  113  GLY A  129  1                                  17    
HELIX    4   4 ASP A  144  ALA A  147  5                                   4    
HELIX    5   5 VAL A  148  TYR A  158  1                                  11    
HELIX    6   6 THR A  191  GLY A  203  1                                  13    
HELIX    7   7 ASP A  207  LYS A  211  5                                   5    
HELIX    8   8 LYS A  212  GLY A  216  5                                   5    
HELIX    9   9 ASP A  219  SER A  228  1                                  10    
HELIX   10  10 VAL A  247  ASP A  261  1                                  15    
HELIX   11  11 PRO A  265  ALA A  286  1                                  22    
HELIX   12  12 GLN A  287  ASP A  289  5                                   3    
HELIX   13  13 GLY A  297  LYS A  301  5                                   5    
HELIX   14  14 ASN A  302  TRP A  313  1                                  12    
HELIX   15  15 GLU A  324  GLU A  339  1                                  16    
HELIX   16  16 THR B   79  GLU B   90  1                                  12    
HELIX   17  17 GLU B   90  ASN B  103  1                                  14    
HELIX   18  18 VAL B  113  GLY B  129  1                                  17    
HELIX   19  19 ASP B  144  ALA B  147  5                                   4    
HELIX   20  20 VAL B  148  TYR B  158  1                                  11    
HELIX   21  21 THR B  191  GLY B  203  1                                  13    
HELIX   22  22 ASP B  207  LYS B  211  5                                   5    
HELIX   23  23 LYS B  212  GLY B  216  5                                   5    
HELIX   24  24 ASP B  219  SER B  228  1                                  10    
HELIX   25  25 VAL B  247  ALA B  262  1                                  16    
HELIX   26  26 PRO B  265  ALA B  286  1                                  22    
HELIX   27  27 GLN B  287  ASP B  289  5                                   3    
HELIX   28  28 GLY B  297  LYS B  301  5                                   5    
HELIX   29  29 ASN B  302  TRP B  313  1                                  12    
HELIX   30  30 GLU B  324  GLU B  339  1                                  16    
HELIX   31  31 THR C   79  GLU C   90  1                                  12    
HELIX   32  32 GLU C   90  ASN C  103  1                                  14    
HELIX   33  33 VAL C  113  GLY C  129  1                                  17    
HELIX   34  34 ASP C  144  ALA C  147  5                                   4    
HELIX   35  35 VAL C  148  GLU C  156  1                                   9    
HELIX   36  36 THR C  191  LEU C  202  1                                  12    
HELIX   37  37 ASP C  207  LYS C  211  5                                   5    
HELIX   38  38 LYS C  212  GLY C  216  5                                   5    
HELIX   39  39 ASP C  219  SER C  228  1                                  10    
HELIX   40  40 VAL C  247  ASP C  261  1                                  15    
HELIX   41  41 PRO C  265  ALA C  286  1                                  22    
HELIX   42  42 GLY C  297  LYS C  301  5                                   5    
HELIX   43  43 ASN C  302  TRP C  313  1                                  12    
HELIX   44  44 GLU C  324  GLU C  339  1                                  16    
HELIX   45  45 THR D   79  GLU D   90  1                                  12    
HELIX   46  46 GLU D   90  ASN D  103  1                                  14    
HELIX   47  47 VAL D  113  GLY D  129  1                                  17    
HELIX   48  48 ASP D  144  ALA D  147  5                                   4    
HELIX   49  49 VAL D  148  TYR D  158  1                                  11    
HELIX   50  50 THR D  191  GLY D  203  1                                  13    
HELIX   51  51 ASP D  207  LYS D  211  5                                   5    
HELIX   52  52 LYS D  212  GLY D  216  5                                   5    
HELIX   53  53 ASP D  219  SER D  228  1                                  10    
HELIX   54  54 VAL D  247  ASP D  261  1                                  15    
HELIX   55  55 PRO D  265  ALA D  286  1                                  22    
HELIX   56  56 GLN D  287  ASP D  289  5                                   3    
HELIX   57  57 GLY D  297  LYS D  301  5                                   5    
HELIX   58  58 ASN D  302  TRP D  313  1                                  12    
HELIX   59  59 GLU D  324  GLU D  339  1                                  16    
SHEET    1  AA12 ALA A 345  CYS A 348  0                                        
SHEET    2  AA12 THR A 132  VAL A 135 -1  O  THR A 132   N  CYS A 348           
SHEET    3  AA12 LEU A 106  THR A 111  1  O  ALA A 107   N  LEU A 133           
SHEET    4  AA12 ARG A  39  LEU A  45  1  O  LEU A  41   N  VAL A 108           
SHEET    5  AA12 GLY A  49  ASN A  56 -1  O  ASP A  51   N  GLN A  44           
SHEET    6  AA12 TRP A  61  GLU A  68 -1  O  GLU A  62   N  VAL A  54           
SHEET    7  AA12 TRP C  61  GLU C  68 -1  O  VAL C  64   N  ILE A  63           
SHEET    8  AA12 GLY C  49  ASN C  56 -1  O  THR C  50   N  GLU C  67           
SHEET    9  AA12 ARG C  39  LEU C  45 -1  O  VAL C  40   N  MET C  55           
SHEET   10  AA12 LEU C 106  THR C 111  1  O  LEU C 106   N  LEU C  41           
SHEET   11  AA12 THR C 132  VAL C 135  1  O  LEU C 133   N  VAL C 109           
SHEET   12  AA12 ALA C 345  CYS C 348 -1  O  LEU C 346   N  ALA C 134           
SHEET    1  AB 2 ARG A 179  PRO A 180  0                                        
SHEET    2  AB 2 MET A 169  ARG A 176  1  O  ARG A 176   N  ARG A 179           
SHEET    1  AC 2 VAL A 186  VAL A 189  0                                        
SHEET    2  AC 2 MET A 169  ARG A 176 -1  O  ALA A 170   N  SER A 188           
SHEET    1  AD 5 VAL A 317  ILE A 319  0                                        
SHEET    2  AD 5 LEU A 293  SER A 296  1  O  LEU A 293   N  SER A 318           
SHEET    3  AD 5 CYS A 161  VAL A 166  1  O  VAL A 162   N  VAL A 294           
SHEET    4  AD 5 MET A 169  ARG A 176 -1  O  VAL A 171   N  ASP A 165           
SHEET    5  AD 5 ARG A 179  PRO A 180  1  O  ARG A 179   N  ARG A 176           
SHEET    1  AE 5 VAL A 317  ILE A 319  0                                        
SHEET    2  AE 5 LEU A 293  SER A 296  1  O  LEU A 293   N  SER A 318           
SHEET    3  AE 5 CYS A 161  VAL A 166  1  O  VAL A 162   N  VAL A 294           
SHEET    4  AE 5 MET A 169  ARG A 176 -1  O  VAL A 171   N  ASP A 165           
SHEET    5  AE 5 VAL A 186  VAL A 189 -1  O  VAL A 186   N  VAL A 172           
SHEET    1  AF 2 ASP A 230  VAL A 231  0                                        
SHEET    2  AF 2 LYS A 234  PRO A 235 -1  O  LYS A 234   N  VAL A 231           
SHEET    1  BA 6 TRP B  61  GLU B  68  0                                        
SHEET    2  BA 6 GLY B  49  ASN B  56 -1  O  THR B  50   N  GLU B  67           
SHEET    3  BA 6 ARG B  39  LEU B  45 -1  O  VAL B  40   N  MET B  55           
SHEET    4  BA 6 LEU B 106  THR B 111  1  O  LEU B 106   N  LEU B  41           
SHEET    5  BA 6 THR B 132  VAL B 135  1  O  LEU B 133   N  VAL B 109           
SHEET    6  BA 6 ALA B 345  CYS B 348 -1  O  LEU B 346   N  ALA B 134           
SHEET    1  BB 2 ARG B 179  PRO B 180  0                                        
SHEET    2  BB 2 MET B 169  ARG B 176  1  O  ARG B 176   N  ARG B 179           
SHEET    1  BC 2 VAL B 186  VAL B 189  0                                        
SHEET    2  BC 2 MET B 169  ARG B 176 -1  O  ALA B 170   N  SER B 188           
SHEET    1  BD 5 ASP B 316  ILE B 319  0                                        
SHEET    2  BD 5 LEU B 292  SER B 296  1  O  LEU B 293   N  SER B 318           
SHEET    3  BD 5 CYS B 161  VAL B 166  1  O  VAL B 162   N  VAL B 294           
SHEET    4  BD 5 MET B 169  ARG B 176 -1  O  VAL B 171   N  ASP B 165           
SHEET    5  BD 5 ARG B 179  PRO B 180  1  O  ARG B 179   N  ARG B 176           
SHEET    1  BE 5 ASP B 316  ILE B 319  0                                        
SHEET    2  BE 5 LEU B 292  SER B 296  1  O  LEU B 293   N  SER B 318           
SHEET    3  BE 5 CYS B 161  VAL B 166  1  O  VAL B 162   N  VAL B 294           
SHEET    4  BE 5 MET B 169  ARG B 176 -1  O  VAL B 171   N  ASP B 165           
SHEET    5  BE 5 VAL B 186  VAL B 189 -1  O  VAL B 186   N  VAL B 172           
SHEET    1  BF 2 ASP B 230  VAL B 231  0                                        
SHEET    2  BF 2 LYS B 234  PRO B 235 -1  O  LYS B 234   N  VAL B 231           
SHEET    1  CA 2 ARG C 179  PRO C 180  0                                        
SHEET    2  CA 2 MET C 169  ARG C 176  1  O  ARG C 176   N  ARG C 179           
SHEET    1  CB 2 VAL C 186  VAL C 189  0                                        
SHEET    2  CB 2 MET C 169  ARG C 176 -1  O  ALA C 170   N  SER C 188           
SHEET    1  CC 5 ASP C 316  ILE C 319  0                                        
SHEET    2  CC 5 LEU C 292  SER C 296  1  O  LEU C 293   N  SER C 318           
SHEET    3  CC 5 CYS C 161  VAL C 166  1  O  VAL C 162   N  VAL C 294           
SHEET    4  CC 5 MET C 169  ARG C 176 -1  O  VAL C 171   N  ASP C 165           
SHEET    5  CC 5 ARG C 179  PRO C 180  1  O  ARG C 179   N  ARG C 176           
SHEET    1  CD 5 ASP C 316  ILE C 319  0                                        
SHEET    2  CD 5 LEU C 292  SER C 296  1  O  LEU C 293   N  SER C 318           
SHEET    3  CD 5 CYS C 161  VAL C 166  1  O  VAL C 162   N  VAL C 294           
SHEET    4  CD 5 MET C 169  ARG C 176 -1  O  VAL C 171   N  ASP C 165           
SHEET    5  CD 5 VAL C 186  VAL C 189 -1  O  VAL C 186   N  VAL C 172           
SHEET    1  CE 2 ASP C 230  VAL C 231  0                                        
SHEET    2  CE 2 LYS C 234  PRO C 235 -1  O  LYS C 234   N  VAL C 231           
SHEET    1  DA 6 TRP D  61  GLU D  68  0                                        
SHEET    2  DA 6 GLY D  49  ASN D  56 -1  O  THR D  50   N  GLU D  67           
SHEET    3  DA 6 ARG D  39  LEU D  45 -1  O  VAL D  40   N  MET D  55           
SHEET    4  DA 6 LEU D 106  THR D 111  1  O  LEU D 106   N  LEU D  41           
SHEET    5  DA 6 THR D 132  VAL D 135  1  O  LEU D 133   N  VAL D 109           
SHEET    6  DA 6 ALA D 345  CYS D 348 -1  O  LEU D 346   N  ALA D 134           
SHEET    1  DB 2 ARG D 179  PRO D 180  0                                        
SHEET    2  DB 2 MET D 169  ARG D 176  1  O  ARG D 176   N  ARG D 179           
SHEET    1  DC 2 VAL D 186  VAL D 189  0                                        
SHEET    2  DC 2 MET D 169  ARG D 176 -1  O  ALA D 170   N  SER D 188           
SHEET    1  DD 5 VAL D 317  ILE D 319  0                                        
SHEET    2  DD 5 LEU D 293  SER D 296  1  O  LEU D 293   N  SER D 318           
SHEET    3  DD 5 CYS D 161  VAL D 166  1  O  VAL D 162   N  VAL D 294           
SHEET    4  DD 5 MET D 169  ARG D 176 -1  O  VAL D 171   N  ASP D 165           
SHEET    5  DD 5 ARG D 179  PRO D 180  1  O  ARG D 179   N  ARG D 176           
SHEET    1  DE 5 VAL D 317  ILE D 319  0                                        
SHEET    2  DE 5 LEU D 293  SER D 296  1  O  LEU D 293   N  SER D 318           
SHEET    3  DE 5 CYS D 161  VAL D 166  1  O  VAL D 162   N  VAL D 294           
SHEET    4  DE 5 MET D 169  ARG D 176 -1  O  VAL D 171   N  ASP D 165           
SHEET    5  DE 5 VAL D 186  VAL D 189 -1  O  VAL D 186   N  VAL D 172           
SHEET    1  DF 2 ASP D 230  VAL D 231  0                                        
SHEET    2  DF 2 LYS D 234  PRO D 235 -1  O  LYS D 234   N  VAL D 231           
LINK         C1  GLC E   1                 O2  FRU E   2     1555   1555  1.41  
LINK         C1  GLC F   1                 O2  FRU F   2     1555   1555  1.41  
LINK         OD2 ASP A 114                 K     K A1351     1555   1555  3.13  
LINK         O   ASP A 138                 K     K A1351     1555   1555  2.81  
LINK         OD2 ASP A 138                 K     K A1352     1555   1555  2.98  
LINK         O   GLY A 141                 K     K A1351     1555   1555  2.88  
LINK         O   ALA A 142                 K     K A1352     1555   1555  2.71  
LINK         O   PRO A 143                 K     K A1351     1555   1555  3.08  
LINK         OD1 ASP A 144                 K     K A1351     1555   1555  3.42  
LINK         OD2 ASP A 144                 K     K A1351     1555   1555  3.15  
LINK         O   PHE A 182                 K     K A1352     1555   1555  2.87  
LINK         O   GLY A 183                 K     K A1352     1555   1555  2.94  
LINK         O   ALA A 185                 K     K A1352     1555   1555  2.85  
LINK         K     K A1351                 O   HOH A2014     1555   1555  3.26  
LINK         OD2 ASP B 114                 K     K B1351     1555   1555  3.05  
LINK         O   ASP B 138                 K     K B1351     1555   1555  2.78  
LINK         OD2 ASP B 138                 K     K B1352     1555   1555  3.04  
LINK         O   GLY B 141                 K     K B1351     1555   1555  2.74  
LINK         O   ALA B 142                 K     K B1352     1555   1555  2.73  
LINK         O   PRO B 143                 K     K B1351     1555   1555  3.12  
LINK         OD2 ASP B 144                 K     K B1351     1555   1555  3.21  
LINK         O   PHE B 182                 K     K B1352     1555   1555  2.86  
LINK         O   GLY B 183                 K     K B1352     1555   1555  3.07  
LINK         O   ALA B 185                 K     K B1352     1555   1555  2.71  
LINK         K     K B1351                 O   HOH B2019     1555   1555  3.12  
LINK        MG    MG B1354                 O2A ADP B1355     1555   1555  2.76  
LINK        MG    MG B1354                 O1B ADP B1355     1555   1555  2.31  
LINK         OD2 ASP C 114                 K     K C1359     1555   1555  3.02  
LINK         O   ASP C 138                 K     K C1359     1555   1555  2.80  
LINK         OD2 ASP C 138                 K     K C1360     1555   1555  2.98  
LINK         O   GLY C 141                 K     K C1359     1555   1555  2.79  
LINK         O   ALA C 142                 K     K C1360     1555   1555  2.70  
LINK         O   PRO C 143                 K     K C1359     1555   1555  3.44  
LINK         OD2 ASP C 144                 K     K C1359     1555   1555  3.23  
LINK         O   PHE C 182                 K     K C1360     1555   1555  2.85  
LINK         O   GLY C 183                 K     K C1360     1555   1555  3.05  
LINK         O   ALA C 185                 K     K C1360     1555   1555  2.78  
LINK         K     K C1359                 O   HOH C2016     1555   1555  3.35  
LINK        MG    MG C1363                 O1A ADP C1364     1555   1555  2.42  
LINK         OD2 ASP D 114                 K     K D1352     1555   1555  2.91  
LINK         OD2 ASP D 138                 K     K D1351     1555   1555  3.05  
LINK         O   ASP D 138                 K     K D1352     1555   1555  2.96  
LINK         O   GLY D 141                 K     K D1352     1555   1555  2.84  
LINK         O   ALA D 142                 K     K D1351     1555   1555  2.87  
LINK         O   PRO D 143                 K     K D1352     1555   1555  2.90  
LINK         OD2 ASP D 144                 K     K D1352     1555   1555  3.16  
LINK         OD1 ASP D 144                 K     K D1352     1555   1555  3.47  
LINK         O   PHE D 182                 K     K D1351     1555   1555  2.84  
LINK         O   GLY D 183                 K     K D1351     1555   1555  3.12  
LINK         O   ALA D 185                 K     K D1351     1555   1555  2.73  
LINK        MG    MG D1355                 O1B ADP D1356     1555   1555  2.38  
LINK        MG    MG D1355                 O2A ADP D1356     1555   1555  2.76  
CISPEP   1 ALA A  142    PRO A  143          0        10.11                     
CISPEP   2 ALA B  142    PRO B  143          0         8.70                     
CISPEP   3 ALA C  142    PRO C  143          0         9.49                     
CISPEP   4 ALA D  142    PRO D  143          0        10.60                     
CRYST1   73.570  111.670   87.880  90.00  89.55  90.00 P 1 21 1      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      0.013592  0.000000 -0.000107        0.00000                         
SCALE2      0.000000  0.008955  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011380        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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