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Database: PDB
Entry: 5B5T
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Original site: 5B5T 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           18-MAY-16   5B5T              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GAMMA-GLUTAMYLTRANSPEPTIDASE IN 
TITLE    2 COMPLEX WITH PEPTIDYL PHOSPHONATE INHIBITOR 1B                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE LARGE CHAIN;                  
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: GLUTATHIONE HYDROLASE, GAMMA-GLUTAMYLTRANSPEPTIDASE LARGE-  
COMPND   5 SUBUNIT;                                                             
COMPND   6 EC: 2.3.2.2,3.4.19.13;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE SMALL CHAIN;                  
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 SYNONYM: GLUTATHIONE HYDROLASE, GAMMA-GLUTAMYLTRANSPEPTIDASE SMALL-  
COMPND  12 SUBUNIT;                                                             
COMPND  13 EC: 2.3.2.2,3.4.19.13;                                               
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: GGT, B3447, JW3412;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE  12 ORGANISM_TAXID: 83333;                                               
SOURCE  13 STRAIN: K12;                                                         
SOURCE  14 GENE: GGT, B3447, JW3412;                                            
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    GLUTATHIONE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.WADA,K.FUKUYAMA                                                     
REVDAT   2   26-OCT-16 5B5T    1       JRNL                                     
REVDAT   1   28-SEP-16 5B5T    0                                                
JRNL        AUTH   A.KAMIYAMA,M.NAKAJIMA,L.HAN,K.WADA,M.MIZUTANI,Y.TABUCHI,     
JRNL        AUTH 2 A.KOJIMA-YUASA,I.MATSUI-YUASA,H.SUZUKI,K.FUKUYAMA,           
JRNL        AUTH 3 B.WATANABE,J.HIRATAKE                                        
JRNL        TITL   PHOSPHONATE-BASED IRREVERSIBLE INHIBITORS OF HUMAN           
JRNL        TITL 2 GAMMA-GLUTAMYL TRANSPEPTIDASE (GGT). GGSTOP IS A NON-TOXIC   
JRNL        TITL 3 AND HIGHLY SELECTIVE INHIBITOR WITH CRITICAL ELECTROSTATIC   
JRNL        TITL 4 INTERACTION WITH AN ACTIVE-SITE RESIDUE LYS562 FOR ENHANCED  
JRNL        TITL 5 INHIBITORY ACTIVITY                                          
JRNL        REF    BIOORG.MED.CHEM.              V.  24  5340 2016              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   27622749                                                     
JRNL        DOI    10.1016/J.BMC.2016.08.050                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 135104                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6679                            
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 37.3377 -  5.2698    0.99     4747   229  0.1762 0.1755        
REMARK   3     2  5.2698 -  4.1846    1.00     4578   241  0.1360 0.1553        
REMARK   3     3  4.1846 -  3.6562    0.99     4505   269  0.1440 0.1609        
REMARK   3     4  3.6562 -  3.3221    0.99     4499   208  0.1593 0.1589        
REMARK   3     5  3.3221 -  3.0841    0.99     4433   241  0.1651 0.1769        
REMARK   3     6  3.0841 -  2.9023    0.98     4427   222  0.1729 0.1727        
REMARK   3     7  2.9023 -  2.7570    0.98     4383   225  0.1712 0.1876        
REMARK   3     8  2.7570 -  2.6371    0.98     4386   235  0.1773 0.1890        
REMARK   3     9  2.6371 -  2.5356    0.98     4395   198  0.1839 0.1926        
REMARK   3    10  2.5356 -  2.4481    0.98     4355   260  0.1859 0.2221        
REMARK   3    11  2.4481 -  2.3716    0.98     4333   239  0.1815 0.1747        
REMARK   3    12  2.3716 -  2.3038    0.99     4345   279  0.1795 0.2209        
REMARK   3    13  2.3038 -  2.2431    0.98     4383   247  0.1788 0.1986        
REMARK   3    14  2.2431 -  2.1884    0.98     4371   224  0.1756 0.1943        
REMARK   3    15  2.1884 -  2.1387    0.98     4383   231  0.1773 0.2033        
REMARK   3    16  2.1387 -  2.0932    0.99     4396   207  0.1806 0.2198        
REMARK   3    17  2.0932 -  2.0513    0.99     4389   232  0.1908 0.2134        
REMARK   3    18  2.0513 -  2.0126    0.99     4406   232  0.2019 0.2065        
REMARK   3    19  2.0126 -  1.9766    0.99     4450   221  0.2044 0.2326        
REMARK   3    20  1.9766 -  1.9431    1.00     4362   260  0.2039 0.2073        
REMARK   3    21  1.9431 -  1.9118    0.99     4425   218  0.2022 0.2280        
REMARK   3    22  1.9118 -  1.8824    0.99     4442   202  0.2177 0.2421        
REMARK   3    23  1.8824 -  1.8547    1.00     4420   200  0.2240 0.2399        
REMARK   3    24  1.8547 -  1.8286    1.00     4472   218  0.2289 0.2654        
REMARK   3    25  1.8286 -  1.8039    0.95     4238   182  0.2414 0.3021        
REMARK   3    26  1.8039 -  1.7804    0.90     3975   216  0.2584 0.2987        
REMARK   3    27  1.7804 -  1.7582    0.86     3819   182  0.2520 0.2587        
REMARK   3    28  1.7582 -  1.7370    0.81     3553   192  0.2615 0.3098        
REMARK   3    29  1.7370 -  1.7168    0.77     3398   192  0.2878 0.2940        
REMARK   3    30  1.7168 -  1.6975    0.72     3157   177  0.2854 0.3327        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.350           
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      :  0.007           8300                                  
REMARK   3   ANGLE     :  0.950          11256                                  
REMARK   3   CHIRALITY :  0.055           1254                                  
REMARK   3   PLANARITY :  0.005           1486                                  
REMARK   3   DIHEDRAL  : 14.444           5024                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5B5T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000581.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135141                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2DBU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5-17.5% PEG 4000, 0.2M CACL2, 0.1M    
REMARK 280  TRIS-HCL, PH 8.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  277K, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.0K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.99500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.53750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.19400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.53750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.99500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.19400            
REMARK 290   SMTRY3   4  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: 12470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 12290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ALA A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     VAL A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     SER A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     GLN A   390                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     PRO C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     PRO C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     VAL C    32                                                      
REMARK 465     SER C    33                                                      
REMARK 465     TYR C    34                                                      
REMARK 465     GLY C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     SER C   388                                                      
REMARK 465     ASN C   389                                                      
REMARK 465     GLN C   390                                                      
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   846     O    HOH A   852              2.01            
REMARK 500   O    HOH C   415     O    HOH C   613              2.04            
REMARK 500   O    HOH B   838     O    HOH B   875              2.15            
REMARK 500   O    HOH A   685     O    HOH A   711              2.16            
REMARK 500   O    HOH A   716     O    HOH B   719              2.16            
REMARK 500   O    HOH D   765     O    HOH D   801              2.16            
REMARK 500   O    HOH C   810     O    HOH D   856              2.17            
REMARK 500   O    HOH D   707     O    HOH D   782              2.17            
REMARK 500   OG   SER C   103     OD1  ASN C   105              2.17            
REMARK 500   O    HOH D   841     O    HOH D   878              2.18            
REMARK 500   O    HOH A   551     O    HOH A   745              2.18            
REMARK 500   O    HOH B   855     O    HOH B   859              2.19            
REMARK 500   O    PRO C   200     NZ   LYS C   206              2.19            
REMARK 500   O    HOH D   856     O    HOH D   886              2.19            
REMARK 500   O    HOH B   863     O    HOH D   889              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   559     O    HOH D   866     2555     2.19            
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    ALA A  90      -42.71   -155.79                                   
REMARK 500    VAL A 198      -43.22   -135.59                                   
REMARK 500    LYS A 244      -12.40   -141.23                                   
REMARK 500    ASN B 411     -104.36     81.93                                   
REMARK 500    TRP B 518      -68.83     74.62                                   
REMARK 500    SER B 552       81.05   -154.44                                   
REMARK 500    ALA C  90      -41.85   -151.81                                   
REMARK 500    VAL C 198      -42.53   -135.26                                   
REMARK 500    ASN D 411     -104.03     81.85                                   
REMARK 500    ASN D 429       50.53   -115.57                                   
REMARK 500    TRP D 518      -67.03     68.41                                   
REMARK 500    SER D 552       83.83   -152.18                                   
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 A 864        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 865        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 866        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH C 825        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D 892        DISTANCE =  5.97 ANGSTROMS                       
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                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 569   O                                                      
REMARK 620 2 SER B 572   O    90.5                                              
REMARK 620 3 ASP B 575   OD1 121.3  80.5                                        
REMARK 620 4 ASP B 575   OD2  73.1  75.3  48.3                                  
REMARK 620 5 HOH B 768   O   100.8  73.2 130.2 147.9                            
REMARK 620 6 HOH B 836   O   156.5  93.6  82.2 130.2  58.7                      
REMARK 620 7 HOH B 839   O    87.4 166.0  88.7  90.8 120.8  93.8                
REMARK 620 8 HOH B 843   O    88.9 128.2 140.2 151.3  56.1  70.4  65.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 569   O                                                      
REMARK 620 2 SER D 572   O    90.7                                              
REMARK 620 3 ASP D 575   OD1 122.2  81.4                                        
REMARK 620 4 ASP D 575   OD2  72.9  73.4  49.9                                  
REMARK 620 5 HOH D 837   O    88.2 164.1  85.7  91.1                            
REMARK 620 6 HOH D 803   O   162.4  92.5  75.4 124.5  93.3                      
REMARK 620 7 HOH D 769   O    96.9  73.7 133.7 145.3 122.2  67.5                
REMARK 620 8 HOH D 840   O    87.8 130.0 138.6 150.7  65.9  76.9  56.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6FY B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6FY D 600 and THR D    
REMARK 800  391                                                                 
DBREF  5B5T A   25   390  UNP    P18956   GGT_ECOLI       25    390             
DBREF  5B5T B  391   580  UNP    P18956   GGT_ECOLI      391    580             
DBREF  5B5T C   25   390  UNP    P18956   GGT_ECOLI       25    390             
DBREF  5B5T D  391   580  UNP    P18956   GGT_ECOLI      391    580             
SEQRES   1 A  366  ALA ALA PRO PRO ALA PRO PRO VAL SER TYR GLY VAL GLU          
SEQRES   2 A  366  GLU ASP VAL PHE HIS PRO VAL ARG ALA LYS GLN GLY MET          
SEQRES   3 A  366  VAL ALA SER VAL ASP ALA THR ALA THR GLN VAL GLY VAL          
SEQRES   4 A  366  ASP ILE LEU LYS GLU GLY GLY ASN ALA VAL ASP ALA ALA          
SEQRES   5 A  366  VAL ALA VAL GLY TYR ALA LEU ALA VAL THR HIS PRO GLN          
SEQRES   6 A  366  ALA GLY ASN LEU GLY GLY GLY GLY PHE MET LEU ILE ARG          
SEQRES   7 A  366  SER LYS ASN GLY ASN THR THR ALA ILE ASP PHE ARG GLU          
SEQRES   8 A  366  MET ALA PRO ALA LYS ALA THR ARG ASP MET PHE LEU ASP          
SEQRES   9 A  366  ASP GLN GLY ASN PRO ASP SER LYS LYS SER LEU THR SER          
SEQRES  10 A  366  HIS LEU ALA SER GLY THR PRO GLY THR VAL ALA GLY PHE          
SEQRES  11 A  366  SER LEU ALA LEU ASP LYS TYR GLY THR MET PRO LEU ASN          
SEQRES  12 A  366  LYS VAL VAL GLN PRO ALA PHE LYS LEU ALA ARG ASP GLY          
SEQRES  13 A  366  PHE ILE VAL ASN ASP ALA LEU ALA ASP ASP LEU LYS THR          
SEQRES  14 A  366  TYR GLY SER GLU VAL LEU PRO ASN HIS GLU ASN SER LYS          
SEQRES  15 A  366  ALA ILE PHE TRP LYS GLU GLY GLU PRO LEU LYS LYS GLY          
SEQRES  16 A  366  ASP THR LEU VAL GLN ALA ASN LEU ALA LYS SER LEU GLU          
SEQRES  17 A  366  MET ILE ALA GLU ASN GLY PRO ASP GLU PHE TYR LYS GLY          
SEQRES  18 A  366  THR ILE ALA GLU GLN ILE ALA GLN GLU MET GLN LYS ASN          
SEQRES  19 A  366  GLY GLY LEU ILE THR LYS GLU ASP LEU ALA ALA TYR LYS          
SEQRES  20 A  366  ALA VAL GLU ARG THR PRO ILE SER GLY ASP TYR ARG GLY          
SEQRES  21 A  366  TYR GLN VAL TYR SER MET PRO PRO PRO SER SER GLY GLY          
SEQRES  22 A  366  ILE HIS ILE VAL GLN ILE LEU ASN ILE LEU GLU ASN PHE          
SEQRES  23 A  366  ASP MET LYS LYS TYR GLY PHE GLY SER ALA ASP ALA MET          
SEQRES  24 A  366  GLN ILE MET ALA GLU ALA GLU LYS TYR ALA TYR ALA ASP          
SEQRES  25 A  366  ARG SER GLU TYR LEU GLY ASP PRO ASP PHE VAL LYS VAL          
SEQRES  26 A  366  PRO TRP GLN ALA LEU THR ASN LYS ALA TYR ALA LYS SER          
SEQRES  27 A  366  ILE ALA ASP GLN ILE ASP ILE ASN LYS ALA LYS PRO SER          
SEQRES  28 A  366  SER GLU ILE ARG PRO GLY LYS LEU ALA PRO TYR GLU SER          
SEQRES  29 A  366  ASN GLN                                                      
SEQRES   1 B  190  THR THR HIS TYR SER VAL VAL ASP LYS ASP GLY ASN ALA          
SEQRES   2 B  190  VAL ALA VAL THR TYR THR LEU ASN THR THR PHE GLY THR          
SEQRES   3 B  190  GLY ILE VAL ALA GLY GLU SER GLY ILE LEU LEU ASN ASN          
SEQRES   4 B  190  GLN MET ASP ASP PHE SER ALA LYS PRO GLY VAL PRO ASN          
SEQRES   5 B  190  VAL TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA VAL GLY          
SEQRES   6 B  190  PRO ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 B  190  VAL VAL LYS ASP GLY LYS THR TRP LEU VAL THR GLY SER          
SEQRES   8 B  190  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN MET          
SEQRES   9 B  190  VAL VAL ASN SER ILE ASP TYR GLY LEU ASN VAL ALA GLU          
SEQRES  10 B  190  ALA THR ASN ALA PRO ARG PHE HIS HIS GLN TRP LEU PRO          
SEQRES  11 B  190  ASP GLU LEU ARG VAL GLU LYS GLY PHE SER PRO ASP THR          
SEQRES  12 B  190  LEU LYS LEU LEU GLU ALA LYS GLY GLN LYS VAL ALA LEU          
SEQRES  13 B  190  LYS GLU ALA MET GLY SER THR GLN SER ILE MET VAL GLY          
SEQRES  14 B  190  PRO ASP GLY GLU LEU TYR GLY ALA SER ASP PRO ARG SER          
SEQRES  15 B  190  VAL ASP ASP LEU THR ALA GLY TYR                              
SEQRES   1 C  366  ALA ALA PRO PRO ALA PRO PRO VAL SER TYR GLY VAL GLU          
SEQRES   2 C  366  GLU ASP VAL PHE HIS PRO VAL ARG ALA LYS GLN GLY MET          
SEQRES   3 C  366  VAL ALA SER VAL ASP ALA THR ALA THR GLN VAL GLY VAL          
SEQRES   4 C  366  ASP ILE LEU LYS GLU GLY GLY ASN ALA VAL ASP ALA ALA          
SEQRES   5 C  366  VAL ALA VAL GLY TYR ALA LEU ALA VAL THR HIS PRO GLN          
SEQRES   6 C  366  ALA GLY ASN LEU GLY GLY GLY GLY PHE MET LEU ILE ARG          
SEQRES   7 C  366  SER LYS ASN GLY ASN THR THR ALA ILE ASP PHE ARG GLU          
SEQRES   8 C  366  MET ALA PRO ALA LYS ALA THR ARG ASP MET PHE LEU ASP          
SEQRES   9 C  366  ASP GLN GLY ASN PRO ASP SER LYS LYS SER LEU THR SER          
SEQRES  10 C  366  HIS LEU ALA SER GLY THR PRO GLY THR VAL ALA GLY PHE          
SEQRES  11 C  366  SER LEU ALA LEU ASP LYS TYR GLY THR MET PRO LEU ASN          
SEQRES  12 C  366  LYS VAL VAL GLN PRO ALA PHE LYS LEU ALA ARG ASP GLY          
SEQRES  13 C  366  PHE ILE VAL ASN ASP ALA LEU ALA ASP ASP LEU LYS THR          
SEQRES  14 C  366  TYR GLY SER GLU VAL LEU PRO ASN HIS GLU ASN SER LYS          
SEQRES  15 C  366  ALA ILE PHE TRP LYS GLU GLY GLU PRO LEU LYS LYS GLY          
SEQRES  16 C  366  ASP THR LEU VAL GLN ALA ASN LEU ALA LYS SER LEU GLU          
SEQRES  17 C  366  MET ILE ALA GLU ASN GLY PRO ASP GLU PHE TYR LYS GLY          
SEQRES  18 C  366  THR ILE ALA GLU GLN ILE ALA GLN GLU MET GLN LYS ASN          
SEQRES  19 C  366  GLY GLY LEU ILE THR LYS GLU ASP LEU ALA ALA TYR LYS          
SEQRES  20 C  366  ALA VAL GLU ARG THR PRO ILE SER GLY ASP TYR ARG GLY          
SEQRES  21 C  366  TYR GLN VAL TYR SER MET PRO PRO PRO SER SER GLY GLY          
SEQRES  22 C  366  ILE HIS ILE VAL GLN ILE LEU ASN ILE LEU GLU ASN PHE          
SEQRES  23 C  366  ASP MET LYS LYS TYR GLY PHE GLY SER ALA ASP ALA MET          
SEQRES  24 C  366  GLN ILE MET ALA GLU ALA GLU LYS TYR ALA TYR ALA ASP          
SEQRES  25 C  366  ARG SER GLU TYR LEU GLY ASP PRO ASP PHE VAL LYS VAL          
SEQRES  26 C  366  PRO TRP GLN ALA LEU THR ASN LYS ALA TYR ALA LYS SER          
SEQRES  27 C  366  ILE ALA ASP GLN ILE ASP ILE ASN LYS ALA LYS PRO SER          
SEQRES  28 C  366  SER GLU ILE ARG PRO GLY LYS LEU ALA PRO TYR GLU SER          
SEQRES  29 C  366  ASN GLN                                                      
SEQRES   1 D  190  THR THR HIS TYR SER VAL VAL ASP LYS ASP GLY ASN ALA          
SEQRES   2 D  190  VAL ALA VAL THR TYR THR LEU ASN THR THR PHE GLY THR          
SEQRES   3 D  190  GLY ILE VAL ALA GLY GLU SER GLY ILE LEU LEU ASN ASN          
SEQRES   4 D  190  GLN MET ASP ASP PHE SER ALA LYS PRO GLY VAL PRO ASN          
SEQRES   5 D  190  VAL TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA VAL GLY          
SEQRES   6 D  190  PRO ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 D  190  VAL VAL LYS ASP GLY LYS THR TRP LEU VAL THR GLY SER          
SEQRES   8 D  190  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN MET          
SEQRES   9 D  190  VAL VAL ASN SER ILE ASP TYR GLY LEU ASN VAL ALA GLU          
SEQRES  10 D  190  ALA THR ASN ALA PRO ARG PHE HIS HIS GLN TRP LEU PRO          
SEQRES  11 D  190  ASP GLU LEU ARG VAL GLU LYS GLY PHE SER PRO ASP THR          
SEQRES  12 D  190  LEU LYS LEU LEU GLU ALA LYS GLY GLN LYS VAL ALA LEU          
SEQRES  13 D  190  LYS GLU ALA MET GLY SER THR GLN SER ILE MET VAL GLY          
SEQRES  14 D  190  PRO ASP GLY GLU LEU TYR GLY ALA SER ASP PRO ARG SER          
SEQRES  15 D  190  VAL ASP ASP LEU THR ALA GLY TYR                              
HET    6FY  B 600      20                                                       
HET     CA  B 601       1                                                       
HET    6FY  D 600      20                                                       
HET     CA  D 601       1                                                       
HETNAM     6FY (2~{S})-2-AZANYL-4-[(2~{R})-1-(2-HYDROXY-2-                      
HETNAM   2 6FY  OXOETHYLAMINO)-1-OXIDANYLIDENE-BUTAN-2-                         
HETNAM   3 6FY  YL]OXYPHOSPHONOYL-BUTANOIC ACID                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  6FY    2(C10 H19 N2 O7 P)                                           
FORMUL   6   CA    2(CA 2+)                                                     
FORMUL   9  HOH   *1274(H2 O)                                                   
HELIX    1 AA1 ASP A   55  GLU A   68  1                                  14    
HELIX    2 AA2 ASN A   71  HIS A   87  1                                  17    
HELIX    3 AA3 ASP A  134  THR A  140  1                                   7    
HELIX    4 AA4 SER A  141  SER A  145  5                                   5    
HELIX    5 AA5 GLY A  149  GLY A  162  1                                  14    
HELIX    6 AA6 PRO A  165  GLY A  180  1                                  16    
HELIX    7 AA7 ASN A  184  TYR A  194  1                                  11    
HELIX    8 AA8 GLY A  195  ASN A  201  5                                   7    
HELIX    9 AA9 HIS A  202  PHE A  209  1                                   8    
HELIX   10 AB1 GLN A  224  GLY A  238  1                                  15    
HELIX   11 AB2 PRO A  239  LYS A  244  1                                   6    
HELIX   12 AB3 GLY A  245  ASN A  258  1                                  14    
HELIX   13 AB4 THR A  263  TYR A  270  1                                   8    
HELIX   14 AB5 SER A  295  GLU A  308  1                                  14    
HELIX   15 AB6 ASP A  311  GLY A  316  1                                   6    
HELIX   16 AB7 SER A  319  LEU A  341  1                                  23    
HELIX   17 AB8 PRO A  350  THR A  355  1                                   6    
HELIX   18 AB9 ASN A  356  ASP A  365  1                                  10    
HELIX   19 AC1 PRO A  374  ILE A  378  5                                   5    
HELIX   20 AC2 LEU A  383  GLU A  387  5                                   5    
HELIX   21 AC3 ALA B  420  GLY B  424  5                                   5    
HELIX   22 AC4 ASN B  429  PHE B  434  5                                   6    
HELIX   23 AC5 GLY B  483  SER B  485  5                                   3    
HELIX   24 AC6 ARG B  486  ASP B  500  1                                  15    
HELIX   25 AC7 ASN B  504  ALA B  511  1                                   8    
HELIX   26 AC8 SER B  530  LYS B  540  1                                  11    
HELIX   27 AC9 ASP C   55  GLU C   68  1                                  14    
HELIX   28 AD1 ASN C   71  HIS C   87  1                                  17    
HELIX   29 AD2 ASP C  134  THR C  140  1                                   7    
HELIX   30 AD3 SER C  141  SER C  145  5                                   5    
HELIX   31 AD4 GLY C  149  GLY C  162  1                                  14    
HELIX   32 AD5 PRO C  165  GLY C  180  1                                  16    
HELIX   33 AD6 ASN C  184  TYR C  194  1                                  11    
HELIX   34 AD7 GLY C  195  ASN C  201  5                                   7    
HELIX   35 AD8 HIS C  202  PHE C  209  1                                   8    
HELIX   36 AD9 GLN C  224  GLY C  238  1                                  15    
HELIX   37 AE1 PRO C  239  GLY C  245  1                                   7    
HELIX   38 AE2 GLY C  245  ASN C  258  1                                  14    
HELIX   39 AE3 THR C  263  TYR C  270  1                                   8    
HELIX   40 AE4 SER C  295  ASN C  309  1                                  15    
HELIX   41 AE5 ASP C  311  GLY C  316  1                                   6    
HELIX   42 AE6 SER C  319  LEU C  341  1                                  23    
HELIX   43 AE7 PRO C  350  THR C  355  1                                   6    
HELIX   44 AE8 ASN C  356  ASP C  365  1                                  10    
HELIX   45 AE9 PRO C  374  ILE C  378  5                                   5    
HELIX   46 AF1 LEU C  383  GLU C  387  5                                   5    
HELIX   47 AF2 ALA D  420  GLY D  424  5                                   5    
HELIX   48 AF3 ASN D  429  PHE D  434  5                                   6    
HELIX   49 AF4 GLY D  483  SER D  485  5                                   3    
HELIX   50 AF5 ARG D  486  ASP D  500  1                                  15    
HELIX   51 AF6 ASN D  504  ALA D  511  1                                   8    
HELIX   52 AF7 SER D  530  LYS D  540  1                                  11    
SHEET    1 AA1 7 VAL A  44  ALA A  46  0                                        
SHEET    2 AA1 7 LEU B 564  SER B 568 -1  O  LEU B 564   N  ALA A  46           
SHEET    3 AA1 7 GLN B 554  VAL B 558 -1  N  MET B 557   O  TYR B 565           
SHEET    4 AA1 7 LYS B 474  THR B 479 -1  N  VAL B 478   O  ILE B 556           
SHEET    5 AA1 7 THR B 467  LYS B 471 -1  N  LYS B 471   O  LYS B 474           
SHEET    6 AA1 7 TYR A 285  SER A 289 -1  N  GLN A 286   O  VAL B 470           
SHEET    7 AA1 7 ILE A 278  TYR A 282 -1  N  TYR A 282   O  TYR A 285           
SHEET    1 AA2 7 VAL A 273  ARG A 275  0                                        
SHEET    2 AA2 7 THR A 108  PHE A 113 -1  N  ASP A 112   O  VAL A 273           
SHEET    3 AA2 7 GLY A  96  ARG A 102 -1  N  MET A  99   O  ILE A 111           
SHEET    4 AA2 7 ALA B 403  THR B 409 -1  O  ALA B 405   N  LEU A 100           
SHEET    5 AA2 7 THR B 392  VAL B 397 -1  N  TYR B 394   O  VAL B 406           
SHEET    6 AA2 7 MET A  50  SER A  53 -1  N  MET A  50   O  VAL B 397           
SHEET    7 AA2 7 LEU B 576  GLY B 579 -1  O  ALA B 578   N  VAL A  51           
SHEET    1 AA3 2 PHE A 181  ILE A 182  0                                        
SHEET    2 AA3 2 THR A 221  LEU A 222 -1  O  LEU A 222   N  PHE A 181           
SHEET    1 AA4 2 TRP A 210  LYS A 211  0                                        
SHEET    2 AA4 2 GLU A 214  PRO A 215 -1  O  GLU A 214   N  LYS A 211           
SHEET    1 AA5 3 PHE B 514  HIS B 515  0                                        
SHEET    2 AA5 3 LEU B 523  VAL B 525 -1  O  ARG B 524   N  HIS B 515           
SHEET    3 AA5 3 VAL B 544  LEU B 546  1  O  ALA B 545   N  VAL B 525           
SHEET    1 AA6 7 VAL C  44  ALA C  46  0                                        
SHEET    2 AA6 7 LEU D 564  SER D 568 -1  O  LEU D 564   N  ALA C  46           
SHEET    3 AA6 7 GLN D 554  VAL D 558 -1  N  MET D 557   O  TYR D 565           
SHEET    4 AA6 7 LYS D 474  THR D 479 -1  N  VAL D 478   O  ILE D 556           
SHEET    5 AA6 7 THR D 467  LYS D 471 -1  N  VAL D 469   O  LEU D 477           
SHEET    6 AA6 7 TYR C 285  SER C 289 -1  N  GLN C 286   O  VAL D 470           
SHEET    7 AA6 7 ILE C 278  TYR C 282 -1  N  GLY C 280   O  VAL C 287           
SHEET    1 AA7 7 VAL C 273  ARG C 275  0                                        
SHEET    2 AA7 7 THR C 108  PHE C 113 -1  N  ASP C 112   O  VAL C 273           
SHEET    3 AA7 7 GLY C  96  ARG C 102 -1  N  MET C  99   O  ILE C 111           
SHEET    4 AA7 7 ALA D 403  THR D 409 -1  O  ALA D 405   N  LEU C 100           
SHEET    5 AA7 7 THR D 392  VAL D 397 -1  N  TYR D 394   O  VAL D 406           
SHEET    6 AA7 7 GLY C  49  SER C  53 -1  N  MET C  50   O  VAL D 397           
SHEET    7 AA7 7 LEU D 576  TYR D 580 -1  O  ALA D 578   N  VAL C  51           
SHEET    1 AA8 2 PHE C 181  ILE C 182  0                                        
SHEET    2 AA8 2 THR C 221  LEU C 222 -1  O  LEU C 222   N  PHE C 181           
SHEET    1 AA9 2 TRP C 210  LYS C 211  0                                        
SHEET    2 AA9 2 GLU C 214  PRO C 215 -1  O  GLU C 214   N  LYS C 211           
SHEET    1 AB1 3 PHE D 514  HIS D 515  0                                        
SHEET    2 AB1 3 LEU D 523  VAL D 525 -1  O  ARG D 524   N  HIS D 515           
SHEET    3 AB1 3 VAL D 544  LEU D 546  1  O  ALA D 545   N  LEU D 523           
LINK         OG1 THR B 391                 P8  6FY B 600     1555   1555  1.66  
LINK         O   ASP B 569                CA    CA B 601     1555   1555  2.35  
LINK         O   SER B 572                CA    CA B 601     1555   1555  2.24  
LINK         OD1 ASP B 575                CA    CA B 601     1555   1555  2.34  
LINK         OD2 ASP B 575                CA    CA B 601     1555   1555  2.87  
LINK         OG1 THR D 391                 P8  6FY D 600     1555   1555  1.65  
LINK         O   ASP D 569                CA    CA D 601     1555   1555  2.32  
LINK         O   SER D 572                CA    CA D 601     1555   1555  2.25  
LINK         OD1 ASP D 575                CA    CA D 601     1555   1555  2.38  
LINK         OD2 ASP D 575                CA    CA D 601     1555   1555  2.78  
LINK        CA    CA B 601                 O   HOH B 768     1555   1555  2.44  
LINK        CA    CA B 601                 O   HOH B 836     1555   1555  2.53  
LINK        CA    CA B 601                 O   HOH B 839     1555   1555  2.43  
LINK        CA    CA B 601                 O   HOH B 843     1555   1555  2.61  
LINK        CA    CA D 601                 O   HOH D 837     1555   1555  2.46  
LINK        CA    CA D 601                 O   HOH D 803     1555   1555  2.38  
LINK        CA    CA D 601                 O   HOH D 769     1555   1555  2.39  
LINK        CA    CA D 601                 O   HOH D 840     1555   1555  2.56  
CISPEP   1 PRO A  292    PRO A  293          0        14.26                     
CISPEP   2 LEU B  519    PRO B  520          0        -0.16                     
CISPEP   3 PRO C  292    PRO C  293          0        13.15                     
CISPEP   4 LEU D  519    PRO D  520          0         0.75                     
SITE     1 AC1 16 ARG A 114  THR B 391  ASN B 411  GLN B 430                    
SITE     2 AC1 16 ASP B 433  TYR B 444  SER B 462  SER B 463                    
SITE     3 AC1 16 MET B 464  PRO B 482  GLY B 483  GLY B 484                    
SITE     4 AC1 16 ILE B 487  GLY B 551  HOH B 732  HOH B 805                    
SITE     1 AC2  7 ASP B 569  SER B 572  ASP B 575  HOH B 768                    
SITE     2 AC2  7 HOH B 836  HOH B 839  HOH B 843                               
SITE     1 AC3  7 ASP D 569  SER D 572  ASP D 575  HOH D 769                    
SITE     2 AC3  7 HOH D 803  HOH D 837  HOH D 840                               
SITE     1 AC4 25 ALA C  90  ARG C 114  HOH C 603  THR D 392                    
SITE     2 AC4 25 THR D 407  TYR D 408  THR D 409  ASN D 411                    
SITE     3 AC4 25 THR D 412  THR D 413  GLN D 430  ASP D 433                    
SITE     4 AC4 25 TYR D 444  SER D 462  SER D 463  MET D 464                    
SITE     5 AC4 25 PRO D 482  GLY D 483  GLY D 484  ILE D 487                    
SITE     6 AC4 25 GLY D 551  HOH D 720  HOH D 762  HOH D 810                    
SITE     7 AC4 25 HOH D 822                                                     
CRYST1   77.990  126.388  129.075  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012822  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007912  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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