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LongText Report for: 6kxh-pdb

Name Class
6kxh-pdb
HEADER    HYDROLASE                               11-SEP-19   6KXH              
TITLE     ALP1U_Y247F MUTANT IN COMPLEX WITH FLUOSTATIN C                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE HYDROLASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: EPOXY HYDROLASE ALP1U;                                      
COMPND   5 EC: 3.3.2.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES AMBOFACIENS (STRAIN ATCC 23877 /   
SOURCE   3 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516);             
SOURCE   4 ORGANISM_TAXID: 278992;                                              
SOURCE   5 GENE: SAMT0137, SAMT0138;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    HYDROLYSE EPOXIDE, CIS-VICINAL DIOL, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG                                   
REVDAT   1   16-SEP-20 6KXH    0                                                
JRNL        AUTH   L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG                          
JRNL        TITL   ALP1U W187F/Y247F MUTANT IN COMPLEX WITH FLUOSTATIN C AND    
JRNL        TITL 2 INTERMEDIATE (SOAKED FLUOSTATIN C FOR 6 HOURS)               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692+SVN                                  
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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.336                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 111737                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.968                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5551                            
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 31.9800 -  5.5229    0.98     3744   176  0.1440 0.1826        
REMARK   3     2  5.5229 -  4.3873    1.00     3668   175  0.1292 0.1674        
REMARK   3     3  4.3873 -  3.8338    1.00     3617   189  0.1296 0.1351        
REMARK   3     4  3.8338 -  3.4837    1.00     3595   178  0.1478 0.1518        
REMARK   3     5  3.4837 -  3.2343    1.00     3605   166  0.1741 0.2393        
REMARK   3     6  3.2343 -  3.0437    1.00     3542   195  0.1872 0.2255        
REMARK   3     7  3.0437 -  2.8914    1.00     3569   192  0.1831 0.2209        
REMARK   3     8  2.8914 -  2.7656    1.00     3531   218  0.1760 0.2187        
REMARK   3     9  2.7656 -  2.6592    1.00     3528   195  0.1760 0.2157        
REMARK   3    10  2.6592 -  2.5675    1.00     3554   184  0.1803 0.2121        
REMARK   3    11  2.5675 -  2.4872    1.00     3543   192  0.1758 0.2030        
REMARK   3    12  2.4872 -  2.4162    1.00     3516   180  0.1895 0.2541        
REMARK   3    13  2.4162 -  2.3526    1.00     3521   186  0.1820 0.2234        
REMARK   3    14  2.3526 -  2.2952    1.00     3581   171  0.1821 0.2209        
REMARK   3    15  2.2952 -  2.2430    1.00     3504   192  0.2270 0.2735        
REMARK   3    16  2.2430 -  2.1953    1.00     3520   197  0.2078 0.2503        
REMARK   3    17  2.1953 -  2.1514    1.00     3491   197  0.1883 0.2396        
REMARK   3    18  2.1514 -  2.1108    1.00     3525   184  0.1823 0.2282        
REMARK   3    19  2.1108 -  2.0731    1.00     3516   172  0.1865 0.2242        
REMARK   3    20  2.0731 -  2.0380    1.00     3535   168  0.1912 0.2106        
REMARK   3    21  2.0380 -  2.0051    1.00     3539   178  0.1856 0.2071        
REMARK   3    22  2.0051 -  1.9743    1.00     3508   192  0.1839 0.2269        
REMARK   3    23  1.9743 -  1.9452    1.00     3500   184  0.1992 0.2373        
REMARK   3    24  1.9452 -  1.9178    1.00     3527   168  0.2418 0.2805        
REMARK   3    25  1.9178 -  1.8919    1.00     3471   200  0.2771 0.3126        
REMARK   3    26  1.8919 -  1.8674    1.00     3549   186  0.1982 0.2329        
REMARK   3    27  1.8674 -  1.8440    1.00     3498   190  0.2014 0.2559        
REMARK   3    28  1.8440 -  1.8218    1.00     3508   189  0.2110 0.2543        
REMARK   3    29  1.8218 -  1.8006    1.00     3477   190  0.2128 0.2757        
REMARK   3    30  1.8006 -  1.7804    0.98     3404   167  0.2262 0.2846        
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)     : 0.176            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.09                          
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           9515                                  
REMARK   3   ANGLE     :  1.087          12984                                  
REMARK   3   CHIRALITY :  0.047           1353                                  
REMARK   3   PLANARITY :  0.005           1796                                  
REMARK   3   DIHEDRAL  : 12.648           3448                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7114 -26.4759  43.6857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1871 T22:   0.1371                                     
REMARK   3      T33:   0.2334 T12:   0.0021                                     
REMARK   3      T13:   0.0449 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5685 L22:   0.2810                                     
REMARK   3      L33:   0.8803 L12:  -0.0615                                     
REMARK   3      L13:   0.5101 L23:  -0.1929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0087 S12:   0.0372 S13:   0.0691                       
REMARK   3      S21:   0.0266 S22:  -0.0224 S23:  -0.0328                       
REMARK   3      S31:  -0.0961 S32:   0.0963 S33:   0.0245                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '                   
REMARK   3     SELECTION          : CHAIN 'B' AND SEGID 'BA '                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '                   
REMARK   3     SELECTION          : CHAIN 'C' AND SEGID 'CA '                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '                   
REMARK   3     SELECTION          : CHAIN 'D' AND SEGID 'DA '                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013505.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97853                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111803                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 1.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.1800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MMT PH5.0, 25% PEG 1500, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
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       48.73850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.74050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.78100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.74050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.73850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.78100            
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: 3540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 3590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     VAL B    13                                                      
REMARK 465     THR B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     SER C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     ALA C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     HIS C    21                                                      
REMARK 465     PRO C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     HIS C    25                                                      
REMARK 465     PRO C    26                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     VAL D    13                                                      
REMARK 465     THR D    14                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     SER D    16                                                      
REMARK 465     PRO D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     ALA D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     HIS D    21                                                      
REMARK 465     PRO D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     HIS D    25                                                      
REMARK 465     PRO D    26                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 274    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 124    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C 274    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 277    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 277    CG   CD   OE1  OE2                                  
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 B   277     NH2  ARG B   280              2.01            
REMARK 500   O    HOH C   528     O    HOH D   645              2.07            
REMARK 500   O    HOH C   503     O    HOH C   507              2.08            
REMARK 500   OG1  THR C   183     O    HOH C   501              2.09            
REMARK 500   O    THR B   264     O    HOH B   501              2.11            
REMARK 500   O6   DY9 C   402     O    HOH C   502              2.12            
REMARK 500   SD   MET B    83     O    HOH B   690              2.14            
REMARK 500   O    HOH A   502     O    HOH A   545              2.14            
REMARK 500   OD2  ASP A   161     O    HOH A   501              2.15            
REMARK 500   OE2  GLU A   277     NH2  ARG A   280              2.16            
REMARK 500   O    HOH B   533     O    HOH B   620              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   NH2  ARG D    88     O    HOH C   560     4546     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 105       76.24   -119.81                                   
REMARK 500    ASP A 137     -133.40     63.37                                   
REMARK 500    ASP A 161      -40.61     71.09                                   
REMARK 500    THR A 180     -121.92    -92.25                                   
REMARK 500    LEU A 184       49.10    -80.75                                   
REMARK 500    ALA A 194      -52.36     72.89                                   
REMARK 500    SER A 215      -53.56   -145.37                                   
REMARK 500    HIS A 300      -41.05   -151.48                                   
REMARK 500    ASP B 137     -133.36     62.97                                   
REMARK 500    ASP B 161      -40.65     70.83                                   
REMARK 500    THR B 180     -125.28   -120.54                                   
REMARK 500    ALA B 194      -50.58     72.08                                   
REMARK 500    SER B 215      -51.83   -144.46                                   
REMARK 500    HIS B 300      -41.78   -152.64                                   
REMARK 500    ASP C 137     -133.26     61.47                                   
REMARK 500    ASP C 161      -40.88     73.82                                   
REMARK 500    THR C 180       23.09   -153.93                                   
REMARK 500    ALA C 194      -50.18     71.91                                   
REMARK 500    SER C 215      -53.62   -144.42                                   
REMARK 500    HIS C 300      -43.28   -150.44                                   
REMARK 500    ASP D 137     -133.38     62.67                                   
REMARK 500    ASP D 161      -40.99     72.84                                   
REMARK 500    ALA D 194      -51.14     71.63                                   
REMARK 500    SER D 215      -54.80   -144.32                                   
REMARK 500    HIS D 300      -43.38   -152.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 197   OE2                                                    
REMARK 620 2 HOH C 548   O   117.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 197   OE2                                                    
REMARK 620 2 HOH D 553   O   116.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT D 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6KXC   RELATED DB: PDB                                   
DBREF  6KXH A    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXH B    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXH C    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXH D    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
SEQADV 6KXH MET A  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY A  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER A  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER A  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER A   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER A   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY A   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH LEU A   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH VAL A   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PRO A   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH ARG A   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY A   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER A   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS A    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PHE A  247  UNP  Q1RQU8    TYR   247 ENGINEERED MUTATION            
SEQADV 6KXH MET B  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY B  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER B  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER B  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER B   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER B   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY B   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH LEU B   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH VAL B   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PRO B   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH ARG B   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY B   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER B   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS B    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PHE B  247  UNP  Q1RQU8    TYR   247 ENGINEERED MUTATION            
SEQADV 6KXH MET C  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY C  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER C  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER C  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER C   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER C   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY C   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH LEU C   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH VAL C   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PRO C   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH ARG C   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY C   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER C   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS C    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PHE C  247  UNP  Q1RQU8    TYR   247 ENGINEERED MUTATION            
SEQADV 6KXH MET D  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY D  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER D  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER D  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER D   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER D   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY D   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH LEU D   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH VAL D   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PRO D   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH ARG D   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH GLY D   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH SER D   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH HIS D    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXH PHE D  247  UNP  Q1RQU8    TYR   247 ENGINEERED MUTATION            
SEQRES   1 A  339  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  339  LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR          
SEQRES   3 A  339  GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA          
SEQRES   4 A  339  ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP          
SEQRES   5 A  339  ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER          
SEQRES   6 A  339  ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL          
SEQRES   7 A  339  SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY          
SEQRES   8 A  339  TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO          
SEQRES   9 A  339  GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU          
SEQRES  10 A  339  ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR          
SEQRES  11 A  339  ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL          
SEQRES  12 A  339  ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS          
SEQRES  13 A  339  ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN          
SEQRES  14 A  339  HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR          
SEQRES  15 A  339  PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU          
SEQRES  16 A  339  CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP TRP ALA          
SEQRES  17 A  339  PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS          
SEQRES  18 A  339  GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN          
SEQRES  19 A  339  SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG          
SEQRES  20 A  339  ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL          
SEQRES  21 A  339  ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP          
SEQRES  22 A  339  ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO          
SEQRES  23 A  339  VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU          
SEQRES  24 A  339  ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET          
SEQRES  25 A  339  VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU          
SEQRES  26 A  339  GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE          
SEQRES  27 A  339  GLY                                                          
SEQRES   1 B  339  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  339  LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR          
SEQRES   3 B  339  GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA          
SEQRES   4 B  339  ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP          
SEQRES   5 B  339  ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER          
SEQRES   6 B  339  ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL          
SEQRES   7 B  339  SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY          
SEQRES   8 B  339  TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO          
SEQRES   9 B  339  GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU          
SEQRES  10 B  339  ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR          
SEQRES  11 B  339  ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL          
SEQRES  12 B  339  ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS          
SEQRES  13 B  339  ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN          
SEQRES  14 B  339  HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR          
SEQRES  15 B  339  PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU          
SEQRES  16 B  339  CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP TRP ALA          
SEQRES  17 B  339  PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS          
SEQRES  18 B  339  GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN          
SEQRES  19 B  339  SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG          
SEQRES  20 B  339  ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL          
SEQRES  21 B  339  ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP          
SEQRES  22 B  339  ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO          
SEQRES  23 B  339  VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU          
SEQRES  24 B  339  ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET          
SEQRES  25 B  339  VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU          
SEQRES  26 B  339  GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE          
SEQRES  27 B  339  GLY                                                          
SEQRES   1 C  339  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  339  LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR          
SEQRES   3 C  339  GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA          
SEQRES   4 C  339  ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP          
SEQRES   5 C  339  ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER          
SEQRES   6 C  339  ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL          
SEQRES   7 C  339  SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY          
SEQRES   8 C  339  TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO          
SEQRES   9 C  339  GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU          
SEQRES  10 C  339  ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR          
SEQRES  11 C  339  ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL          
SEQRES  12 C  339  ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS          
SEQRES  13 C  339  ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN          
SEQRES  14 C  339  HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR          
SEQRES  15 C  339  PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU          
SEQRES  16 C  339  CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP TRP ALA          
SEQRES  17 C  339  PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS          
SEQRES  18 C  339  GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN          
SEQRES  19 C  339  SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG          
SEQRES  20 C  339  ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL          
SEQRES  21 C  339  ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP          
SEQRES  22 C  339  ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO          
SEQRES  23 C  339  VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU          
SEQRES  24 C  339  ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET          
SEQRES  25 C  339  VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU          
SEQRES  26 C  339  GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE          
SEQRES  27 C  339  GLY                                                          
SEQRES   1 D  339  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  339  LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR          
SEQRES   3 D  339  GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA          
SEQRES   4 D  339  ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP          
SEQRES   5 D  339  ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER          
SEQRES   6 D  339  ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL          
SEQRES   7 D  339  SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY          
SEQRES   8 D  339  TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO          
SEQRES   9 D  339  GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU          
SEQRES  10 D  339  ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR          
SEQRES  11 D  339  ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL          
SEQRES  12 D  339  ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS          
SEQRES  13 D  339  ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN          
SEQRES  14 D  339  HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR          
SEQRES  15 D  339  PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU          
SEQRES  16 D  339  CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP TRP ALA          
SEQRES  17 D  339  PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS          
SEQRES  18 D  339  GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN          
SEQRES  19 D  339  SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG          
SEQRES  20 D  339  ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL          
SEQRES  21 D  339  ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP          
SEQRES  22 D  339  ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO          
SEQRES  23 D  339  VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU          
SEQRES  24 D  339  ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET          
SEQRES  25 D  339  VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU          
SEQRES  26 D  339  GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE          
SEQRES  27 D  339  GLY                                                          
HET    DY9  A 401      36                                                       
HET    MLT  A 402      13                                                       
HET     NA  B 401       1                                                       
HET    DY9  B 402      36                                                       
HET     NA  C 401       1                                                       
HET    DY9  C 402      36                                                       
HET     NA  D 401       1                                                       
HET    DY9  D 402      36                                                       
HET    MLT  D 403      13                                                       
HETNAM     DY9 FLUOSTATIN C                                                     
HETNAM     MLT D-MALATE                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
FORMUL   5  DY9    4(C18 H12 O6)                                                
FORMUL   6  MLT    2(C4 H6 O5)                                                  
FORMUL   7   NA    3(NA 1+)                                                     
FORMUL  14  HOH   *770(H2 O)                                                    
HELIX    1 AA1 SER A   31  LEU A   39  1                                   9    
HELIX    2 AA2 THR A   75  ARG A   80  5                                   6    
HELIX    3 AA3 VAL A   82  ARG A   88  1                                   7    
HELIX    4 AA4 ASP A  111  LEU A  126  1                                  16    
HELIX    5 AA5 ASP A  137  HIS A  150  1                                  14    
HELIX    6 AA6 ASP A  166  MET A  172  5                                   7    
HELIX    7 AA7 LEU A  184  ASN A  190  1                                   7    
HELIX    8 AA8 ALA A  194  HIS A  201  1                                   8    
HELIX    9 AA9 ARG A  203  ASN A  214  1                                  12    
HELIX   10 AB1 ASP A  218  VAL A  222  5                                   5    
HELIX   11 AB2 GLY A  223  ASN A  235  1                                  13    
HELIX   12 AB3 SER A  236  ALA A  249  1                                  14    
HELIX   13 AB4 ALA A  249  TYR A  260  1                                  12    
HELIX   14 AB5 THR A  275  ALA A  287  1                                  13    
HELIX   15 AB6 TYR A  301  GLU A  306  1                                   6    
HELIX   16 AB7 GLU A  306  GLY A  319  1                                  14    
HELIX   17 AB8 SER B   31  LEU B   39  1                                   9    
HELIX   18 AB9 THR B   75  ARG B   80  5                                   6    
HELIX   19 AC1 VAL B   82  ARG B   88  1                                   7    
HELIX   20 AC2 ASP B  111  LEU B  126  1                                  16    
HELIX   21 AC3 ASP B  137  HIS B  150  1                                  14    
HELIX   22 AC4 ASP B  166  MET B  172  5                                   7    
HELIX   23 AC5 LEU B  184  ASN B  190  1                                   7    
HELIX   24 AC6 ALA B  194  HIS B  201  1                                   8    
HELIX   25 AC7 ARG B  203  ASN B  214  1                                  12    
HELIX   26 AC8 ASP B  218  VAL B  222  5                                   5    
HELIX   27 AC9 GLY B  223  ASN B  235  1                                  13    
HELIX   28 AD1 SER B  236  ALA B  249  1                                  14    
HELIX   29 AD2 ALA B  249  GLY B  259  1                                  11    
HELIX   30 AD3 THR B  275  ALA B  287  1                                  13    
HELIX   31 AD4 TYR B  301  GLU B  306  1                                   6    
HELIX   32 AD5 GLU B  306  GLY B  319  1                                  14    
HELIX   33 AD6 SER C   31  LEU C   39  1                                   9    
HELIX   34 AD7 THR C   75  ARG C   80  5                                   6    
HELIX   35 AD8 VAL C   82  ARG C   88  1                                   7    
HELIX   36 AD9 ASP C  111  LEU C  126  1                                  16    
HELIX   37 AE1 ASP C  137  HIS C  150  1                                  14    
HELIX   38 AE2 ASP C  166  MET C  172  5                                   7    
HELIX   39 AE3 LEU C  184  ASN C  190  1                                   7    
HELIX   40 AE4 ALA C  194  HIS C  201  1                                   8    
HELIX   41 AE5 ARG C  203  ASN C  214  1                                  12    
HELIX   42 AE6 ASP C  218  VAL C  222  5                                   5    
HELIX   43 AE7 GLY C  223  ASN C  235  1                                  13    
HELIX   44 AE8 SER C  236  ALA C  249  1                                  14    
HELIX   45 AE9 ALA C  249  GLY C  259  1                                  11    
HELIX   46 AF1 THR C  275  ALA C  287  1                                  13    
HELIX   47 AF2 TYR C  301  GLU C  306  1                                   6    
HELIX   48 AF3 GLU C  306  GLY C  319  1                                  14    
HELIX   49 AF4 SER D   31  LEU D   39  1                                   9    
HELIX   50 AF5 THR D   75  ARG D   80  5                                   6    
HELIX   51 AF6 VAL D   82  ARG D   88  1                                   7    
HELIX   52 AF7 ASP D  111  LEU D  126  1                                  16    
HELIX   53 AF8 ASP D  137  HIS D  150  1                                  14    
HELIX   54 AF9 ASP D  166  MET D  172  5                                   7    
HELIX   55 AG1 LEU D  184  ASN D  190  1                                   7    
HELIX   56 AG2 ALA D  194  HIS D  201  1                                   8    
HELIX   57 AG3 ARG D  203  ASN D  214  1                                  12    
HELIX   58 AG4 ASP D  218  VAL D  222  5                                   5    
HELIX   59 AG5 GLY D  223  ASN D  235  1                                  13    
HELIX   60 AG6 SER D  236  ALA D  249  1                                  14    
HELIX   61 AG7 ALA D  249  TYR D  260  1                                  12    
HELIX   62 AG8 THR D  275  ALA D  287  1                                  13    
HELIX   63 AG9 TYR D  301  GLU D  306  1                                   6    
HELIX   64 AH1 GLU D  306  GLY D  319  1                                  14    
SHEET    1 AA1 8 ARG A  44  VAL A  50  0                                        
SHEET    2 AA1 8 VAL A  53  GLY A  60 -1  O  TYR A  57   N  ARG A  46           
SHEET    3 AA1 8 HIS A  91  VAL A  95 -1  O  ALA A  94   N  VAL A  58           
SHEET    4 AA1 8 PRO A  65  VAL A  69  1  N  LEU A  66   O  ILE A  93           
SHEET    5 AA1 8 VAL A 131  HIS A 136  1  O  ASN A 132   N  LEU A  67           
SHEET    6 AA1 8 THR A 154  LEU A 160  1  O  LEU A 160   N  GLY A 135           
SHEET    7 AA1 8 VAL A 267  GLY A 272  1  O  LEU A 268   N  LEU A 159           
SHEET    8 AA1 8 VAL A 290  ALA A 295  1  O  ALA A 295   N  GLY A 271           
SHEET    1 AA2 8 ARG B  44  VAL B  50  0                                        
SHEET    2 AA2 8 VAL B  53  GLY B  60 -1  O  TYR B  57   N  ARG B  46           
SHEET    3 AA2 8 TYR B  90  VAL B  95 -1  O  ALA B  94   N  VAL B  58           
SHEET    4 AA2 8 GLU B  64  VAL B  69  1  N  LEU B  66   O  ILE B  93           
SHEET    5 AA2 8 VAL B 131  HIS B 136  1  O  ASN B 132   N  LEU B  67           
SHEET    6 AA2 8 THR B 154  LEU B 160  1  O  LEU B 160   N  GLY B 135           
SHEET    7 AA2 8 VAL B 267  GLY B 272  1  O  LEU B 268   N  LEU B 159           
SHEET    8 AA2 8 VAL B 290  ALA B 295  1  O  ALA B 295   N  GLY B 271           
SHEET    1 AA3 8 ARG C  44  VAL C  50  0                                        
SHEET    2 AA3 8 VAL C  53  GLY C  61 -1  O  TYR C  57   N  ARG C  46           
SHEET    3 AA3 8 TYR C  90  VAL C  95 -1  O  ALA C  94   N  VAL C  58           
SHEET    4 AA3 8 GLU C  64  VAL C  69  1  N  LEU C  66   O  ILE C  93           
SHEET    5 AA3 8 VAL C 131  HIS C 136  1  O  ASN C 132   N  LEU C  67           
SHEET    6 AA3 8 THR C 154  LEU C 160  1  O  LEU C 160   N  GLY C 135           
SHEET    7 AA3 8 VAL C 267  GLY C 272  1  O  LEU C 268   N  LEU C 159           
SHEET    8 AA3 8 VAL C 290  ALA C 295  1  O  ALA C 295   N  GLY C 271           
SHEET    1 AA4 8 ARG D  44  VAL D  50  0                                        
SHEET    2 AA4 8 VAL D  53  GLY D  60 -1  O  LEU D  55   N  ALA D  48           
SHEET    3 AA4 8 HIS D  91  VAL D  95 -1  O  ALA D  94   N  VAL D  58           
SHEET    4 AA4 8 PRO D  65  VAL D  69  1  N  LEU D  66   O  ILE D  93           
SHEET    5 AA4 8 VAL D 131  HIS D 136  1  O  ASN D 132   N  LEU D  67           
SHEET    6 AA4 8 THR D 154  LEU D 160  1  O  LEU D 160   N  GLY D 135           
SHEET    7 AA4 8 VAL D 267  GLY D 272  1  O  LEU D 268   N  LEU D 159           
SHEET    8 AA4 8 VAL D 290  ALA D 295  1  O  ALA D 295   N  GLY D 271           
LINK         OE2 GLU C 197                NA    NA C 401     1555   1555  2.79  
LINK        NA    NA C 401                 O   HOH C 548     1555   1555  2.80  
LINK         OE2 GLU D 197                NA    NA D 401     1555   1555  2.81  
LINK        NA    NA D 401                 O   HOH D 553     1555   1555  2.88  
CISPEP   1 TRP A   72    PRO A   73          0       -13.05                     
CISPEP   2 TRP B   72    PRO B   73          0       -14.05                     
CISPEP   3 TRP C   72    PRO C   73          0       -12.09                     
CISPEP   4 THR C  180    GLY C  181          0        -3.55                     
CISPEP   5 TRP D   72    PRO D   73          0       -13.15                     
SITE     1 AC1 15 TRP A  72  ASP A 137  MET A 141  THR A 162                    
SITE     2 AC1 15 TRP A 186  TRP A 187  LEU A 211  ASN A 214                    
SITE     3 AC1 15 PHE A 247  VAL A 299  HIS A 300  TYR A 301                    
SITE     4 AC1 15 HOH A 501  HOH A 508  HOH A 535                               
SITE     1 AC2 11 HIS A 201  GLY A 202  ASN A 235  PRO A 237                    
SITE     2 AC2 11 HOH A 539  HOH A 565  HOH A 650  HOH A 700                    
SITE     3 AC2 11 ARG C 205  GLN C 219  ARG C 227                               
SITE     1 AC3  3 ARG B  37  ARG B  44  SER B  45                               
SITE     1 AC4 17 TRP B  72  ASP B 137  MET B 141  THR B 162                    
SITE     2 AC4 17 TRP B 186  TRP B 187  LEU B 211  ASN B 214                    
SITE     3 AC4 17 PHE B 247  VAL B 299  HIS B 300  TYR B 301                    
SITE     4 AC4 17 HOH B 505  HOH B 514  HOH B 563  HOH B 632                    
SITE     5 AC4 17 HOH B 634                                                     
SITE     1 AC5  4 ALA C 194  PRO C 196  GLU C 197  HOH C 548                    
SITE     1 AC6 15 TRP C  72  ASP C 137  MET C 141  TRP C 186                    
SITE     2 AC6 15 TRP C 187  LEU C 211  ASN C 214  SER C 215                    
SITE     3 AC6 15 PHE C 247  VAL C 299  HIS C 300  TYR C 301                    
SITE     4 AC6 15 HOH C 502  HOH C 504  HOH C 517                               
SITE     1 AC7  4 ALA D 194  PRO D 196  GLU D 197  HOH D 553                    
SITE     1 AC8 15 TRP D  72  ASP D 137  MET D 141  THR D 162                    
SITE     2 AC8 15 TRP D 186  TRP D 187  LEU D 211  ASN D 214                    
SITE     3 AC8 15 PHE D 247  HIS D 300  TYR D 301  HOH D 506                    
SITE     4 AC8 15 HOH D 507  HOH D 520  HOH D 551                               
SITE     1 AC9 13 HIS B 201  GLY B 202  ASN B 235  PRO B 237                    
SITE     2 AC9 13 HOH B 510  HOH B 608  ARG D 205  GLN D 219                    
SITE     3 AC9 13 VAL D 222  GLY D 223  ASP D 224  ARG D 227                    
SITE     4 AC9 13 HOH D 557                                                     
CRYST1   97.477  101.562  117.481  90.00  90.00  90.00 P 21 21 21   16          
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      0.010259  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008512        0.00000                         
TER    2296      GLY A 319                                                      
TER    4589      GLY B 319                                                      
TER    6853      GLY C 319                                                      
TER    9129      GLY D 319                                                      
MASTER      610    0    9   64   32    0   27    6 9996    4  176  108          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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