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LongText Report for: 6kxr-pdb

Name Class
6kxr-pdb
HEADER    HYDROLASE                               12-SEP-19   6KXR              
TITLE     CRYSTAL STRUCTURE OF WILD TYPE ALP1U FROM THE BIOSYNTHESIS OF         
TITLE    2 KINAMYCINS                                                           
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                                                      
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 6KXR    0                                                
JRNL        AUTH   L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG                          
JRNL        TITL   CRYSTAL STRUCTURE OF WILD TYPE ALP1U FROM THE BIOSYNTHESIS   
JRNL        TITL 2 OF KINAMYCINS.                                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.344                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 43053                          
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) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.766                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2052                            
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 70.1867 -  6.0428    0.99     2924   143  0.1355 0.1839        
REMARK   3     2  6.0428 -  4.7967    0.98     2749   135  0.1502 0.1816        
REMARK   3     3  4.7967 -  4.1905    1.00     2795   128  0.1267 0.1937        
REMARK   3     4  4.1905 -  3.8074    1.00     2754   127  0.1380 0.1840        
REMARK   3     5  3.8074 -  3.5345    1.00     2765   141  0.1670 0.2372        
REMARK   3     6  3.5345 -  3.3261    1.00     2724   151  0.1892 0.2595        
REMARK   3     7  3.3261 -  3.1595    1.00     2722   150  0.2132 0.2726        
REMARK   3     8  3.1595 -  3.0220    0.98     2655   143  0.2126 0.3174        
REMARK   3     9  3.0220 -  2.9056    0.99     2717   125  0.2188 0.3275        
REMARK   3    10  2.9056 -  2.8054    1.00     2724   121  0.2091 0.2662        
REMARK   3    11  2.8054 -  2.7177    0.99     2682   154  0.2086 0.2767        
REMARK   3    12  2.7177 -  2.6400    0.99     2679   137  0.2103 0.2831        
REMARK   3    13  2.6400 -  2.5705    0.99     2709   150  0.2105 0.3155        
REMARK   3    14  2.5705 -  2.5077    0.99     2691   124  0.2083 0.3068        
REMARK   3    15  2.5077 -  2.4507    1.00     2711   123  0.2189 0.3099        
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)     : 0.339            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.167           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.28                          
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      :  0.008           9365                                  
REMARK   3   ANGLE     :  1.109          12747                                  
REMARK   3   CHIRALITY :  0.043           1337                                  
REMARK   3   PLANARITY :  0.005           1678                                  
REMARK   3   DIHEDRAL  : 14.567           3342                                  
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 6KXR 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_1300013813.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-18                          
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                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97894                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43063                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.451                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.02819                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.7300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20040                            
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   (%): 37.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
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       48.54500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.71000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.79000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.71000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.54500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.79000            
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: 3090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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: 3210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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     PRO B    26                                                      
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     GLY C   319                                                      
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 465     GLY D   319                                                      
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  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  89    CG   CD   NE   CZ   NH1  NH2                        
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     ARG D  49    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG D  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 297    CG   CD   CE   NZ                                   
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    PRO A  73       75.12   -101.27                                   
REMARK 500    ARG A  98      120.70    -39.41                                   
REMARK 500    ASP A 137     -132.13     57.39                                   
REMARK 500    HIS A 150       58.46   -142.26                                   
REMARK 500    ASP A 161      -46.61     68.63                                   
REMARK 500    ASP A 166     -157.23   -141.64                                   
REMARK 500    ALA A 194      -49.50     72.47                                   
REMARK 500    SER A 215      -52.57   -136.85                                   
REMARK 500    HIS A 300      -48.00   -148.06                                   
REMARK 500    PRO B  73       77.96   -106.29                                   
REMARK 500    LYS B 105       72.97   -118.99                                   
REMARK 500    ASP B 137     -128.88     59.17                                   
REMARK 500    ARG B 155      -75.55    -61.05                                   
REMARK 500    ASP B 161      -37.10     64.68                                   
REMARK 500    ASP B 166     -156.49   -147.35                                   
REMARK 500    THR B 180     -126.58   -108.71                                   
REMARK 500    ALA B 194      -47.01     69.63                                   
REMARK 500    SER B 215      -48.89   -143.90                                   
REMARK 500    HIS B 300      -43.02   -152.83                                   
REMARK 500    ALA C  48      132.85   -178.00                                   
REMARK 500    PRO C  73       73.34   -104.09                                   
REMARK 500    PRO C 106      178.37    -59.28                                   
REMARK 500    ASP C 137     -121.65     57.62                                   
REMARK 500    ARG C 155      -72.55    -58.15                                   
REMARK 500    ASP C 161      -38.57     74.16                                   
REMARK 500    THR C 180     -150.10    -81.09                                   
REMARK 500    ALA C 194      -53.57     78.42                                   
REMARK 500    SER C 215      -60.28   -143.78                                   
REMARK 500    ALA C 295       78.67   -115.84                                   
REMARK 500    LYS C 297        4.26     81.55                                   
REMARK 500    HIS C 300      -39.48   -148.75                                   
REMARK 500    PRO D  73       76.09   -100.68                                   
REMARK 500    ASP D 137     -124.97     59.32                                   
REMARK 500    ASP D 161      -46.56     74.62                                   
REMARK 500    ALA D 194      -48.98     76.86                                   
REMARK 500    SER D 215      -62.27   -141.51                                   
REMARK 500    HIS D 300      -40.47   -158.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT C 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6KXP   RELATED DB: PDB                                   
REMARK 900 W187F/Y247F DOUBLE MUTANT OF ALP1U SOAKED WITH SUBSTRATE FLUOSTATIN  
REMARK 900 C                                                                    
REMARK 900 RELATED ID: 6KXH   RELATED DB: PDB                                   
REMARK 900 Y247F MUTANT OF ALP1U SOAKED WITH THE SUBSTRATE FLUOSTATIN C         
DBREF  6KXR A    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXR B    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXR C    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
DBREF  6KXR D    1   319  UNP    Q1RQU8   Q1RQU8_STRA7     1    319             
SEQADV 6KXR MET A  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY A  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER A  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER A  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER A   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER A   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY A   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR LEU A   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR VAL A   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR PRO A   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR ARG A   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY A   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER A   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS A    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR MET B  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY B  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER B  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER B  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER B   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER B   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY B   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR LEU B   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR VAL B   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR PRO B   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR ARG B   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY B   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER B   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS B    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR MET C  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY C  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER C  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER C  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER C   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER C   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY C   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR LEU C   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR VAL C   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR PRO C   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR ARG C   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY C   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER C   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS C    0  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR MET D  -19  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY D  -18  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER D  -17  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER D  -16  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -15  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -14  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -13  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -12  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -11  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D  -10  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER D   -9  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER D   -8  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY D   -7  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR LEU D   -6  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR VAL D   -5  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR PRO D   -4  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR ARG D   -3  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR GLY D   -2  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR SER D   -1  UNP  Q1RQU8              EXPRESSION TAG                 
SEQADV 6KXR HIS D    0  UNP  Q1RQU8              EXPRESSION TAG                 
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 TYR 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 TYR 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 TYR 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 TYR 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    MLT  C 401      13                                                       
HETNAM     MLT D-MALATE                                                         
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
FORMUL   5  MLT    C4 H6 O5                                                     
FORMUL   6  HOH   *127(H2 O)                                                    
HELIX    1 AA1 SER A   31  SER A   38  1                                   8    
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  GLY A  259  1                                  11    
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  SER B   38  1                                   8    
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  285  1                                  11    
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  SER C   38  1                                   8    
HELIX   34 AD7 THR C   75  ARG C   80  5                                   6    
HELIX   35 AD8 VAL C   82  ARG C   89  1                                   8    
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 TRP C  185  ASN C  190  1                                   6    
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  ALA C  258  1                                  10    
HELIX   46 AF1 THR C  275  ALA C  285  1                                  11    
HELIX   47 AF2 TYR C  301  GLU C  306  1                                   6    
HELIX   48 AF3 GLU C  306  PHE C  318  1                                  13    
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  ALA D  258  1                                  10    
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  PHE D  318  1                                  13    
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 TYR A  90  VAL A  95 -1  O  ALA A  94   N  VAL A  58           
SHEET    4 AA1 8 GLU A  64  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  ALA A 158   N  VAL A 133           
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  ALA B 158   N  VAL B 133           
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  VAL B 293   N  GLY B 269           
SHEET    1 AA3 8 ARG C  44  VAL C  50  0                                        
SHEET    2 AA3 8 VAL C  53  GLY C  60 -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  HIS C 291   N  VAL C 267           
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 TYR D  90  VAL D  95 -1  O  ALA D  94   N  VAL D  58           
SHEET    4 AA4 8 GLU D  64  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 271  1  O  LEU D 268   N  LEU D 159           
SHEET    8 AA4 8 VAL D 290  ARG D 294  1  O  HIS D 291   N  VAL D 267           
CISPEP   1 PRO A   40    GLY A   41          0        -9.27                     
CISPEP   2 TRP A   72    PRO A   73          0       -13.08                     
CISPEP   3 PRO B   40    GLY B   41          0       -11.24                     
CISPEP   4 TRP B   72    PRO B   73          0        -2.56                     
CISPEP   5 PRO C   40    GLY C   41          0        -3.83                     
CISPEP   6 TRP C   72    PRO C   73          0        -6.60                     
CISPEP   7 PRO D   40    GLY D   41          0        -1.72                     
CISPEP   8 TRP D   72    PRO D   73          0        -9.01                     
SITE     1 AC1  7 GLY C 202  ARG C 203  HIS C 206  HOH C 515                    
SITE     2 AC1  7 HOH C 519  GLY D 202  HIS D 206                               
CRYST1   97.090  101.580  117.420  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      0.010300  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009844  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008516        0.00000                         
TER    2281      GLY A 319                                                      
TER    4568      GLY B 319                                                      
TER    6833      PHE C 318                                                      
TER    9101      PHE D 318                                                      
MASTER      494    0    1   64   32    0    2    6 9233    4   13  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
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