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LongText Report for: 4H18-pdb

Name Class
4H18-pdb
HEADER    TRANSFERASE                             10-SEP-12   4H18              
TITLE     THREE DIMENSIONAL STRUCTURE OF CORYNOMYCOLOYL TRANFERASE C            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CMT1;                                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HYPOTHETICAL ESTERASE, PUTATIVE UNCHARACTERIZED PROTEIN     
COMPND   5 CGL0343, TREHALOSE CORYNOMYCOLYL TRANSFERASE;                        
COMPND   6 EC: 2.3.1.122;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;                     
SOURCE   3 ORGANISM_TAXID: 196627;                                              
SOURCE   4 STRAIN: ATCC 13032;                                                  
SOURCE   5 GENE: CMT1, CMT1, CG0413, CGL0343, WA5_0336;                         
SOURCE   6 EXPRESSION_SYSTEM: CORYNEBACTERIUM GLUTAMICUM;                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 196627;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCGL482                                   
KEYWDS    ALPHA / BETA HYDROLASE, MYCOLOYLTRANSFERASE, TREHALOSE O-             
KEYWDS   2 MYCOLYLTRANSFERASE, EXTERNAL MEMBRANE, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.HUC,C.DE SOUSA D'AURIA,I.LI DE LA SIERRA-GALLAY,CH.SALMERON,H.VAN   
AUTHOR   2 TILBEURGH,N.BAYAN,CH.HOUSSIN,M.DAFFE,M.TROPIS                        
REVDAT   1   25-SEP-13 4H18    0                                                
JRNL        AUTH   E.HUC,C.DE SOUSA-D'AURIA,I.L.DE LA SIERRA-GALLAY,C.SALMERON, 
JRNL        AUTH 2 H.VAN TILBEURGH,N.BAYAN,C.HOUSSIN,M.DAFFE,M.TROPIS           
JRNL        TITL   IDENTIFICATION OF A MYCOLOYL TRANSFERASE SELECTIVELY         
JRNL        TITL 2 INVOLVED IN O-ACYLATION OF POLYPEPTIDES IN                   
JRNL        TITL 3 CORYNEBACTERIALES.                                           
JRNL        REF    J.BACTERIOL.                  V. 195  4121 2013              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   23852866                                                     
JRNL        DOI    10.1128/JB.00285-13                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 128479                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6424                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.6549 -  5.4474    0.97     4258   224  0.1701 0.1591        
REMARK   3     2  5.4474 -  4.3258    0.99     4164   219  0.1408 0.1669        
REMARK   3     3  4.3258 -  3.7796    0.99     4119   217  0.1344 0.1651        
REMARK   3     4  3.7796 -  3.4342    0.99     4084   215  0.1500 0.1934        
REMARK   3     5  3.4342 -  3.1882    0.99     4129   218  0.1564 0.1858        
REMARK   3     6  3.1882 -  3.0003    0.99     4090   215  0.1611 0.1906        
REMARK   3     7  3.0003 -  2.8501    0.99     4091   215  0.1644 0.1925        
REMARK   3     8  2.8501 -  2.7261    1.00     4082   215  0.1675 0.2123        
REMARK   3     9  2.7261 -  2.6212    1.00     4075   214  0.1663 0.2180        
REMARK   3    10  2.6212 -  2.5308    1.00     4064   214  0.1645 0.2065        
REMARK   3    11  2.5308 -  2.4516    1.00     4074   215  0.1615 0.2125        
REMARK   3    12  2.4516 -  2.3816    1.00     4064   214  0.1601 0.2179        
REMARK   3    13  2.3816 -  2.3189    1.00     4078   214  0.1593 0.2000        
REMARK   3    14  2.3189 -  2.2623    1.00     4067   214  0.1622 0.2013        
REMARK   3    15  2.2623 -  2.2109    1.00     4062   214  0.1612 0.2219        
REMARK   3    16  2.2109 -  2.1639    1.00     4052   213  0.1590 0.2116        
REMARK   3    17  2.1639 -  2.1206    1.00     4044   213  0.1596 0.2112        
REMARK   3    18  2.1206 -  2.0806    1.00     4068   214  0.1625 0.2212        
REMARK   3    19  2.0806 -  2.0434    1.00     4022   212  0.1606 0.2149        
REMARK   3    20  2.0434 -  2.0088    1.00     4034   212  0.1591 0.2210        
REMARK   3    21  2.0088 -  1.9764    1.00     4075   215  0.1678 0.2126        
REMARK   3    22  1.9764 -  1.9460    1.00     4027   212  0.1727 0.2163        
REMARK   3    23  1.9460 -  1.9173    1.00     4056   213  0.1729 0.2444        
REMARK   3    24  1.9173 -  1.8903    1.00     4076   215  0.1849 0.2440        
REMARK   3    25  1.8903 -  1.8648    1.00     4012   211  0.1896 0.2509        
REMARK   3    26  1.8648 -  1.8406    1.00     4059   214  0.1904 0.2430        
REMARK   3    27  1.8406 -  1.8176    1.00     4020   211  0.1968 0.2589        
REMARK   3    28  1.8176 -  1.7957    1.00     4058   214  0.2085 0.2745        
REMARK   3    29  1.7957 -  1.7748    1.00     4049   213  0.2256 0.2637        
REMARK   3    30  1.7748 -  1.7550    0.97     3902   205  0.2391 0.2834        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           9832                                  
REMARK   3   ANGLE     :  1.386          13435                                  
REMARK   3   CHIRALITY :  0.096           1439                                  
REMARK   3   PLANARITY :  0.008           1761                                  
REMARK   3   DIHEDRAL  : 14.003           3483                                  
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 4H18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074890.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 128495                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.755                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.811                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.890                              
REMARK 200  R MERGE                    (I) : 0.15400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.4600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.91                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
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: 1VA5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M MAGNESIUM CHLORIDE,   
REMARK 280  0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       42.90200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       95.34400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.90200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       95.34400            
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, 3, 4, 5, 6, 7                                     
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       42.90200            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       95.34400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       78.49700            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       42.90200            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       95.34400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000       42.90200            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000       95.34400            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000       78.49700            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       42.90200            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       95.34400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 434  LIES ON A SPECIAL POSITION.                          
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     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     ILE A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     ILE A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     SER A   281                                                      
REMARK 465     VAL A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     PRO A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     PHE A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     GLN A   292                                                      
REMARK 465     GLN A   293                                                      
REMARK 465     VAL A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     SER A   296                                                      
REMARK 465     ILE A   297                                                      
REMARK 465     ALA A   298                                                      
REMARK 465     MET A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     THR A   302                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     VAL A   304                                                      
REMARK 465     ALA A   365                                                      
REMARK 465     HIS A   366                                                      
REMARK 465     HIS A   367                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ILE B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     MET B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     ILE B    21                                                      
REMARK 465     VAL B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     GLY B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     SER B   281                                                      
REMARK 465     VAL B   282                                                      
REMARK 465     ASP B   283                                                      
REMARK 465     SER B   284                                                      
REMARK 465     PRO B   285                                                      
REMARK 465     ARG B   286                                                      
REMARK 465     PHE B   287                                                      
REMARK 465     GLU B   288                                                      
REMARK 465     GLY B   289                                                      
REMARK 465     LEU B   290                                                      
REMARK 465     ASN B   291                                                      
REMARK 465     GLN B   292                                                      
REMARK 465     GLN B   293                                                      
REMARK 465     VAL B   294                                                      
REMARK 465     GLN B   295                                                      
REMARK 465     SER B   296                                                      
REMARK 465     ILE B   297                                                      
REMARK 465     ALA B   298                                                      
REMARK 465     MET B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     GLU B   301                                                      
REMARK 465     THR B   302                                                      
REMARK 465     VAL B   303                                                      
REMARK 465     VAL B   304                                                      
REMARK 465     GLU B   364                                                      
REMARK 465     ALA B   365                                                      
REMARK 465     HIS B   366                                                      
REMARK 465     HIS B   367                                                      
REMARK 465     HIS B   368                                                      
REMARK 465     HIS B   369                                                      
REMARK 465     HIS B   370                                                      
REMARK 465     HIS B   371                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     ILE C    12                                                      
REMARK 465     ALA C    13                                                      
REMARK 465     LEU C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     ILE C    16                                                      
REMARK 465     ALA C    17                                                      
REMARK 465     MET C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     THR C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     LEU C   275                                                      
REMARK 465     ALA C   276                                                      
REMARK 465     GLY C   277                                                      
REMARK 465     GLU C   278                                                      
REMARK 465     TRP C   279                                                      
REMARK 465     GLU C   280                                                      
REMARK 465     SER C   281                                                      
REMARK 465     VAL C   282                                                      
REMARK 465     ASP C   283                                                      
REMARK 465     SER C   284                                                      
REMARK 465     PRO C   285                                                      
REMARK 465     ARG C   286                                                      
REMARK 465     PHE C   287                                                      
REMARK 465     GLU C   288                                                      
REMARK 465     GLY C   289                                                      
REMARK 465     LEU C   290                                                      
REMARK 465     ASN C   291                                                      
REMARK 465     GLN C   292                                                      
REMARK 465     GLN C   293                                                      
REMARK 465     VAL C   294                                                      
REMARK 465     GLN C   295                                                      
REMARK 465     SER C   296                                                      
REMARK 465     ILE C   297                                                      
REMARK 465     ALA C   298                                                      
REMARK 465     MET C   299                                                      
REMARK 465     ALA C   300                                                      
REMARK 465     THR C   338                                                      
REMARK 465     GLY C   339                                                      
REMARK 465     THR C   340                                                      
REMARK 465     ALA C   365                                                      
REMARK 465     HIS C   366                                                      
REMARK 465     HIS C   367                                                      
REMARK 465     HIS C   368                                                      
REMARK 465     HIS C   369                                                      
REMARK 465     HIS C   370                                                      
REMARK 465     HIS C   371                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     ALA D    11                                                      
REMARK 465     ILE D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     LEU D    14                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     ILE D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     MET D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     THR D    20                                                      
REMARK 465     ILE D    21                                                      
REMARK 465     VAL D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     THR D    26                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     GLY D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     LEU D   275                                                      
REMARK 465     ALA D   276                                                      
REMARK 465     GLY D   277                                                      
REMARK 465     GLU D   278                                                      
REMARK 465     TRP D   279                                                      
REMARK 465     GLU D   280                                                      
REMARK 465     SER D   281                                                      
REMARK 465     VAL D   282                                                      
REMARK 465     ASP D   283                                                      
REMARK 465     SER D   284                                                      
REMARK 465     PRO D   285                                                      
REMARK 465     ARG D   286                                                      
REMARK 465     PHE D   287                                                      
REMARK 465     GLU D   288                                                      
REMARK 465     GLY D   289                                                      
REMARK 465     LEU D   290                                                      
REMARK 465     ASN D   291                                                      
REMARK 465     GLN D   292                                                      
REMARK 465     GLN D   293                                                      
REMARK 465     VAL D   294                                                      
REMARK 465     GLN D   295                                                      
REMARK 465     SER D   296                                                      
REMARK 465     ILE D   297                                                      
REMARK 465     ALA D   298                                                      
REMARK 465     MET D   299                                                      
REMARK 465     ALA D   300                                                      
REMARK 465     GLY D   339                                                      
REMARK 465     THR D   340                                                      
REMARK 465     GLU D   364                                                      
REMARK 465     ALA D   365                                                      
REMARK 465     HIS D   366                                                      
REMARK 465     HIS D   367                                                      
REMARK 465     HIS D   368                                                      
REMARK 465     HIS D   369                                                      
REMARK 465     HIS D   370                                                      
REMARK 465     HIS D   371                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG C  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG C  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
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    TYR A 144       14.39     52.39                                   
REMARK 500    SER A 189     -121.82     62.49                                   
REMARK 500    THR A 218       -7.95   -142.84                                   
REMARK 500    SER A 342     -174.78    -66.34                                   
REMARK 500    ALA B 115       76.24   -100.31                                   
REMARK 500    TYR B 144       15.98     54.27                                   
REMARK 500    SER B 189     -120.67     61.32                                   
REMARK 500    THR B 218      -13.43   -143.30                                   
REMARK 500    ASN B 253       37.01    -99.66                                   
REMARK 500    SER B 342     -173.30    -60.34                                   
REMARK 500    TYR C 144       15.50     56.04                                   
REMARK 500    SER C 189     -121.43     51.94                                   
REMARK 500    THR C 218       -6.26   -145.04                                   
REMARK 500    ASN C 271     -158.95    -92.40                                   
REMARK 500    ASP D 122       37.18    -91.83                                   
REMARK 500    ASN D 131       78.28   -101.69                                   
REMARK 500    TYR D 144       13.33     57.26                                   
REMARK 500    SER D 189     -127.04     59.67                                   
REMARK 500    THR D 218       -6.18   -143.97                                   
REMARK 500    ASN D 271     -158.91    -90.52                                   
REMARK 500    SER D 273      111.99   -169.49                                   
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                              MG D 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 139   OE2                                                    
REMARK 620 2 HOH D 721   O    88.6                                              
REMARK 620 3 HOH D 508   O    89.5  90.3                                        
REMARK 620 4 HOH D 585   O    91.7 177.9  91.8                                  
REMARK 620 5 HOH D 686   O   174.4  87.4  86.6  92.4                            
REMARK 620 6 HOH D 572   O    90.5  91.7 178.0  86.2  93.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401                  
DBREF  4H18 A    1   365  UNP    Q8NTG4   Q8NTG4_CORGL     1    365             
DBREF  4H18 B    1   365  UNP    Q8NTG4   Q8NTG4_CORGL     1    365             
DBREF  4H18 C    1   365  UNP    Q8NTG4   Q8NTG4_CORGL     1    365             
DBREF  4H18 D    1   365  UNP    Q8NTG4   Q8NTG4_CORGL     1    365             
SEQADV 4H18 HIS A  366  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS A  367  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS A  368  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS A  369  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS A  370  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS A  371  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  366  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  367  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  368  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  369  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  370  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS B  371  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  366  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  367  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  368  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  369  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  370  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS C  371  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  366  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  367  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  368  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  369  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  370  UNP  Q8NTG4              EXPRESSION TAG                 
SEQADV 4H18 HIS D  371  UNP  Q8NTG4              EXPRESSION TAG                 
SEQRES   1 A  371  MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA          
SEQRES   2 A  371  LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR          
SEQRES   3 A  371  ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY          
SEQRES   4 A  371  ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA          
SEQRES   5 A  371  ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN          
SEQRES   6 A  371  ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER          
SEQRES   7 A  371  PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR          
SEQRES   8 A  371  ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU          
SEQRES   9 A  371  LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP          
SEQRES  10 A  371  VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS          
SEQRES  11 A  371  ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER          
SEQRES  12 A  371  TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY          
SEQRES  13 A  371  GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU          
SEQRES  14 A  371  PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN          
SEQRES  15 A  371  ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER          
SEQRES  16 A  371  LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA          
SEQRES  17 A  371  ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU          
SEQRES  18 A  371  LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY          
SEQRES  19 A  371  ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY          
SEQRES  20 A  371  GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP          
SEQRES  21 A  371  LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER          
SEQRES  22 A  371  GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG          
SEQRES  23 A  371  PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET          
SEQRES  24 A  371  ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA          
SEQRES  25 A  371  THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP          
SEQRES  26 A  371  SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR          
SEQRES  27 A  371  GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG          
SEQRES  28 A  371  GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU          
SEQRES  29 A  371  ALA HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  371  MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA          
SEQRES   2 B  371  LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR          
SEQRES   3 B  371  ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY          
SEQRES   4 B  371  ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA          
SEQRES   5 B  371  ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN          
SEQRES   6 B  371  ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER          
SEQRES   7 B  371  PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR          
SEQRES   8 B  371  ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU          
SEQRES   9 B  371  LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP          
SEQRES  10 B  371  VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS          
SEQRES  11 B  371  ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER          
SEQRES  12 B  371  TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY          
SEQRES  13 B  371  GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU          
SEQRES  14 B  371  PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN          
SEQRES  15 B  371  ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER          
SEQRES  16 B  371  LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA          
SEQRES  17 B  371  ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU          
SEQRES  18 B  371  LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY          
SEQRES  19 B  371  ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY          
SEQRES  20 B  371  GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP          
SEQRES  21 B  371  LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER          
SEQRES  22 B  371  GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG          
SEQRES  23 B  371  PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET          
SEQRES  24 B  371  ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA          
SEQRES  25 B  371  THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP          
SEQRES  26 B  371  SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR          
SEQRES  27 B  371  GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG          
SEQRES  28 B  371  GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU          
SEQRES  29 B  371  ALA HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  371  MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA          
SEQRES   2 C  371  LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR          
SEQRES   3 C  371  ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY          
SEQRES   4 C  371  ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA          
SEQRES   5 C  371  ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN          
SEQRES   6 C  371  ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER          
SEQRES   7 C  371  PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR          
SEQRES   8 C  371  ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU          
SEQRES   9 C  371  LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP          
SEQRES  10 C  371  VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS          
SEQRES  11 C  371  ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER          
SEQRES  12 C  371  TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY          
SEQRES  13 C  371  GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU          
SEQRES  14 C  371  PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN          
SEQRES  15 C  371  ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER          
SEQRES  16 C  371  LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA          
SEQRES  17 C  371  ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU          
SEQRES  18 C  371  LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY          
SEQRES  19 C  371  ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY          
SEQRES  20 C  371  GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP          
SEQRES  21 C  371  LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER          
SEQRES  22 C  371  GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG          
SEQRES  23 C  371  PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET          
SEQRES  24 C  371  ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA          
SEQRES  25 C  371  THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP          
SEQRES  26 C  371  SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR          
SEQRES  27 C  371  GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG          
SEQRES  28 C  371  GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU          
SEQRES  29 C  371  ALA HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 D  371  MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA          
SEQRES   2 D  371  LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR          
SEQRES   3 D  371  ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY          
SEQRES   4 D  371  ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA          
SEQRES   5 D  371  ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN          
SEQRES   6 D  371  ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER          
SEQRES   7 D  371  PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR          
SEQRES   8 D  371  ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU          
SEQRES   9 D  371  LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP          
SEQRES  10 D  371  VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS          
SEQRES  11 D  371  ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER          
SEQRES  12 D  371  TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY          
SEQRES  13 D  371  GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU          
SEQRES  14 D  371  PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN          
SEQRES  15 D  371  ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER          
SEQRES  16 D  371  LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA          
SEQRES  17 D  371  ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU          
SEQRES  18 D  371  LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY          
SEQRES  19 D  371  ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY          
SEQRES  20 D  371  GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP          
SEQRES  21 D  371  LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER          
SEQRES  22 D  371  GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG          
SEQRES  23 D  371  PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET          
SEQRES  24 D  371  ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA          
SEQRES  25 D  371  THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP          
SEQRES  26 D  371  SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR          
SEQRES  27 D  371  GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG          
SEQRES  28 D  371  GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU          
SEQRES  29 D  371  ALA HIS HIS HIS HIS HIS HIS                                  
HET     MG  D 401       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  HOH   *978(H2 O)                                                    
HELIX    1   1 THR A   33  GLY A   39  1                                   7    
HELIX    2   2 TRP A   60  ALA A   66  1                                   7    
HELIX    3   3 ASN A  116  THR A  121  1                                   6    
HELIX    4   4 ASP A  122  ASN A  131  1                                  10    
HELIX    5   5 ASN A  152  GLY A  156  5                                   5    
HELIX    6   6 MET A  160  LYS A  167  1                                   8    
HELIX    7   7 LEU A  169  LEU A  177  1                                   9    
HELIX    8   8 MET A  190  PHE A  202  1                                  13    
HELIX    9   9 SER A  220  ARG A  233  1                                  14    
HELIX   10  10 THR A  237  GLY A  243  1                                   7    
HELIX   11  11 GLY A  247  ASN A  253  1                                   7    
HELIX   12  12 ASN A  258  ARG A  263  5                                   6    
HELIX   13  13 ALA A  272  TRP A  279  5                                   8    
HELIX   14  14 GLY A  306  GLY A  328  1                                  23    
HELIX   15  15 SER A  342  GLU A  362  1                                  21    
HELIX   16  16 THR B   33  GLY B   39  1                                   7    
HELIX   17  17 TRP B   60  ALA B   66  1                                   7    
HELIX   18  18 ASN B  116  THR B  121  1                                   6    
HELIX   19  19 ASP B  122  ASN B  131  1                                  10    
HELIX   20  20 ASN B  152  GLY B  156  5                                   5    
HELIX   21  21 MET B  160  LYS B  167  1                                   8    
HELIX   22  22 LEU B  169  ASN B  178  1                                  10    
HELIX   23  23 MET B  190  PHE B  202  1                                  13    
HELIX   24  24 SER B  220  ARG B  233  1                                  14    
HELIX   25  25 THR B  237  GLY B  243  1                                   7    
HELIX   26  26 GLY B  247  ASN B  253  1                                   7    
HELIX   27  27 ASN B  258  ARG B  263  5                                   6    
HELIX   28  28 ALA B  272  GLU B  280  5                                   9    
HELIX   29  29 GLY B  306  GLY B  328  1                                  23    
HELIX   30  30 SER B  342  GLU B  362  1                                  21    
HELIX   31  31 THR C   33  GLY C   39  1                                   7    
HELIX   32  32 TRP C   60  ALA C   67  1                                   8    
HELIX   33  33 ASP C   93  GLY C   97  5                                   5    
HELIX   34  34 ASN C  116  THR C  121  1                                   6    
HELIX   35  35 ASP C  122  GLU C  129  1                                   8    
HELIX   36  36 ASN C  152  GLY C  156  5                                   5    
HELIX   37  37 MET C  160  LYS C  167  1                                   8    
HELIX   38  38 LEU C  169  ASN C  178  1                                  10    
HELIX   39  39 SER C  189  PHE C  202  1                                  14    
HELIX   40  40 SER C  220  ASP C  232  1                                  13    
HELIX   41  41 ARG C  233  ASN C  235  5                                   3    
HELIX   42  42 THR C  237  GLY C  243  1                                   7    
HELIX   43  43 GLY C  247  ASN C  253  1                                   7    
HELIX   44  44 ASN C  258  ARG C  263  5                                   6    
HELIX   45  45 THR C  302  GLY C  328  1                                  27    
HELIX   46  46 SER C  342  PHE C  361  1                                  20    
HELIX   47  47 THR D   33  GLY D   39  1                                   7    
HELIX   48  48 TRP D   60  ALA D   67  1                                   8    
HELIX   49  49 ASP D   93  GLY D   97  5                                   5    
HELIX   50  50 ASN D  116  THR D  121  1                                   6    
HELIX   51  51 ASP D  122  GLU D  129  1                                   8    
HELIX   52  52 ASN D  152  GLY D  156  5                                   5    
HELIX   53  53 MET D  160  LYS D  167  1                                   8    
HELIX   54  54 LEU D  169  ASN D  178  1                                  10    
HELIX   55  55 SER D  189  PHE D  202  1                                  14    
HELIX   56  56 SER D  220  ASP D  232  1                                  13    
HELIX   57  57 ARG D  233  ASN D  235  5                                   3    
HELIX   58  58 THR D  237  GLY D  243  1                                   7    
HELIX   59  59 GLY D  247  ASN D  253  1                                   7    
HELIX   60  60 ASN D  258  ARG D  263  5                                   6    
HELIX   61  61 THR D  302  GLY D  328  1                                  27    
HELIX   62  62 SER D  342  PHE D  361  1                                  20    
SHEET    1   A 9 THR A  45  SER A  47  0                                        
SHEET    2   A 9 VAL A  71  SER A  78 -1  O  TRP A  75   N  SER A  47           
SHEET    3   A 9 ARG A  83  ILE A  90 -1  O  ARG A  83   N  SER A  78           
SHEET    4   A 9 ASN A 133  PRO A 137 -1  O  ILE A 136   N  VAL A  88           
SHEET    5   A 9 VAL A 101  LEU A 105  1  N  ILE A 102   O  VAL A 135           
SHEET    6   A 9 ARG A 183  MET A 188  1  O  ALA A 186   N  LEU A 105           
SHEET    7   A 9 ALA A 208  PHE A 212  1  O  PHE A 212   N  GLY A 187           
SHEET    8   A 9 GLU A 266  SER A 270  1  O  TYR A 268   N  SER A 211           
SHEET    9   A 9 ASP A 332  ASN A 334  1  O  ASP A 332   N  LEU A 267           
SHEET    1   B 9 THR B  45  SER B  47  0                                        
SHEET    2   B 9 VAL B  71  SER B  78 -1  O  TRP B  75   N  SER B  47           
SHEET    3   B 9 ARG B  83  ILE B  90 -1  O  VAL B  85   N  ALA B  76           
SHEET    4   B 9 ASN B 133  PRO B 137 -1  O  ILE B 136   N  VAL B  88           
SHEET    5   B 9 ARG B  99  LEU B 105  1  N  PRO B 100   O  ASN B 133           
SHEET    6   B 9 THR B 179  MET B 188  1  O  ALA B 186   N  LEU B 105           
SHEET    7   B 9 ALA B 208  PHE B 212  1  O  PHE B 212   N  GLY B 187           
SHEET    8   B 9 GLU B 266  SER B 270  1  O  TYR B 268   N  SER B 211           
SHEET    9   B 9 ASP B 332  ASN B 334  1  O  ASP B 332   N  LEU B 267           
SHEET    1   C 9 THR C  45  SER C  47  0                                        
SHEET    2   C 9 VAL C  71  SER C  78 -1  O  TRP C  75   N  SER C  47           
SHEET    3   C 9 ARG C  83  ILE C  90 -1  O  LEU C  87   N  MET C  74           
SHEET    4   C 9 ASN C 133  PRO C 137 -1  O  ILE C 136   N  VAL C  88           
SHEET    5   C 9 VAL C 101  LEU C 105  1  N  ILE C 102   O  VAL C 135           
SHEET    6   C 9 ARG C 183  MET C 188  1  O  ALA C 184   N  TYR C 103           
SHEET    7   C 9 ALA C 208  PHE C 212  1  O  PHE C 212   N  GLY C 187           
SHEET    8   C 9 GLU C 266  SER C 270  1  O  GLU C 266   N  ALA C 209           
SHEET    9   C 9 ASP C 332  ASN C 334  1  O  ASP C 332   N  VAL C 269           
SHEET    1   D 9 THR D  45  SER D  47  0                                        
SHEET    2   D 9 VAL D  71  SER D  78 -1  O  TRP D  75   N  SER D  47           
SHEET    3   D 9 ARG D  83  ILE D  90 -1  O  LEU D  87   N  MET D  74           
SHEET    4   D 9 ASN D 133  PRO D 137 -1  O  VAL D 134   N  ILE D  90           
SHEET    5   D 9 VAL D 101  LEU D 105  1  N  ILE D 102   O  VAL D 135           
SHEET    6   D 9 ARG D 183  MET D 188  1  O  ALA D 186   N  LEU D 105           
SHEET    7   D 9 ALA D 208  PHE D 212  1  O  PHE D 212   N  GLY D 187           
SHEET    8   D 9 GLU D 266  SER D 270  1  O  GLU D 266   N  ALA D 209           
SHEET    9   D 9 ASP D 332  ASN D 334  1  O  ASP D 332   N  LEU D 267           
SSBOND   1 CYS A  215    CYS A  316                          1555   1555  2.06  
SSBOND   2 CYS B  215    CYS B  316                          1555   1555  2.05  
SSBOND   3 CYS C  215    CYS C  316                          1555   1555  2.05  
SSBOND   4 CYS D  215    CYS D  316                          1555   1555  2.05  
LINK         OE2 GLU D 139                MG    MG D 401     1555   1555  2.13  
LINK        MG    MG D 401                 O   HOH D 721     1555   1555  2.00  
LINK        MG    MG D 401                 O   HOH D 508     1555   1555  2.05  
LINK        MG    MG D 401                 O   HOH D 585     1555   1555  2.10  
LINK        MG    MG D 401                 O   HOH D 686     1555   1555  2.16  
LINK        MG    MG D 401                 O   HOH D 572     1555   1555  2.19  
SITE     1 AC1  6 GLU D 139  HOH D 508  HOH D 572  HOH D 585                    
SITE     2 AC1  6 HOH D 686  HOH D 721                                          
CRYST1   85.804  190.688   78.497  90.00  90.00  90.00 P 21 21 2    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      0.011654  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005244  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012739        0.00000                         
TER    2417      GLU A 364                                                      
TER    4812      LEU B 363                                                      
TER    7199      GLU C 364                                                      
TER    9565      LEU D 363                                                      
MASTER      632    0    1   62   36    0    2    610474    4   16  116          
END                                                                             

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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:
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