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LongText Report for: 4KAC-pdb

Name Class
4KAC-pdb
HEADER    HYDROLASE                               22-APR-13   4KAC              
TITLE     X-RAY STRUCTURE OF THE COMPLEX HALOTAG2 WITH HALTS. NORTHEAST         
TITLE    2 STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET OR150.                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;                                
SOURCE   3 ORGANISM_TAXID: 1831;                                                
SOURCE   4 GENE: DHAA                                                           
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,       
KEYWDS   2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,   
AUTHOR   2 E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,G.KORNHABER,G.T.MONTELIONE,     
AUTHOR   3 C.M.CREWS,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM   
AUTHOR   4 (NESG)                                                               
REVDAT   1   05-JUN-13 4KAC    0                                                
JRNL        AUTH   A.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,M.MAGLAQUI, 
JRNL        AUTH 2 R.XIAO,E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,G.KORNHABER,     
JRNL        AUTH 3 G.T.MONTELIONE,C.M.CREWS,J.F.HUNT,L.TONG                     
JRNL        TITL   NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR150        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1269)                     
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) : 2.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.890                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 28743                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1456                            
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 42.7895 -  4.7868    1.00     2784   160  0.1650 0.1987        
REMARK   3     2  4.7868 -  3.8002    1.00     2777   137  0.1474 0.2040        
REMARK   3     3  3.8002 -  3.3200    1.00     2734   153  0.1746 0.2177        
REMARK   3     4  3.3200 -  3.0165    1.00     2775   139  0.1857 0.2766        
REMARK   3     5  3.0165 -  2.8004    1.00     2729   143  0.1878 0.2460        
REMARK   3     6  2.8004 -  2.6353    0.99     2729   143  0.1881 0.2674        
REMARK   3     7  2.6353 -  2.5033    0.99     2706   160  0.1812 0.2725        
REMARK   3     8  2.5033 -  2.3944    0.99     2718   138  0.1802 0.3219        
REMARK   3     9  2.3944 -  2.3022    0.99     2744   133  0.1822 0.2435        
REMARK   3    10  2.3022 -  2.2228    0.95     2591   150  0.1907 0.3189        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.01                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.62                          
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           4910                                  
REMARK   3   ANGLE     :  1.163           6708                                  
REMARK   3   CHIRALITY :  0.081            700                                  
REMARK   3   PLANARITY :  0.007            880                                  
REMARK   3   DIHEDRAL  : 14.127           1806                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0749  11.0063  20.6503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0999 T22:   0.1057                                     
REMARK   3      T33:   0.1286 T12:  -0.0090                                     
REMARK   3      T13:  -0.0091 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1544 L22:   0.2979                                     
REMARK   3      L33:   0.6525 L12:  -0.1125                                     
REMARK   3      L13:  -0.2151 L23:   0.3831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0097 S12:   0.0054 S13:   0.0064                       
REMARK   3      S21:  -0.0008 S22:  -0.0276 S23:   0.0248                       
REMARK   3      S31:  -0.0067 S32:  -0.0343 S33:   0.0424                       
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 4KAC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079090.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51681                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.223                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BN7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,   
REMARK 280  0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION: AMMONIUM   
REMARK 280  NITRATE 0.1M, SODIUM ACETATE 0.1M, MICROBATCH UNDER OIL,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.49200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     MSE A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     MSE A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A   306                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     MSE B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLY B   306                                                      
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  53       58.29   -103.96                                   
REMARK 500    THR A  54     -155.83   -114.71                                   
REMARK 500    LYS A  85       74.68   -119.36                                   
REMARK 500    GLU A 109      -93.16   -105.85                                   
REMARK 500    ASP A 117     -126.76     53.02                                   
REMARK 500    ARG A 164       42.85    -86.35                                   
REMARK 500    ASP A 167      -71.48    -92.27                                   
REMARK 500    VAL A 256      -63.66   -124.86                                   
REMARK 500    LEU A 282      -96.34   -123.49                                   
REMARK 500    PRO B  53       46.12   -103.17                                   
REMARK 500    THR B  54     -154.80   -107.92                                   
REMARK 500    LEU B  77      155.74    -49.39                                   
REMARK 500    GLU B 109      -93.17    -97.93                                   
REMARK 500    ASP B 117     -130.59     56.64                                   
REMARK 500    GLU B 151       45.32    -69.88                                   
REMARK 500    ARG B 164       38.06    -91.33                                   
REMARK 500    ASP B 167      -66.66    -94.56                                   
REMARK 500    VAL B 256      -66.84   -137.92                                   
REMARK 500    LEU B 282      -91.72   -110.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE4 B  403                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BN7   RELATED DB: PDB                                   
REMARK 900 HOMOLOGY IS 97.95%                                                   
REMARK 900 RELATED ID: NESG-OR150   RELATED DB: TARGETTRACK                     
DBREF  4KAC A   13   304  UNP    P0A3G3   DHAA_RHOSO       2    293             
DBREF  4KAC B   13   304  UNP    P0A3G3   DHAA_RHOSO       2    293             
SEQADV 4KAC MSE A    1  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY A    2  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    4  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    5  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    6  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    7  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A    8  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC SER A    9  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS A   10  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC MSE A   11  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY A   12  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC MSE A  186  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 4KAC GLY A  187  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 4KAC PHE A  283  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 4KAC LEU A  284  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 4KAC GLY A  303  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 4KAC ALA A  305  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY A  306  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC MSE B    1  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY B    2  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    4  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    5  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    6  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    7  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B    8  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC SER B    9  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC HIS B   10  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC MSE B   11  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY B   12  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC MSE B  186  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 4KAC GLY B  187  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 4KAC PHE B  283  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 4KAC LEU B  284  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 4KAC GLY B  303  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 4KAC ALA B  305  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4KAC GLY B  306  UNP  P0A3G3              EXPRESSION TAG                 
SEQRES   1 A  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER          
SEQRES   2 A  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   3 A  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY          
SEQRES   4 A  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   5 A  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS          
SEQRES   6 A  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   7 A  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE          
SEQRES   8 A  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU          
SEQRES   9 A  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  10 A  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  11 A  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE          
SEQRES  12 A  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  13 A  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY          
SEQRES  14 A  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY          
SEQRES  15 A  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  16 A  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL          
SEQRES  17 A  306  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  18 A  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  19 A  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  20 A  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  21 A  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS          
SEQRES  22 A  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN          
SEQRES  23 A  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  24 A  306  TRP LEU PRO GLY LEU ALA GLY                                  
SEQRES   1 B  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER          
SEQRES   2 B  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   3 B  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY          
SEQRES   4 B  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   5 B  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS          
SEQRES   6 B  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   7 B  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE          
SEQRES   8 B  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU          
SEQRES   9 B  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  10 B  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  11 B  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE          
SEQRES  12 B  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  13 B  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY          
SEQRES  14 B  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY          
SEQRES  15 B  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  16 B  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL          
SEQRES  17 B  306  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  18 B  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  19 B  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  20 B  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  21 B  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS          
SEQRES  22 B  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN          
SEQRES  23 B  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  24 B  306  TRP LEU PRO GLY LEU ALA GLY                                  
MODRES 4KAC MSE A   33  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE A   80  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE A  186  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE A  197  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE A  237  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B   33  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B   80  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B  140  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B  186  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B  197  MET  SELENOMETHIONINE                                   
MODRES 4KAC MSE B  237  MET  SELENOMETHIONINE                                   
HET    MSE  A  33       8                                                       
HET    MSE  A  80       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 186       8                                                       
HET    MSE  A 197       8                                                       
HET    MSE  A 237       8                                                       
HET    MSE  B  33       8                                                       
HET    MSE  B  80       8                                                       
HET    MSE  B 140       8                                                       
HET    MSE  B 186       8                                                       
HET    MSE  B 197       8                                                       
HET    MSE  B 237       8                                                       
HET    1Q9  A 401      18                                                       
HET    NH4  B 401       1                                                       
HET    1Q9  B 402      18                                                       
HET    PE4  B 403      26                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     1Q9 N-(2-ETHOXY-3,5-DIMETHYLBENZYL)-1H-TETRAZOL-5-AMINE              
HETNAM     NH4 AMMONIUM ION                                                     
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-              
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                                 
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3  1Q9    2(C12 H17 N5 O)                                              
FORMUL   4  NH4    H4 N 1+                                                      
FORMUL   6  PE4    C16 H34 O8                                                   
FORMUL   7  HOH   *274(H2 O)                                                    
HELIX    1   1 SER A   55  ARG A   60  5                                   6    
HELIX    2   2 ILE A   62  ALA A   67  1                                   6    
HELIX    3   3 PHE A   91  LEU A  106  1                                  16    
HELIX    4   4 ASP A  117  ASN A  130  1                                  14    
HELIX    5   5 THR A  148  TRP A  152  5                                   5    
HELIX    6   6 PRO A  153  PHE A  155  5                                   3    
HELIX    7   7 ALA A  156  ARG A  164  1                                   9    
HELIX    8   8 ASP A  167  ILE A  174  1                                   8    
HELIX    9   9 ASN A  177  GLY A  182  1                                   6    
HELIX   10  10 GLY A  182  GLY A  187  1                                   6    
HELIX   11  11 THR A  193  GLU A  202  1                                  10    
HELIX   12  12 PRO A  203  LEU A  205  5                                   3    
HELIX   13  13 LYS A  206  ASP A  209  5                                   4    
HELIX   14  14 ARG A  210  GLU A  219  1                                  10    
HELIX   15  15 PRO A  226  SER A  243  1                                  18    
HELIX   16  16 PRO A  259  LEU A  270  1                                  12    
HELIX   17  17 LEU A  284  ASP A  288  5                                   5    
HELIX   18  18 ASN A  289  LEU A  301  1                                  13    
HELIX   19  19 PRO A  302  LEU A  304  5                                   3    
HELIX   20  20 SER B   55  ARG B   60  5                                   6    
HELIX   21  21 ILE B   62  ALA B   67  1                                   6    
HELIX   22  22 PHE B   91  LEU B  106  1                                  16    
HELIX   23  23 ASP B  117  ASN B  130  1                                  14    
HELIX   24  24 PRO B  153  ARG B  164  1                                  12    
HELIX   25  25 ASP B  167  ILE B  174  1                                   8    
HELIX   26  26 ASN B  177  GLY B  182  1                                   6    
HELIX   27  27 GLY B  182  GLY B  187  1                                   6    
HELIX   28  28 THR B  193  GLU B  202  1                                  10    
HELIX   29  29 PRO B  203  LEU B  205  5                                   3    
HELIX   30  30 LYS B  206  ASP B  209  5                                   4    
HELIX   31  31 ARG B  210  PHE B  216  1                                   7    
HELIX   32  32 PRO B  226  SER B  243  1                                  18    
HELIX   33  33 PRO B  259  LEU B  270  1                                  12    
HELIX   34  34 LEU B  284  ASN B  289  1                                   6    
HELIX   35  35 ASN B  289  LEU B  301  1                                  13    
HELIX   36  36 PRO B  302  ALA B  305  5                                   4    
SHEET    1   A 8 HIS A  24  VAL A  28  0                                        
SHEET    2   A 8 GLU A  31  VAL A  38 -1  O  GLU A  31   N  VAL A  28           
SHEET    3   A 8 CYS A  72  PRO A  75 -1  O  CYS A  72   N  VAL A  38           
SHEET    4   A 8 VAL A  46  LEU A  49  1  N  PHE A  48   O  ILE A  73           
SHEET    5   A 8 VAL A 111  HIS A 116  1  O  VAL A 112   N  LEU A  47           
SHEET    6   A 8 VAL A 134  MSE A 140  1  O  ALA A 138   N  LEU A 113           
SHEET    7   A 8 LYS A 247  PRO A 254  1  O  LEU A 248   N  CYS A 139           
SHEET    8   A 8 CYS A 273  GLY A 281  1  O  LYS A 274   N  LEU A 249           
SHEET    1   B 8 HIS B  24  VAL B  28  0                                        
SHEET    2   B 8 GLU B  31  VAL B  38 -1  O  MSE B  33   N  VAL B  26           
SHEET    3   B 8 CYS B  72  PRO B  75 -1  O  CYS B  72   N  VAL B  38           
SHEET    4   B 8 VAL B  46  LEU B  49  1  N  PHE B  48   O  ILE B  73           
SHEET    5   B 8 VAL B 111  HIS B 116  1  O  VAL B 112   N  LEU B  47           
SHEET    6   B 8 VAL B 134  MSE B 140  1  O  ALA B 138   N  LEU B 113           
SHEET    7   B 8 LYS B 247  PRO B 254  1  O  LEU B 248   N  CYS B 139           
SHEET    8   B 8 CYS B 273  GLY B 281  1  O  LYS B 274   N  LEU B 249           
LINK         C   ARG A  32                 N   MSE A  33     1555   1555  1.32  
LINK         C   MSE A  33                 N   HIS A  34     1555   1555  1.33  
LINK         C   GLY A  79                 N   MSE A  80     1555   1555  1.32  
LINK         C   MSE A  80                 N   GLY A  81     1555   1555  1.33  
LINK         C   CYS A 139                 N   MSE A 140     1555   1555  1.32  
LINK         C   MSE A 140                 N   GLU A 141     1555   1555  1.33  
LINK         C   PRO A 185                 N   MSE A 186     1555   1555  1.33  
LINK         C   MSE A 186                 N   GLY A 187     1555   1555  1.33  
LINK         C   GLU A 196                 N   MSE A 197     1555   1555  1.33  
LINK         C   MSE A 197                 N   ASP A 198     1555   1555  1.33  
LINK         C   TYR A 236                 N   MSE A 237     1555   1555  1.33  
LINK         C   MSE A 237                 N   ASN A 238     1555   1555  1.33  
LINK         C   ARG B  32                 N   MSE B  33     1555   1555  1.33  
LINK         C   MSE B  33                 N   HIS B  34     1555   1555  1.33  
LINK         C   GLY B  79                 N   MSE B  80     1555   1555  1.33  
LINK         C   MSE B  80                 N   GLY B  81     1555   1555  1.33  
LINK         C   CYS B 139                 N   MSE B 140     1555   1555  1.33  
LINK         C   MSE B 140                 N   GLU B 141     1555   1555  1.33  
LINK         C   PRO B 185                 N   MSE B 186     1555   1555  1.32  
LINK         C   MSE B 186                 N   GLY B 187     1555   1555  1.32  
LINK         C   GLU B 196                 N   MSE B 197     1555   1555  1.33  
LINK         C   MSE B 197                 N   ASP B 198     1555   1555  1.33  
LINK         C   TYR B 236                 N   MSE B 237     1555   1555  1.33  
LINK         C   MSE B 237                 N   ASN B 238     1555   1555  1.33  
CISPEP   1 ASN A   52    PRO A   53          0       -12.85                     
CISPEP   2 GLU A  225    PRO A  226          0        -5.35                     
CISPEP   3 THR A  253    PRO A  254          0         9.70                     
CISPEP   4 ASN B   52    PRO B   53          0        -5.37                     
CISPEP   5 GLU B  225    PRO B  226          0        -4.45                     
CISPEP   6 THR B  253    PRO B  254          0         4.93                     
SITE     1 AC1 14 ASN A  52  PRO A  53  ASP A 117  TRP A 118                    
SITE     2 AC1 14 TRP A 152  ALA A 156  PHE A 160  PHE A 179                    
SITE     3 AC1 14 ALA A 183  GLY A 187  PRO A 217  LEU A 220                    
SITE     4 AC1 14 VAL A 256  PHE A 283                                          
SITE     1 AC2  4 GLY B  30  ILE B 278  PRO B 280  ASN B 289                    
SITE     1 AC3 12 ASN B  52  PRO B  53  ASP B 117  TRP B 118                    
SITE     2 AC3 12 TRP B 152  PHE B 160  PHE B 179  ALA B 183                    
SITE     3 AC3 12 PRO B 217  VAL B 256  LEU B 257  PHE B 283                    
SITE     1 AC4  2 LYS B  85  ASP B  87                                          
CRYST1   42.846   94.984   73.587  90.00  93.14  90.00 P 1 21 1      4          
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      0.023339  0.000000  0.001280        0.00000                         
SCALE2      0.000000  0.010528  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013610        0.00000                         
TER    2345      ALA A 305                                                      
TER    4688      ALA B 305                                                      
MASTER      317    0   16   36   16    0    9    6 4996    2  182   48          
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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