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LongText Report for: 4H7K-pdb

Name Class
4H7K-pdb
HEADER    HYDROLASE                               20-SEP-12   4H7K              
TITLE     CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB I253M MUTANT FROM   
TITLE    2 SPHINGOBIUM SP. MI1205                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPHINGOBIUM;                                    
SOURCE   3 ORGANISM_TAXID: 407020;                                              
SOURCE   4 STRAIN: MI1205;                                                      
SOURCE   5 GENE: LINB, DHAA;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA HYDROLASE FOLD, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.OKAI,J.OHTSUKA,L.F.IMAI,T.MASE,R.MORIUCHI,M.TSUDA,K.NAGATA,         
AUTHOR   2 Y.NAGATA,M.TANOKURA                                                  
REVDAT   1   05-JUN-13 4H7K    0                                                
JRNL        AUTH   M.OKAI,J.OHTSUKA,L.F.IMAI,T.MASE,R.MORIUCHI,M.TSUDA,         
JRNL        AUTH 2 K.NAGATA,Y.NAGATA,M.TANOKURA                                 
JRNL        TITL   CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS ANALYSES OF  
JRNL        TITL 2 HALOALKANE DEHALOGENASE LINB FROM SPHINGOBIUM SP. STRAIN     
JRNL        TITL 3 MI1205.                                                      
JRNL        REF    J.BACTERIOL.                  V. 195  2642 2013              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   23564170                                                     
JRNL        DOI    10.1128/JB.02020-12                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26351                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1394                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1720                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.2250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2332                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 268                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.99000                                             
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 1.39000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.063         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2396 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3258 ; 1.298 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   293 ; 5.588 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;32.805 ;22.773       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   377 ;12.908 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;15.611 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   341 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1890 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4H7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075118.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: 4H77                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 278K                                                    
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       25.26900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.07650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.26900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.07650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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     ALA A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 465     HIS A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     HIS A   302                                                      
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    LEU A   3     -166.89    -74.11                                   
REMARK 500    PRO A  39       44.80   -100.55                                   
REMARK 500    THR A  40     -160.83   -101.44                                   
REMARK 500    ASP A 108     -130.50     59.70                                   
REMARK 500    ARG A 155       33.06    -85.16                                   
REMARK 500    HIS A 247      -83.94   -152.66                                   
REMARK 500    ALA A 271      -92.89   -106.16                                   
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                              CA A 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 175   O                                                      
REMARK 620 2 HOH A 522   O    84.8                                              
REMARK 620 3 ILE A 178   O    86.4  81.9                                        
REMARK 620 4 HOH A 549   O    94.2 158.4  76.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403                  
DBREF  4H7K A    1   296  UNP    A4PEU6   A4PEU6_9SPHN     1    296             
SEQADV 4H7K MET A  253  UNP  A4PEU6    ILE   253 ENGINEERED MUTATION            
SEQADV 4H7K HIS A  297  UNP  A4PEU6              EXPRESSION TAG                 
SEQADV 4H7K HIS A  298  UNP  A4PEU6              EXPRESSION TAG                 
SEQADV 4H7K HIS A  299  UNP  A4PEU6              EXPRESSION TAG                 
SEQADV 4H7K HIS A  300  UNP  A4PEU6              EXPRESSION TAG                 
SEQADV 4H7K HIS A  301  UNP  A4PEU6              EXPRESSION TAG                 
SEQADV 4H7K HIS A  302  UNP  A4PEU6              EXPRESSION TAG                 
SEQRES   1 A  302  MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE          
SEQRES   2 A  302  ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU          
SEQRES   3 A  302  GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO          
SEQRES   4 A  302  THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS          
SEQRES   5 A  302  ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY          
SEQRES   6 A  302  MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU          
SEQRES   7 A  302  ARG TYR THR TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA          
SEQRES   8 A  302  LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU          
SEQRES   9 A  302  VAL VAL HIS ASP TRP GLY SER VAL LEU GLY PHE ASP TRP          
SEQRES  10 A  302  ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR          
SEQRES  11 A  302  MET GLU ALA VAL THR MET PRO LEU GLU TRP ALA ASP PHE          
SEQRES  12 A  302  PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER          
SEQRES  13 A  302  GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE          
SEQRES  14 A  302  VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU          
SEQRES  15 A  302  SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU          
SEQRES  16 A  302  ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO          
SEQRES  17 A  302  ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL          
SEQRES  18 A  302  ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER          
SEQRES  19 A  302  PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY HIS          
SEQRES  20 A  302  LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP          
SEQRES  21 A  302  PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE          
SEQRES  22 A  302  ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE          
SEQRES  23 A  302  ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS HIS          
SEQRES  24 A  302  HIS HIS HIS                                                  
HET     CL  A 401       1                                                       
HET     CL  A 402       1                                                       
HET     CA  A 403       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  HOH   *268(H2 O)                                                    
HELIX    1   1 SER A   41  ARG A   46  5                                   6    
HELIX    2   2 ILE A   48  ALA A   53  5                                   6    
HELIX    3   3 THR A   81  LEU A   96  1                                  16    
HELIX    4   4 ASP A  108  HIS A  121  1                                  14    
HELIX    5   5 GLU A  139  PHE A  143  5                                   5    
HELIX    6   6 PRO A  144  GLN A  146  5                                   3    
HELIX    7   7 ASP A  147  ARG A  155  1                                   9    
HELIX    8   8 ALA A  158  LEU A  164  1                                   7    
HELIX    9   9 ASN A  167  GLN A  172  1                                   6    
HELIX   10  10 GLN A  172  LEU A  177  1                                   6    
HELIX   11  11 SER A  183  GLU A  192  1                                  10    
HELIX   12  12 PRO A  193  LEU A  195  5                                   3    
HELIX   13  13 GLY A  198  ARG A  201  5                                   4    
HELIX   14  14 ARG A  202  ILE A  211  1                                  10    
HELIX   15  15 PRO A  217  SER A  232  1                                  16    
HELIX   16  16 THR A  250  ARG A  258  1                                   9    
HELIX   17  17 PHE A  273  ASP A  277  5                                   5    
HELIX   18  18 SER A  278  ARG A  294  1                                  17    
SHEET    1   A 8 LYS A  11  ILE A  16  0                                        
SHEET    2   A 8 ARG A  19  GLU A  26 -1  O  ARG A  19   N  ILE A  16           
SHEET    3   A 8 ARG A  57  CYS A  61 -1  O  LEU A  58   N  GLU A  26           
SHEET    4   A 8 PRO A  31  GLN A  35  1  N  PHE A  34   O  ILE A  59           
SHEET    5   A 8 VAL A 102  HIS A 107  1  O  VAL A 103   N  LEU A  33           
SHEET    6   A 8 VAL A 125  MET A 131  1  O  ALA A 129   N  LEU A 104           
SHEET    7   A 8 LYS A 238  PRO A 245  1  O  ILE A 241   N  TYR A 130           
SHEET    8   A 8 GLN A 263  GLY A 270  1  O  THR A 264   N  PHE A 240           
LINK         O   PRO A 175                CA    CA A 403     1555   1555  2.31  
LINK        CA    CA A 403                 O   HOH A 522     1555   1555  2.31  
LINK         O   ILE A 178                CA    CA A 403     1555   1555  2.31  
LINK        CA    CA A 403                 O   HOH A 549     1555   1555  2.40  
CISPEP   1 ASN A   38    PRO A   39          0       -11.65                     
CISPEP   2 ASP A   73    PRO A   74          0        -1.87                     
CISPEP   3 THR A  216    PRO A  217          0        -2.97                     
CISPEP   4 GLU A  244    PRO A  245          0         1.02                     
SITE     1 AC1  4 ASN A  38  TRP A 109  PHE A 169  PRO A 208                    
SITE     1 AC2  4 HOH A 511  HOH A 536  HOH A 556  HOH A 615                    
SITE     1 AC3  6 ASP A 166  PRO A 175  ILE A 178  HOH A 522                    
SITE     2 AC3  6 HOH A 543  HOH A 549                                          
CRYST1   50.538   72.153   73.584  90.00  90.00  90.00 P 21 21 2     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      0.019787  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013859  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013590        0.00000                         
TER    2333      PRO A 295                                                      
MASTER      295    0    3   18    8    0    4    6 2603    1    5   24          
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.
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