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LongText Report for: 3G9X-pdb

Name Class
3G9X-pdb
HEADER    HYDROLASE                               15-FEB-09   3G9X              
TITLE     STRUCTURE OF HALOALKANE DEHALOGENASE DHAA14 MUTANT I135F FROM         
TITLE    2 RHODOCOCCUS RHODOCHROUS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;                                
SOURCE   3 ORGANISM_TAXID: 1831;                                                
SOURCE   4 STRAIN: NCIMB 13064;                                                 
SOURCE   5 GENE: DHAA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PUC18                                     
KEYWDS    ALPHA/BETA HYDROLASE, HELICAL CAP DOMAIN, CATALYTIC TRIAD (ASP106,    
KEYWDS   2 HIS272, GLU130), MUTANT, I135F, HALOALKANES, DETOXIFICATION,         
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.GAVIRA,A.STSIAPANAVA,M.KUTY,M.LAPKOUSKI,J.DOHNALEK,I.KUTA         
AUTHOR   2 SMATANOVA                                                            
REVDAT   1   28-APR-10 3G9X    0                                                
JRNL        AUTH   A.STSIAPANAVA,J.A.GAVIRA,J.DOHNALEK,M.KUTY,T.KOUDELAKOVA,    
JRNL        AUTH 2 J.DAMBORSKY,I.KUTA SMATANOVA                                 
JRNL        TITL   ATOMIC RESOLUTION STUDIES OF MUTATED HALOALKANE              
JRNL        TITL 2 DEHALOGENASE DHAA FROM RHODOCOCCUS RHODOCHROUS               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.STSIAPANAVA,T.KOUDELAKOVA,M.LAPKOUSKI,M.PAVLOVA,           
REMARK   1  AUTH 2 J.DAMBORSKY,I.KUTA SMATANOVA                                 
REMARK   1  TITL   CRYSTALS OF DHAA MUTANTS FROM RHODOCOCCUS RHODOCHROUS NCIMB  
REMARK   1  TITL 2 13064 DIFFRACTED TO ULTRAHIGH RESOLUTION: CRYSTALLIZATION    
REMARK   1  TITL 3 AND PRELIMINARY DIFFRACTION ANALYSIS                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  64   137 2008              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   18259069                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.KLVANA,M.PAVLOVA,T.KOUDELAKOVA,R.CHALOUPKOVA,P.DVORAK,     
REMARK   1  AUTH 2 A.STSIAPANAVA,M.KUTY,I.KUTA SMATANOVA,J.DOHNALEK,            
REMARK   1  AUTH 3 P.KULHANEK,R.C.WADE,J.DAMBORSKY                              
REMARK   1  TITL   PATHWAYS AND MECHANISMS FOR PRODUCT RELEASE IN ENGINEERED    
REMARK   1  TITL 2 HALOALKANE DEHALOGENASE DHAA EXPLORED USING CLASSICAL AND    
REMARK   1  TITL 3 RANDOM ACCELERATION MOLECULAR DYNAMICS SIMULATIONS           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.115                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.115                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.137                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.006                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 8179                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 163371                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.111                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.111                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.133                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.023                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 7281                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 144939                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2372                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 9                                             
REMARK   3   SOLVENT ATOMS      : 520                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2881.55                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2132.70                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 64                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 25397                   
REMARK   3   NUMBER OF RESTRAINTS                     : 32628                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.028                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.104                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.100                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.036                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.033                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MASK                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT IN SHELXL97 WITH ANISOTROPIC   
REMARK   3  ADPS FOR ALL PROTEIN ATOMS                                          
REMARK   4                                                                      
REMARK   4 3G9X COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051607.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8158                             
REMARK 200  MONOCHROMATOR                  : GE(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 163495                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200   FOR THE DATA SET  : 26.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41800                            
REMARK 200   FOR SHELL         : 4.400                              
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: PDB ENTRY 1BN6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: [PROTEIN]=7-10 MG/ML IN 50MM TRIS-HCL    
REMARK 280  BUFFER PH 7.5; [PRECIPITANT]=25% PEG 4000, 8% 2-PROPANOL IN 100MM   
REMARK 280  SODIUM ACETATE., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
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 A  21   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH1 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A  86   CD  -  NE  -  CZ  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 146   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A 146   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ASP A 156   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 164   CB  -  CG  -  OD1 ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ASP A 164   CB  -  CG  -  OD2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 204   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 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    PRO A  42       46.40   -104.99                                   
REMARK 500    THR A  43     -160.53   -101.07                                   
REMARK 500    GLU A  98      -95.84   -109.58                                   
REMARK 500    ASP A 106     -129.59     55.67                                   
REMARK 500    ARG A 153       47.85    -87.66                                   
REMARK 500    ASP A 156      -73.20   -104.28                                   
REMARK 500    VAL A 245      -73.76   -135.69                                   
REMARK 500    LEU A 271      -99.52   -113.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1003                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FBW   RELATED DB: PDB                                   
REMARK 900 HALOALKANE DEHALOGENASE MUTANT DHAA-04 (C176Y)                       
REMARK 900 RELATED ID: 3FWH   RELATED DB: PDB                                   
REMARK 900 HALOALKANE DEHALOGENASE MUTANT DHAA-15(I135F/C176Y)                  
DBREF  3G9X A    1   293  UNP    P0A3G3   DHAA_RHOSO       1    293             
SEQADV 3G9X PHE A  135  UNP  P0A3G3    ILE   135 ENGINEERED                     
SEQADV 3G9X HIS A  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 3G9X HIS A  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 3G9X HIS A  296  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 3G9X HIS A  297  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 3G9X HIS A  298  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 3G9X HIS A  299  UNP  P0A3G3              EXPRESSION TAG                 
SEQRES   1 A  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 A  299  TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP          
SEQRES   3 A  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 A  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 A  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 A  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 A  299  TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 A  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 A  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 A  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU          
SEQRES  11 A  299  PHE ILE ARG PRO PHE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 A  299  PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP          
SEQRES  13 A  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 A  299  GLU GLY ALA LEU PRO LYS CYS VAL VAL ARG PRO LEU THR          
SEQRES  15 A  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 A  299  PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 A  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU          
SEQRES  18 A  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 A  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 A  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 A  299  ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 A  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 A  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
HET    IPA  A1001       4                                                       
HET    ACT  A1002       4                                                       
HET     CL  A1003       1                                                       
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   2  IPA    C3 H8 O                                                      
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  HOH   *520(H2 O)                                                    
HELIX    1   1 SER A   44  ARG A   49  5                                   6    
HELIX    2   2 ILE A   51  ALA A   56  1                                   6    
HELIX    3   3 PHE A   80  LEU A   95  1                                  16    
HELIX    4   4 ASP A  106  ASN A  119  1                                  14    
HELIX    5   5 THR A  137  TRP A  141  5                                   5    
HELIX    6   6 PRO A  142  PHE A  144  5                                   3    
HELIX    7   7 ALA A  145  ARG A  153  1                                   9    
HELIX    8   8 ASP A  156  ILE A  163  1                                   8    
HELIX    9   9 ASN A  166  GLY A  171  1                                   6    
HELIX   10  10 GLY A  171  CYS A  176  1                                   6    
HELIX   11  11 THR A  182  GLU A  191  1                                  10    
HELIX   12  12 PRO A  192  LEU A  194  5                                   3    
HELIX   13  13 LYS A  195  ASP A  198  5                                   4    
HELIX   14  14 ARG A  199  LEU A  209  1                                  11    
HELIX   15  15 PRO A  215  SER A  232  1                                  18    
HELIX   16  16 PRO A  248  LEU A  259  1                                  12    
HELIX   17  17 TYR A  273  ASN A  278  1                                   6    
HELIX   18  18 ASN A  278  LEU A  290  1                                  13    
HELIX   19  19 PRO A  291  HIS A  294  5                                   4    
SHEET    1   A 8 HIS A  13  VAL A  17  0                                        
SHEET    2   A 8 GLU A  20  VAL A  27 -1  O  GLU A  20   N  VAL A  17           
SHEET    3   A 8 CYS A  61  PRO A  64 -1  O  CYS A  61   N  VAL A  27           
SHEET    4   A 8 VAL A  35  LEU A  38  1  N  VAL A  35   O  ILE A  62           
SHEET    5   A 8 VAL A 100  HIS A 105  1  O  VAL A 101   N  LEU A  36           
SHEET    6   A 8 VAL A 123  MET A 129  1  O  ALA A 127   N  LEU A 102           
SHEET    7   A 8 LYS A 236  PRO A 243  1  O  LEU A 237   N  CYS A 128           
SHEET    8   A 8 CYS A 262  GLY A 270  1  O  ILE A 267   N  TRP A 240           
CISPEP   1 ASN A   41    PRO A   42          0        -3.66                     
CISPEP   2 GLU A  214    PRO A  215          0       -12.04                     
CISPEP   3 THR A  242    PRO A  243          0         8.27                     
SITE     1 AC1  6 ASN A  41  ASP A 106  HIS A 272  TYR A 273                    
SITE     2 AC1  6  CL A1003  HOH A2453                                          
SITE     1 AC2  9 THR A  33  HIS A  59  LYS A 124  LEU A 290                    
SITE     2 AC2  9 HIS A 294  HOH A2067  HOH A2130  HOH A2438                    
SITE     3 AC2  9 HOH A2452                                                     
SITE     1 AC3  5 ASN A  41  TRP A 107  PHE A 205  PRO A 206                    
SITE     2 AC3  5 IPA A1001                                                     
CRYST1   42.730   44.440   46.630 115.50  97.87 109.52 P 1           1          
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      0.023403  0.008297  0.008682        0.00000                         
SCALE2      0.000000  0.023874  0.014159        0.00000                         
SCALE3      0.000000  0.000000  0.025170        0.00000                         
MASTER      273    0    3   19    8    0    7    6 2901    1    8   23          
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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