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LongText Report for: 7cy0-pdb

Name Class
7cy0-pdb
HEADER    HYDROLASE                               03-SEP-20   7CY0              
TITLE     CRYSTAL STRUCTURE OF A NEW PETASE TRIPLE MUTANT                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PETASE,PET-DIGESTING ENZYME;                                
COMPND   5 EC: 3.1.1.101;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /      
SOURCE   3 TISTR 2288 / 201-F6);                                                
SOURCE   4 ORGANISM_TAXID: 1547922;                                             
SOURCE   5 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;                           
SOURCE   6 GENE: ISF6_4831;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET32A                                    
KEYWDS    POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, SUBSTRATE BINDING, INHIBITOR, 
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO                              
REVDAT   1   26-MAY-21 7CY0    0                                                
JRNL        AUTH   X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO                     
JRNL        TITL   CRYSTAL STRUCTURE OF A NEW PETASE TRIPLE MUTANT              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0266                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 48671                          
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) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.166                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2481                            
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) : 1.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3409                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 208                          
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1915                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 330                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52000                                             
REMARK   3    B22 (A**2) : -0.61000                                             
REMARK   3    B33 (A**2) : 1.13000                                              
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): 0.047         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.049         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.029         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.685         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.971                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1984 ; 0.010 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  1792 ; 0.000 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2707 ; 1.495 ; 1.641       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4129 ; 1.539 ; 1.572       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   266 ; 6.828 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;31.495 ;21.798       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   285 ;10.390 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;15.846 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   270 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2359 ; 0.016 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   473 ; 0.007 ; 0.020       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7CY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300018376.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL15A1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51200                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5XG0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 6000, GLYCEROL,      
REMARK 280  MES, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.46250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.14350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.90300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.14350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.46250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.90300            
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 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 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    ASN A  44       38.37   -149.27                                   
REMARK 500    THR A  59       -4.15     74.12                                   
REMARK 500    ALA A 131     -118.19     65.37                                   
REMARK 500    ALA A 180       67.20   -118.44                                   
REMARK 500    HIS A 185      -84.07   -122.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF1 7CY0 A    1   261  UNP                  PETH_IDESA                       
DBREF2 7CY0 A     A0A0K8P6T7                         30         290             
SEQADV 7CY0 GLY A  103  UNP  A0A0K8P6T ARG   132 ENGINEERED MUTATION            
SEQADV 7CY0 ALA A  131  UNP  A0A0K8P6T SER   160 ENGINEERED MUTATION            
SEQADV 7CY0 HIS A  185  UNP  A0A0K8P6T SER   214 ENGINEERED MUTATION            
SEQRES   1 A  261  ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA SER          
SEQRES   2 A  261  LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER PHE          
SEQRES   3 A  261  THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR VAL          
SEQRES   4 A  261  TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA ILE          
SEQRES   5 A  261  ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER ILE          
SEQRES   6 A  261  LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE VAL          
SEQRES   7 A  261  VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN PRO          
SEQRES   8 A  261  SER SER ARG SER SER GLN GLN MET ALA ALA LEU GLY GLN          
SEQRES   9 A  261  VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE TYR          
SEQRES  10 A  261  GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY TRP          
SEQRES  11 A  261  ALA MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA ASN          
SEQRES  12 A  261  ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO TRP          
SEQRES  13 A  261  ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO THR          
SEQRES  14 A  261  LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO VAL          
SEQRES  15 A  261  ASN SER HIS ALA LEU PRO ILE TYR ASP SER MET SER ARG          
SEQRES  16 A  261  ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER HIS          
SEQRES  17 A  261  SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU ILE          
SEQRES  18 A  261  GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET ASP          
SEQRES  19 A  261  ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN PRO          
SEQRES  20 A  261  ASN SER THR ARG VAL SER ASP PHE ARG THR ALA ASN CYS          
SEQRES  21 A  261  SER                                                          
HET    ACY  A 301       4                                                       
HET    ACY  A 302       4                                                       
HET    ACY  A 303       4                                                       
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2  ACY    3(C2 H4 O2)                                                  
FORMUL   5  HOH   *330(H2 O)                                                    
HELIX    1 AA1 THR A   10  ALA A   16  1                                   7    
HELIX    2 AA2 ARG A   61  LYS A   66  5                                   6    
HELIX    3 AA3 TRP A   67  SER A   74  1                                   8    
HELIX    4 AA4 GLN A   90  GLY A  110  1                                  21    
HELIX    5 AA5 ALA A  131  ASN A  144  1                                  14    
HELIX    6 AA6 HIS A  185  MET A  193  1                                   9    
HELIX    7 AA7 ASN A  217  ASP A  234  1                                  18    
HELIX    8 AA8 ASP A  236  ARG A  238  5                                   3    
HELIX    9 AA9 TYR A  239  GLU A  245  1                                   7    
SHEET    1 AA1 6 VAL A  23  THR A  27  0                                        
SHEET    2 AA1 6 ALA A  36  PRO A  42 -1  O  VAL A  39   N  PHE A  26           
SHEET    3 AA1 6 VAL A  78  ASP A  83 -1  O  VAL A  79   N  TYR A  40           
SHEET    4 AA1 6 VAL A  49  VAL A  55  1  N  ILE A  54   O  ILE A  80           
SHEET    5 AA1 6 VAL A 120  GLY A 129  1  O  ASP A 121   N  VAL A  49           
SHEET    6 AA1 6 ALA A 149  ALA A 150  1  O  ALA A 149   N  VAL A 127           
SHEET    1 AA2 3 THR A 169  CYS A 174  0                                        
SHEET    2 AA2 3 LYS A 198  ILE A 203  1  O  GLN A 199   N  ILE A 171           
SHEET    3 AA2 3 VAL A 252  ALA A 258 -1  O  ASP A 254   N  GLU A 202           
SSBOND   1 CYS A  174    CYS A  210                          1555   1555  2.05  
SSBOND   2 CYS A  244    CYS A  260                          1555   1555  2.09  
CRYST1   50.925   51.806   84.287  90.00  90.00  90.00 P 21 21 21    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      0.019637  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019303  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011864        0.00000                         
TER    1928      SER A 261                                                      
MASTER      256    0    3    9    9    0    0    6 2257    1   16   21          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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