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LongText Report for: 6tj2-pdb

Name Class
6tj2-pdb
HEADER    HYDROLASE                               24-NOV-19   6TJ2              
TITLE     EXTRACELLULAR ALPHA/BETA-HYDROLASE FROM PAENIBACILLUS SPECIES SHARES  
TITLE    2 STRUCTURAL AND FUNCTIONAL HOMOLOGY TO TOBACCO SALICYLIC ACID BINDING 
TITLE    3 PROTEIN 2                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE;                                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PAENIBACILLUS SP. VTT E-133280;                 
SOURCE   3 ORGANISM_TAXID: 1986222;                                             
SOURCE   4 GENE: CA600_10415;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA-HYDROLASE, METHYL SALICYLATE ESTERASE, PAENIBACILLUS,      
KEYWDS   2 RHIZOSPHERE, SABP2, SALICYLIC ACID, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.FULOP,R.C.WILKINSON                                                 
REVDAT   1   22-APR-20 6TJ2    0                                                
JRNL        AUTH   R.C.WILKINSON,R.RAHMAN POUR,S.JAMSHIDI,V.FULOP,T.D.H.BUGG    
JRNL        TITL   EXTRACELLULAR ALPHA/BETA-HYDROLASE FROM PAENIBACILLUS        
JRNL        TITL 2 SPECIES SHARES STRUCTURAL AND FUNCTIONAL HOMOLOGY TO TOBACCO 
JRNL        TITL 3 SALICYLIC ACID BINDING PROTEIN 2.                            
JRNL        REF    J.STRUCT.BIOL.                       07496 2020              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   32224091                                                     
JRNL        DOI    10.1016/J.JSB.2020.107496                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 153475                         
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6430                            
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) : 1.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10113                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 449                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5762                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 667                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.56000                                             
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): 0.048         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.050         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.034         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.824         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5938 ; 0.015 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  5403 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8063 ; 1.930 ; 1.651       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12591 ; 1.555 ; 1.573       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   729 ; 6.238 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   297 ;32.273 ;23.131       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   970 ;11.530 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   774 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6632 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1252 ; 0.001 ; 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 : NULL                                                 
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 6TJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105096.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91587                            
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 159905                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200   FOR THE DATA SET  : 17.7000                            
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) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.73900                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 3DQZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD                                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 20% PEG 3350,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
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       23.93000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.42500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.21500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.42500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.93000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.21500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -31                                                      
REMARK 465     LYS A   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     ILE A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     ILE A   -26                                                      
REMARK 465     LYS A   -25                                                      
REMARK 465     ILE A   -24                                                      
REMARK 465     VAL A   -23                                                      
REMARK 465     LEU A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     CYS A   -19                                                      
REMARK 465     ILE A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     ILE A   -16                                                      
REMARK 465     PHE A   -15                                                      
REMARK 465     THR A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLN A    -9                                                      
REMARK 465     PRO A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     THR A    -2                                                      
REMARK 465     VAL A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     MET B   -31                                                      
REMARK 465     LYS B   -30                                                      
REMARK 465     SER B   -29                                                      
REMARK 465     ILE B   -28                                                      
REMARK 465     HIS B   -27                                                      
REMARK 465     ILE B   -26                                                      
REMARK 465     LYS B   -25                                                      
REMARK 465     ILE B   -24                                                      
REMARK 465     VAL B   -23                                                      
REMARK 465     LEU B   -22                                                      
REMARK 465     ALA B   -21                                                      
REMARK 465     LEU B   -20                                                      
REMARK 465     CYS B   -19                                                      
REMARK 465     ILE B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     ILE B   -16                                                      
REMARK 465     PHE B   -15                                                      
REMARK 465     THR B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLN B    -9                                                      
REMARK 465     PRO B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     GLN B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     THR B    -2                                                      
REMARK 465     VAL B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     MET C   -31                                                      
REMARK 465     LYS C   -30                                                      
REMARK 465     SER C   -29                                                      
REMARK 465     ILE C   -28                                                      
REMARK 465     HIS C   -27                                                      
REMARK 465     ILE C   -26                                                      
REMARK 465     LYS C   -25                                                      
REMARK 465     ILE C   -24                                                      
REMARK 465     VAL C   -23                                                      
REMARK 465     LEU C   -22                                                      
REMARK 465     ALA C   -21                                                      
REMARK 465     LEU C   -20                                                      
REMARK 465     CYS C   -19                                                      
REMARK 465     ILE C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     ILE C   -16                                                      
REMARK 465     PHE C   -15                                                      
REMARK 465     THR C   -14                                                      
REMARK 465     ILE C   -13                                                      
REMARK 465     MET C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     LEU C   -10                                                      
REMARK 465     GLN C    -9                                                      
REMARK 465     PRO C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     ASN C    -6                                                      
REMARK 465     GLN C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     THR C    -2                                                      
REMARK 465     VAL C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     THR C    11                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 227   CD    GLU A 227   OE2    -0.078                       
REMARK 500    GLU B 227   CD    GLU B 227   OE2    -0.066                       
REMARK 500    GLU C  34   CD    GLU C  34   OE2    -0.067                       
REMARK 500    GLU C 227   CD    GLU C 227   OE1    -0.082                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG B 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLN C  96   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG C 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG C 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 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    ASN A  55       88.82   -157.58                                   
REMARK 500    SER A  85     -127.50     49.69                                   
REMARK 500    ASN A 140       20.25   -140.00                                   
REMARK 500    ASN B  55       88.65   -153.99                                   
REMARK 500    ASN B  55       88.65   -163.43                                   
REMARK 500    SER B  85     -123.17     60.28                                   
REMARK 500    SER B  85     -130.38     40.61                                   
REMARK 500    ASN B 140       24.24   -140.54                                   
REMARK 500    SER C  85     -128.80     48.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 537        DISTANCE =  6.19 ANGSTROMS                       
DBREF1 6TJ2 A  -31   253  UNP                  A0A264DUQ2_9BACL                 
DBREF2 6TJ2 A     A0A264DUQ2                          1         285             
DBREF1 6TJ2 B  -31   253  UNP                  A0A264DUQ2_9BACL                 
DBREF2 6TJ2 B     A0A264DUQ2                          1         285             
DBREF1 6TJ2 C  -31   253  UNP                  A0A264DUQ2_9BACL                 
DBREF2 6TJ2 C     A0A264DUQ2                          1         285             
SEQRES   1 A  285  MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS          
SEQRES   2 A  285  ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN          
SEQRES   3 A  285  GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER          
SEQRES   4 A  285  THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY          
SEQRES   5 A  285  SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER          
SEQRES   6 A  285  GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU          
SEQRES   7 A  285  TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR          
SEQRES   8 A  285  HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS          
SEQRES   9 A  285  GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER          
SEQRES  10 A  285  PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL          
SEQRES  11 A  285  PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE          
SEQRES  12 A  285  ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO          
SEQRES  13 A  285  ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA          
SEQRES  14 A  285  SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE          
SEQRES  15 A  285  ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA          
SEQRES  16 A  285  GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR          
SEQRES  17 A  285  PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER          
SEQRES  18 A  285  LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP          
SEQRES  19 A  285  THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR          
SEQRES  20 A  285  GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY          
SEQRES  21 A  285  LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS          
SEQRES  22 A  285  MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP              
SEQRES   1 B  285  MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS          
SEQRES   2 B  285  ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN          
SEQRES   3 B  285  GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER          
SEQRES   4 B  285  THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY          
SEQRES   5 B  285  SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER          
SEQRES   6 B  285  GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU          
SEQRES   7 B  285  TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR          
SEQRES   8 B  285  HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS          
SEQRES   9 B  285  GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER          
SEQRES  10 B  285  PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL          
SEQRES  11 B  285  PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE          
SEQRES  12 B  285  ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO          
SEQRES  13 B  285  ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA          
SEQRES  14 B  285  SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE          
SEQRES  15 B  285  ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA          
SEQRES  16 B  285  GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR          
SEQRES  17 B  285  PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER          
SEQRES  18 B  285  LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP          
SEQRES  19 B  285  THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR          
SEQRES  20 B  285  GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY          
SEQRES  21 B  285  LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS          
SEQRES  22 B  285  MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP              
SEQRES   1 C  285  MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS          
SEQRES   2 C  285  ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN          
SEQRES   3 C  285  GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER          
SEQRES   4 C  285  THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY          
SEQRES   5 C  285  SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER          
SEQRES   6 C  285  GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU          
SEQRES   7 C  285  TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR          
SEQRES   8 C  285  HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS          
SEQRES   9 C  285  GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER          
SEQRES  10 C  285  PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL          
SEQRES  11 C  285  PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE          
SEQRES  12 C  285  ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO          
SEQRES  13 C  285  ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA          
SEQRES  14 C  285  SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE          
SEQRES  15 C  285  ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA          
SEQRES  16 C  285  GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR          
SEQRES  17 C  285  PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER          
SEQRES  18 C  285  LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP          
SEQRES  19 C  285  THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR          
SEQRES  20 C  285  GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY          
SEQRES  21 C  285  LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS          
SEQRES  22 C  285  MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP              
FORMUL   4  HOH   *667(H2 O)                                                    
HELIX    1 AA1 THR A   24  PHE A   27  5                                   4    
HELIX    2 AA2 TRP A   28  LEU A   38  1                                  11    
HELIX    3 AA3 THR A   59  LYS A   74  1                                  16    
HELIX    4 AA4 PHE A   86  VAL A   98  1                                  13    
HELIX    5 AA5 VAL A  119  PHE A  123  5                                   5    
HELIX    6 AA6 PRO A  124  GLY A  139  1                                  16    
HELIX    7 AA7 PRO A  146  PHE A  154  1                                   9    
HELIX    8 AA8 SER A  159  GLN A  169  1                                  11    
HELIX    9 AA9 ALA A  175  GLU A  180  1                                   6    
HELIX   10 AB1 LEU A  184  LEU A  190  1                                   7    
HELIX   11 AB2 PRO A  214  HIS A  219  1                                   6    
HELIX   12 AB3 THR A  234  GLU A  239  1                                   6    
HELIX   13 AB4 GLU A  239  ARG A  252  1                                  14    
HELIX   14 AB5 THR B   24  PHE B   27  5                                   4    
HELIX   15 AB6 TRP B   28  LEU B   38  1                                  11    
HELIX   16 AB7 THR B   59  ASP B   75  1                                  17    
HELIX   17 AB8 PHE B   86  VAL B   98  1                                  13    
HELIX   18 AB9 VAL B  119  PHE B  123  5                                   5    
HELIX   19 AC1 PRO B  124  GLY B  139  1                                  16    
HELIX   20 AC2 PRO B  146  PHE B  154  1                                   9    
HELIX   21 AC3 SER B  159  LYS B  168  1                                  10    
HELIX   22 AC4 ALA B  175  GLU B  180  1                                   6    
HELIX   23 AC5 LEU B  184  LEU B  190  1                                   7    
HELIX   24 AC6 PRO B  214  HIS B  219  1                                   6    
HELIX   25 AC7 THR B  234  GLU B  239  1                                   6    
HELIX   26 AC8 GLU B  239  ARG B  252  1                                  14    
HELIX   27 AC9 THR C   24  PHE C   27  5                                   4    
HELIX   28 AD1 TRP C   28  LEU C   38  1                                  11    
HELIX   29 AD2 THR C   59  LYS C   74  1                                  16    
HELIX   30 AD3 PHE C   86  VAL C   98  1                                  13    
HELIX   31 AD4 VAL C  119  PHE C  123  5                                   5    
HELIX   32 AD5 PRO C  124  GLY C  139  1                                  16    
HELIX   33 AD6 PRO C  146  PHE C  154  1                                   9    
HELIX   34 AD7 SER C  159  GLN C  169  1                                  11    
HELIX   35 AD8 ALA C  175  GLU C  180  1                                   6    
HELIX   36 AD9 LEU C  184  LEU C  190  1                                   7    
HELIX   37 AE1 PRO C  214  HIS C  219  1                                   6    
HELIX   38 AE2 THR C  234  GLU C  239  1                                   6    
HELIX   39 AE3 GLU C  239  ARG C  252  1                                  14    
SHEET    1 AA1 6 THR A  41  TYR A  43  0                                        
SHEET    2 AA1 6 THR A  14  ILE A  18  1  N  LEU A  17   O  TYR A  43           
SHEET    3 AA1 6 PHE A  79  SER A  85  1  O  ILE A  80   N  THR A  14           
SHEET    4 AA1 6 ILE A 102  ALA A 110  1  O  PHE A 108   N  GLY A  83           
SHEET    5 AA1 6 LYS A 194  LEU A 199  1  O  SER A 195   N  PHE A 107           
SHEET    6 AA1 6 ARG A 224  GLY A 228  1  O  ARG A 224   N  TYR A 196           
SHEET    1 AA2 2 THR A 142  ILE A 143  0                                        
SHEET    2 AA2 2 GLU A 173  PRO A 174 -1  O  GLU A 173   N  ILE A 143           
SHEET    1 AA3 6 THR B  41  TYR B  43  0                                        
SHEET    2 AA3 6 THR B  14  ILE B  18  1  N  PHE B  15   O  THR B  41           
SHEET    3 AA3 6 PHE B  79  SER B  85  1  O  ILE B  80   N  THR B  14           
SHEET    4 AA3 6 ILE B 102  ALA B 110  1  O  PHE B 108   N  GLY B  83           
SHEET    5 AA3 6 LYS B 194  LEU B 199  1  O  SER B 195   N  PHE B 107           
SHEET    6 AA3 6 ARG B 224  GLY B 228  1  O  GLY B 228   N  TYR B 198           
SHEET    1 AA4 2 THR B 142  ILE B 143  0                                        
SHEET    2 AA4 2 GLU B 173  PRO B 174 -1  O  GLU B 173   N  ILE B 143           
SHEET    1 AA5 6 THR C  41  TYR C  43  0                                        
SHEET    2 AA5 6 THR C  14  ILE C  18  1  N  LEU C  17   O  TYR C  43           
SHEET    3 AA5 6 PHE C  79  SER C  85  1  O  ILE C  80   N  THR C  14           
SHEET    4 AA5 6 ILE C 102  ALA C 110  1  O  PHE C 108   N  GLY C  83           
SHEET    5 AA5 6 LYS C 194  LEU C 199  1  O  SER C 195   N  PHE C 107           
SHEET    6 AA5 6 ARG C 224  GLY C 228  1  O  ILE C 226   N  TYR C 198           
SHEET    1 AA6 2 THR C 142  ILE C 143  0                                        
SHEET    2 AA6 2 GLU C 173  PRO C 174 -1  O  GLU C 173   N  ILE C 143           
CISPEP   1 HIS A  213    PRO A  214          0         6.65                     
CISPEP   2 HIS B  213    PRO B  214          0         3.53                     
CISPEP   3 HIS C  213    PRO C  214          0         6.59                     
CRYST1   47.860  112.430  126.850  90.00  90.00  90.00 P 21 21 21   12          
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      0.020894  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007883        0.00000                         
TER    1924      ASP A 253                                                      
TER    3863      ASP B 253                                                      
TER    5780      ASP C 253                                                      
MASTER      459    0    0   39   24    0    0    6 6429    3    0   66          
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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