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LongText Report for: 1JMK-pdb

Name Class
1JMK-pdb
HEADER    HYDROLASE                               18-JUL-01   1JMK              
TITLE     STRUCTURAL BASIS FOR THE CYCLIZATION OF THE LIPOPEPTIDE               
TITLE    2 ANTIBIOTIC SURFACTIN BY THE THIOESTERASE DOMAIN SRFTE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SURFACTIN SYNTHETASE;                                      
COMPND   3 CHAIN: C, O;                                                         
COMPND   4 FRAGMENT: THIOESTERASE DOMAIN;                                       
COMPND   5 SYNONYM: SRFTE;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 GENE: SRFA-C;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    THIOESTERASE, NON-RIBOSOMAL PEPTIDE SYNTHESIS, ALPHA-BETA             
KEYWDS   2 HYDROLASE, CYCLIC PEPTIDE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.D.BRUNER,T.WEBER,R.M.KOHLI,D.SCHWARZER,M.A.MARAHIEL,                
AUTHOR   2 C.T.WALSH,M.T.STUBBS                                                 
REVDAT   1   27-MAR-02 1JMK    0                                                
JRNL        AUTH   S.D.BRUNER,T.WEBER,R.M.KOHLI,D.SCHWARZER,                    
JRNL        AUTH 2 M.A.MARAHIEL,C.T.WALSH,M.T.STUBBS                            
JRNL        TITL   STRUCTURAL BASIS FOR THE CYCLIZATION OF THE                  
JRNL        TITL 2 LIPOPEPTIDE ANTIBIOTIC SURFACTIN BY THE                      
JRNL        TITL 3 THIOESTERASE DOMAIN SRFTE                                    
JRNL        REF    STRUCTURE FOLD DES.           V.  10   301 2002              
JRNL        REFN                UK ISSN 0969-2126                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.71 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 62391                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2838                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.71                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 896                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3531                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 238                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.73                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JMK COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-2001.                
REMARK 100 THE RCSB ID CODE IS RCSB013939.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-2001; 27-FEB-2001           
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG ; CHESS         
REMARK 200  BEAMLINE                       : BW6; A1                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95, 0.9799, 0.9807; 0.979        
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC QUANTUM 4     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62391                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 0.1M HEPES        
REMARK 280  7.5, 2% MPD                                                         
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-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   SMTRY1   2 -1.000000  0.000000  0.000000       31.50500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.85500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.85500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.50500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.18500            
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: C, O                                  
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     ASP C   116                                                      
REMARK 465     LEU C   117                                                      
REMARK 465     ASP C   118                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     ARG C   120                                                      
REMARK 465     THR C   121                                                      
REMARK 465     VAL C   122                                                      
REMARK 465     GLU C   123                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER C 115    OG                                                  
REMARK 470     ASP C 135    CG    OD1   OD2                                     
REMARK 470     ASN C 140    CG    OD1   ND2                                     
REMARK 470     GLN C 230    CG    CD    OE1   NE2                               
REMARK 470     GLU O 137    CG    CD    OE1   OE2                               
REMARK 470     GLN O 230    CG    CD    OE1   NE2                               
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    LEU C    68     N    GLY O     6     2664     1.93            
REMARK 500   OD2  ASP C    16     OG   SER O   141     2664     1.97            
REMARK 500   O    VAL C    10     O    HOH       2     2664     2.11            
REMARK 500   O    VAL O    10     O    HOH      89     2665     2.11            
REMARK 500   N    GLY C     6     O    LEU O    68     2664     2.12            
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),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY C   2   CA    GLY C   2   N      0.039                        
REMARK 500    MET C 105   CE    MET C 105   SD     0.049                        
REMARK 500    SER C 124   CA    SER C 124   N      0.033                        
REMARK 500    HIS C 146   CD2   HIS C 146   CG     0.045                        
REMARK 500    MET C 200   CE    MET C 200   SD    -0.055                        
REMARK 500    THR C 231   CB    THR C 231   CA    -0.034                        
REMARK 500    GLY O   2   CA    GLY O   2   N      0.042                        
REMARK 500    PRO O  25   CD    PRO O  25   CG     0.033                        
REMARK 500    MET O 105   CE    MET O 105   SD     0.035                        
REMARK 500    HIS O 146   CD2   HIS O 146   CG     0.045                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN C  15   N   -  CA  -  C   ANGL. DEV. =  8.5 DEGREES           
REMARK 500    PRO C  25   N   -  CA  -  C   ANGL. DEV. =  9.3 DEGREES           
REMARK 500    GLY C  29   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    CYS C  47   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    ASP C  50   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    VAL C 100   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES           
REMARK 500    ASP C 107   N   -  CA  -  C   ANGL. DEV. =  9.6 DEGREES           
REMARK 500    LEU C 175   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES           
REMARK 500    ALA C 208   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES           
REMARK 500    MET C 210   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES           
REMARK 500    GLN O  15   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES           
REMARK 500    PRO O  25   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    GLY O  29   N   -  CA  -  C   ANGL. DEV. = 10.4 DEGREES           
REMARK 500    CYS O  47   N   -  CA  -  C   ANGL. DEV. = -9.4 DEGREES           
REMARK 500    ASP O  50   N   -  CA  -  C   ANGL. DEV. =-10.0 DEGREES           
REMARK 500    ASP O 107   N   -  CA  -  C   ANGL. DEV. =  7.7 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER O 141      143.67     63.78                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH   262        DISTANCE =  6.53 ANGSTROMS                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAIN C REFERS TO CLOSED MONOMER.                                    
REMARK 999 CHAIN O REFERS TO OPEN MONOMER.                                      
REMARK 999 SEQUENCE IS PUBLISHED IN BIOCHEMISTRY. 2001                          
REMARK 999 JUN 19;40(24):7099-108                                               
SEQRES   1 C  230  GLY GLY SER ASP GLY LEU GLN ASP VAL THR ILE MET ASN          
SEQRES   2 C  230  GLN ASP GLN GLU GLN ILE ILE PHE ALA PHE PRO PRO VAL          
SEQRES   3 C  230  LEU GLY TYR GLY LEU MET TYR GLN ASN LEU SER SER ARG          
SEQRES   4 C  230  LEU PRO SER TYR LYS LEU CYS ALA PHE ASP PHE ILE GLU          
SEQRES   5 C  230  GLU GLU ASP ARG LEU ASP ARG TYR ALA ASP LEU ILE GLN          
SEQRES   6 C  230  LYS LEU GLN PRO GLU GLY PRO LEU THR LEU PHE GLY TYR          
SEQRES   7 C  230  SER ALA GLY CYS SER LEU ALA PHE GLU ALA ALA LYS LYS          
SEQRES   8 C  230  LEU GLU GLY GLN GLY ARG ILE VAL GLN ARG ILE ILE MET          
SEQRES   9 C  230  VAL ASP SER TYR LYS LYS GLN GLY VAL SER ASP LEU ASP          
SEQRES  10 C  230  GLY ARG THR VAL GLU SER ASP VAL GLU ALA LEU MET ASN          
SEQRES  11 C  230  VAL ASN ARG ASP ASN GLU ALA LEU ASN SER GLU ALA VAL          
SEQRES  12 C  230  LYS HIS GLY LEU LYS GLN LYS THR HIS ALA PHE TYR SER          
SEQRES  13 C  230  TYR TYR VAL ASN LEU ILE SER THR GLY GLN VAL LYS ALA          
SEQRES  14 C  230  ASP ILE ASP LEU LEU THR SER GLY ALA ASP PHE ASP ILE          
SEQRES  15 C  230  PRO GLU TRP LEU ALA SER TRP GLU GLU ALA THR THR GLY          
SEQRES  16 C  230  ALA TYR ARG MET LYS ARG GLY PHE GLY THR HIS ALA GLU          
SEQRES  17 C  230  MET LEU GLN GLY GLU THR LEU ASP ARG ASN ALA GLY ILE          
SEQRES  18 C  230  LEU LEU GLU PHE LEU ASN THR GLN THR                          
SEQRES   1 O  230  GLY GLY SER ASP GLY LEU GLN ASP VAL THR ILE MET ASN          
SEQRES   2 O  230  GLN ASP GLN GLU GLN ILE ILE PHE ALA PHE PRO PRO VAL          
SEQRES   3 O  230  LEU GLY TYR GLY LEU MET TYR GLN ASN LEU SER SER ARG          
SEQRES   4 O  230  LEU PRO SER TYR LYS LEU CYS ALA PHE ASP PHE ILE GLU          
SEQRES   5 O  230  GLU GLU ASP ARG LEU ASP ARG TYR ALA ASP LEU ILE GLN          
SEQRES   6 O  230  LYS LEU GLN PRO GLU GLY PRO LEU THR LEU PHE GLY TYR          
SEQRES   7 O  230  SER ALA GLY CYS SER LEU ALA PHE GLU ALA ALA LYS LYS          
SEQRES   8 O  230  LEU GLU GLY GLN GLY ARG ILE VAL GLN ARG ILE ILE MET          
SEQRES   9 O  230  VAL ASP SER TYR LYS LYS GLN GLY VAL SER ASP LEU ASP          
SEQRES  10 O  230  GLY ARG THR VAL GLU SER ASP VAL GLU ALA LEU MET ASN          
SEQRES  11 O  230  VAL ASN ARG ASP ASN GLU ALA LEU ASN SER GLU ALA VAL          
SEQRES  12 O  230  LYS HIS GLY LEU LYS GLN LYS THR HIS ALA PHE TYR SER          
SEQRES  13 O  230  TYR TYR VAL ASN LEU ILE SER THR GLY GLN VAL LYS ALA          
SEQRES  14 O  230  ASP ILE ASP LEU LEU THR SER GLY ALA ASP PHE ASP ILE          
SEQRES  15 O  230  PRO GLU TRP LEU ALA SER TRP GLU GLU ALA THR THR GLY          
SEQRES  16 O  230  ALA TYR ARG MET LYS ARG GLY PHE GLY THR HIS ALA GLU          
SEQRES  17 O  230  MET LEU GLN GLY GLU THR LEU ASP ARG ASN ALA GLY ILE          
SEQRES  18 O  230  LEU LEU GLU PHE LEU ASN THR GLN THR                          
HET    SO4    501       5                                                       
HET    SO4    502       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S1 2-)                                                  
FORMUL   5  HOH   *238(H2 O1)                                                   
HELIX    1   1 TYR C   30  MET C   33  5                                   4    
HELIX    2   2 TYR C   34  LEU C   41  1                                   8    
HELIX    3   3 ASP C   56  GLN C   69  1                                  14    
HELIX    4   4 SER C   80  GLN C   96  1                                  17    
HELIX    5   5 ASP C  125  ASN C  133  1                                   9    
HELIX    6   6 GLU C  137  ASN C  140  5                                   4    
HELIX    7   7 SER C  141  LEU C  162  1                                  22    
HELIX    8   8 TRP C  190  ALA C  193  5                                   4    
HELIX    9   9 THR C  206  MET C  210  5                                   5    
HELIX   10  10 GLN C  212  ASN C  228  1                                  17    
HELIX   11  11 TYR O   30  MET O   33  5                                   4    
HELIX   12  12 TYR O   34  LEU O   41  1                                   8    
HELIX   13  13 ASP O   56  GLN O   69  1                                  14    
HELIX   14  14 ALA O   81  GLN O   96  1                                  16    
HELIX   15  15 THR O  121  MET O  130  1                                  10    
HELIX   16  16 ASN O  136  LEU O  139  5                                   4    
HELIX   17  17 ASN O  140  LEU O  162  1                                  23    
HELIX   18  18 TRP O  190  ALA O  193  5                                   4    
HELIX   19  19 THR O  206  MET O  210  5                                   5    
HELIX   20  20 GLN O  212  ASN O  228  1                                  17    
SHEET    1   A14 VAL C  10  MET C  13  0                                        
SHEET    2   A14 TYR C  44  PHE C  49 -1  O  LEU C  46   N  MET C  13           
SHEET    3   A14 GLN C  19  PHE C  24  1  O  GLN C  19   N  LYS C  45           
SHEET    4   A14 LEU C  74  TYR C  79  1  O  THR C  75   N  PHE C  22           
SHEET    5   A14 VAL C 100  VAL C 106  1  N  GLN C 101   O  LEU C  74           
SHEET    6   A14 ASP C 171  THR C 176  1  O  ASP C 171   N  ILE C 103           
SHEET    7   A14 TYR C 198  ARG C 202  1  N  ARG C 199   O  ILE C 172           
SHEET    8   A14 TYR O 198  ARG O 202 -1  N  TYR O 198   O  MET C 200           
SHEET    9   A14 ASP O 171  THR O 176  1  O  ILE O 172   N  ARG O 199           
SHEET   10   A14 VAL O 100  VAL O 106  1  O  GLN O 101   N  ASP O 171           
SHEET   11   A14 LEU O  74  TYR O  79  1  O  LEU O  74   N  GLN O 101           
SHEET   12   A14 GLN O  19  PHE O  24  1  N  PHE O  22   O  THR O  75           
SHEET   13   A14 TYR O  44  PHE O  49  1  N  LYS O  45   O  GLN O  19           
SHEET   14   A14 VAL O  10  MET O  13 -1  O  THR O  11   N  ALA O  48           
SHEET    1   B 2 LYS C 110  LYS C 111  0                                        
SHEET    2   B 2 LEU C 187  ALA C 188 -1  O  ALA C 188   N  LYS C 110           
SHEET    1   C 2 LYS O 110  LYS O 111  0                                        
SHEET    2   C 2 LEU O 187  ALA O 188 -1  O  ALA O 188   N  LYS O 110           
CRYST1   63.010   76.370  119.710  90.00  90.00  90.00 P 21 21 21    8          
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      0.015870  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013094  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008354        0.00000                         
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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