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LongText Report for: 1IMJ-pdb

Name Class
1IMJ-pdb
HEADER    HYDROLASE                               11-MAY-01   1IMJ              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING              
TITLE    2 FACTOR B (CIB)                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CCG1-INTERACTING FACTOR B;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CIB;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BACTERIA                                   
KEYWDS    ALPHA/BETA HYDROLASE, CCG1 INTERACTOR                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.PADMANABHAN,T.KUZUHARA,M.HORIKOSHI                                  
REVDAT   2   25-DEC-02 1IMJ    1       REMARK                                   
REVDAT   1   11-MAY-02 1IMJ    0                                                
JRNL        AUTH   B.PADMANABHAN,T.KUZUHARA,M.HORIKOSHI                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN                               
JRNL        TITL 2 CCG1/TAFII250-INTERACTING FACTOR B (CIB)                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.20 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10801                          
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 SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 568                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1592                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1559                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 192                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.90000                                             
REMARK   3    B22 (A**2) : -1.63000                                             
REMARK   3    B33 (A**2) : 2.53000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
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) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.06                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.220 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.850 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.030 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 31.18                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IMJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-2001.                
REMARK 100 THE RCSB ID CODE IS RCSB013411.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
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               : PHOTON FACTORY ; PHOTON            
REMARK 200                                   FACTORY                            
REMARK 200  BEAMLINE                       : BL18B; BL6A                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00; 1.00                         
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; IMAGE PLATE                   
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; FUJI               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10809                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.03900                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10500                            
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: MIR                          
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: 1.45-1.55M AMMONIUM SULFATE, 12MM        
REMARK 280  UREA, 70MM TRIS-HCL, PH 7.50, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   1/2-X,1/2+Y,-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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       55.35200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.22250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.35200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.22250            
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 1 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: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLN A   210                                                      
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   NE2  GLN A    30     NE2  GLN A    30     2645     2.18            
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    PRO A 105   CD    PRO A 105   CG     0.036                        
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    GLU A   9   N   -  CA  -  C   ANGL. DEV. = -8.0 DEGREES           
REMARK 500    ARG A  63   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    ILE A  84   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    GLY A 103   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    VAL A 106   N   -  CA  -  C   ANGL. DEV. = -9.8 DEGREES           
REMARK 500    LEU A 121   CA  -  CB  -  CG  ANGL. DEV. = 10.9 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 A 111     -118.20     40.36                                   
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   248        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH   264        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH   272        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH   288        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH   301        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH   302        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH   396        DISTANCE =  6.67 ANGSTROMS                       
DBREF  1IMJ A    1   210  GB     13938225 AAH07234         1    210             
SEQRES   1 A  210  MET ALA ALA SER VAL GLU GLN ARG GLU GLY THR ILE GLN          
SEQRES   2 A  210  VAL GLN GLY GLN ALA LEU PHE PHE ARG GLU ALA LEU PRO          
SEQRES   3 A  210  GLY SER GLY GLN ALA ARG PHE SER VAL LEU LEU LEU HIS          
SEQRES   4 A  210  GLY ILE ARG PHE SER SER GLU THR TRP GLN ASN LEU GLY          
SEQRES   5 A  210  THR LEU HIS ARG LEU ALA GLN ALA GLY TYR ARG ALA VAL          
SEQRES   6 A  210  ALA ILE ASP LEU PRO GLY LEU GLY HIS SER LYS GLU ALA          
SEQRES   7 A  210  ALA ALA PRO ALA PRO ILE GLY GLU LEU ALA PRO GLY SER          
SEQRES   8 A  210  PHE LEU ALA ALA VAL VAL ASP ALA LEU GLU LEU GLY PRO          
SEQRES   9 A  210  PRO VAL VAL ILE SER PRO SER LEU SER GLY MET TYR SER          
SEQRES  10 A  210  LEU PRO PHE LEU THR ALA PRO GLY SER GLN LEU PRO GLY          
SEQRES  11 A  210  PHE VAL PRO VAL ALA PRO ILE CYS THR ASP LYS ILE ASN          
SEQRES  12 A  210  ALA ALA ASN TYR ALA SER VAL LYS THR PRO ALA LEU ILE          
SEQRES  13 A  210  VAL TYR GLY ASP GLN ASP PRO MET GLY GLN THR SER PHE          
SEQRES  14 A  210  GLU HIS LEU LYS GLN LEU PRO ASN HIS ARG VAL LEU ILE          
SEQRES  15 A  210  MET LYS GLY ALA GLY HIS PRO CYS TYR LEU ASP LYS PRO          
SEQRES  16 A  210  GLU GLU TRP HIS THR GLY LEU LEU ASP PHE LEU GLN GLY          
SEQRES  17 A  210  LEU GLN                                                      
HET    SO4    210       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    O4 S1 2-                                                     
FORMUL   3  HOH   *192(H2 O1)                                                   
HELIX    1   1 SER A   44  GLY A   52  1                                   9    
HELIX    2   2 GLY A   52  ALA A   60  1                                   9    
HELIX    3   3 LEU A   72  LYS A   76  5                                   5    
HELIX    4   4 GLY A   90  GLU A  101  1                                  12    
HELIX    5   5 SER A  113  THR A  122  1                                  10    
SHEET    1   A 6 VAL A   5  GLN A   7  0                                        
SHEET    2   A 6 PHE A  21  LEU A  25 -1  N  GLU A  23   O  GLN A   7           
SHEET    3   A 6 ARG A  63  ILE A  67 -1  N  ALA A  64   O  ALA A  24           
SHEET    4   A 6 SER A  34  LEU A  37  1  O  VAL A  35   N  VAL A  65           
SHEET    5   A 6 VAL A 106  PRO A 110  1  O  VAL A 106   N  LEU A  36           
SHEET    1   B 2 ILE A  12  VAL A  14  0                                        
SHEET    2   B 2 GLN A  17  LEU A  19 -1  O  GLN A  17   N  VAL A  14           
CRYST1  110.704   44.445   43.601  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009030  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022500  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022940        0.00000                         
TER    1560      LEU A 209                                                      
MASTER      306    0    1    5    7    0    0    6 1756    1    5   17          
END                                                                             

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