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LongText Report for: 2UZ0-pdb

Name Class
2UZ0-pdb
HEADER    HYDROLASE                               23-APR-07   2UZ0              
TITLE     THE CRYSTAL CRYSTAL STRUCTURE OF THE ESTA PROTEIN, A                  
TITLE    2 VIRULENCE FACTOR ESTA PROTEIN FROM STREPTOCOCCUS PNEUMONIA           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRIBUTYRIN ESTERASE;                                       
COMPND   3 SYNONYM: ESTERASE;                                                   
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: RESIDUES 2-259;                                            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   3 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   4 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   5 ATCC: BAA-255D                                                       
KEYWDS    ESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE,                            
KEYWDS   2 A VIRULENCE FACTOR FOR LUNG INFECTION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.H.KIM,B.S.KANG,K.J.KIM,T.K.OH                                       
REVDAT   1   23-OCT-07 2UZ0    0                                                
JRNL        AUTH   M.H.KIM,B.S.KANG,S.KIM,K.J.KIM,C.H.LEE,B.C.OH,               
JRNL        AUTH 2 S.C.PARK,T.K.OH                                              
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE ESTA PROTEIN, A                 
JRNL        TITL 2 VIRULENCE FACTOR FROM STREPTOCOCCUS PNEUMONIAE.              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.7  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3   REFINEMENT TARGET : MAXIMUM LIKELIHOOD                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.65                          
REMARK   3   NUMBER OF REFLECTIONS             : 107413                         
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) : 0.18421                         
REMARK   3   R VALUE            (WORKING SET) : 0.18270                         
REMARK   3   FREE R VALUE                     : 0.21274                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5662                            
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) : 1.702                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.746                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7607                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.232                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 378                          
REMARK   3   BIN FREE R VALUE                    : 0.271                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7884                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 318                                     
REMARK   3   SOLVENT ATOMS            : 563                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.251                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28                                                
REMARK   3    B22 (A**2) : -0.42                                                
REMARK   3    B33 (A**2) : 0.78                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.55                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.105         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.949         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  8401 ; 0.011 ; 0.022          
REMARK   3   BOND LENGTHS OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   BOND ANGLES REFINED      (DEGREES): 11390 ; 1.307 ; 1.943          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):  1006 ; 6.113 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):   391 ;31.784 ;23.990          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):  1364 ;14.103 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):    32 ;20.207 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):  1188 ; 0.091 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  6405 ; 0.005 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  4269 ; 0.318 ; 0.200          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION REFINED     (A):  5664 ; 0.328 ; 0.200          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  NULL ;  NULL ;  NULL          
REMARK   3   H-BOND (X...Y) REFINED         (A):   602 ; 0.104 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):    36 ; 0.167 ; 0.200          
REMARK   3   SYMMETRY VDW OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY H-BOND REFINED        (A):    16 ; 0.161 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  5118 ; 1.110 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  7981 ; 1.111 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  3924 ; 2.083 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  3401 ; 2.896 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -4        A   257                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5520   0.1450  44.6390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0580 T22:  -0.0526                                     
REMARK   3      T33:   0.0248 T12:   0.0033                                     
REMARK   3      T13:   0.0117 T23:   0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7928 L22:   0.4305                                     
REMARK   3      L33:   0.3158 L12:  -0.0324                                     
REMARK   3      L13:   0.0329 L23:   0.0270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.0039 S13:  -0.0461                       
REMARK   3      S21:   0.0004 S22:  -0.0003 S23:  -0.0407                       
REMARK   3      S31:   0.0237 S32:   0.0013 S33:   0.0027                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -4        B   257                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6970   5.7370  40.2130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0651 T22:  -0.0448                                     
REMARK   3      T33:   0.0310 T12:  -0.0027                                     
REMARK   3      T13:   0.0068 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8877 L22:   0.2579                                     
REMARK   3      L33:   0.3666 L12:   0.0903                                     
REMARK   3      L13:  -0.1923 L23:  -0.0265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0014 S12:   0.0612 S13:  -0.0660                       
REMARK   3      S21:  -0.0013 S22:  -0.0085 S23:   0.0459                       
REMARK   3      S31:  -0.0127 S32:   0.0002 S33:   0.0100                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     3                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -4        C   253                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7910  20.5190  14.0280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0287 T22:   0.0000                                     
REMARK   3      T33:  -0.0519 T12:   0.0025                                     
REMARK   3      T13:   0.0230 T23:   0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6578 L22:   0.5797                                     
REMARK   3      L33:   0.8875 L12:   0.1670                                     
REMARK   3      L13:  -0.0453 L23:   0.0481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:   0.1182 S13:   0.0170                       
REMARK   3      S21:  -0.1141 S22:  -0.0051 S23:  -0.0079                       
REMARK   3      S31:  -0.0754 S32:   0.0513 S33:   0.0028                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     4                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    -4        D   257                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6200 -10.3970  10.3370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0493 T22:   0.0017                                     
REMARK   3      T33:   0.0302 T12:  -0.0040                                     
REMARK   3      T13:  -0.0181 T23:  -0.1199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1255 L22:   0.5264                                     
REMARK   3      L33:   1.0113 L12:   0.0132                                     
REMARK   3      L13:   0.0740 L23:   0.0340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0349 S12:   0.2256 S13:  -0.2615                       
REMARK   3      S21:  -0.1059 S22:  -0.0519 S23:   0.0940                       
REMARK   3      S31:   0.1423 S32:  -0.0605 S33:   0.0170                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2UZ0 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 23-APR-2007.                
REMARK 100 THE EBI ID CODE IS EBI-32331.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS BEAMLINE 4A                
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113097                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: STARTING MODEL FOR MR WAS A PARTIALLY REFINED MODEL          
REMARK 200  OF THE SEMET CRYSTAL AT A 1.9A.                                     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (V/V) PEG 6000,8% (V/V)              
REMARK 280  ETHYLENE GLYCOL,4% (V/V) 2-METHYL-2,4-PENTANEDIOL,10 MM             
REMARK 280  CYSTEINE,0.1 M TRIS-HCL PH 7.0                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.06400            
REMARK 290   SMTRY3   2  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 PROGRAM                   
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK ALSO PROVIDES INFORMATION ON                 
REMARK 300 BURIED SURFACE AREA.                                                 
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 AVERAGE BURIED SURFACE AREA: 3232.4 ANGSTROM**2                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     CYS A    33                                                      
REMARK 465     THR A   258                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     CYS B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     THR B   258                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     ASN C    26                                                      
REMARK 465     ARG C    27                                                      
REMARK 465     VAL C    28                                                      
REMARK 465     GLU C    29                                                      
REMARK 465     GLU C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     CYS C    33                                                      
REMARK 465     GLU C   254                                                      
REMARK 465     GLU C   255                                                      
REMARK 465     ARG C   256                                                      
REMARK 465     LEU C   257                                                      
REMARK 465     THR C   258                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     ASN D    26                                                      
REMARK 465     ARG D    27                                                      
REMARK 465     VAL D    28                                                      
REMARK 465     GLU D    29                                                      
REMARK 465     GLU D    30                                                      
REMARK 465     PRO D    31                                                      
REMARK 465     GLU D    32                                                      
REMARK 465     CYS D    33                                                      
REMARK 465     PHE D   151                                                      
REMARK 465     SER D   152                                                      
REMARK 465     PRO D   153                                                      
REMARK 465     GLU D   154                                                      
REMARK 465     SER D   155                                                      
REMARK 465     GLN D   156                                                      
REMARK 465     ASN D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     THR D   258                                                      
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     VAL A  18    CG1  CG2                                            
REMARK 470     VAL B  18    CG1  CG2                                            
REMARK 470     ARG B 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C  18    CG1  CG2                                            
REMARK 470     VAL D  18    CG1  CG2                                            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A 252    CD   CE   NZ                                        
REMARK 480     LYS B 252    CG   CD   CE   NZ                                   
REMARK 480     GLU B 255    CG   CD  OE1  OE2                                   
REMARK 480     LYS C 101    CD   CE   NZ                                        
REMARK 480     ARG C 172    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     LYS C 191    CE   NZ                                             
REMARK 480     ARG D 172    CB   CG   CD   NE   CZ  NH1  NH2                    
REMARK 480     LYS D 193    CD   CE   NZ                                        
REMARK 480     ASP D 250    CG  OD1  OD2                                        
REMARK 480     LYS D 252    CG   CD   CE   NZ                                   
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, 1999                                
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 252   CB  -  CG  -  CD  ANGL. DEV. =  19.0 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 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    MSE A  -2      -13.16     77.74                                   
REMARK 500    SER A  46       -9.61     77.84                                   
REMARK 500    SER A 120     -114.38     50.76                                   
REMARK 500    MSE B  -2      -12.34     80.29                                   
REMARK 500    SER B  46       -4.29     78.40                                   
REMARK 500    SER B 120     -114.56     50.66                                   
REMARK 500    MSE C  -2      -13.44     82.30                                   
REMARK 500    SER C  46       -7.11     78.18                                   
REMARK 500    ASN C  57       34.32    -92.56                                   
REMARK 500    SER C 120     -119.15     52.16                                   
REMARK 500    MSE D  -2      -11.27     78.05                                   
REMARK 500    SER D  46       -8.41     77.21                                   
REMARK 500    ASN D  57       34.60    -88.67                                   
REMARK 500    SER D 120     -116.79     58.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS C  252     LEU C  253          0       140.63                    
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1258  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU C  53   O                                                      
REMARK 620 2 HOH A2039   O    82.6                                              
REMARK 620 3 HOH A2043   O    94.1  88.0                                        
REMARK 620 4 HOH C2038   O    91.5 168.4  82.5                                  
REMARK 620 5 HOH C2043   O    86.3  96.6 175.4  92.9                            
REMARK 620 6 LEU A  53   O   162.3  79.7  85.8 106.0  95.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1258  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU D  53   O                                                      
REMARK 620 2 LEU B  53   O   163.0                                              
REMARK 620 3 HOH B2038   O    83.0  80.0                                        
REMARK 620 4 HOH B2040   O    95.9  84.8  93.4                                  
REMARK 620 5 HOH B2035   O    98.9  98.0 177.5  84.8                            
REMARK 620 6 HOH D2036   O    87.1  94.4  94.0 172.3  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN B                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CFN   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF A VIRULENCE FACTOR                         
REMARK 900   ESTA FROM STREPTOCOCCUS PNEUMONIAE                                 
DBREF  2UZ0 A   -4     0  PDB    2UZ0     2UZ0            -4      0             
DBREF  2UZ0 A    1   258  UNP    Q97S09   Q97S09_STRPN     2    259             
DBREF  2UZ0 B   -4     0  PDB    2UZ0     2UZ0            -4      0             
DBREF  2UZ0 B    1   258  UNP    Q97S09   Q97S09_STRPN     2    259             
DBREF  2UZ0 C   -4     0  PDB    2UZ0     2UZ0            -4      0             
DBREF  2UZ0 C    1   258  UNP    Q97S09   Q97S09_STRPN     2    259             
DBREF  2UZ0 D   -4     0  PDB    2UZ0     2UZ0            -4      0             
DBREF  2UZ0 D    1   258  UNP    Q97S09   Q97S09_STRPN     2    259             
SEQRES   1 A  263  GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR          
SEQRES   2 A  263  SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU          
SEQRES   3 A  263  TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU          
SEQRES   4 A  263  ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY          
SEQRES   5 A  263  ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG          
SEQRES   6 A  263  LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN          
SEQRES   7 A  263  THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE          
SEQRES   8 A  263  ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL          
SEQRES   9 A  263  LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU          
SEQRES  10 A  263  LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY          
SEQRES  11 A  263  CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS          
SEQRES  12 A  263  ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE          
SEQRES  13 A  263  SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP          
SEQRES  14 A  263  ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER          
SEQRES  15 A  263  PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS          
SEQRES  16 A  263  LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE          
SEQRES  17 A  263  LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS          
SEQRES  18 A  263  LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY          
SEQRES  19 A  263  THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL          
SEQRES  20 A  263  PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU          
SEQRES  21 A  263  ARG LEU THR                                                  
SEQRES   1 B  263  GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR          
SEQRES   2 B  263  SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU          
SEQRES   3 B  263  TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU          
SEQRES   4 B  263  ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY          
SEQRES   5 B  263  ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG          
SEQRES   6 B  263  LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN          
SEQRES   7 B  263  THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE          
SEQRES   8 B  263  ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL          
SEQRES   9 B  263  LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU          
SEQRES  10 B  263  LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY          
SEQRES  11 B  263  CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS          
SEQRES  12 B  263  ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE          
SEQRES  13 B  263  SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP          
SEQRES  14 B  263  ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER          
SEQRES  15 B  263  PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS          
SEQRES  16 B  263  LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE          
SEQRES  17 B  263  LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS          
SEQRES  18 B  263  LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY          
SEQRES  19 B  263  THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL          
SEQRES  20 B  263  PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU          
SEQRES  21 B  263  ARG LEU THR                                                  
SEQRES   1 C  263  GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR          
SEQRES   2 C  263  SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU          
SEQRES   3 C  263  TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU          
SEQRES   4 C  263  ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY          
SEQRES   5 C  263  ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG          
SEQRES   6 C  263  LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN          
SEQRES   7 C  263  THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE          
SEQRES   8 C  263  ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL          
SEQRES   9 C  263  LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU          
SEQRES  10 C  263  LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY          
SEQRES  11 C  263  CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS          
SEQRES  12 C  263  ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE          
SEQRES  13 C  263  SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP          
SEQRES  14 C  263  ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER          
SEQRES  15 C  263  PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS          
SEQRES  16 C  263  LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE          
SEQRES  17 C  263  LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS          
SEQRES  18 C  263  LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY          
SEQRES  19 C  263  THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL          
SEQRES  20 C  263  PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU          
SEQRES  21 C  263  ARG LEU THR                                                  
SEQRES   1 D  263  GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR          
SEQRES   2 D  263  SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU          
SEQRES   3 D  263  TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU          
SEQRES   4 D  263  ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY          
SEQRES   5 D  263  ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG          
SEQRES   6 D  263  LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN          
SEQRES   7 D  263  THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE          
SEQRES   8 D  263  ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL          
SEQRES   9 D  263  LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU          
SEQRES  10 D  263  LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY          
SEQRES  11 D  263  CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS          
SEQRES  12 D  263  ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE          
SEQRES  13 D  263  SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP          
SEQRES  14 D  263  ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER          
SEQRES  15 D  263  PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS          
SEQRES  16 D  263  LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE          
SEQRES  17 D  263  LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS          
SEQRES  18 D  263  LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY          
SEQRES  19 D  263  THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL          
SEQRES  20 D  263  PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU          
SEQRES  21 D  263  ARG LEU THR                                                  
MODRES 2UZ0 MSE A   -2  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A    3  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A   14  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A   45  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A   71  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A  107  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE A  121  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B   -2  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B    3  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B   14  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B   45  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B   71  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B  107  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE B  121  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C   -2  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C    3  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C   14  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C   45  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C   71  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C  107  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE C  121  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D   -2  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D    3  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D   14  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D   45  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D   71  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D  107  MET  SELENOMETHIONINE                                   
MODRES 2UZ0 MSE D  121  MET  SELENOMETHIONINE                                   
HET    MSE  A  -2       8                                                       
HET    MSE  A   3      13                                                       
HET    MSE  A  14      13                                                       
HET    MSE  A  45       8                                                       
HET    MSE  A  71       8                                                       
HET    MSE  A 107       8                                                       
HET    MSE  A 121       8                                                       
HET    MSE  B  -2       8                                                       
HET    MSE  B   3      13                                                       
HET    MSE  B  14      13                                                       
HET    MSE  B  45       8                                                       
HET    MSE  B  71       8                                                       
HET    MSE  B 107       8                                                       
HET    MSE  B 121       8                                                       
HET    MSE  C  -2       8                                                       
HET    MSE  C   3      13                                                       
HET    MSE  C  14      13                                                       
HET    MSE  C  45       8                                                       
HET    MSE  C  71       8                                                       
HET    MSE  C 107       8                                                       
HET    MSE  C 121       8                                                       
HET    MSE  D  -2       8                                                       
HET    MSE  D   3      13                                                       
HET    MSE  D  14      13                                                       
HET    MSE  D  45       8                                                       
HET    MSE  D  71       8                                                       
HET    MSE  D 107       8                                                       
HET    MSE  D 121       8                                                       
HET     CA  A1258       1                                                       
HET     CA  B1258       1                                                       
HET    GOL  A1259       6                                                       
HET    GOL  A1260       6                                                       
HET    GOL  C1254       6                                                       
HET    GOL  D1258       6                                                       
HET    GOL  C1255       6                                                       
HET    GOL  D1259       6                                                       
HET    EDO  C1256       4                                                       
HET    EDO  A1261       4                                                       
HET    EDO  C1257       4                                                       
HET    EDO  B1259       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   5  EDO    4(C2 H6 O2)                                                  
FORMUL   6   CA    2(CA 2+)                                                     
FORMUL   7  GOL    6(C3 H8 O3)                                                  
FORMUL   8  MSE    28(C5 H11 N O2 SE)                                           
FORMUL   9  HOH   *563(H2 O1)                                                   
HELIX    1   1 ASN A   50  THR A   56  1                                   7    
HELIX    2   2 ASN A   57  LEU A   62  1                                   6    
HELIX    3   3 ASP A   87  GLU A   94  1                                   8    
HELIX    4   4 GLU A   94  PHE A  104  1                                  11    
HELIX    5   5 LYS A  110  GLU A  112  5                                   3    
HELIX    6   6 SER A  120  ASN A  134  1                                  15    
HELIX    7   7 SER A  152  GLN A  156  5                                   5    
HELIX    8   8 SER A  160  GLY A  169  1                                  10    
HELIX    9   9 SER A  180  ALA A  185  1                                   6    
HELIX   10  10 LYS A  186  SER A  188  5                                   3    
HELIX   11  11 LEU A  204  LEU A  218  1                                  15    
HELIX   12  12 GLU A  232  LEU A  247  1                                  16    
HELIX   13  13 ASN B   50  THR B   56  1                                   7    
HELIX   14  14 ASN B   57  LEU B   62  1                                   6    
HELIX   15  15 ASP B   87  GLU B   94  1                                   8    
HELIX   16  16 GLU B   94  PHE B  104  1                                  11    
HELIX   17  17 LYS B  110  GLU B  112  5                                   3    
HELIX   18  18 SER B  120  ASN B  134  1                                  15    
HELIX   19  19 SER B  152  ASN B  157  5                                   6    
HELIX   20  20 SER B  160  GLY B  169  1                                  10    
HELIX   21  21 SER B  180  ALA B  185  1                                   6    
HELIX   22  22 LYS B  186  SER B  188  5                                   3    
HELIX   23  23 LEU B  204  LEU B  218  1                                  15    
HELIX   24  24 GLU B  232  THR B  245  1                                  14    
HELIX   25  25 ASN C   50  THR C   56  1                                   7    
HELIX   26  26 ASN C   57  LEU C   62  1                                   6    
HELIX   27  27 ASP C   87  GLU C   94  1                                   8    
HELIX   28  28 GLU C   94  PHE C  104  1                                  11    
HELIX   29  29 LYS C  110  GLU C  112  5                                   3    
HELIX   30  30 SER C  120  ASN C  134  1                                  15    
HELIX   31  31 SER C  152  ASN C  157  5                                   6    
HELIX   32  32 SER C  160  GLY C  169  1                                  10    
HELIX   33  33 SER C  180  ALA C  185  1                                   6    
HELIX   34  34 LYS C  186  SER C  188  5                                   3    
HELIX   35  35 LEU C  204  LEU C  218  1                                  15    
HELIX   36  36 GLU C  232  THR C  246  1                                  15    
HELIX   37  37 ASN D   50  THR D   56  1                                   7    
HELIX   38  38 ASN D   57  LEU D   62  1                                   6    
HELIX   39  39 ASP D   87  GLU D   94  1                                   8    
HELIX   40  40 GLU D   94  PHE D  104  1                                  11    
HELIX   41  41 LYS D  110  GLU D  112  5                                   3    
HELIX   42  42 SER D  120  ASN D  134  1                                  15    
HELIX   43  43 SER D  160  GLY D  169  1                                  10    
HELIX   44  44 SER D  180  ALA D  185  1                                   6    
HELIX   45  45 LYS D  186  SER D  188  5                                   3    
HELIX   46  46 LEU D  204  LEU D  218  1                                  15    
HELIX   47  47 GLU D  232  THR D  245  1                                  14    
SHEET    1  AA16 ASP A 221  SER A 227  0                                        
SHEET    2  AA16 LYS A 193  GLY A 199  1  O  LEU A 194   N  THR A 223           
SHEET    3  AA16 HIS A 138  PHE A 142  1  O  ALA A 139   N  TRP A 195           
SHEET    4  AA16 THR A 114  LEU A 119  1  O  ILE A 116   N  ALA A 140           
SHEET    5  AA16 VAL A  38  LEU A  42  1  O  VAL A  38   N  PHE A 115           
SHEET    6  AA16 ILE A  68  MSE A  71  1  O  ILE A  68   N  LEU A  39           
SHEET    7  AA16 MSE A  14  TYR A  22 -1  O  ASN A  19   N  MSE A  71           
SHEET    8  AA16 ALA A   1  SER A   9 -1  O  ALA A   1   N  TYR A  22           
SHEET    9  AA16 ALA D   1  SER D   9 -1  O  VAL D   2   N  GLU A   6           
SHEET   10  AA16 MSE D  14  TYR D  22 -1  O  MSE D  14   N  SER D   9           
SHEET   11  AA16 ILE D  68  MSE D  71 -1  O  VAL D  69   N  LEU D  21           
SHEET   12  AA16 VAL D  38  LEU D  42  1  O  LEU D  39   N  VAL D  70           
SHEET   13  AA16 THR D 114  LEU D 119  1  O  PHE D 115   N  TYR D  40           
SHEET   14  AA16 HIS D 138  PHE D 142  1  O  HIS D 138   N  ILE D 116           
SHEET   15  AA16 LYS D 193  GLY D 199  1  O  LYS D 193   N  ALA D 139           
SHEET   16  AA16 VAL D 222  SER D 227  1  O  THR D 223   N  ALA D 196           
SHEET    1  BA16 VAL B 222  SER B 227  0                                        
SHEET    2  BA16 LYS B 193  GLY B 199  1  O  LEU B 194   N  THR B 223           
SHEET    3  BA16 HIS B 138  PHE B 142  1  O  ALA B 139   N  TRP B 195           
SHEET    4  BA16 THR B 114  LEU B 119  1  O  ILE B 116   N  ALA B 140           
SHEET    5  BA16 VAL B  38  LEU B  42  1  O  VAL B  38   N  PHE B 115           
SHEET    6  BA16 ILE B  68  MSE B  71  1  O  ILE B  68   N  LEU B  39           
SHEET    7  BA16 MSE B  14  TYR B  22 -1  O  ASN B  19   N  MSE B  71           
SHEET    8  BA16 ALA B   1  SER B   9 -1  O  ALA B   1   N  TYR B  22           
SHEET    9  BA16 ALA C   1  SER C   9 -1  O  VAL C   2   N  GLU B   6           
SHEET   10  BA16 MSE C  14  TYR C  22 -1  O  MSE C  14   N  SER C   9           
SHEET   11  BA16 ILE C  68  MSE C  71 -1  O  VAL C  69   N  LEU C  21           
SHEET   12  BA16 VAL C  38  LEU C  42  1  O  LEU C  39   N  VAL C  70           
SHEET   13  BA16 THR C 114  LEU C 119  1  O  PHE C 115   N  TYR C  40           
SHEET   14  BA16 HIS C 138  PHE C 142  1  O  HIS C 138   N  ILE C 116           
SHEET   15  BA16 LYS C 193  GLY C 199  1  O  LYS C 193   N  ALA C 139           
SHEET   16  BA16 VAL C 222  SER C 227  1  O  THR C 223   N  ALA C 196           
LINK         C   ALA A  -3                 N   MSE A  -2     1555   1555  1.33  
LINK         C   MSE A  -2                 N   ASP A  -1     1555   1555  1.33  
LINK         C   VAL A   2                 N   MSE A   3     1555   1555  1.33  
LINK         C   MSE A   3                 N   LYS A   4     1555   1555  1.33  
LINK         C   ASP A  13                 N   MSE A  14     1555   1555  1.33  
LINK         C   MSE A  14                 N   GLU A  15     1555   1555  1.33  
LINK         C   GLY A  44                 N   MSE A  45     1555   1555  1.32  
LINK         C   MSE A  45                 N   SER A  46     1555   1555  1.33  
LINK         C   VAL A  70                 N   MSE A  71     1555   1555  1.33  
LINK         C   MSE A  71                 N   PRO A  72     1555   1555  1.35  
LINK         C   ASN A 106                 N   MSE A 107     1555   1555  1.33  
LINK         C   MSE A 107                 N   THR A 108     1555   1555  1.33  
LINK         C   SER A 120                 N   MSE A 121     1555   1555  1.34  
LINK         C   MSE A 121                 N   GLY A 122     1555   1555  1.33  
LINK        CA    CA A1258                 O   LEU C  53     1555   1555  2.32  
LINK        CA    CA A1258                 O   HOH A2039     1555   1555  2.32  
LINK        CA    CA A1258                 O   HOH C2043     1555   1555  2.33  
LINK        CA    CA A1258                 O   LEU A  53     1555   1555  2.32  
LINK        CA    CA A1258                 O   HOH A2043     1555   1555  2.39  
LINK        CA    CA A1258                 O   HOH C2038     1555   1555  2.29  
LINK         C   ALA B  -3                 N   MSE B  -2     1555   1555  1.33  
LINK         C   MSE B  -2                 N   ASP B  -1     1555   1555  1.33  
LINK         C   VAL B   2                 N   MSE B   3     1555   1555  1.34  
LINK         C   MSE B   3                 N   LYS B   4     1555   1555  1.33  
LINK         C   ASP B  13                 N   MSE B  14     1555   1555  1.33  
LINK         C   MSE B  14                 N   GLU B  15     1555   1555  1.33  
LINK         C   GLY B  44                 N   MSE B  45     1555   1555  1.33  
LINK         C   MSE B  45                 N   SER B  46     1555   1555  1.34  
LINK         C   VAL B  70                 N   MSE B  71     1555   1555  1.33  
LINK         C   MSE B  71                 N   PRO B  72     1555   1555  1.35  
LINK         C   ASN B 106                 N   MSE B 107     1555   1555  1.33  
LINK         C   MSE B 107                 N   THR B 108     1555   1555  1.33  
LINK         C   SER B 120                 N   MSE B 121     1555   1555  1.34  
LINK         C   MSE B 121                 N   GLY B 122     1555   1555  1.33  
LINK        CA    CA B1258                 O   HOH B2040     1555   1555  2.41  
LINK        CA    CA B1258                 O   HOH B2038     1555   1555  2.33  
LINK        CA    CA B1258                 O   LEU B  53     1555   1555  2.30  
LINK        CA    CA B1258                 O   LEU D  53     1555   1555  2.30  
LINK        CA    CA B1258                 O   HOH D2036     1555   1555  2.40  
LINK        CA    CA B1258                 O   HOH B2035     1555   1555  2.34  
LINK         C   MSE C  -2                 N   ASP C  -1     1555   1555  1.33  
LINK         C   ALA C  -3                 N   MSE C  -2     1555   1555  1.33  
LINK         C   VAL C   2                 N   MSE C   3     1555   1555  1.33  
LINK         C   MSE C   3                 N   LYS C   4     1555   1555  1.33  
LINK         C   ASP C  13                 N   MSE C  14     1555   1555  1.33  
LINK         C   MSE C  14                 N   GLU C  15     1555   1555  1.33  
LINK         C   GLY C  44                 N   MSE C  45     1555   1555  1.33  
LINK         C   MSE C  45                 N   SER C  46     1555   1555  1.34  
LINK         C   VAL C  70                 N   MSE C  71     1555   1555  1.33  
LINK         C   MSE C  71                 N   PRO C  72     1555   1555  1.34  
LINK         C   ASN C 106                 N   MSE C 107     1555   1555  1.33  
LINK         C   MSE C 107                 N   THR C 108     1555   1555  1.33  
LINK         C   SER C 120                 N   MSE C 121     1555   1555  1.34  
LINK         C   MSE C 121                 N   GLY C 122     1555   1555  1.33  
LINK         C   MSE D  -2                 N   ASP D  -1     1555   1555  1.33  
LINK         C   ALA D  -3                 N   MSE D  -2     1555   1555  1.33  
LINK         C   VAL D   2                 N   MSE D   3     1555   1555  1.32  
LINK         C   MSE D   3                 N   LYS D   4     1555   1555  1.33  
LINK         C   ASP D  13                 N   MSE D  14     1555   1555  1.33  
LINK         C   MSE D  14                 N   GLU D  15     1555   1555  1.33  
LINK         C   GLY D  44                 N   MSE D  45     1555   1555  1.33  
LINK         C   MSE D  45                 N   SER D  46     1555   1555  1.34  
LINK         C   VAL D  70                 N   MSE D  71     1555   1555  1.33  
LINK         C   MSE D  71                 N   PRO D  72     1555   1555  1.34  
LINK         C   ASN D 106                 N   MSE D 107     1555   1555  1.33  
LINK         C   MSE D 107                 N   THR D 108     1555   1555  1.33  
LINK         C   SER D 120                 N   MSE D 121     1555   1555  1.33  
LINK         C   MSE D 121                 N   GLY D 122     1555   1555  1.33  
SITE     1 AC1  6 LEU A  53  HOH A2039  HOH A2043  LEU C  53                    
SITE     2 AC1  6 HOH C2038  HOH C2043                                          
SITE     1 AC2  6 LEU B  53  HOH B2035  HOH B2038  HOH B2040                    
SITE     2 AC2  6 LEU D  53  HOH D2036                                          
SITE     1 AC3  6 GLY A  44  SER A  46  SER A 120  HIS A 231                    
SITE     2 AC3  6 TRP A 236  HOH A2027                                          
SITE     1 AC4  9 LEU A  12  ASP A  13  GLY A  85  PHE A  86                    
SITE     2 AC4  9 HOH A2010  HOH A2153  ASN B  76  GLY B 159                    
SITE     3 AC4  9 TYR B 163                                                     
SITE     1 AC5  8 LEU C  12  GLY C  85  PHE C  86  HOH C2015                    
SITE     2 AC5  8 HOH C2063  ASN D  76  GLY D 159  TYR D 163                    
SITE     1 AC6  8 ASN C  76  GLY C 159  TYR C 163  LEU D  12                    
SITE     2 AC6  8 GLY D  85  PHE D  86  HOH D2016  HOH D2017                    
SITE     1 AC7  6 GLY C  44  LEU C 119  SER C 120  HIS C 231                    
SITE     2 AC7  6 HOH C2080  HOH C2139                                          
SITE     1 AC8  6 GLY D  44  LEU D 119  SER D 120  HIS D 231                    
SITE     2 AC8  6 HOH D2063  HOH D2091                                          
SITE     1 AC9  8 TRP C  16  ASN C  73  SER C  75  HOH C2019                    
SITE     2 AC9  8 HOH C2140  TRP D  16  ASN D  73  SER D  75                    
SITE     1 BC1  8 TRP A  16  ASN A  73  SER A  75  HOH A2154                    
SITE     2 BC1  8 TRP B  16  ASN B  73  SER B  75  HOH B2009                    
SITE     1 BC2  7 SER C 109  LYS C 110  ARG C 111  THR C 114                    
SITE     2 BC2  7 ARG C 135  HOH C2079  HOH C2141                               
SITE     1 BC3  5 ASN A  76  TYR A 163  LEU B  12  GLY B  85                    
SITE     2 BC3  5 PHE B  86                                                     
CRYST1   71.695   72.128  101.827  90.00  94.31  90.00 P 1 21 1      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      0.013948  0.000000  0.001051        0.00000                         
SCALE2      0.000000  0.013864  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009848        0.00000                         
TER    2067      LEU A 257                                                      
TER    4119      LEU B 257                                                      
TER    6149      LEU C 253                                                      
TER    8152      LEU D 257                                                      
MASTER      513    0   40   47   32    0   25    6 8765    4  385   84          
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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