GenomeNet

Database: PDB
Entry: 4IVK
LinkDB: 4IVK
Original site: 4IVK 
HEADER    HYDROLASE                               23-JAN-13   4IVK              
TITLE     CRYSTAL STRUCTURE OF A FAMMILY VIII CARBOXYLESTERASE IN A COMPLEX WITH
TITLE    2 CEPHALOTHIN.                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLESTERASES;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 OTHER_DETAILS: DEEP SEA SEDIMENT                                     
KEYWDS    HELICAL DOMAIN AND A ALPHA/BETA DOMAIN, DEEP SEA SEDIMENT, HYDROLASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.J.AN,M.-K.KIM,C.-S.JEONG,S.-S.CHA                                   
REVDAT   3   20-SEP-23 4IVK    1       REMARK SEQADV LINK                       
REVDAT   2   30-OCT-13 4IVK    1       JRNL                                     
REVDAT   1   19-JUN-13 4IVK    0                                                
JRNL        AUTH   S.S.CHA,Y.J.AN,C.S.JEONG,M.K.KIM,J.H.JEON,C.M.LEE,H.S.LEE,   
JRNL        AUTH 2 S.G.KANG,J.H.LEE                                             
JRNL        TITL   STRUCTURAL BASIS FOR THE BETA-LACTAMASE ACTIVITY OF ESTU1, A 
JRNL        TITL 2 FAMILY VIII CARBOXYLESTERASE.                                
JRNL        REF    PROTEINS                      V.  81  2045 2013              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   23737193                                                     
JRNL        DOI    10.1002/PROT.24334                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 84680                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4471                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6197                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 327                          
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 338                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.18000                                             
REMARK   3    B22 (A**2) : -1.18000                                             
REMARK   3    B33 (A**2) : 2.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.039         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.725         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3197 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3037 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4329 ; 1.139 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7009 ; 0.749 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   403 ; 5.566 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;29.294 ;23.651       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   529 ;12.004 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;13.039 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   472 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3594 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   698 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6234 ; 1.564 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    93 ;27.141 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6410 ; 8.950 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4IVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000077263.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89398                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 4IVI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE AND 0.1 M TRIS    
REMARK 280  -HCL (PH 8.5), MICROBATCH, TEMPERATURE 295KK                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       74.55100            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       86.28550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       74.55100            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       86.28550            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       74.55100            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       86.28550            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       74.55100            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       86.28550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.55100            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       86.28550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.55100            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       86.28550            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       74.55100            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       86.28550            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       74.55100            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       74.55100            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       86.28550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 109670 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 914  LIES ON A SPECIAL POSITION.                          
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     LYS A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     PHE A    24                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS A   434                                                      
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     GLU A  26    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  26      -56.58    161.41                                   
REMARK 500    TYR A  99     -119.05     43.24                                   
REMARK 500    LEU A 245      -59.37   -131.69                                   
REMARK 500    ASP A 274       45.25   -141.80                                   
REMARK 500    GLN A 296       -8.63   -154.79                                   
REMARK 500    VAL A 369      -68.15     70.52                                   
REMARK 500    PRO A 371       32.37    -83.07                                   
REMARK 500    VAL A 406      -70.12   -127.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CEP A  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IVI   RELATED DB: PDB                                   
DBREF  4IVK A    1   426  UNP    K4HQE7   K4HQE7_9BACT     1    426             
SEQADV 4IVK LEU A  427  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK GLU A  428  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  429  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  430  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  431  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  432  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  433  UNP  K4HQE7              EXPRESSION TAG                 
SEQADV 4IVK HIS A  434  UNP  K4HQE7              EXPRESSION TAG                 
SEQRES   1 A  434  MET LYS THR SER ALA LYS PHE LEU SER PHE ALA VAL SER          
SEQRES   2 A  434  PHE VAL LEU LEU ILE ILE ALA SER THR SER PHE ALA GLU          
SEQRES   3 A  434  GLY PRO VAL THR ALA THR LYS PRO LYS GLU ALA GLY PHE          
SEQRES   4 A  434  THR SER GLU GLY LEU ALA ARG ILE ASP ALA TYR LEU LYS          
SEQRES   5 A  434  ASN GLU ILE GLN ALA LYS THR MET PRO GLY ALA VAL MET          
SEQRES   6 A  434  MET ILE LYS ARG ASN GLY GLU THR ALA TYR PHE SER SER          
SEQRES   7 A  434  PHE GLY LEU ARG ASP PRO ASP THR LYS GLU PRO MET THR          
SEQRES   8 A  434  ALA GLU THR ILE PHE ARG ILE TYR SER MET SER LYS PRO          
SEQRES   9 A  434  ILE THR THR VAL ALA ALA MET MET LEU VAL GLU GLU GLY          
SEQRES  10 A  434  LYS LEU GLN LEU ASP GLU PRO VAL SER LYS TYR ILE PRO          
SEQRES  11 A  434  SER PHE ALA ASN VAL LYS VAL GLY VAL GLU THR LYS GLY          
SEQRES  12 A  434  GLU ASN GLY MET ALA LEU GLU THR GLY PRO VAL LYS ARG          
SEQRES  13 A  434  ALA ILE THR ILE GLN ASP LEU MET ARG HIS THR SER GLY          
SEQRES  14 A  434  ILE THR TYR GLY PHE VAL GLY ASP GLY LEU VAL LYS LYS          
SEQRES  15 A  434  ALA TYR ILE ALA SER ASN LEU PHE ASP GLY ASP PHE ASP          
SEQRES  16 A  434  ASN ALA GLU PHE ALA GLU ARG ILE ALA LYS LEU PRO LEU          
SEQRES  17 A  434  VAL TYR GLN PRO GLY THR THR TRP ASP TYR GLY HIS SER          
SEQRES  18 A  434  THR ASP ILE LEU GLY ARG VAL VAL GLU VAL VAL SER GLY          
SEQRES  19 A  434  LYS SER LEU TYR GLN PHE GLU LYS GLU ARG LEU LEU ASP          
SEQRES  20 A  434  PRO LEU GLY MET LYS ASP THR GLY PHE TYR VAL THR ASP          
SEQRES  21 A  434  PRO ALA LYS LYS SER LEU VAL ALA GLU ALA MET PRO ASN          
SEQRES  22 A  434  ASP ARG LYS ILE GLY GLY SER GLU MET PHE ASP PRO ARG          
SEQRES  23 A  434  VAL GLN LYS LYS TRP GLU PRO GLY GLY GLN GLY MET VAL          
SEQRES  24 A  434  SER THR ILE GLY ASP TYR ALA ARG PHE THR GLN MET VAL          
SEQRES  25 A  434  LEU ASN GLY GLY THR LEU ASP GLY LYS ARG TYR LEU SER          
SEQRES  26 A  434  PRO LYS THR ILE ALA TYR MET GLY SER ASN HIS ILE PRO          
SEQRES  27 A  434  GLN ALA SER GLY ILE VAL PRO GLY ALA TYR TYR LEU PRO          
SEQRES  28 A  434  GLY PRO GLY VAL GLY PHE GLY LEU GLY PHE ALA VAL ARG          
SEQRES  29 A  434  THR GLU ALA GLY VAL THR PRO VAL GLU GLY SER VAL GLY          
SEQRES  30 A  434  ASP LEU SER TRP GLY GLY ALA GLY GLY THR VAL PHE TRP          
SEQRES  31 A  434  ILE ASP PRO LYS GLU ASN LEU THR VAL VAL PHE MET ALA          
SEQRES  32 A  434  PRO MET VAL SER PRO ARG ALA ARG VAL TRP ARG THR LEU          
SEQRES  33 A  434  ARG ASN ILE VAL TYR GLY ALA PHE ASP ARG LEU GLU HIS          
SEQRES  34 A  434  HIS HIS HIS HIS HIS                                          
HET    CEP  A 501      22                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HETNAM     CEP CEPHALOTHIN GROUP                                                
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  CEP    C16 H18 N2 O6 S2                                             
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  HOH   *338(H2 O)                                                    
HELIX    1   1 THR A   40  ALA A   57  1                                  18    
HELIX    2   2 MET A  101  GLU A  116  1                                  16    
HELIX    3   3 PRO A  124  TYR A  128  5                                   5    
HELIX    4   4 ILE A  129  ALA A  133  5                                   5    
HELIX    5   5 THR A  159  HIS A  166  1                                   8    
HELIX    6   6 GLY A  178  SER A  187  1                                  10    
HELIX    7   7 ASP A  195  LYS A  205  1                                  11    
HELIX    8   8 HIS A  220  GLY A  234  1                                  15    
HELIX    9   9 SER A  236  LEU A  245  1                                  10    
HELIX   10  10 LEU A  245  GLY A  250  1                                   6    
HELIX   11  11 LYS A  263  VAL A  267  5                                   5    
HELIX   12  12 MET A  271  ASP A  274  5                                   4    
HELIX   13  13 THR A  301  ASN A  314  1                                  14    
HELIX   14  14 SER A  325  GLY A  333  1                                   9    
HELIX   15  15 PRO A  338  GLY A  342  5                                   5    
HELIX   16  16 PRO A  408  ALA A  423  1                                  16    
SHEET    1   A 8 GLU A  26  PRO A  28  0                                        
SHEET    2   A 8 GLU A  72  GLY A  80 -1  O  SER A  78   N  GLY A  27           
SHEET    3   A 8 GLY A  62  ARG A  69 -1  N  ILE A  67   O  TYR A  75           
SHEET    4   A 8 LEU A 397  MET A 402 -1  O  THR A 398   N  LYS A  68           
SHEET    5   A 8 VAL A 388  ASP A 392 -1  N  ASP A 392   O  LEU A 397           
SHEET    6   A 8 LEU A 379  GLY A 382 -1  N  LEU A 379   O  ILE A 391           
SHEET    7   A 8 ALA A 362  ARG A 364 -1  N  ALA A 362   O  SER A 380           
SHEET    8   A 8 VAL A 355  PHE A 357 -1  N  GLY A 356   O  VAL A 363           
SHEET    1   B 2 PHE A  96  ARG A  97  0                                        
SHEET    2   B 2 VAL A 299  SER A 300 -1  O  SER A 300   N  PHE A  96           
SHEET    1   C 2 LYS A 136  GLY A 143  0                                        
SHEET    2   C 2 GLY A 146  PRO A 153 -1  O  GLU A 150   N  VAL A 139           
SHEET    1   D 2 THR A 215  TRP A 216  0                                        
SHEET    2   D 2 VAL A 344  PRO A 345  1  O  VAL A 344   N  TRP A 216           
SHEET    1   E 2 LYS A 276  ILE A 277  0                                        
SHEET    2   E 2 SER A 280  GLU A 281 -1  O  SER A 280   N  ILE A 277           
SHEET    1   F 2 THR A 317  LEU A 318  0                                        
SHEET    2   F 2 LYS A 321  ARG A 322 -1  O  LYS A 321   N  LEU A 318           
LINK         OG  SER A 100                 C8  CEP A 501     1555   1555  1.37  
SITE     1 AC1 11 TYR A  99  SER A 100  PHE A 174  VAL A 175                    
SITE     2 AC1 11 TYR A 218  ILE A 277  GLN A 296  GLY A 383                    
SITE     3 AC1 11 ALA A 384  ARG A 409  HOH A 865                               
SITE     1 AC2  4 LYS A  33  PRO A  34  LYS A  35  GLU A  36                    
SITE     1 AC3  7 VAL A  29  SER A  78  THR A  91  ALA A  92                    
SITE     2 AC3  7 GLU A  93  HOH A 869  HOH A 880                               
SITE     1 AC4  7 GLY A 250  GLY A 303  ASP A 304  ARG A 307                    
SITE     2 AC4  7 HOH A 667  HOH A 732  HOH A 772                               
SITE     1 AC5  3 GLY A 279  SER A 280  GLU A 281                               
CRYST1  149.102  149.102  172.571  90.00  90.00  90.00 I 4 2 2      16          
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      0.006707  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006707  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005795        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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