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LongText Report for: 5BOV-pdb

Name Class
5BOV-pdb
HEADER    HYDROLASE                               27-MAY-15   5BOV              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE (KPN_01808) FROM    
TITLE    2 KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 78578 AT 1.60 A          
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE EPOXIDE HYDROLASE PROTEIN;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE (STRAIN 
SOURCE   3 ATCC 700721 / MGH 78578);                                            
SOURCE   4 ORGANISM_TAXID: 272620;                                              
SOURCE   5 STRAIN: ATCC 700721 / MGH 78578;                                     
SOURCE   6 GENE: KPN_01808;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    PUTATIVE EPOXIDE HYDROLASE, STRUCTURAL GENOMICS, JOINT CENTER FOR     
KEYWDS   2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-        
KEYWDS   3 BIOLOGY, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   1   10-JUN-15 5BOV    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE            
JRNL        TITL 2 (KPN_01808) FROM KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 
JRNL        TITL 3 78578 AT 1.60 A RESOLUTION                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 146328                         
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) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.174                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7372                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10164                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 529                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9395                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1880                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : 0.22000                                              
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : -0.49000                                             
REMARK   3    B13 (A**2) : -0.51000                                             
REMARK   3    B23 (A**2) : 0.04000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.085         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.082         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.449         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9843 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9140 ; 0.013 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13485 ; 1.785 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20967 ; 1.910 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1241 ; 6.056 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   480 ;36.868 ;23.354       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1415 ;10.562 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    75 ;16.128 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1408 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11495 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2454 ; 0.011 ; 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):  4838 ; 0.882 ; 1.043       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4837 ; 0.881 ; 1.043       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6052 ; 1.397 ; 1.561       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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    38        A   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9308  -7.5371  40.4715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0103 T22:   0.0223                                     
REMARK   3      T33:   0.0087 T12:   0.0057                                     
REMARK   3      T13:   0.0004 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4018 L22:   0.3028                                     
REMARK   3      L33:   0.5315 L12:   0.2096                                     
REMARK   3      L13:   0.2425 L23:  -0.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:   0.0470 S13:  -0.0443                       
REMARK   3      S21:   0.0110 S22:   0.0350 S23:  -0.0197                       
REMARK   3      S31:  -0.0267 S32:   0.0460 S33:  -0.0305                       
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    37        B   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9272 -35.6327  -0.7875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0147 T22:   0.0078                                     
REMARK   3      T33:   0.0069 T12:   0.0042                                     
REMARK   3      T13:  -0.0091 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2983 L22:   0.3135                                     
REMARK   3      L33:   0.4148 L12:   0.0982                                     
REMARK   3      L13:   0.0750 L23:  -0.0871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0371 S12:  -0.0004 S13:   0.0138                       
REMARK   3      S21:   0.0052 S22:   0.0344 S23:  -0.0134                       
REMARK   3      S31:  -0.0107 S32:  -0.0016 S33:   0.0028                       
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    41        C   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.2354   5.4567   1.8599              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0094 T22:   0.0093                                     
REMARK   3      T33:   0.0081 T12:  -0.0008                                     
REMARK   3      T13:   0.0029 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2391 L22:   0.4925                                     
REMARK   3      L33:   0.7209 L12:  -0.0369                                     
REMARK   3      L13:   0.2353 L23:  -0.4051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0314 S12:  -0.0091 S13:   0.0145                       
REMARK   3      S21:  -0.0004 S22:   0.0081 S23:   0.0525                       
REMARK   3      S31:   0.0377 S32:  -0.0043 S33:  -0.0395                       
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    41        D   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9545 -47.0996  43.2845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0167 T22:   0.0263                                     
REMARK   3      T33:   0.0311 T12:  -0.0082                                     
REMARK   3      T13:  -0.0161 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4593 L22:   1.2296                                     
REMARK   3      L33:   1.0845 L12:   0.4477                                     
REMARK   3      L13:   0.3771 L23:  -0.3009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:  -0.0584 S13:   0.0952                       
REMARK   3      S21:  -0.0880 S22:   0.0288 S23:   0.1628                       
REMARK   3      S31:   0.0976 S32:  -0.1211 S33:  -0.0153                       
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: 1. A MET-INHIBITION PROTOCOL WAS USED     
REMARK   3  FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.       
REMARK   3  THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO    
REMARK   3  0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET          
REMARK   3  INCORPORATION. 2. THE MAD PHASES WERE USED AS RESTRAINTS DURING     
REMARK   3  REFINEMENT. 3. HYDROGENS HAVE BEEN ADDED IN THE RIDING              
REMARK   3  POSITIONS. 4. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B        
REMARK   3  FACTORS. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U           
REMARK   3  FACTORS.                                                            
REMARK   4                                                                      
REMARK   4 5BOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210294.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97907                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR; DOUBLE   
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS, XSCALE NOVEMBER 3, 2014       
REMARK 200                                   BUILT=20141118                     
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 146333                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.848                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.916                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE PH 9, 30% POLYETHYLENE       
REMARK 280  GLYCOL 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -44.19900            
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                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -18.05761            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       22.47589            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -83.05400            
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     GLY A     0                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ALA C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     ASP C    38                                                      
REMARK 465     ALA C    39                                                      
REMARK 465     GLY C    40                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     ALA D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     ASP D    38                                                      
REMARK 465     ALA D    39                                                      
REMARK 465     GLY D    40                                                      
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 B  37    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 136    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C  44    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A   312     O    HOH A   401              2.04            
REMARK 500   OE2  GLU A   258     O    HOH A   402              2.15            
REMARK 500   NH1  ARG C   160     O    HOH C   401              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   694     O    HOH A   776     1655     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 310   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 310   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 160   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 236   CG  -  CD  -  NE  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ARG B 254   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG C  49   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C  49   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP C 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 160   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG C 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG C 254   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG C 310   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG D 310   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D 337   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG D 337   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 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                                                                      
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    ASP A 144     -128.94     54.21                                   
REMARK 500    GLN A 225       59.95    -90.51                                   
REMARK 500    PRO B  75       74.07   -100.07                                   
REMARK 500    ASP B 144     -128.47     54.11                                   
REMARK 500    GLN B 225       59.39    -90.42                                   
REMARK 500    PRO C  75       75.14   -101.67                                   
REMARK 500    ASP C 144     -130.50     56.18                                   
REMARK 500    ASP D 144     -126.76     55.38                                   
REMARK 500    ASN D 240      131.49    -39.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 911        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A 912        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A 913        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH B 915        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B 916        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B 917        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B 918        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH B 919        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B 920        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH C 854        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH C 855        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH C 856        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH C 857        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH D 789        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH D 790        DISTANCE =  6.73 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-420280   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT (36-338) WAS EXPRESSED WITH A PURIFICATION TAG         
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.                  
DBREF  5BOV A   36   338  UNP    A6T9G8   A6T9G8_KLEP7    36    338             
DBREF  5BOV B   36   338  UNP    A6T9G8   A6T9G8_KLEP7    36    338             
DBREF  5BOV C   36   338  UNP    A6T9G8   A6T9G8_KLEP7    36    338             
DBREF  5BOV D   36   338  UNP    A6T9G8   A6T9G8_KLEP7    36    338             
SEQADV 5BOV GLY A    0  UNP  A6T9G8              LEADER SEQUENCE                
SEQADV 5BOV GLY B    0  UNP  A6T9G8              LEADER SEQUENCE                
SEQADV 5BOV GLY C    0  UNP  A6T9G8              LEADER SEQUENCE                
SEQADV 5BOV GLY D    0  UNP  A6T9G8              LEADER SEQUENCE                
SEQRES   1 A  304  GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN          
SEQRES   2 A  304  ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE          
SEQRES   3 A  304  GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY          
SEQRES   4 A  304  TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO          
SEQRES   5 A  304  ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR          
SEQRES   6 A  304  LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER          
SEQRES   7 A  304  THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP          
SEQRES   8 A  304  ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA          
SEQRES   9 A  304  ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP          
SEQRES  10 A  304  ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU          
SEQRES  11 A  304  VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE          
SEQRES  12 A  304  GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP          
SEQRES  13 A  304  TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA          
SEQRES  14 A  304  GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE          
SEQRES  15 A  304  TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA          
SEQRES  16 A  304  THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP          
SEQRES  17 A  304  HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU          
SEQRES  18 A  304  GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU          
SEQRES  19 A  304  GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR          
SEQRES  20 A  304  ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO          
SEQRES  21 A  304  ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR          
SEQRES  22 A  304  GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO          
SEQRES  23 A  304  PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL          
SEQRES  24 A  304  ASP ALA ASP ARG LEU                                          
SEQRES   1 B  304  GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN          
SEQRES   2 B  304  ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE          
SEQRES   3 B  304  GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY          
SEQRES   4 B  304  TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO          
SEQRES   5 B  304  ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR          
SEQRES   6 B  304  LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER          
SEQRES   7 B  304  THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP          
SEQRES   8 B  304  ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA          
SEQRES   9 B  304  ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP          
SEQRES  10 B  304  ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU          
SEQRES  11 B  304  VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE          
SEQRES  12 B  304  GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP          
SEQRES  13 B  304  TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA          
SEQRES  14 B  304  GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE          
SEQRES  15 B  304  TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA          
SEQRES  16 B  304  THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP          
SEQRES  17 B  304  HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU          
SEQRES  18 B  304  GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU          
SEQRES  19 B  304  GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR          
SEQRES  20 B  304  ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO          
SEQRES  21 B  304  ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR          
SEQRES  22 B  304  GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO          
SEQRES  23 B  304  PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL          
SEQRES  24 B  304  ASP ALA ASP ARG LEU                                          
SEQRES   1 C  304  GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN          
SEQRES   2 C  304  ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE          
SEQRES   3 C  304  GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY          
SEQRES   4 C  304  TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO          
SEQRES   5 C  304  ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR          
SEQRES   6 C  304  LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER          
SEQRES   7 C  304  THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP          
SEQRES   8 C  304  ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA          
SEQRES   9 C  304  ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP          
SEQRES  10 C  304  ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU          
SEQRES  11 C  304  VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE          
SEQRES  12 C  304  GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP          
SEQRES  13 C  304  TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA          
SEQRES  14 C  304  GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE          
SEQRES  15 C  304  TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA          
SEQRES  16 C  304  THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP          
SEQRES  17 C  304  HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU          
SEQRES  18 C  304  GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU          
SEQRES  19 C  304  GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR          
SEQRES  20 C  304  ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO          
SEQRES  21 C  304  ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR          
SEQRES  22 C  304  GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO          
SEQRES  23 C  304  PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL          
SEQRES  24 C  304  ASP ALA ASP ARG LEU                                          
SEQRES   1 D  304  GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN          
SEQRES   2 D  304  ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE          
SEQRES   3 D  304  GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY          
SEQRES   4 D  304  TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO          
SEQRES   5 D  304  ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR          
SEQRES   6 D  304  LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER          
SEQRES   7 D  304  THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP          
SEQRES   8 D  304  ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA          
SEQRES   9 D  304  ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP          
SEQRES  10 D  304  ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU          
SEQRES  11 D  304  VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE          
SEQRES  12 D  304  GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP          
SEQRES  13 D  304  TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA          
SEQRES  14 D  304  GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE          
SEQRES  15 D  304  TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA          
SEQRES  16 D  304  THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP          
SEQRES  17 D  304  HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU          
SEQRES  18 D  304  GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU          
SEQRES  19 D  304  GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR          
SEQRES  20 D  304  ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO          
SEQRES  21 D  304  ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR          
SEQRES  22 D  304  GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO          
SEQRES  23 D  304  PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL          
SEQRES  24 D  304  ASP ALA ASP ARG LEU                                          
MODRES 5BOV MSE A  122  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE A  130  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE B  122  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE B  130  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE C  122  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE C  130  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE D  122  MET  MODIFIED RESIDUE                                   
MODRES 5BOV MSE D  130  MET  MODIFIED RESIDUE                                   
HET    MSE  A 122       8                                                       
HET    MSE  A 130       8                                                       
HET    MSE  B 122       8                                                       
HET    MSE  B 130       8                                                       
HET    MSE  C 122       8                                                       
HET    MSE  C 130       8                                                       
HET    MSE  D 122       8                                                       
HET    MSE  D 130       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   5  HOH   *1880(H2 O)                                                   
HELIX    1 AA1 GLY A   40  LYS A   44  5                                   5    
HELIX    2 AA2 ASP A   77  ALA A   82  5                                   6    
HELIX    3 AA3 GLN A   83  LYS A   91  1                                   9    
HELIX    4 AA4 GLN A  118  LEU A  133  1                                  16    
HELIX    5 AA5 ASP A  144  TRP A  157  1                                  14    
HELIX    6 AA6 SER A  174  GLU A  179  1                                   6    
HELIX    7 AA7 PRO A  183  TRP A  190  1                                   8    
HELIX    8 AA8 TRP A  190  ALA A  197  1                                   8    
HELIX    9 AA9 THR A  198  ASN A  208  1                                  11    
HELIX   10 AB1 ASN A  208  SER A  221  1                                  14    
HELIX   11 AB2 SER A  227  ARG A  236  1                                  10    
HELIX   12 AB3 ALA A  237  ASN A  240  5                                   4    
HELIX   13 AB4 ASP A  242  LEU A  255  1                                  14    
HELIX   14 AB5 GLU A  261  LYS A  263  5                                   3    
HELIX   15 AB6 TYR A  264  ALA A  273  1                                  10    
HELIX   16 AB7 ALA A  295  ARG A  300  1                                   6    
HELIX   17 AB8 ALA A  301  PHE A  303  5                                   3    
HELIX   18 AB9 ASN A  319  ASP A  324  1                                   6    
HELIX   19 AC1 ASP A  324  LEU A  338  1                                  15    
HELIX   20 AC2 GLY B   40  LYS B   44  5                                   5    
HELIX   21 AC3 ASP B   77  ALA B   82  5                                   6    
HELIX   22 AC4 GLN B   83  LYS B   91  1                                   9    
HELIX   23 AC5 GLN B  118  LEU B  133  1                                  16    
HELIX   24 AC6 ASP B  144  TRP B  157  1                                  14    
HELIX   25 AC7 SER B  174  GLU B  179  1                                   6    
HELIX   26 AC8 PRO B  183  TRP B  190  1                                   8    
HELIX   27 AC9 TRP B  190  ALA B  197  1                                   8    
HELIX   28 AD1 THR B  198  ASN B  208  1                                  11    
HELIX   29 AD2 ASN B  208  SER B  221  1                                  14    
HELIX   30 AD3 SER B  227  LEU B  238  1                                  12    
HELIX   31 AD4 ASP B  242  LEU B  255  1                                  14    
HELIX   32 AD5 GLU B  261  LYS B  263  5                                   3    
HELIX   33 AD6 TYR B  264  ALA B  273  1                                  10    
HELIX   34 AD7 ALA B  295  ARG B  300  1                                   6    
HELIX   35 AD8 ALA B  301  PHE B  303  5                                   3    
HELIX   36 AD9 ASN B  319  ASP B  324  1                                   6    
HELIX   37 AE1 ASP B  324  LEU B  338  1                                  15    
HELIX   38 AE2 ASP C   77  ALA C   82  5                                   6    
HELIX   39 AE3 GLN C   83  LYS C   91  1                                   9    
HELIX   40 AE4 GLN C  118  LEU C  133  1                                  16    
HELIX   41 AE5 ASP C  144  TRP C  157  1                                  14    
HELIX   42 AE6 SER C  174  GLU C  179  1                                   6    
HELIX   43 AE7 PRO C  183  TRP C  190  1                                   8    
HELIX   44 AE8 TRP C  190  ALA C  197  1                                   8    
HELIX   45 AE9 THR C  198  ASN C  208  1                                  11    
HELIX   46 AF1 ASN C  208  SER C  221  1                                  14    
HELIX   47 AF2 SER C  227  ASP C  239  1                                  13    
HELIX   48 AF3 ASP C  242  LEU C  255  1                                  14    
HELIX   49 AF4 GLU C  261  LYS C  263  5                                   3    
HELIX   50 AF5 TYR C  264  ALA C  273  1                                  10    
HELIX   51 AF6 ALA C  295  ARG C  300  1                                   6    
HELIX   52 AF7 ALA C  301  PHE C  303  5                                   3    
HELIX   53 AF8 ASN C  319  ASP C  324  1                                   6    
HELIX   54 AF9 ASP C  324  LEU C  338  1                                  15    
HELIX   55 AG1 ASP D   77  ALA D   82  5                                   6    
HELIX   56 AG2 GLN D   83  LYS D   91  1                                   9    
HELIX   57 AG3 GLN D  118  LEU D  133  1                                  16    
HELIX   58 AG4 ASP D  144  TRP D  157  1                                  14    
HELIX   59 AG5 SER D  174  GLU D  179  1                                   6    
HELIX   60 AG6 PRO D  183  TRP D  190  1                                   8    
HELIX   61 AG7 TRP D  190  ALA D  197  1                                   8    
HELIX   62 AG8 THR D  198  ASN D  208  1                                  11    
HELIX   63 AG9 ASN D  208  SER D  221  1                                  14    
HELIX   64 AH1 SER D  227  ASP D  239  1                                  13    
HELIX   65 AH2 ASP D  242  LEU D  255  1                                  14    
HELIX   66 AH3 GLU D  261  LYS D  263  5                                   3    
HELIX   67 AH4 TYR D  264  ALA D  273  1                                  10    
HELIX   68 AH5 ALA D  295  PHE D  303  5                                   9    
HELIX   69 AH6 ASN D  319  ASP D  324  1                                   6    
HELIX   70 AH7 ASP D  324  LEU D  338  1                                  15    
SHEET    1 AA1 3 GLN A  46  ALA A  50  0                                        
SHEET    2 AA1 3 LEU A  53  ILE A  60 -1  O  TYR A  57   N  GLN A  46           
SHEET    3 AA1 3 ARG A 107  PHE A 108 -1  O  ARG A 107   N  ASN A  54           
SHEET    1 AA2 8 GLN A  46  ALA A  50  0                                        
SHEET    2 AA2 8 LEU A  53  ILE A  60 -1  O  TYR A  57   N  GLN A  46           
SHEET    3 AA2 8 TYR A  93  PRO A  98 -1  O  VAL A  95   N  ILE A  60           
SHEET    4 AA2 8 GLN A  66  LEU A  71  1  N  VAL A  68   O  ILE A  96           
SHEET    5 AA2 8 ALA A 138  GLY A 142  1  O  ALA A 141   N  LEU A  71           
SHEET    6 AA2 8 VAL A 161  VAL A 167  1  O  SER A 163   N  LEU A 140           
SHEET    7 AA2 8 THR A 281  GLY A 286  1  O  ILE A 282   N  LEU A 164           
SHEET    8 AA2 8 TYR A 307  LEU A 312  1  O  LEU A 312   N  GLU A 285           
SHEET    1 AA3 3 GLN B  46  ALA B  50  0                                        
SHEET    2 AA3 3 LEU B  53  ILE B  60 -1  O  TYR B  57   N  GLN B  46           
SHEET    3 AA3 3 ARG B 107  PHE B 108 -1  O  ARG B 107   N  ASN B  54           
SHEET    1 AA4 8 GLN B  46  ALA B  50  0                                        
SHEET    2 AA4 8 LEU B  53  ILE B  60 -1  O  TYR B  57   N  GLN B  46           
SHEET    3 AA4 8 ARG B  94  PRO B  98 -1  O  VAL B  95   N  ILE B  60           
SHEET    4 AA4 8 PRO B  67  LEU B  71  1  N  VAL B  68   O  ILE B  96           
SHEET    5 AA4 8 ALA B 138  GLY B 142  1  O  ALA B 141   N  LEU B  71           
SHEET    6 AA4 8 VAL B 161  VAL B 167  1  O  SER B 163   N  LEU B 140           
SHEET    7 AA4 8 THR B 281  GLY B 286  1  O  ILE B 282   N  LEU B 164           
SHEET    8 AA4 8 TYR B 307  LEU B 312  1  O  LEU B 312   N  GLU B 285           
SHEET    1 AA5 3 GLN C  46  ALA C  50  0                                        
SHEET    2 AA5 3 LEU C  53  ILE C  60 -1  O  TYR C  57   N  GLN C  46           
SHEET    3 AA5 3 ARG C 107  PHE C 108 -1  O  ARG C 107   N  ASN C  54           
SHEET    1 AA6 8 GLN C  46  ALA C  50  0                                        
SHEET    2 AA6 8 LEU C  53  ILE C  60 -1  O  TYR C  57   N  GLN C  46           
SHEET    3 AA6 8 ARG C  94  PRO C  98 -1  O  VAL C  95   N  ILE C  60           
SHEET    4 AA6 8 PRO C  67  LEU C  71  1  N  VAL C  68   O  ILE C  96           
SHEET    5 AA6 8 ALA C 138  GLY C 142  1  O  ALA C 141   N  LEU C  71           
SHEET    6 AA6 8 VAL C 161  VAL C 167  1  O  SER C 163   N  LEU C 140           
SHEET    7 AA6 8 THR C 281  GLY C 286  1  O  ILE C 282   N  LEU C 164           
SHEET    8 AA6 8 TYR C 307  LEU C 312  1  O  LEU C 312   N  GLU C 285           
SHEET    1 AA7 3 GLN D  46  ALA D  50  0                                        
SHEET    2 AA7 3 LEU D  53  ILE D  60 -1  O  TYR D  57   N  GLN D  46           
SHEET    3 AA7 3 ARG D 107  PHE D 108 -1  O  ARG D 107   N  ASN D  54           
SHEET    1 AA8 8 GLN D  46  ALA D  50  0                                        
SHEET    2 AA8 8 LEU D  53  ILE D  60 -1  O  TYR D  57   N  GLN D  46           
SHEET    3 AA8 8 ARG D  94  PRO D  98 -1  O  VAL D  95   N  ILE D  60           
SHEET    4 AA8 8 PRO D  67  LEU D  71  1  N  VAL D  68   O  ILE D  96           
SHEET    5 AA8 8 ALA D 138  GLY D 142  1  O  ALA D 141   N  LEU D  71           
SHEET    6 AA8 8 VAL D 161  VAL D 167  1  O  SER D 163   N  LEU D 140           
SHEET    7 AA8 8 THR D 281  GLY D 286  1  O  ILE D 282   N  LEU D 164           
SHEET    8 AA8 8 TYR D 307  LEU D 312  1  O  LEU D 312   N  GLU D 285           
LINK         C   ALA A 121                 N   MSE A 122     1555   1555  1.33  
LINK         C   MSE A 122                 N   ALA A 123     1555   1555  1.34  
LINK         C   LEU A 129                 N   MSE A 130     1555   1555  1.33  
LINK         C   MSE A 130                 N   ASP A 131     1555   1555  1.33  
LINK         C   ALA B 121                 N   MSE B 122     1555   1555  1.35  
LINK         C   MSE B 122                 N   ALA B 123     1555   1555  1.34  
LINK         C   LEU B 129                 N   MSE B 130     1555   1555  1.32  
LINK         C   MSE B 130                 N   ASP B 131     1555   1555  1.33  
LINK         C   ALA C 121                 N   MSE C 122     1555   1555  1.34  
LINK         C   MSE C 122                 N   ALA C 123     1555   1555  1.34  
LINK         C   LEU C 129                 N   MSE C 130     1555   1555  1.33  
LINK         C   MSE C 130                 N   ASP C 131     1555   1555  1.33  
LINK         C   ALA D 121                 N   MSE D 122     1555   1555  1.35  
LINK         C   MSE D 122                 N   ALA D 123     1555   1555  1.32  
LINK         C   LEU D 129                 N   MSE D 130     1555   1555  1.33  
LINK         C   MSE D 130                 N   ASP D 131     1555   1555  1.32  
CISPEP   1 TRP A   74    PRO A   75          0        -9.30                     
CISPEP   2 TRP B   74    PRO B   75          0        -9.93                     
CISPEP   3 TRP C   74    PRO C   75          0        -4.45                     
CISPEP   4 TRP D   74    PRO D   75          0       -10.83                     
CRYST1   44.199   81.866   89.925 101.00 106.90 100.84 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022625  0.004332  0.008295        0.00000                         
SCALE2      0.000000  0.012437  0.003365        0.00000                         
SCALE3      0.000000  0.000000  0.012040        0.00000                         
TER    2408      LEU A 338                                                      
TER    4805      LEU B 338                                                      
TER    7155      LEU C 338                                                      
TER    9531      LEU D 338                                                      
MASTER      511    0    8   70   44    0    0    611275    4   80   96          
END                                                                             

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