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Database: PDB
Entry: 3FFX
LinkDB: 3FFX
Original site: 3FFX 
HEADER    SIGNALING PROTEIN                       04-DEC-08   3FFX              
TITLE     CRYSTAL STRUCTURE OF CHEY TRIPLE MUTANT F14E, N59R, E89H COMPLEXED    
TITLE    2 WITH BEF3- AND MN2+                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHEMOTAXIS PROTEIN CHEY;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 GENE: B1882, CHEY, JW1871;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: KO641RECA;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    RESPONSE REGULATOR, RECEIVER DOMAIN, BEF3, TWO-COMPONENT SIGNAL       
KEYWDS   2 TRANSDUCTION, CHEMOTAXIS, FLAGELLAR ROTATION, MAGNESIUM, METAL-      
KEYWDS   3 BINDING, PHOSPHOPROTEIN, TWO-COMPONENT REGULATORY SYSTEM, SIGNALING  
KEYWDS   4 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.PAZY,E.J.COLLINS,R.B.BOURRET                                        
REVDAT   5   21-FEB-24 3FFX    1       REMARK                                   
REVDAT   4   20-OCT-21 3FFX    1       REMARK SEQADV LINK                       
REVDAT   3   01-NOV-17 3FFX    1       REMARK                                   
REVDAT   2   13-JUL-11 3FFX    1       VERSN                                    
REVDAT   1   22-SEP-09 3FFX    0                                                
JRNL        AUTH   Y.PAZY,A.C.WOLLISH,S.A.THOMAS,P.J.MILLER,E.J.COLLINS,        
JRNL        AUTH 2 R.B.BOURRET,R.E.SILVERSMITH                                  
JRNL        TITL   MATCHING BIOCHEMICAL REACTION KINETICS TO THE TIMESCALES OF  
JRNL        TITL 2 LIFE: STRUCTURAL DETERMINANTS THAT INFLUENCE THE             
JRNL        TITL 3 AUTODEPHOSPHORYLATION RATE OF RESPONSE REGULATOR PROTEINS.   
JRNL        REF    J.MOL.BIOL.                   V. 392  1205 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19646451                                                     
JRNL        DOI    10.1016/J.JMB.2009.07.064                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31770                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1607                            
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2185                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1962                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 348                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.56000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.87000                                             
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): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.640         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2102 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1453 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2828 ; 1.546 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3570 ; 1.022 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   272 ; 6.046 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    88 ;38.963 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;14.166 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ; 8.865 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   317 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2303 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   392 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   420 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1563 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   972 ; 0.169 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1099 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   268 ; 0.166 ; 0.200       
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):    14 ; 0.095 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    40 ; 0.276 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.204 ; 0.200       
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):  1713 ; 1.035 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   536 ; 0.196 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2083 ; 1.204 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   903 ; 2.275 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   739 ; 3.405 ; 4.500       
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  : 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 3FFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050541.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31825                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.9510                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42700                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS BUFFER, AMMONIUM SULFATE,           
REMARK 280  GLYCEROL, BECL2, NAF, MNCL2, PH 8.4, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.78200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.91950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.70400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.91950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.78200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.70400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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    HOH A   291     O    HOH A   334              2.19            
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    TRP A  58      -67.26   -100.12                                   
REMARK 500    ASN A  62      -56.95     74.54                                   
REMARK 500    MET A  78       18.32   -142.40                                   
REMARK 500    TRP B  58      -67.39    -96.96                                   
REMARK 500    ASN B  62      -56.71     78.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 202  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  13   OD1                                                    
REMARK 620 2 ASP A  57   OD2  81.6                                              
REMARK 620 3 ARG A  59   O    87.5  87.8                                        
REMARK 620 4 BEF A 130   F1  176.1  94.7  91.3                                  
REMARK 620 5 HOH A 223   O    88.0  87.6 174.0  93.0                            
REMARK 620 6 HOH A 318   O    98.1 173.8  86.0  85.5  98.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BEF A 130  BE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   OD1                                                    
REMARK 620 2 BEF A 130   F1  113.1                                              
REMARK 620 3 BEF A 130   F2  106.5 114.0                                        
REMARK 620 4 BEF A 130   F3  102.4 111.5 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 202  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  13   OD1                                                    
REMARK 620 2 ASP B  57   OD2  82.6                                              
REMARK 620 3 ARG B  59   O    88.2  88.9                                        
REMARK 620 4 BEF B 130   F1  177.8  95.8  93.3                                  
REMARK 620 5 HOH B 199   O    88.2  81.9 170.5  90.0                            
REMARK 620 6 HOH B 319   O    99.0 177.0  93.7  82.5  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BEF B 130  BE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  57   OD1                                                    
REMARK 620 2 BEF B 130   F1  116.4                                              
REMARK 620 3 BEF B 130   F2  101.9 114.0                                        
REMARK 620 4 BEF B 130   F3  108.2 110.8 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3F7N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FFT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FFW   RELATED DB: PDB                                   
DBREF  3FFX A    2   129  UNP    P0AE67   CHEY_ECOLI       2    129             
DBREF  3FFX B    2   129  UNP    P0AE67   CHEY_ECOLI       2    129             
SEQADV 3FFX GLU A   14  UNP  P0AE67    PHE    14 ENGINEERED MUTATION            
SEQADV 3FFX ARG A   59  UNP  P0AE67    ASN    59 ENGINEERED MUTATION            
SEQADV 3FFX HIS A   89  UNP  P0AE67    GLU    89 ENGINEERED MUTATION            
SEQADV 3FFX GLU B   14  UNP  P0AE67    PHE    14 ENGINEERED MUTATION            
SEQADV 3FFX ARG B   59  UNP  P0AE67    ASN    59 ENGINEERED MUTATION            
SEQADV 3FFX HIS B   89  UNP  P0AE67    GLU    89 ENGINEERED MUTATION            
SEQRES   1 A  128  ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP GLU          
SEQRES   2 A  128  SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU          
SEQRES   3 A  128  LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL          
SEQRES   4 A  128  ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE          
SEQRES   5 A  128  VAL ILE SER ASP TRP ARG MET PRO ASN MET ASP GLY LEU          
SEQRES   6 A  128  GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER          
SEQRES   7 A  128  ALA LEU PRO VAL LEU MET VAL THR ALA HIS ALA LYS LYS          
SEQRES   8 A  128  GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY          
SEQRES   9 A  128  TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU          
SEQRES  10 A  128  LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET                  
SEQRES   1 B  128  ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP GLU          
SEQRES   2 B  128  SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU          
SEQRES   3 B  128  LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL          
SEQRES   4 B  128  ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE          
SEQRES   5 B  128  VAL ILE SER ASP TRP ARG MET PRO ASN MET ASP GLY LEU          
SEQRES   6 B  128  GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER          
SEQRES   7 B  128  ALA LEU PRO VAL LEU MET VAL THR ALA HIS ALA LYS LYS          
SEQRES   8 B  128  GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY          
SEQRES   9 B  128  TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU          
SEQRES  10 B  128  LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET                  
HET     MN  A 202       1                                                       
HET    BEF  A 130       4                                                       
HET    SO4  A   1       5                                                       
HET    SO4  A 131       5                                                       
HET    GOL  A 501       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  A 505       6                                                       
HET     MN  B 202       1                                                       
HET    BEF  B 130       4                                                       
HET    SO4  B 131       5                                                       
HET    GOL  B 502       6                                                       
HET    GOL  B 503       6                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     BEF BERYLLIUM TRIFLUORIDE ION                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   4  BEF    2(BE F3 1-)                                                  
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   7  GOL    5(C3 H8 O3)                                                  
FORMUL  15  HOH   *348(H2 O)                                                    
HELIX    1   1 GLU A   14  LEU A   28  1                                  15    
HELIX    2   2 ASP A   38  GLY A   49  1                                  12    
HELIX    3   3 ASP A   64  ASP A   75  1                                  12    
HELIX    4   4 LYS A   91  ALA A  101  1                                  11    
HELIX    5   5 THR A  112  LEU A  127  1                                  16    
HELIX    6   6 GLU B   14  GLY B   29  1                                  16    
HELIX    7   7 ASP B   38  GLY B   49  1                                  12    
HELIX    8   8 ASP B   64  ASP B   75  1                                  12    
HELIX    9   9 LYS B   91  ALA B  101  1                                  11    
HELIX   10  10 THR B  112  GLY B  128  1                                  17    
SHEET    1   A 5 VAL A  33  ALA A  36  0                                        
SHEET    2   A 5 PHE A   8  VAL A  11  1  N  VAL A  10   O  GLU A  34           
SHEET    3   A 5 PHE A  53  SER A  56  1  O  ILE A  55   N  VAL A  11           
SHEET    4   A 5 VAL A  83  THR A  87  1  O  VAL A  86   N  SER A  56           
SHEET    5   A 5 GLY A 105  VAL A 108  1  O  VAL A 107   N  MET A  85           
SHEET    1   B 5 VAL B  33  ALA B  36  0                                        
SHEET    2   B 5 PHE B   8  VAL B  11  1  N  VAL B  10   O  GLU B  34           
SHEET    3   B 5 PHE B  53  SER B  56  1  O  ILE B  55   N  VAL B  11           
SHEET    4   B 5 VAL B  83  THR B  87  1  O  LEU B  84   N  VAL B  54           
SHEET    5   B 5 GLY B 105  VAL B 108  1  O  VAL B 107   N  MET B  85           
LINK         OD1 ASP A  13                MN    MN A 202     1555   1555  2.18  
LINK         OD1 ASP A  57                BE   BEF A 130     1555   1555  1.70  
LINK         OD2 ASP A  57                MN    MN A 202     1555   1555  2.18  
LINK         O   ARG A  59                MN    MN A 202     1555   1555  2.28  
LINK         F1  BEF A 130                MN    MN A 202     1555   1555  1.96  
LINK        MN    MN A 202                 O   HOH A 223     1555   1555  2.28  
LINK        MN    MN A 202                 O   HOH A 318     1555   1555  2.04  
LINK         OD1 ASP B  13                MN    MN B 202     1555   1555  2.25  
LINK         OD1 ASP B  57                BE   BEF B 130     1555   1555  1.78  
LINK         OD2 ASP B  57                MN    MN B 202     1555   1555  2.16  
LINK         O   ARG B  59                MN    MN B 202     1555   1555  2.27  
LINK         F1  BEF B 130                MN    MN B 202     1555   1555  2.03  
LINK         O   HOH B 199                MN    MN B 202     1555   1555  2.33  
LINK        MN    MN B 202                 O   HOH B 319     1555   1555  2.07  
CISPEP   1 LYS A  109    PRO A  110          0        -4.48                     
CISPEP   2 LYS B  109    PRO B  110          0        -9.64                     
SITE     1 AC1  6 ASP A  13  ASP A  57  ARG A  59  BEF A 130                    
SITE     2 AC1  6 HOH A 223  HOH A 318                                          
SITE     1 AC2 12 ASP A  57  TRP A  58  ARG A  59  THR A  87                    
SITE     2 AC2 12 ALA A  88  LYS A 109   MN A 202  HOH A 216                    
SITE     3 AC2 12 HOH A 223  HOH A 318  HOH A 335  HOH A 343                    
SITE     1 AC3  3 LYS A  91  LYS A  92  HOH A 245                               
SITE     1 AC4  3 GLU A  37  ASP A  41  HOH A 294                               
SITE     1 AC5  4 ARG A  19  LYS A  70  HOH A 277  LYS B 126                    
SITE     1 AC6  5 TRP A  58  ARG A  59  ASP A  64  HIS A  89                    
SITE     2 AC6  5 HOH A 323                                                     
SITE     1 AC7  4 LYS A   7  ASN A  32  GLY A  49  HOH A 262                    
SITE     1 AC8  6 ASP B  13  ASP B  57  ARG B  59  BEF B 130                    
SITE     2 AC8  6 HOH B 199  HOH B 319                                          
SITE     1 AC9 12 ASP B  57  TRP B  58  ARG B  59  THR B  87                    
SITE     2 AC9 12 ALA B  88  HIS B  89  LYS B 109  HOH B 199                    
SITE     3 AC9 12  MN B 202  HOH B 319  HOH B 331  HOH B 332                    
SITE     1 BC1  5 LYS A  92  LYS B  91  LYS B  92  HOH B 140                    
SITE     2 BC1  5 HOH B 239                                                     
SITE     1 BC2  4 ARG B  19  LYS B  70  HOH B 136  HOH B 253                    
SITE     1 BC3  4 LYS B   7  ASN B  32  GLY B  50  HOH B 270                    
CRYST1   53.564   53.408  161.839  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018669  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006179        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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