GenomeNet

Database: PDB
Entry: 6H6O
LinkDB: 6H6O
Original site: 6H6O 
HEADER    LIPID BINDING PROTEIN                   28-JUL-18   6H6O              
TITLE     UBIJ-SCP2 UBIQUINONE SYNTHESIS PROTEIN                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUINONE BIOSYNTHESIS PROTEIN UBIJ;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: UBIJ, YIGP, B3834, JW3811;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    SCP2 LIPID BINDING PROTEIN UBIQUINONE SYNTHESIS PROTEIN, LIPID        
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.FYFE,P.LEGRAND,L.PECQUEUR,L.CICCONE,M.LOMBARD,M.FONTECAVE         
REVDAT   2   01-MAY-19 6H6O    1       JRNL                                     
REVDAT   1   13-FEB-19 6H6O    0                                                
JRNL        AUTH   M.HAJJ CHEHADE,L.PELOSI,C.D.FYFE,L.LOISEAU,B.RASCALOU,       
JRNL        AUTH 2 S.BRUGIERE,K.KAZEMZADEH,C.D.VO,L.CICCONE,L.AUSSEL,Y.COUTE,   
JRNL        AUTH 3 M.FONTECAVE,F.BARRAS,M.LOMBARD,F.PIERREL                     
JRNL        TITL   A SOLUBLE METABOLON SYNTHESIZES THE ISOPRENOID LIPID         
JRNL        TITL 2 UBIQUINONE.                                                  
JRNL        REF    CELL CHEM BIOL                V.  26   482 2019              
JRNL        REFN                   ESSN 2451-9456                               
JRNL        PMID   30686758                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2018.12.001                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24371                          
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)  : 0.204                          
REMARK   3   R VALUE            (WORKING SET)  : 0.202                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 7.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1722                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.70                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.78                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 58.72                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1970                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2400                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1834                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2380                   
REMARK   3   BIN FREE R VALUE                        : 0.2700                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.90                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 136                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 185                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.84730                                             
REMARK   3    B22 (A**2) : -0.49830                                             
REMARK   3    B33 (A**2) : 1.34560                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.250               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.136               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.118               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.130               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.115               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1953   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2678   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 695    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 46     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 281    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 1953   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 252    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2294   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.91                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.48                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.9734    5.1487  -25.5014           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0570 T22:   -0.0512                                    
REMARK   3     T33:   -0.0111 T12:   -0.0042                                    
REMARK   3     T13:   -0.0186 T23:   -0.0232                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6218 L22:    0.8275                                    
REMARK   3     L33:    0.8166 L12:   -0.1746                                    
REMARK   3     L13:    0.1168 L23:   -0.0834                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0026 S12:    0.1073 S13:   -0.0947                     
REMARK   3     S21:   -0.0521 S22:    0.0037 S23:    0.1073                     
REMARK   3     S31:    0.0639 S32:    0.0487 S33:   -0.0011                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -41.6259   -8.8007  -26.4142           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0743 T22:   -0.0763                                    
REMARK   3     T33:   -0.0224 T12:   -0.0061                                    
REMARK   3     T13:   -0.0006 T23:    0.0070                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7804 L22:    1.9221                                    
REMARK   3     L33:    1.3632 L12:   -0.1662                                    
REMARK   3     L13:   -0.1402 L23:    0.0777                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0612 S12:    0.1689 S13:   -0.0616                     
REMARK   3     S21:   -0.1951 S22:    0.0611 S23:    0.0333                     
REMARK   3     S31:   -0.0331 S32:   -0.0605 S33:    0.0001                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6H6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011165.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 177660                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6H6N                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 225 MM CALCIUM CHLORIDE, 100 MM MMT      
REMARK 280  BUFFER PH 9, 11% W/V PEG 8000, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
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       24.33000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.30350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.93500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.30350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.33000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.93500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     ALA B   131                                                      
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     LYS B  15    CG   CD   CE   NZ                                   
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 207  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  23   OE1                                                    
REMARK 620 2 GLU A  23   OE2  55.4                                              
REMARK 620 3 ASP A  69   OD1  97.2  89.1                                        
REMARK 620 4 HOH A 373   O    82.5  85.2 173.3                                  
REMARK 620 5 HOH A 349   O    76.6 132.0  99.0  87.5                            
REMARK 620 6 HOH A 392   O   148.4 155.0  93.0  90.6  72.2                      
REMARK 620 7 HOH A 314   O   127.5  72.1  81.4  93.3 155.8  83.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 208  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  77   OD1                                                    
REMARK 620 2 ASP A  77   OD2  52.6                                              
REMARK 620 3 HOH A 396   O   117.9  81.1                                        
REMARK 620 4 HOH A 399   O   166.4 131.3  75.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  79   OD1                                                    
REMARK 620 2 ASP A  79   OD2  51.9                                              
REMARK 620 3 HOH A 342   O    90.1  87.8                                        
REMARK 620 4 HOH A 306   O   145.0  93.2  88.2                                  
REMARK 620 5 GLU B  23   OE1  90.7  40.1  76.5  55.0                            
REMARK 620 6 GLU B  23   OE2  94.1  43.4  76.3  51.7   3.4                      
REMARK 620 7 ASP B  69   OD1  92.4  41.7  76.5  53.4   1.7   1.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 206  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A  93   O                                                      
REMARK 620 2 ASP A 124   OD1  83.1                                              
REMARK 620 3 GLU A 127   OE1 152.0 106.2                                        
REMARK 620 4 HOH A 355   O   126.5  66.2  80.7                                  
REMARK 620 5 HOH A 362   O    69.7 100.7  82.6 154.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 126   O                                                      
REMARK 620 2 ASP A 129   O    87.6                                              
REMARK 620 3 ALA A 131   O   169.7  92.7                                        
REMARK 620 4 HOH A 313   O    94.2 172.9  84.3                                  
REMARK 620 5 HOH A 326   O    92.4  91.5  77.3  81.6                            
REMARK 620 6 HOH A 384   O    89.9  89.0 100.4  97.9 177.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B  42   O                                                      
REMARK 620 2 HOH B 337   O   115.7                                              
REMARK 620 3 HOH B 374   O   101.9  82.1                                        
REMARK 620 4 HOH B 338   O    65.1 178.0  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 124   O                                                      
REMARK 620 2 ASP B 124   OD1  82.0                                              
REMARK 620 3 GLU B 127   O    81.2 162.4                                        
REMARK 620 4 ASP B 129   OD1 168.9 102.5  93.1                                  
REMARK 620 5 HOH B 315   O   103.9  85.5 103.5  86.7                            
REMARK 620 6 HOH A 371   O    81.1  90.6  81.7  88.6 173.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMR A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMR A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 204                  
DBREF  6H6O A   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
DBREF  6H6O B   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
SEQADV 6H6O MET A    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6O GLU A    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O LEU A    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS A    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O GLU A   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O GLU A   11  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O MET B    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6O GLU B    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O LEU B    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O HIS B    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O GLU B   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6O GLU B   11  UNP  P0ADP7              EXPRESSION TAG                 
SEQRES   1 A  131  MET GLU LEU HIS HIS HIS HIS HIS HIS GLU GLU MET PRO          
SEQRES   2 A  131  PHE LYS PRO LEU VAL THR ALA GLY ILE GLU SER LEU LEU          
SEQRES   3 A  131  ASN THR PHE LEU TYR ARG SER PRO ALA LEU LYS THR ALA          
SEQRES   4 A  131  ARG SER ARG LEU LEU GLY LYS VAL LEU ARG VAL GLU VAL          
SEQRES   5 A  131  LYS GLY PHE SER THR SER LEU ILE LEU VAL PHE SER GLU          
SEQRES   6 A  131  ARG GLN VAL ASP VAL LEU GLY GLU TRP ALA GLY ASP ALA          
SEQRES   7 A  131  ASP CYS THR VAL ILE ALA TYR ALA SER VAL LEU PRO LYS          
SEQRES   8 A  131  LEU ARG ASP ARG GLN GLN LEU THR ALA LEU ILE ARG SER          
SEQRES   9 A  131  GLY GLU LEU GLU VAL GLN GLY ASP ILE GLN VAL VAL GLN          
SEQRES  10 A  131  ASN PHE VAL ALA LEU ALA ASP LEU ALA GLU PHE ASP PRO          
SEQRES  11 A  131  ALA                                                          
SEQRES   1 B  131  MET GLU LEU HIS HIS HIS HIS HIS HIS GLU GLU MET PRO          
SEQRES   2 B  131  PHE LYS PRO LEU VAL THR ALA GLY ILE GLU SER LEU LEU          
SEQRES   3 B  131  ASN THR PHE LEU TYR ARG SER PRO ALA LEU LYS THR ALA          
SEQRES   4 B  131  ARG SER ARG LEU LEU GLY LYS VAL LEU ARG VAL GLU VAL          
SEQRES   5 B  131  LYS GLY PHE SER THR SER LEU ILE LEU VAL PHE SER GLU          
SEQRES   6 B  131  ARG GLN VAL ASP VAL LEU GLY GLU TRP ALA GLY ASP ALA          
SEQRES   7 B  131  ASP CYS THR VAL ILE ALA TYR ALA SER VAL LEU PRO LYS          
SEQRES   8 B  131  LEU ARG ASP ARG GLN GLN LEU THR ALA LEU ILE ARG SER          
SEQRES   9 B  131  GLY GLU LEU GLU VAL GLN GLY ASP ILE GLN VAL VAL GLN          
SEQRES  10 B  131  ASN PHE VAL ALA LEU ALA ASP LEU ALA GLU PHE ASP PRO          
SEQRES  11 B  131  ALA                                                          
HET    LMR  A 201      13                                                       
HET    PEG  A 202      17                                                       
HET    LMR  A 203      13                                                       
HET     CA  A 204       1                                                       
HET     CA  A 205       1                                                       
HET     CA  A 206       1                                                       
HET     CA  A 207       1                                                       
HET     CA  A 208       1                                                       
HET    PEG  B 201      17                                                       
HET    PEG  B 202      17                                                       
HET     CA  B 203       1                                                       
HET     CA  B 204       1                                                       
HETNAM     LMR (2S)-2-HYDROXYBUTANEDIOIC ACID                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CA CALCIUM ION                                                      
HETSYN     LMR L-MALATE                                                         
FORMUL   3  LMR    2(C4 H6 O5)                                                  
FORMUL   4  PEG    3(C4 H10 O3)                                                 
FORMUL   6   CA    7(CA 2+)                                                     
FORMUL  15  HOH   *185(H2 O)                                                    
HELIX    1 AA1 PRO A   13  TYR A   31  1                                  19    
HELIX    2 AA2 SER A   33  ALA A   35  5                                   3    
HELIX    3 AA3 LEU A   36  ARG A   42  1                                   7    
HELIX    4 AA4 ALA A   86  LEU A   92  5                                   7    
HELIX    5 AA5 ASP A   94  SER A  104  1                                  11    
HELIX    6 AA6 ASP A  112  ASP A  129  1                                  18    
HELIX    7 AA7 LYS B   15  TYR B   31  1                                  17    
HELIX    8 AA8 SER B   33  ALA B   35  5                                   3    
HELIX    9 AA9 LEU B   36  ARG B   42  1                                   7    
HELIX   10 AB1 TYR B   85  LEU B   92  5                                   8    
HELIX   11 AB2 ASP B   94  SER B  104  1                                  11    
HELIX   12 AB3 ASP B  112  ALA B  126  1                                  15    
SHEET    1 AA1 5 VAL A  68  LEU A  71  0                                        
SHEET    2 AA1 5 SER A  58  PHE A  63 -1  N  VAL A  62   O  ASP A  69           
SHEET    3 AA1 5 VAL A  47  VAL A  52 -1  N  VAL A  50   O  LEU A  59           
SHEET    4 AA1 5 CYS A  80  ALA A  84  1  O  VAL A  82   N  GLU A  51           
SHEET    5 AA1 5 LEU A 107  GLY A 111 -1  O  GLN A 110   N  THR A  81           
SHEET    1 AA2 5 VAL B  68  LEU B  71  0                                        
SHEET    2 AA2 5 SER B  58  PHE B  63 -1  N  VAL B  62   O  ASP B  69           
SHEET    3 AA2 5 VAL B  47  VAL B  52 -1  N  VAL B  50   O  LEU B  59           
SHEET    4 AA2 5 CYS B  80  ALA B  84  1  O  VAL B  82   N  GLU B  51           
SHEET    5 AA2 5 GLU B 108  GLY B 111 -1  O  GLN B 110   N  THR B  81           
LINK         OE1 GLU A  23                CA    CA A 207     1555   1555  2.34  
LINK         OE2 GLU A  23                CA    CA A 207     1555   1555  2.40  
LINK         OD1 ASP A  69                CA    CA A 207     1555   1555  2.48  
LINK         OD1AASP A  77                CA    CA A 208     1555   1555  2.27  
LINK         OD2AASP A  77                CA    CA A 208     1555   1555  2.65  
LINK         OD1 ASP A  79                CA    CA A 204     1555   1555  2.41  
LINK         OD2 ASP A  79                CA    CA A 204     1555   1555  2.56  
LINK         O   ARG A  93                CA    CA A 206     1555   1555  2.51  
LINK         OD1 ASP A 124                CA    CA A 206     1555   1555  2.67  
LINK         O   ALA A 126                CA    CA A 205     1555   1555  2.23  
LINK         OE1 GLU A 127                CA    CA A 206     1555   1555  2.85  
LINK         O   ASP A 129                CA    CA A 205     1555   1555  2.33  
LINK         O   ALA A 131                CA    CA A 205     1555   1555  2.57  
LINK         O   ARG B  42                CA    CA B 204     1555   1555  3.01  
LINK         O   ASP B 124                CA    CA B 203     1555   1555  2.32  
LINK         OD1 ASP B 124                CA    CA B 203     1555   1555  2.40  
LINK         O   GLU B 127                CA    CA B 203     1555   1555  2.33  
LINK         OD1 ASP B 129                CA    CA B 203     1555   1555  2.52  
LINK        CA    CA A 204                 O   HOH A 342     1555   1555  2.35  
LINK        CA    CA A 204                 O   HOH A 306     1555   1555  2.29  
LINK        CA    CA A 205                 O   HOH A 313     1555   1555  2.39  
LINK        CA    CA A 205                 O   HOH A 326     1555   1555  2.34  
LINK        CA    CA A 205                 O   HOH A 384     1555   1555  2.30  
LINK        CA    CA A 206                 O   HOH A 355     1555   1555  2.57  
LINK        CA    CA A 206                 O   HOH A 362     1555   1555  2.59  
LINK        CA    CA A 207                 O   HOH A 373     1555   1555  2.24  
LINK        CA    CA A 207                 O   HOH A 349     1555   1555  2.43  
LINK        CA    CA A 207                 O   HOH A 392     1555   1555  2.38  
LINK        CA    CA A 207                 O   HOH A 314     1555   1555  2.20  
LINK        CA    CA A 208                 O   HOH A 396     1555   1555  3.16  
LINK        CA    CA B 203                 O   HOH B 315     1555   1555  2.34  
LINK        CA    CA B 204                 O   HOH B 337     1555   1555  2.51  
LINK        CA    CA B 204                 O   HOH B 374     1555   1555  2.66  
LINK        CA    CA B 204                 O   HOH B 338     1555   1555  2.94  
LINK         OE1 GLU B  23                CA    CA A 204     1555   3444  2.48  
LINK         OE2 GLU B  23                CA    CA A 204     1555   3444  2.45  
LINK         OD1 ASP B  69                CA    CA A 204     1555   3444  2.27  
LINK        CA    CA A 208                 O   HOH A 399     1555   3454  2.48  
LINK        CA    CA B 203                 O   HOH A 371     1555   1455  2.50  
SITE     1 AC1  2 TYR A  85  ARG B  32                                          
SITE     1 AC2  7 LYS A  53  ILE A  83  TYR A  85  GLY A 105                    
SITE     2 AC2  7 GLU A 108  HOH A 310  HOH A 370                               
SITE     1 AC3 11 ASP A  77  ALA A  78  ASP A  79  GLY A 111                    
SITE     2 AC3 11 ASP A 112  HOH A 311  HOH A 332  GLU B  23                    
SITE     3 AC3 11 ARG B  66  GLN B  67  PEG B 201                               
SITE     1 AC4  5 ASP A  79  HOH A 306  HOH A 342  GLU B  23                    
SITE     2 AC4  5 ASP B  69                                                     
SITE     1 AC5  6 ALA A 126  ASP A 129  ALA A 131  HOH A 313                    
SITE     2 AC5  6 HOH A 326  HOH A 384                                          
SITE     1 AC6  5 ARG A  93  ASP A 124  GLU A 127  HOH A 355                    
SITE     2 AC6  5 HOH A 362                                                     
SITE     1 AC7  6 GLU A  23  ASP A  69  HOH A 314  HOH A 349                    
SITE     2 AC7  6 HOH A 373  HOH A 392                                          
SITE     1 AC8  2 ASP A  77  HOH A 399                                          
SITE     1 AC9  6 LMR A 203  ASN B  27  THR B  28  ARG B  32                    
SITE     2 AC9  6 ARG B  66  GLN B  67                                          
SITE     1 AD1  6 GLU A  65  ASP B  77  ALA B  78  ASP B  79                    
SITE     2 AD1  6 HOH B 314  HOH B 330                                          
SITE     1 AD2  5 HOH A 371  ASP B 124  GLU B 127  ASP B 129                    
SITE     2 AD2  5 HOH B 315                                                     
SITE     1 AD3  4 ARG B  42  HOH B 337  HOH B 338  HOH B 374                    
CRYST1   48.660   67.870   74.607  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      0.020551  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014734  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013404        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system