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Database: PDB
Entry: 6H6P
LinkDB: 6H6P
Original site: 6H6P 
HEADER    LIPID BINDING PROTEIN                   28-JUL-18   6H6P              
TITLE     UBIJ-SCP2 UBIQUINONE SYNTHESIS PROTEIN                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUINONE BIOSYNTHESIS PROTEIN UBIJ;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
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 6H6P    1       JRNL                                     
REVDAT   1   13-FEB-19 6H6P    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18749                          
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)  : 0.236                          
REMARK   3   R VALUE            (WORKING SET)  : 0.233                          
REMARK   3   FREE R VALUE                      : 0.289                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 938                            
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.65                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2980                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2260                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2831                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2240                   
REMARK   3   BIN FREE R VALUE                        : 0.2580                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 149                      
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            : 3579                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.87240                                             
REMARK   3    B22 (A**2) : -3.36690                                             
REMARK   3    B33 (A**2) : 8.23930                                              
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) : 0.410               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.589               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.319               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.584               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.321               
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      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3710   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5062   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1315   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 85     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 526    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3710   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 480    ; 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   : 4092   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.27                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.58                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.66                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.9041   14.1337   -2.1779           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.6319 T22:   -0.8711                                    
REMARK   3     T33:   -0.6931 T12:    0.0420                                    
REMARK   3     T13:   -0.0191 T23:   -0.0731                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8796 L22:    4.1325                                    
REMARK   3     L33:    6.4022 L12:   -0.4861                                    
REMARK   3     L13:    0.7301 L23:    2.3004                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0781 S12:   -0.0870 S13:    0.1830                     
REMARK   3     S21:   -0.2995 S22:   -0.1373 S23:   -0.0616                     
REMARK   3     S31:   -0.5656 S32:   -0.3854 S33:    0.2153                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.2716  -14.4072   -1.8235           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.6739 T22:   -0.9046                                    
REMARK   3     T33:   -0.7355 T12:    0.0124                                    
REMARK   3     T13:   -0.0145 T23:    0.0106                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0404 L22:    2.5750                                    
REMARK   3     L33:    3.5646 L12:    0.5719                                    
REMARK   3     L13:   -0.6284 L23:    1.4852                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0748 S12:    0.0176 S13:   -0.0252                     
REMARK   3     S21:    0.2087 S22:   -0.0096 S23:    0.0893                     
REMARK   3     S31:    0.5228 S32:   -0.0716 S33:   -0.0652                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.8903    8.0217   24.0140           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.7959 T22:   -0.7679                                    
REMARK   3     T33:   -0.7507 T12:    0.0252                                    
REMARK   3     T13:   -0.0301 T23:   -0.0326                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3259 L22:    2.5026                                    
REMARK   3     L33:    4.7842 L12:   -0.0998                                    
REMARK   3     L13:   -0.5987 L23:    0.6469                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0037 S12:    0.0154 S13:   -0.1008                     
REMARK   3     S21:   -0.0279 S22:   -0.0522 S23:    0.2291                     
REMARK   3     S31:   -0.2579 S32:   -0.4229 S33:    0.0559                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.4150   -9.5877   24.0835           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.7831 T22:   -0.8175                                    
REMARK   3     T33:   -0.7698 T12:    0.0255                                    
REMARK   3     T13:    0.0238 T23:   -0.0365                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.8148 L22:    3.0469                                    
REMARK   3     L33:    3.8420 L12:   -1.1862                                    
REMARK   3     L13:   -0.2472 L23:    0.9697                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1662 S12:   -0.2173 S13:   -0.1180                     
REMARK   3     S21:    0.2396 S22:    0.0583 S23:   -0.4324                     
REMARK   3     S31:    0.3301 S32:    0.4267 S33:    0.1079                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6H6P 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_1200011166.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-17                          
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 2                          
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 EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
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   (%): 44.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
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       23.84500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.83000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.27500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.83000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.84500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.27500            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLU A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     PHE A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     PRO A   130                                                      
REMARK 465     ALA A   131                                                      
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     GLU B   127                                                      
REMARK 465     PHE B   128                                                      
REMARK 465     ASP B   129                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     ALA B   131                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     MET C    12                                                      
REMARK 465     PRO C   130                                                      
REMARK 465     ALA C   131                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     GLU D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ASP D   129                                                      
REMARK 465     PRO D   130                                                      
REMARK 465     ALA D   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     ARG B  32    CG   CD   NE   CZ   NH1  NH2                        
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    LEU A  92       45.67    -90.06                                   
REMARK 500    LEU D  92       39.86    -79.44                                   
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                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  45   O                                                      
REMARK 620 2 ASP A  79   OD1  93.9                                              
REMARK 620 3 GLY C  45   O    95.1 132.1                                        
REMARK 620 4 HOH C 312   O   156.2  63.3  95.9                                  
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 SER A  58   OG                                                     
REMARK 620 2 GLU A  73   OE2  99.4                                              
REMARK 620 N                    1                                               
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 SER A  87   OG                                                     
REMARK 620 2 SER D  87   OG   88.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 124   O                                                      
REMARK 620 2 ASP A 124   OD1  59.7                                              
REMARK 620 3 HOH A 311   O    96.5  72.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  23   OE1                                                    
REMARK 620 2 GLU B  23   OE2  47.5                                              
REMARK 620 3 GLU D  65   OE2 100.6 132.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B  45   O                                                      
REMARK 620 2 GLY D  45   O    54.2                                              
REMARK 620 3 HOH B 308   O    53.1  73.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B  96   OE1                                                    
REMARK 620 2 HOH B 306   O    80.3                                              
REMARK 620 N                    1                                               
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 ASP B 124   O                                                      
REMARK 620 2 ASP B 124   OD1  66.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C  87   OG                                                     
REMARK 620 2 SER B  87   OG   91.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D  96   OE1                                                    
REMARK 620 2 ASP D 124   OD1 134.2                                              
REMARK 620 3 ASP D 124   OD2  91.1  49.5                                        
REMARK 620 4 ASP C 124   O   129.5  20.6  62.4                                  
REMARK 620 5 ASP C 124   OD1 131.3  21.8  65.0   2.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 124   O                                                      
REMARK 620 2 ASP D 124   OD1  68.6                                              
REMARK 620 3 HOH D 320   O    97.9  75.3                                        
REMARK 620 4 ASP C 124   OD1  61.3 103.8  60.2                                  
REMARK 620 5 ASP C 124   OD2  60.6 105.3  62.6   2.5                            
REMARK 620 6 HOH C 304   O    70.8 138.2 120.4  63.7  61.2                      
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 1PE A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 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 CA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 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                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202                  
DBREF  6H6P A   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
DBREF  6H6P B   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
DBREF  6H6P C   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
DBREF  6H6P D   12   131  UNP    P0ADP7   UBIJ_ECOLI       1    120             
SEQADV 6H6P MET A    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6P GLU A    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P LEU A    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS A    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU A   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU A   11  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P MET B    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6P GLU B    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P LEU B    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS B    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU B   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU B   11  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P MET C    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6P GLU C    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P LEU C    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS C    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU C   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU C   11  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P MET D    1  UNP  P0ADP7              INITIATING METHIONINE          
SEQADV 6H6P GLU D    2  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P LEU D    3  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    4  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    5  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    6  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    7  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    8  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P HIS D    9  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU D   10  UNP  P0ADP7              EXPRESSION TAG                 
SEQADV 6H6P GLU D   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                                                          
SEQRES   1 C  131  MET GLU LEU HIS HIS HIS HIS HIS HIS GLU GLU MET PRO          
SEQRES   2 C  131  PHE LYS PRO LEU VAL THR ALA GLY ILE GLU SER LEU LEU          
SEQRES   3 C  131  ASN THR PHE LEU TYR ARG SER PRO ALA LEU LYS THR ALA          
SEQRES   4 C  131  ARG SER ARG LEU LEU GLY LYS VAL LEU ARG VAL GLU VAL          
SEQRES   5 C  131  LYS GLY PHE SER THR SER LEU ILE LEU VAL PHE SER GLU          
SEQRES   6 C  131  ARG GLN VAL ASP VAL LEU GLY GLU TRP ALA GLY ASP ALA          
SEQRES   7 C  131  ASP CYS THR VAL ILE ALA TYR ALA SER VAL LEU PRO LYS          
SEQRES   8 C  131  LEU ARG ASP ARG GLN GLN LEU THR ALA LEU ILE ARG SER          
SEQRES   9 C  131  GLY GLU LEU GLU VAL GLN GLY ASP ILE GLN VAL VAL GLN          
SEQRES  10 C  131  ASN PHE VAL ALA LEU ALA ASP LEU ALA GLU PHE ASP PRO          
SEQRES  11 C  131  ALA                                                          
SEQRES   1 D  131  MET GLU LEU HIS HIS HIS HIS HIS HIS GLU GLU MET PRO          
SEQRES   2 D  131  PHE LYS PRO LEU VAL THR ALA GLY ILE GLU SER LEU LEU          
SEQRES   3 D  131  ASN THR PHE LEU TYR ARG SER PRO ALA LEU LYS THR ALA          
SEQRES   4 D  131  ARG SER ARG LEU LEU GLY LYS VAL LEU ARG VAL GLU VAL          
SEQRES   5 D  131  LYS GLY PHE SER THR SER LEU ILE LEU VAL PHE SER GLU          
SEQRES   6 D  131  ARG GLN VAL ASP VAL LEU GLY GLU TRP ALA GLY ASP ALA          
SEQRES   7 D  131  ASP CYS THR VAL ILE ALA TYR ALA SER VAL LEU PRO LYS          
SEQRES   8 D  131  LEU ARG ASP ARG GLN GLN LEU THR ALA LEU ILE ARG SER          
SEQRES   9 D  131  GLY GLU LEU GLU VAL GLN GLY ASP ILE GLN VAL VAL GLN          
SEQRES  10 D  131  ASN PHE VAL ALA LEU ALA ASP LEU ALA GLU PHE ASP PRO          
SEQRES  11 D  131  ALA                                                          
HET    1PE  A 201      38                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
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     CA  B 201       1                                                       
HET     CA  B 202       1                                                       
HET     CA  B 203       1                                                       
HET     CA  B 204       1                                                       
HET     CA  B 205       1                                                       
HET     CA  B 206       1                                                       
HET    1PE  C 201      38                                                       
HET     CA  C 202       1                                                       
HET     CA  D 201       1                                                       
HET     CA  D 202       1                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      CA CALCIUM ION                                                      
HETSYN     1PE PEG400                                                           
FORMUL   5  1PE    2(C10 H22 O6)                                                
FORMUL   6   CA    16(CA 2+)                                                    
FORMUL  23  HOH   *89(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 VAL A   88  LEU A   92  5                                   5    
HELIX    5 AA5 ASP A   94  SER A  104  1                                  11    
HELIX    6 AA6 ASP A  112  GLU A  127  1                                  16    
HELIX    7 AA7 PHE B   14  TYR B   31  1                                  18    
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 VAL B   88  LEU B   92  5                                   5    
HELIX   11 AB2 ASP B   94  SER B  104  1                                  11    
HELIX   12 AB3 ASP B  112  ALA B  126  1                                  15    
HELIX   13 AB4 PHE C   14  TYR C   31  1                                  18    
HELIX   14 AB5 SER C   33  ALA C   35  5                                   3    
HELIX   15 AB6 LEU C   36  ARG C   42  1                                   7    
HELIX   16 AB7 VAL C   88  LEU C   92  5                                   5    
HELIX   17 AB8 ASP C   94  SER C  104  1                                  11    
HELIX   18 AB9 ASP C  112  LEU C  125  1                                  14    
HELIX   19 AC1 PRO D   13  TYR D   31  1                                  19    
HELIX   20 AC2 SER D   33  ALA D   35  5                                   3    
HELIX   21 AC3 LEU D   36  ARG D   42  1                                   7    
HELIX   22 AC4 VAL D   88  LEU D   92  5                                   5    
HELIX   23 AC5 ASP D   94  SER D  104  1                                  11    
HELIX   24 AC6 ASP D  112  ALA D  126  1                                  15    
SHEET    1 AA1 5 VAL A  68  LEU A  71  0                                        
SHEET    2 AA1 5 THR A  57  PHE A  63 -1  N  ILE A  60   O  LEU A  71           
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 GLU A 108  GLY A 111 -1  O  GLU A 108   N  ILE A  83           
SHEET    1 AA2 5 VAL B  68  LEU B  71  0                                        
SHEET    2 AA2 5 THR B  57  PHE B  63 -1  N  ILE B  60   O  LEU B  71           
SHEET    3 AA2 5 VAL B  47  VAL B  52 -1  N  LEU B  48   O  LEU B  61           
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  GLU B 108   N  ILE B  83           
SHEET    1 AA3 5 VAL C  68  LEU C  71  0                                        
SHEET    2 AA3 5 SER C  58  PHE C  63 -1  N  ILE C  60   O  LEU C  71           
SHEET    3 AA3 5 VAL C  47  VAL C  52 -1  N  LEU C  48   O  LEU C  61           
SHEET    4 AA3 5 CYS C  80  ALA C  84  1  O  VAL C  82   N  GLU C  51           
SHEET    5 AA3 5 GLU C 108  GLY C 111 -1  O  GLU C 108   N  ILE C  83           
SHEET    1 AA4 5 VAL D  68  LEU D  71  0                                        
SHEET    2 AA4 5 THR D  57  PHE D  63 -1  N  ILE D  60   O  LEU D  71           
SHEET    3 AA4 5 VAL D  47  VAL D  52 -1  N  LEU D  48   O  LEU D  61           
SHEET    4 AA4 5 CYS D  80  ALA D  84  1  O  CYS D  80   N  ARG D  49           
SHEET    5 AA4 5 GLU D 108  GLY D 111 -1  O  GLU D 108   N  ILE D  83           
LINK         O   GLY A  45                CA    CA A 203     1555   1555  2.53  
LINK         OE1 GLU A  51                CA    CA A 205     1555   1555  2.78  
LINK         OG  SER A  58                CA    CA A 204     1555   1555  3.15  
LINK         OE2AGLU A  73                CA    CA A 204     1555   1555  2.76  
LINK         OD1 ASP A  79                CA    CA A 203     1555   1555  3.20  
LINK         OG  SER A  87                CA    CA A 206     1555   1555  2.81  
LINK         O   ASP A 124                CA    CA A 202     1555   1555  3.02  
LINK         OD1 ASP A 124                CA    CA A 202     1555   1555  2.85  
LINK         OE1 GLU B  23                CA    CA B 201     1555   1555  2.63  
LINK         OE2 GLU B  23                CA    CA B 201     1555   1555  2.82  
LINK         O   GLY B  45                CA    CA B 202     1555   1555  3.04  
LINK         OG  SER B  58                CA    CA B 206     1555   1555  3.10  
LINK         OE1 GLN B  96                CA    CA B 205     1555   1555  2.97  
LINK         O   ASP B 124                CA    CA B 204     1555   1555  2.57  
LINK         OD1 ASP B 124                CA    CA B 204     1555   1555  2.73  
LINK         O   GLY C  45                CA    CA A 203     1555   1555  3.00  
LINK         OG  SER C  87                CA    CA C 202     1555   1555  2.39  
LINK         O   GLY D  45                CA    CA B 202     1555   1555  2.76  
LINK         OE2 GLU D  65                CA    CA B 201     1555   1555  3.01  
LINK         OE1 GLN D  96                CA    CA D 201     1555   1555  2.33  
LINK         O   ASP D 124                CA    CA D 202     1555   1555  2.45  
LINK         OD1 ASP D 124                CA    CA D 201     1555   1555  2.45  
LINK         OD1 ASP D 124                CA    CA D 202     1555   1555  2.67  
LINK         OD2 ASP D 124                CA    CA D 201     1555   1555  2.70  
LINK        CA    CA A 202                 O   HOH A 311     1555   1555  3.19  
LINK        CA    CA A 203                 O   HOH C 312     1555   1555  2.50  
LINK        CA    CA A 208                 O   HOH A 321     1555   1555  2.98  
LINK        CA    CA B 202                 O   HOH B 308     1555   1555  3.04  
LINK        CA    CA B 205                 O   HOH B 306     1555   1555  2.62  
LINK        CA    CA D 202                 O   HOH D 320     1555   1555  2.66  
LINK         OG  SER B  87                CA    CA C 202     1555   2454  2.48  
LINK         O   ASP C 124                CA    CA D 201     1555   1455  2.42  
LINK         OD1 ASP C 124                CA    CA D 201     1555   1455  2.62  
LINK         OD1 ASP C 124                CA    CA D 202     1555   1455  2.58  
LINK         OD2 ASP C 124                CA    CA D 202     1555   1455  3.03  
LINK         OG  SER D  87                CA    CA A 206     1555   2455  2.09  
LINK        CA    CA D 202                 O   HOH C 304     1555   1655  2.40  
SITE     1 AC1  2 LEU A  17  LEU B  17                                          
SITE     1 AC2  2 ASP A 124  GLU A 127                                          
SITE     1 AC3  5 GLY A  45  ASP A  79  GLY C  45  ASP C  79                    
SITE     2 AC3  5 HOH C 312                                                     
SITE     1 AC4  2 SER A  58  GLU A  73                                          
SITE     1 AC5  1 GLU A  51                                                     
SITE     1 AC6  2 SER A  87  SER D  87                                          
SITE     1 AC7  3 ALA A  75  GLY A  76  ASP A  77                               
SITE     1 AC8  1 HOH A 321                                                     
SITE     1 AC9  2 GLU B  23  GLU D  65                                          
SITE     1 AD1  4 GLY B  45  ASP B  79  HOH B 308  GLY D  45                    
SITE     1 AD2  3 VAL B  52  PHE B  55  SER B  56                               
SITE     1 AD3  1 ASP B 124                                                     
SITE     1 AD4  2 GLN B  96  HOH B 306                                          
SITE     1 AD5  1 SER B  58                                                     
SITE     1 AD6  1 SER C  87                                                     
SITE     1 AD7  3 TYR B  85  SER B  87  SER C  87                               
SITE     1 AD8  4 ASP C 124  ASP D  94  GLN D  96  ASP D 124                    
SITE     1 AD9  4 ASP C 124  HOH C 304  ASP D 124  HOH D 320                    
CRYST1   47.690   94.550  115.660  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020969  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008646        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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