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Database: PDB
Entry: 4PXF
LinkDB: 4PXF
Original site: 4PXF 
HEADER    SIGNALING PROTEIN                       23-MAR-14   4PXF              
TITLE     CRYSTAL STRUCTURE OF THE ACTIVE G-PROTEIN-COUPLED RECEPTOR OPSIN IN   
TITLE    2 COMPLEX WITH THE FINGER-LOOP PEPTIDE DERIVED FROM THE FULL-LENGTH    
TITLE    3 ARRESTIN-1                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: S-ARRESTIN;                                                
COMPND   6 CHAIN: B;                                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 OTHER_DETAILS: BOVINE EYE;                                           
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   9 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;            
SOURCE  10 ORGANISM_TAXID: 9913                                                 
KEYWDS    RETINAL PROTEIN, PHOTORECEPTOR, G-PROTEIN COUPLED RECEPTOR,           
KEYWDS   2 PHOSPHOPROTEIN, PHOTORECEPTOR PROTEIN, SENSORY TRANSDUCTION,         
KEYWDS   3 TRANSDUCER, TRANSMEMBRANE, VISION, SIGNALING PROTEIN, VISUAL         
KEYWDS   4 ARRESTIN, DESENSITISATION OF THE VISUAL TRANSDUCTION CASCADE,        
KEYWDS   5 BINDING TO ACTICATED AND PHOSPHORYLATED RHODOPSIN, RHODOPSIN, OPSIN  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SZCZEPEK,P.SCHEERER                                                 
REVDAT   3   20-SEP-23 4PXF    1       HETSYN                                   
REVDAT   2   29-JUL-20 4PXF    1       COMPND REMARK HET    HETNAM              
REVDAT   2 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   2 3                   1       ATOM                                     
REVDAT   1   17-SEP-14 4PXF    0                                                
JRNL        AUTH   M.SZCZEPEK,F.BEYRIERE,K.P.HOFMANN,M.ELGETI,R.KAZMIN,A.ROSE,  
JRNL        AUTH 2 F.J.BARTL,D.VON STETTEN,M.HECK,M.E.SOMMER,P.W.HILDEBRAND,    
JRNL        AUTH 3 P.SCHEERER                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF A COMMON GPCR-BINDING INTERFACE FOR G   
JRNL        TITL 2 PROTEIN AND ARRESTIN.                                        
JRNL        REF    NAT COMMUN                    V.   5  4801 2014              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25205354                                                     
JRNL        DOI    10.1038/NCOMMS5801                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30511                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1637                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2238                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2635                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 159                                     
REMARK   3   SOLVENT ATOMS            : 11                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.17000                                             
REMARK   3    B22 (A**2) : -1.17000                                             
REMARK   3    B33 (A**2) : 3.79000                                              
REMARK   3    B12 (A**2) : -1.17000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2872 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2702 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3911 ; 1.187 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6211 ; 0.798 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   332 ; 5.104 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;36.438 ;23.421       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   419 ;15.713 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;12.246 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   454 ; 0.154 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3080 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   681 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1329 ;13.846 ; 3.493       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1327 ;13.834 ; 3.490       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1657 ;16.286 ; 5.258       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1658 ;16.284 ; 5.258       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1542 ;16.421 ; 4.237       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1542 ;16.412 ; 4.237       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2254 ;19.421 ; 6.147       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3394 ;19.062 ;31.142       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3393 ;19.038 ;31.102       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5571 ; 6.208 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):     2 ;40.117 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5497 ;42.816 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.5021 248.1880  38.3901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5966 T22:   0.6075                                     
REMARK   3      T33:   0.3793 T12:   0.0030                                     
REMARK   3      T13:  -0.0364 T23:   0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2922 L22:   1.0499                                     
REMARK   3      L33:   0.3591 L12:   0.1504                                     
REMARK   3      L13:  -0.1493 L23:   0.0503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:   0.0247 S13:   0.0738                       
REMARK   3      S21:  -0.0665 S22:  -0.0080 S23:   0.0276                       
REMARK   3      S31:   0.0420 S32:   0.0569 S33:   0.0165                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    71        B    77                          
REMARK   3    ORIGIN FOR THE GROUP (A): 122.6938 226.4295  39.1501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7873 T22:   0.7445                                     
REMARK   3      T33:   0.8968 T12:  -0.1184                                     
REMARK   3      T13:   0.1236 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3056 L22:   4.5566                                     
REMARK   3      L33:   1.1300 L12:  -1.0004                                     
REMARK   3      L13:   0.5268 L23:  -2.2240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1380 S12:  -0.1658 S13:  -0.0316                       
REMARK   3      S21:  -0.3816 S22:   0.3045 S23:  -0.0074                       
REMARK   3      S31:   0.0938 S32:  -0.2005 S33:  -0.1664                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   411                          
REMARK   3    ORIGIN FOR THE GROUP (A): 146.9902 256.1458  41.5382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5661 T22:   0.5190                                     
REMARK   3      T33:   0.5318 T12:   0.0325                                     
REMARK   3      T13:  -0.1350 T23:   0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0182 L22:   0.1477                                     
REMARK   3      L33:   0.6370 L12:   0.3058                                     
REMARK   3      L13:   0.1307 L23:   0.1958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1535 S12:   0.0835 S13:   0.4692                       
REMARK   3      S21:  -0.0482 S22:   0.0118 S23:   0.2168                       
REMARK   3      S31:   0.2025 S32:  -0.1684 S33:   0.1417                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   501        A   511                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.1363 251.4432  40.2838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7520 T22:   0.8678                                     
REMARK   3      T33:   0.4436 T12:  -0.1793                                     
REMARK   3      T13:  -0.0587 T23:   0.1893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4392 L22:   3.5892                                     
REMARK   3      L33:   1.1831 L12:   2.1043                                     
REMARK   3      L13:   0.6801 L23:   1.8437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0899 S12:   0.3198 S13:  -0.1382                       
REMARK   3      S21:   0.1979 S22:  -0.0375 S23:  -0.3643                       
REMARK   3      S31:   0.0321 S32:  -0.2306 S33:  -0.0524                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085339.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : SI(311) MONOCHROMATOR              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.00000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: 3DQB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2 M (NH4)2SO4 IN 0.1 M 2-(N            
REMARK 280  -MORPHOLINO)ETHANESULFONIC ACID (MES), PH 6.0, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000      121.31100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       70.03894            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       36.73867            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000      121.31100            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       70.03894            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       36.73867            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000      121.31100            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       70.03894            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       36.73867            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000      121.31100            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       70.03894            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       36.73867            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000      121.31100            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       70.03894            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       36.73867            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000      121.31100            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       70.03894            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       36.73867            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      140.07788            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       73.47733            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      140.07788            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       73.47733            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      140.07788            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       73.47733            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      140.07788            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       73.47733            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      140.07788            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       73.47733            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      140.07788            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       73.47733            
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: 11090 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      110.21600            
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     PRO A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     THR A   336                                                      
REMARK 465     VAL A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     LYS A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     GLU A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     GLN A   344                                                      
REMARK 465     VAL A   345                                                      
REMARK 465     ALA A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     TYR B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     GLN B    69                                                      
REMARK 465     GLU B    70                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A    15     O5   NAG C     1              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  27      154.09    -48.33                                   
REMARK 500    SER A 176     -168.49     67.62                                   
REMARK 500    PHE A 212      -60.30   -135.69                                   
REMARK 500    ILE A 307      -64.68   -129.25                                   
REMARK 500    LYS A 325      171.59     69.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4PXF A    1   348  UNP    P02699   OPSD_BOVIN       1    348             
DBREF  4PXF B   67    77  UNP    P08168   ARRS_BOVIN      67     77             
SEQRES   1 A  348  MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE          
SEQRES   2 A  348  SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA          
SEQRES   3 A  348  PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET          
SEQRES   4 A  348  LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE          
SEQRES   5 A  348  PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS          
SEQRES   6 A  348  LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN          
SEQRES   7 A  348  LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE          
SEQRES   8 A  348  THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL          
SEQRES   9 A  348  PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA          
SEQRES  10 A  348  THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL          
SEQRES  11 A  348  LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET          
SEQRES  12 A  348  SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY          
SEQRES  13 A  348  VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA          
SEQRES  14 A  348  PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY          
SEQRES  15 A  348  MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS          
SEQRES  16 A  348  GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE          
SEQRES  17 A  348  VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE          
SEQRES  18 A  348  CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA          
SEQRES  19 A  348  ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU          
SEQRES  20 A  348  LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA          
SEQRES  21 A  348  PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE          
SEQRES  22 A  348  TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE          
SEQRES  23 A  348  PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA          
SEQRES  24 A  348  VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN          
SEQRES  25 A  348  PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS          
SEQRES  26 A  348  ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER          
SEQRES  27 A  348  LYS THR GLU THR SER GLN VAL ALA PRO ALA                      
SEQRES   1 B   11  TYR GLY GLN GLU ASP ILE ASP VAL MET GLY LEU                  
MODRES 4PXF ASN A   15  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    GLC  D   1      11                                                       
HET    GLC  D   2      12                                                       
HET    BOG  A 405      20                                                       
HET    BOG  A 406      20                                                       
HET    BOG  A 407      20                                                       
HET    PLM  A 408      17                                                       
HET    SO4  A 409       5                                                       
HET    ACT  A 410       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                              
HETSYN     BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-            
HETSYN   2 BOG  GLUCOSIDE; OCTYL GLUCOSIDE                                      
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   4  GLC    2(C6 H12 O6)                                                 
FORMUL   5  BOG    3(C14 H28 O6)                                                
FORMUL   8  PLM    C16 H32 O2                                                   
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  ACT    C2 H3 O2 1-                                                  
FORMUL  11  HOH   *11(H2 O)                                                     
HELIX    1   1 SER A   14  GLY A   18  5                                   5    
HELIX    2   2 GLU A   33  HIS A   65  1                                  33    
HELIX    3   3 LYS A   66  ARG A   69  5                                   4    
HELIX    4   4 THR A   70  GLY A   90  1                                  21    
HELIX    5   5 GLY A   90  LEU A   99  1                                  10    
HELIX    6   6 PHE A  105  LYS A  141  1                                  37    
HELIX    7   7 GLY A  149  VAL A  173  1                                  25    
HELIX    8   8 HIS A  195  THR A  198  5                                   4    
HELIX    9   9 ASN A  199  PHE A  212  1                                  14    
HELIX   10  10 PHE A  212  GLN A  236  1                                  25    
HELIX   11  11 SER A  240  HIS A  278  1                                  39    
HELIX   12  12 GLY A  284  THR A  297  1                                  14    
HELIX   13  13 THR A  297  ILE A  307  1                                  11    
HELIX   14  14 ASN A  310  CYS A  322  1                                  13    
HELIX   15  15 ILE B   72  GLY B   76  5                                   5    
SHEET    1   A 2 THR A   4  GLY A   6  0                                        
SHEET    2   A 2 PHE A   9  VAL A  11 -1  O  VAL A  11   N  THR A   4           
SHEET    1   B 2 TYR A 178  GLU A 181  0                                        
SHEET    2   B 2 SER A 186  ILE A 189 -1  O  SER A 186   N  GLU A 181           
SSBOND   1 CYS A  110    CYS A  187                          1555   1555  2.04  
LINK         ND2 ASN A  15                 C1  NAG C   1     1555   1555  1.33  
LINK         SG  CYS A 323                 C1  PLM A 408     1555   1555  1.87  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.44  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.45  
LINK         C1  GLC D   1                 O1  GLC D   2     1555   1555  1.44  
CRYST1  242.622  242.622  110.216  90.00  90.00 120.00 H 3 2        18          
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      0.004122  0.002380  0.000000        0.00000                         
SCALE2      0.000000  0.004759  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009073        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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