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Database: PDB
Entry: 4I0Y
LinkDB: 4I0Y
Original site: 4I0Y 
HEADER    METAL TRANSPORT                         19-NOV-12   4I0Y              
TITLE     CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES 1-536)     
TITLE    2 DISEASE MUTANT C36R                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RYANODINE RECEPTOR 1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DISEASE HOT SPOT, RESIDUES 1-536;               
COMPND   5 SYNONYM: RYR-1, RYR1, SKELETAL MUSCLE CALCIUM RELEASE CHANNEL,       
COMPND   6 SKELETAL MUSCLE RYANODINE RECEPTOR, SKELETAL MUSCLE-TYPE RYANODINE   
COMPND   7 RECEPTOR, TYPE 1 RYANODINE RECEPTOR;                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 GENE: RYR1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA                                    
KEYWDS    CALCIUM CHANNEL, ER/SR MEMBRANE, METAL TRANSPORT                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN PETEGEM,L.KIMLICKA                                              
REVDAT   2   06-MAR-13 4I0Y    1       JRNL                                     
REVDAT   1   20-FEB-13 4I0Y    0                                                
JRNL        AUTH   L.KIMLICKA,K.LAU,C.C.TUNG,F.VAN PETEGEM                      
JRNL        TITL   DISEASE MUTATIONS IN THE RYANODINE RECEPTOR N-TERMINAL       
JRNL        TITL 2 REGION COUPLE TO A MOBILE INTERSUBUNIT INTERFACE.            
JRNL        REF    NAT COMMUN                    V.   4  1506 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23422674                                                     
JRNL        DOI    10.1038/NCOMMS2501                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 39670                          
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) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2088                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2909                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 152                          
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3495                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 17                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.98000                                             
REMARK   3    B22 (A**2) : -1.98000                                             
REMARK   3    B33 (A**2) : 2.97000                                              
REMARK   3    B12 (A**2) : -0.99000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.256         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.209         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.184         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.835        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3566 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4849 ; 0.975 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   464 ; 4.999 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   140 ;32.473 ;22.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   521 ;19.128 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.265 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   570 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2672 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2339 ; 0.241 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3674 ; 0.456 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1227 ; 0.443 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1175 ; 0.772 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
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    12        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.9780  53.7970  -9.6710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6380 T22:   0.9753                                     
REMARK   3      T33:   0.2719 T12:  -0.1335                                     
REMARK   3      T13:  -0.1996 T23:  -0.1093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3833 L22:   3.4158                                     
REMARK   3      L33:   6.3831 L12:   0.9395                                     
REMARK   3      L13:   0.4772 L23:   0.2941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2965 S12:  -0.2843 S13:  -0.3373                       
REMARK   3      S21:   0.3218 S22:   0.0494 S23:  -0.2125                       
REMARK   3      S31:   0.0179 S32:   0.1841 S33:  -0.3458                       
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 :   A   206        A   394                          
REMARK   3    ORIGIN FOR THE GROUP (A): -71.4780  62.1500 -25.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5780 T22:   0.5643                                     
REMARK   3      T33:   0.1011 T12:  -0.0502                                     
REMARK   3      T13:   0.0323 T23:  -0.0900                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9267 L22:   1.5885                                     
REMARK   3      L33:   1.8000 L12:   0.1522                                     
REMARK   3      L13:  -0.3067 L23:  -0.3306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1617 S12:  -0.0830 S13:   0.3336                       
REMARK   3      S21:   0.1326 S22:   0.0780 S23:  -0.1840                       
REMARK   3      S31:  -0.2443 S32:   0.0729 S33:  -0.2397                       
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   395        A   532                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.9830  54.5360 -40.5980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4335 T22:   0.9247                                     
REMARK   3      T33:   0.1694 T12:  -0.0863                                     
REMARK   3      T13:  -0.0262 T23:  -0.2125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2056 L22:   2.4319                                     
REMARK   3      L33:   5.6923 L12:  -0.2946                                     
REMARK   3      L13:  -1.5921 L23:  -0.0838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1672 S12:   0.1768 S13:  -0.1292                       
REMARK   3      S21:   0.0394 S22:   0.1225 S23:  -0.4376                       
REMARK   3      S31:  -0.2315 S32:   0.8580 S33:  -0.2896                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 4I0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076166.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : ACCEL/BRUKER DOUBLE CRYSTAL        
REMARK 200                                   MONOCHROMATOR (DCM)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SCALA                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41758                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.400                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.50                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 82.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 9.5, EVAPORATION                      
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       85.19050            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.18476            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      100.70433            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       85.19050            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.18476            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      100.70433            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       85.19050            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.18476            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      100.70433            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       85.19050            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       49.18476            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      100.70433            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       85.19050            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       49.18476            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      100.70433            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       85.19050            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       49.18476            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      100.70433            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       98.36952            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      201.40867            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       98.36952            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      201.40867            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       98.36952            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      201.40867            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       98.36952            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      201.40867            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       98.36952            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      201.40867            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       98.36952            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      201.40867            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     GLU A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     SER A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     SER A   124                                                      
REMARK 465     ARG A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     MET A   127                                                      
REMARK 465     THR A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     ALA A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     MET A   227                                                      
REMARK 465     ASP A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     ASP A   363                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     ALA A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     ARG A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLY A   370                                                      
REMARK 465     VAL A   371                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     PRO A   430                                                      
REMARK 465     PRO A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     ASN A   533                                                      
REMARK 465     ARG A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     ASN A   536                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  28    CG1  CG2                                            
REMARK 470     LEU A  29    CG   CD1  CD2                                       
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     GLU A  31    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  32    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  33    CG   CD1  CD2                                       
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     ASN A  54    CG   OD1  ND2                                       
REMARK 470     ASN A  57    CG   OD1  ND2                                       
REMARK 470     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     MET A  81    CG   SD   CE                                        
REMARK 470     ASN A  84    CG   OD1  ND2                                       
REMARK 470     HIS A  98    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 133    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 140    CG   OD1  OD2                                       
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 155    CG   CD   CE   NZ                                   
REMARK 470     GLN A 156    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 177    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 188    CG   CD   OE1  OE2                                  
REMARK 470     MET A 196    CG   SD   CE                                        
REMARK 470     LEU A 199    CG   CD1  CD2                                       
REMARK 470     GLN A 241    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 267    CG1  CG2  CD1                                       
REMARK 470     ARG A 275    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 296    CG   OD1  OD2                                       
REMARK 470     LYS A 306    CG   CD   CE   NZ                                   
REMARK 470     HIS A 308    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     ARG A 329    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 380    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 416    CG   CD   CE   NZ                                   
REMARK 470     SER A 420    OG                                                  
REMARK 470     LYS A 424    CG   CD   CE   NZ                                   
REMARK 470     ARG A 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 439    CG   CD   OE1  OE2                                  
REMARK 470     SER A 456    OG                                                  
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 458    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 459    CG   CD1  CD2                                       
REMARK 470     GLN A 460    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 462    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     GLN A 465    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 467    CG   CD   CE   NZ                                   
REMARK 470     ARG A 469    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 509    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 510    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XOA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N-TERMINAL THREE DOMAINS OF THE             
REMARK 900 SKELETAL MUSCLE RYANODINE RECEPTOR (RYR1)                            
REMARK 900 RELATED ID: 4I1E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT G249R                                                  
REMARK 900 RELATED ID: 4I2S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT I404M                                                  
REMARK 900 RELATED ID: 4I37   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT R402G                                                  
REMARK 900 RELATED ID: 4I3N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT D61N                                                   
REMARK 900 RELATED ID: 4I6I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT R45C                                                   
REMARK 900 RELATED ID: 4I7I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT L14R                                                   
REMARK 900 RELATED ID: 4I8M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT V219I                                                  
REMARK 900 RELATED ID: 4I96   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 217-536)                                                             
DBREF  4I0Y A    1   536  UNP    P11716   RYR1_RABIT       1    536             
SEQADV 4I0Y ARG A   36  UNP  P11716    CYS    36 ENGINEERED MUTATION            
SEQRES   1 A  536  MET GLY ASP GLY GLY GLU GLY GLU ASP GLU VAL GLN PHE          
SEQRES   2 A  536  LEU ARG THR ASP ASP GLU VAL VAL LEU GLN CYS SER ALA          
SEQRES   3 A  536  THR VAL LEU LYS GLU GLN LEU LYS LEU ARG LEU ALA ALA          
SEQRES   4 A  536  GLU GLY PHE GLY ASN ARG LEU CYS PHE LEU GLU PRO THR          
SEQRES   5 A  536  SER ASN ALA GLN ASN VAL PRO PRO ASP LEU ALA ILE CYS          
SEQRES   6 A  536  CYS PHE THR LEU GLU GLN SER LEU SER VAL ARG ALA LEU          
SEQRES   7 A  536  GLN GLU MET LEU ALA ASN THR VAL GLU ALA GLY VAL GLU          
SEQRES   8 A  536  SER SER GLN GLY GLY GLY HIS ARG THR LEU LEU TYR GLY          
SEQRES   9 A  536  HIS ALA ILE LEU LEU ARG HIS ALA HIS SER ARG MET TYR          
SEQRES  10 A  536  LEU SER CYS LEU THR THR SER ARG SER MET THR ASP LYS          
SEQRES  11 A  536  LEU ALA PHE ASP VAL GLY LEU GLN GLU ASP ALA THR GLY          
SEQRES  12 A  536  GLU ALA CYS TRP TRP THR MET HIS PRO ALA SER LYS GLN          
SEQRES  13 A  536  ARG SER GLU GLY GLU LYS VAL ARG VAL GLY ASP ASP LEU          
SEQRES  14 A  536  ILE LEU VAL SER VAL SER SER GLU ARG TYR LEU HIS LEU          
SEQRES  15 A  536  SER THR ALA SER GLY GLU LEU GLN VAL ASP ALA SER PHE          
SEQRES  16 A  536  MET GLN THR LEU TRP ASN MET ASN PRO ILE CYS SER CYS          
SEQRES  17 A  536  CYS GLU GLU GLY TYR VAL THR GLY GLY HIS VAL LEU ARG          
SEQRES  18 A  536  LEU PHE HIS GLY HIS MET ASP GLU CYS LEU THR ILE SER          
SEQRES  19 A  536  ALA ALA ASP SER ASP ASP GLN ARG ARG LEU VAL TYR TYR          
SEQRES  20 A  536  GLU GLY GLY ALA VAL CYS THR HIS ALA ARG SER LEU TRP          
SEQRES  21 A  536  ARG LEU GLU PRO LEU ARG ILE SER TRP SER GLY SER HIS          
SEQRES  22 A  536  LEU ARG TRP GLY GLN PRO LEU ARG ILE ARG HIS VAL THR          
SEQRES  23 A  536  THR GLY ARG TYR LEU ALA LEU THR GLU ASP GLN GLY LEU          
SEQRES  24 A  536  VAL VAL VAL ASP ALA CYS LYS ALA HIS THR LYS ALA THR          
SEQRES  25 A  536  SER PHE CYS PHE ARG VAL SER LYS GLU LYS LEU ASP THR          
SEQRES  26 A  536  ALA PRO LYS ARG ASP VAL GLU GLY MET GLY PRO PRO GLU          
SEQRES  27 A  536  ILE LYS TYR GLY GLU SER LEU CYS PHE VAL GLN HIS VAL          
SEQRES  28 A  536  ALA SER GLY LEU TRP LEU THR TYR ALA ALA PRO ASP PRO          
SEQRES  29 A  536  LYS ALA LEU ARG LEU GLY VAL LEU LYS LYS LYS ALA ILE          
SEQRES  30 A  536  LEU HIS GLN GLU GLY HIS MET ASP ASP ALA LEU PHE LEU          
SEQRES  31 A  536  THR ARG CYS GLN GLN GLU GLU SER GLN ALA ALA ARG MET          
SEQRES  32 A  536  ILE HIS SER THR ALA GLY LEU TYR ASN GLN PHE ILE LYS          
SEQRES  33 A  536  GLY LEU ASP SER PHE SER GLY LYS PRO ARG GLY SER GLY          
SEQRES  34 A  536  PRO PRO ALA GLY PRO ALA LEU PRO ILE GLU ALA VAL ILE          
SEQRES  35 A  536  LEU SER LEU GLN ASP LEU ILE GLY TYR PHE GLU PRO PRO          
SEQRES  36 A  536  SER GLU GLU LEU GLN HIS GLU GLU LYS GLN SER LYS LEU          
SEQRES  37 A  536  ARG SER LEU ARG ASN ARG GLN SER LEU PHE GLN GLU GLU          
SEQRES  38 A  536  GLY MET LEU SER LEU VAL LEU ASN CYS ILE ASP ARG LEU          
SEQRES  39 A  536  ASN VAL TYR THR THR ALA ALA HIS PHE ALA GLU TYR ALA          
SEQRES  40 A  536  GLY GLU GLU ALA ALA GLU SER TRP LYS GLU ILE VAL ASN          
SEQRES  41 A  536  LEU LEU TYR GLU LEU LEU ALA SER LEU ILE ARG GLY ASN          
SEQRES  42 A  536  ARG ALA ASN                                                  
HET    GOL  A 601       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    C3 H8 O3                                                     
FORMUL   3  HOH   *17(H2 O)                                                     
HELIX    1   1 SER A   74  ASN A   84  1                                  11    
HELIX    2   2 ALA A  251  SER A  258  5                                   8    
HELIX    3   3 ASP A  303  ALA A  307  5                                   5    
HELIX    4   4 HIS A  308  SER A  313  1                                   6    
HELIX    5   5 GLN A  394  SER A  420  1                                  27    
HELIX    6   6 PRO A  437  GLU A  453  1                                  17    
HELIX    7   7 GLN A  460  GLU A  480  1                                  21    
HELIX    8   8 GLY A  482  VAL A  496  1                                  15    
HELIX    9   9 THR A  499  GLU A  505  1                                   7    
HELIX   10  10 GLY A  508  GLU A  513  1                                   6    
HELIX   11  11 SER A  514  ARG A  531  1                                  18    
SHEET    1   A 9 PHE A  48  SER A  53  0                                        
SHEET    2   A 9 GLU A  31  ALA A  38 -1  N  ALA A  38   O  PHE A  48           
SHEET    3   A 9 GLU A  19  VAL A  28 -1  N  ALA A  26   O  LEU A  33           
SHEET    4   A 9 TRP A 200  CYS A 206 -1  O  ASN A 201   N  GLN A  23           
SHEET    5   A 9 ASP A 168  SER A 173 -1  N  LEU A 169   O  TRP A 200           
SHEET    6   A 9 TRP A 147  PRO A 152 -1  N  THR A 149   O  VAL A 172           
SHEET    7   A 9 ALA A 106  HIS A 111 -1  N  ILE A 107   O  TRP A 148           
SHEET    8   A 9 PHE A  67  LEU A  69 -1  N  THR A  68   O  ARG A 110           
SHEET    9   A 9 GLU A  19  VAL A  28 -1  N  VAL A  20   O  PHE A  67           
SHEET    1   B 2 TYR A 117  LEU A 121  0                                        
SHEET    2   B 2 ASP A 134  GLN A 138 -1  O  ASP A 134   N  LEU A 121           
SHEET    1   C 2 TYR A 179  SER A 183  0                                        
SHEET    2   C 2 GLN A 190  SER A 194 -1  O  GLN A 190   N  SER A 183           
SHEET    1   D 7 VAL A 219  PHE A 223  0                                        
SHEET    2   D 7 TRP A 260  PRO A 264 -1  O  TRP A 260   N  LEU A 220           
SHEET    3   D 7 LEU A 280  HIS A 284 -1  O  ARG A 281   N  GLU A 263           
SHEET    4   D 7 PHE A 314  ARG A 317 -1  O  PHE A 314   N  LEU A 280           
SHEET    5   D 7 LEU A 345  HIS A 350 -1  O  PHE A 347   N  ARG A 317           
SHEET    6   D 7 LEU A 388  ARG A 392 -1  O  LEU A 388   N  CYS A 346           
SHEET    7   D 7 VAL A 219  PHE A 223 -1  N  PHE A 223   O  PHE A 389           
SHEET    1   E 4 CYS A 230  THR A 232  0                                        
SHEET    2   E 4 TYR A 246  GLU A 248 -1  O  TYR A 246   N  THR A 232           
SHEET    3   E 4 LYS A 373  HIS A 379 -1  O  LYS A 374   N  TYR A 247           
SHEET    4   E 4 TRP A 356  TYR A 359 -1  N  TRP A 356   O  HIS A 379           
SHEET    1   F 2 TYR A 290  LEU A 293  0                                        
SHEET    2   F 2 LEU A 299  VAL A 302 -1  O  VAL A 302   N  TYR A 290           
SITE     1 AC1  3 ASN A 203  ILE A 267  SER A 268                               
CRYST1  170.381  170.381  302.113  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      0.005869  0.003389  0.000000        0.00000                         
SCALE2      0.000000  0.006777  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003310        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system