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Database: PDB
Entry: 4L4I
LinkDB: 4L4I
Original site: 4L4I 
HEADER    METAL TRANSPORT                         07-JUN-13   4L4I              
TITLE     CRYSTAL STRUCTURE OF MOUSE RYANODINE RECEPTOR ISOFORM 2 (RYR2) 1-547  
TITLE    2 DISEASE MUTANT R420Q                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RYANODINE RECEPTOR 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAINS (UNP RESIDUES 1-547);                   
COMPND   5 SYNONYM: RYR-2, RYR2, CARDIAC MUSCLE RYANODINE RECEPTOR, CARDIAC     
COMPND   6 MUSCLE RYANODINE RECEPTOR-CALCIUM RELEASE CHANNEL, TYPE 2 RYANODINE  
COMPND   7 RECEPTOR, CARDIAC CA2+ RELEASE CHANNEL;                              
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RYR2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA                                    
KEYWDS    CA2+ RELEASE, ION CHANNEL, ER/SR MEMBRANE, METAL TRANSPORT            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.KIMLICKA,F.VAN PETEGEM                                              
REVDAT   1   24-JUL-13 4L4I    0                                                
JRNL        AUTH   L.KIMLICKA,C.C.TUNG,A.C.CARLSSON,P.A.LOBO,F.VAN PETEGEM      
JRNL        TITL   CRYSTAL STRUCTURE OF RYANODINE RECEPTOR DISEASE MUTANT       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40856                          
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) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2151                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2976                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3510                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 64                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.185         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.268        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3634 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4951 ; 1.430 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   482 ; 6.027 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;35.581 ;23.133       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   542 ;16.908 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.806 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   576 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2750 ; 0.006 ; 0.020       
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):  2360 ; 0.737 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3722 ; 1.404 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1274 ; 2.256 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1222 ; 3.563 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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    11        A   217                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4270 -22.2200  49.2980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2162 T22:   0.5044                                     
REMARK   3      T33:   0.1333 T12:   0.1676                                     
REMARK   3      T13:  -0.0332 T23:   0.0924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7543 L22:   3.1737                                     
REMARK   3      L33:   6.4269 L12:  -2.0260                                     
REMARK   3      L13:  -0.8218 L23:   0.4732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5673 S12:   1.2883 S13:   0.0015                       
REMARK   3      S21:  -0.1649 S22:  -0.4233 S23:  -0.2225                       
REMARK   3      S31:  -0.0742 S32:  -0.5042 S33:  -0.1440                       
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   218        A   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9890 -21.6240  18.4540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3625 T22:   0.6971                                     
REMARK   3      T33:   0.0683 T12:   0.3047                                     
REMARK   3      T13:   0.0445 T23:   0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4721 L22:   3.2536                                     
REMARK   3      L33:   6.2946 L12:  -2.0637                                     
REMARK   3      L13:  -1.0172 L23:   0.7062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0425 S12:  -0.5109 S13:  -0.4405                       
REMARK   3      S21:  -0.3344 S22:   0.0325 S23:   0.0968                       
REMARK   3      S31:   0.6994 S32:   0.7611 S33:   0.0099                       
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   410        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0020  -8.7930  39.5590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2175 T22:   0.3089                                     
REMARK   3      T33:   0.1301 T12:   0.1177                                     
REMARK   3      T13:  -0.0135 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3751 L22:   1.2509                                     
REMARK   3      L33:   5.8541 L12:  -0.1585                                     
REMARK   3      L13:  -1.5113 L23:   0.2051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0353 S12:  -0.0180 S13:   0.0920                       
REMARK   3      S21:   0.0319 S22:   0.0556 S23:  -0.0178                       
REMARK   3      S31:   0.4165 S32:   0.2676 S33:  -0.0909                       
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 4L4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080170.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43007                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 14.300                             
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.88800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: PDB ENTRY 4L4H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.15, 5-10% PEG3350, 1%   
REMARK 280  ETHANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294.0K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.02500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.02500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      124.05000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.02500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.02500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      124.05000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.02500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.02500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      124.05000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.02500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.02500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      124.05000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 746  LIES ON A SPECIAL POSITION.                          
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     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA 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     ARG A    76                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     LEU A    78                                                      
REMARK 465     GLN A    79                                                      
REMARK 465     GLU A    80                                                      
REMARK 465     MET A    81                                                      
REMARK 465     LEU A    82                                                      
REMARK 465     ALA A    83                                                      
REMARK 465     ASN A    84                                                      
REMARK 465     THR A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     GLU A    87                                                      
REMARK 465     LYS A    88                                                      
REMARK 465     SER A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLY A    91                                                      
REMARK 465     GLN A    92                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     VAL A    95                                                      
REMARK 465     GLU A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     TRP A    98                                                      
REMARK 465     LYS A    99                                                      
REMARK 465     PHE A   100                                                      
REMARK 465     MET A   101                                                      
REMARK 465     MET A   102                                                      
REMARK 465     LYS A   103                                                      
REMARK 465     THR A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     GLN A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     ARG A   137                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     THR A   140                                                      
REMARK 465     ASP A   141                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     LEU A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     VAL A   340                                                      
REMARK 465     GLY A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     ALA A   382                                                      
REMARK 465     ARG A   383                                                      
REMARK 465     MET A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     LYS A   439                                                      
REMARK 465     VAL A   440                                                      
REMARK 465     LYS A   441                                                      
REMARK 465     LEU A   442                                                      
REMARK 465     PRO A   443                                                      
REMARK 465     ASN A   544                                                      
REMARK 465     ARG A   545                                                      
REMARK 465     LYS A   546                                                      
REMARK 465     ASN A   547                                                      
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     ILE A  11    CG1  CG2  CD1                                       
REMARK 470     ASP A  17    CG   OD1  OD2                                       
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  28    CG1  CG2  CD1                                       
REMARK 470     HIS A  29    CG   ND1  CD2  CE1  NE2                             
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     GLN A  33    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     SER A  53    OG                                                  
REMARK 470     ASN A  54    CG   OD1  ND2                                       
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     ASN A  57    CG   OD1  ND2                                       
REMARK 470     GLU A  70    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     GLU A 151    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 156    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     GLN A 168    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 174    CG   CD   CE   NZ                                   
REMARK 470     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 196    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 198    CG   OD1  ND2                                       
REMARK 470     SER A 199    OG                                                  
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 240    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 251    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 254    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 312    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     LYS A 325    CG   CD   CE   NZ                                   
REMARK 470     GLU A 336    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 337    CG   CD   CE   NZ                                   
REMARK 470     VAL A 346    CG1  CG2                                            
REMARK 470     THR A 351    OG1  CG2                                            
REMARK 470     SER A 386    OG                                                  
REMARK 470     ILE A 387    CG1  CG2  CD1                                       
REMARK 470     LYS A 390    CG   CD   CE   NZ                                   
REMARK 470     LYS A 438    CG   CD   CE   NZ                                   
REMARK 470     THR A 444    OG1  CG2                                            
REMARK 470     GLN A 457    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 464    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 467    CG   OD1  OD2                                       
REMARK 470     GLU A 468    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 469    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 471    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 472    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 477    CG   OD1  ND2                                       
REMARK 470     ARG A 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 480    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 483    CG   CD   CE   NZ                                   
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    GLU A  40      -68.95   -100.69                                   
REMARK 500    ASN A  57      -20.85   -143.20                                   
REMARK 500    SER A  72      106.42   -164.81                                   
REMARK 500    ILE A 217      -61.11    -98.47                                   
REMARK 500    ILE A 387      -50.92    -26.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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: 4L4H   RELATED DB: PDB                                   
DBREF  4L4I A    1   547  UNP    E9Q401   RYR2_MOUSE       1    547             
SEQADV 4L4I GLN A  420  UNP  E9Q401    ARG   420 ENGINEERED MUTATION            
SEQRES   1 A  547  MET ALA ASP ALA GLY GLU GLY GLU ASP GLU ILE GLN PHE          
SEQRES   2 A  547  LEU ARG THR ASP ASP GLU VAL VAL LEU GLN CYS THR ALA          
SEQRES   3 A  547  THR ILE HIS LYS GLU GLN GLN LYS LEU CYS LEU ALA ALA          
SEQRES   4 A  547  GLU GLY PHE GLY ASN ARG LEU CYS PHE LEU GLU SER THR          
SEQRES   5 A  547  SER ASN SER LYS ASN VAL PRO PRO ASP LEU SER ILE CYS          
SEQRES   6 A  547  THR PHE VAL LEU GLU GLN SER LEU SER VAL ARG ALA LEU          
SEQRES   7 A  547  GLN GLU MET LEU ALA ASN THR VAL GLU LYS SER GLU GLY          
SEQRES   8 A  547  GLN VAL ASP VAL GLU LYS TRP LYS PHE MET MET LYS THR          
SEQRES   9 A  547  ALA GLN GLY GLY GLY HIS ARG THR LEU LEU TYR GLY HIS          
SEQRES  10 A  547  ALA ILE LEU LEU ARG HIS SER TYR SER GLY MET TYR LEU          
SEQRES  11 A  547  CYS CYS LEU SER THR SER ARG SER SER THR ASP LYS LEU          
SEQRES  12 A  547  ALA PHE ASP VAL GLY LEU GLN GLU ASP THR THR GLY GLU          
SEQRES  13 A  547  ALA CYS TRP TRP THR ILE HIS PRO ALA SER LYS GLN ARG          
SEQRES  14 A  547  SER GLU GLY GLU LYS VAL ARG VAL GLY ASP ASP LEU ILE          
SEQRES  15 A  547  LEU VAL SER VAL SER SER GLU ARG TYR LEU HIS LEU SER          
SEQRES  16 A  547  TYR GLY ASN SER SER TRP HIS VAL ASP ALA ALA PHE GLN          
SEQRES  17 A  547  GLN THR LEU TRP SER VAL ALA PRO ILE SER SER GLY SER          
SEQRES  18 A  547  GLU ALA ALA GLN GLY TYR LEU ILE GLY GLY ASP VAL LEU          
SEQRES  19 A  547  ARG LEU LEU HIS GLY HIS MET ASP GLU CYS LEU THR VAL          
SEQRES  20 A  547  PRO SER GLY GLU HIS GLY GLU GLU GLN ARG ARG THR VAL          
SEQRES  21 A  547  HIS TYR GLU GLY GLY ALA VAL SER VAL HIS ALA ARG SER          
SEQRES  22 A  547  LEU TRP ARG LEU GLU THR LEU ARG VAL ALA TRP SER GLY          
SEQRES  23 A  547  SER HIS ILE ARG TRP GLY GLN PRO PHE ARG LEU ARG HIS          
SEQRES  24 A  547  VAL THR THR GLY LYS TYR LEU SER LEU MET GLU ASP LYS          
SEQRES  25 A  547  ASN LEU LEU LEU MET ASP LYS GLU LYS ALA ASP VAL LYS          
SEQRES  26 A  547  SER THR ALA PHE ALA PHE ARG SER SER LYS GLU LYS LEU          
SEQRES  27 A  547  ASP VAL GLY VAL ARG LYS GLU VAL ASP GLY MET GLY THR          
SEQRES  28 A  547  SER GLU ILE LYS TYR GLY ASP SER ILE CYS TYR ILE GLN          
SEQRES  29 A  547  HIS VAL ASP THR GLY LEU TRP LEU THR TYR GLN ALA VAL          
SEQRES  30 A  547  ASP VAL LYS SER ALA ARG MET GLY SER ILE GLN ARG LYS          
SEQRES  31 A  547  ALA ILE MET HIS HIS GLU GLY HIS MET ASP ASP GLY LEU          
SEQRES  32 A  547  ASN LEU SER ARG SER GLN HIS GLU GLU SER ARG THR ALA          
SEQRES  33 A  547  ARG VAL ILE GLN SER THR VAL PHE LEU PHE ASN ARG PHE          
SEQRES  34 A  547  ILE ARG GLY LEU ASP ALA LEU SER LYS LYS VAL LYS LEU          
SEQRES  35 A  547  PRO THR ILE ASP LEU PRO ILE GLU SER VAL SER LEU SER          
SEQRES  36 A  547  LEU GLN ASP LEU ILE GLY TYR PHE HIS PRO PRO ASP GLU          
SEQRES  37 A  547  HIS LEU GLU HIS GLU ASP LYS GLN ASN ARG LEU ARG ALA          
SEQRES  38 A  547  LEU LYS ASN ARG GLN ASN LEU PHE GLN GLU GLU GLY MET          
SEQRES  39 A  547  ILE ASN LEU VAL LEU GLU CYS ILE ASP ARG LEU HIS VAL          
SEQRES  40 A  547  TYR SER SER ALA ALA HIS PHE ALA ASP VAL ALA GLY ARG          
SEQRES  41 A  547  GLU ALA GLY GLU SER TRP LYS SER ILE LEU ASN SER LEU          
SEQRES  42 A  547  TYR GLU LEU LEU ALA ALA LEU ILE ARG GLY ASN ARG LYS          
SEQRES  43 A  547  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   *64(H2 O)                                                     
HELIX    1   1 ASP A   61  CYS A   65  5                                   5    
HELIX    2   2 SER A  221  ALA A  223  5                                   3    
HELIX    3   3 GLY A  253  THR A  259  5                                   7    
HELIX    4   4 ALA A  266  SER A  273  5                                   8    
HELIX    5   5 ASP A  318  ALA A  322  5                                   5    
HELIX    6   6 ASP A  323  ALA A  328  1                                   6    
HELIX    7   7 GLN A  409  SER A  437  1                                  29    
HELIX    8   8 PRO A  448  PHE A  463  1                                  16    
HELIX    9   9 GLU A  471  GLU A  492  1                                  22    
HELIX   10  10 GLY A  493  HIS A  506  1                                  14    
HELIX   11  11 SER A  510  GLY A  519  1                                  10    
HELIX   12  12 GLY A  519  ARG A  542  1                                  24    
SHEET    1   A 9 PHE A  48  SER A  51  0                                        
SHEET    2   A 9 GLU A  31  ALA A  38 -1  N  ALA A  38   O  PHE A  48           
SHEET    3   A 9 ASP A  18  ILE A  28 -1  N  CYS A  24   O  LEU A  35           
SHEET    4   A 9 TRP A 212  SER A 219 -1  O  SER A 213   N  GLN A  23           
SHEET    5   A 9 ASP A 180  SER A 185 -1  N  LEU A 181   O  TRP A 212           
SHEET    6   A 9 TRP A 159  PRO A 164 -1  N  THR A 161   O  VAL A 184           
SHEET    7   A 9 ALA A 118  HIS A 123 -1  N  ILE A 119   O  TRP A 160           
SHEET    8   A 9 PHE A  67  LEU A  73 -1  N  VAL A  68   O  ARG A 122           
SHEET    9   A 9 ASP A  18  ILE A  28 -1  N  VAL A  20   O  PHE A  67           
SHEET    1   B 4 TYR A 129  CYS A 132  0                                        
SHEET    2   B 4 PHE A 145  GLN A 150 -1  O  GLY A 148   N  CYS A 131           
SHEET    3   B 4 SER A 200  ALA A 206 -1  O  ALA A 205   N  PHE A 145           
SHEET    4   B 4 TYR A 191  GLY A 197 -1  N  TYR A 191   O  ALA A 206           
SHEET    1   C13 VAL A 233  HIS A 238  0                                        
SHEET    2   C13 TRP A 275  THR A 279 -1  O  TRP A 275   N  LEU A 234           
SHEET    3   C13 PRO A 294  HIS A 299 -1  O  ARG A 298   N  ARG A 276           
SHEET    4   C13 PHE A 329  ARG A 332 -1  O  PHE A 329   N  PHE A 295           
SHEET    5   C13 ILE A 360  HIS A 365 -1  O  TYR A 362   N  ARG A 332           
SHEET    6   C13 VAL A 233  HIS A 238  0                                        
SHEET    7   C13 GLU A 243  THR A 246 -1  O  GLU A 243   N  HIS A 238           
SHEET    8   C13 HIS A 261  GLY A 264 -1  O  HIS A 261   N  THR A 246           
SHEET    9   C13 ARG A 389  HIS A 394 -1  O  ARG A 389   N  TYR A 262           
SHEET   10   C13 TRP A 371  TYR A 374 -1  N  THR A 373   O  ILE A 392           
SHEET   11   C13 ILE A 360  HIS A 365 -1  N  ILE A 363   O  LEU A 372           
SHEET   12   C13 LEU A 403  ARG A 407 -1  O  LEU A 403   N  CYS A 361           
SHEET   13   C13 ILE A 360  HIS A 365 -1  N  CYS A 361   O  LEU A 403           
SHEET    1   D 2 TYR A 305  LEU A 308  0                                        
SHEET    2   D 2 LEU A 314  MET A 317 -1  O  MET A 317   N  TYR A 305           
SITE     1 AC1  4 PHE A  42  ARG A 414  ASP A 458  HOH A 761                    
CRYST1   78.050   78.050  248.100  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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