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Database: PDB
Entry: 4ESU
LinkDB: 4ESU
Original site: 4ESU 
HEADER    METAL TRANSPORT                         23-APR-12   4ESU              
TITLE     CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 MUTANT S2776M        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RYANODINE RECEPTOR 1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RYR-1, RYR1, SKELETAL MUSCLE CALCIUM RELEASE CHANNEL,       
COMPND   5 SKELETAL MUSCLE RYANODINE RECEPTOR, SKELETAL MUSCLE-TYPE RYANODINE   
COMPND   6 RECEPTOR, TYPE 1 RYANODINE RECEPTOR;                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLACI;                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28HMT                                  
KEYWDS    RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL, PHOSPHORYLATION, MUSCLE,  
KEYWDS   2 SKELETAL, METAL TRANSPORT                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.YUCHI,K.LAU,F.VAN PETEGEM                                           
REVDAT   3   17-OCT-12 4ESU    1       JRNL                                     
REVDAT   2   20-JUN-12 4ESU    1       REMARK                                   
REVDAT   1   13-JUN-12 4ESU    0                                                
JRNL        AUTH   Z.YUCHI,K.LAU,F.VAN PETEGEM                                  
JRNL        TITL   DISEASE MUTATIONS IN THE RYANODINE RECEPTOR CENTRAL REGION:  
JRNL        TITL 2 CRYSTAL STRUCTURES OF A PHOSPHORYLATION HOT SPOT DOMAIN.     
JRNL        REF    STRUCTURE                     V.  20  1201 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22705209                                                     
JRNL        DOI    10.1016/J.STR.2012.04.015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27144                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1361                            
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) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1586                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1498                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.41000                                             
REMARK   3    B22 (A**2) : 1.21000                                              
REMARK   3    B33 (A**2) : 0.20000                                              
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): 0.098         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.098         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.888         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1645 ; 0.013 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2240 ; 1.097 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   204 ; 5.418 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;39.249 ;24.706       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   290 ;13.531 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;15.608 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   236 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1266 ; 0.008 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4ESU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072025.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : SHUTTERLESS DATA COLLECTION;       
REMARK 200                                   FINE PHI SLICING EXPERIMENTS       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27184                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.090                              
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: 4ERT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 25% GLYCEROL, 0.1M HEPES,   
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.09650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.88750            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.09650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.88750            
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 A3198  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     SER A  2731                                                      
REMARK 465     ASN A  2732                                                      
REMARK 465     ALA A  2733                                                      
REMARK 465     GLU A  2832                                                      
REMARK 465     ARG A  2833                                                      
REMARK 465     THR A  2834                                                      
REMARK 465     GLU A  2835                                                      
REMARK 465     LYS A  2836                                                      
REMARK 465     LYS A  2837                                                      
REMARK 465     LYS A  2838                                                      
REMARK 465     THR A  2839                                                      
REMARK 465     ARG A  2840                                                      
REMARK 465     LYS A  2841                                                      
REMARK 465     ILE A  2842                                                      
REMARK 465     SER A  2843                                                      
REMARK 465     GLN A  2844                                                      
REMARK 465     THR A  2845                                                      
REMARK 465     ALA A  2846                                                      
REMARK 465     GLN A  2847                                                      
REMARK 465     THR A  2848                                                      
REMARK 465     TYR A  2849                                                      
REMARK 465     ASP A  2850                                                      
REMARK 465     PRO A  2851                                                      
REMARK 465     ARG A  2852                                                      
REMARK 465     GLU A  2853                                                      
REMARK 465     GLY A  2854                                                      
REMARK 465     GLY A  2940                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A2765    CG   CD   CE   NZ                                   
REMARK 470     GLU A2779    CG   CD   OE1  OE2                                  
REMARK 470     ASN A2780    CG   OD1  ND2                                       
REMARK 470     LYS A2795    CG   CD   CE   NZ                                   
REMARK 470     LYS A2800    CG   CD   CE   NZ                                   
REMARK 470     GLU A2830    CG   CD   OE1  OE2                                  
REMARK 470     GLU A2831    CG   CD   OE1  OE2                                  
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A3240        DISTANCE =  5.22 ANGSTROMS                       
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 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3005                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ERT   RELATED DB: PDB                                   
REMARK 900 RYR1 2734-2940                                                       
REMARK 900 RELATED ID: 4ERV   RELATED DB: PDB                                   
REMARK 900 RYR3 2597-2800                                                       
REMARK 900 RELATED ID: 4ETT   RELATED DB: PDB                                   
REMARK 900 RYR1 E2764K                                                          
REMARK 900 RELATED ID: 4ETU   RELATED DB: PDB                                   
REMARK 900 RYR1 R2939S                                                          
REMARK 900 RELATED ID: 4ETV   RELATED DB: PDB                                   
REMARK 900 RYR2 K2879A                                                          
DBREF  4ESU A 2734  2940  UNP    P11716   RYR1_RABIT    2734   2940             
SEQADV 4ESU SER A 2731  UNP  P11716              EXPRESSION TAG                 
SEQADV 4ESU ASN A 2732  UNP  P11716              EXPRESSION TAG                 
SEQADV 4ESU ALA A 2733  UNP  P11716              EXPRESSION TAG                 
SEQADV 4ESU MET A 2776  UNP  P11716    SER  2776 ENGINEERED MUTATION            
SEQRES   1 A  210  SER ASN ALA ASN PHE ASP PRO ARG PRO VAL GLU THR LEU          
SEQRES   2 A  210  ASN VAL ILE ILE PRO GLU LYS LEU ASP SER PHE ILE ASN          
SEQRES   3 A  210  LYS PHE ALA GLU TYR THR HIS GLU LYS TRP ALA PHE ASP          
SEQRES   4 A  210  LYS ILE GLN ASN ASN TRP MET TYR GLY GLU ASN VAL ASP          
SEQRES   5 A  210  GLU GLU LEU LYS THR HIS PRO MET LEU ARG PRO TYR LYS          
SEQRES   6 A  210  THR PHE SER GLU LYS ASP LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 A  210  ILE LYS GLU SER LEU LYS ALA MET ILE ALA TRP GLU TRP          
SEQRES   8 A  210  THR ILE GLU LYS ALA ARG GLU GLY GLU GLU GLU ARG THR          
SEQRES   9 A  210  GLU LYS LYS LYS THR ARG LYS ILE SER GLN THR ALA GLN          
SEQRES  10 A  210  THR TYR ASP PRO ARG GLU GLY TYR ASN PRO GLN PRO PRO          
SEQRES  11 A  210  ASP LEU SER GLY VAL THR LEU SER ARG GLU LEU GLN ALA          
SEQRES  12 A  210  MET ALA GLU GLN LEU ALA GLU ASN TYR HIS ASN THR TRP          
SEQRES  13 A  210  GLY ARG LYS LYS LYS GLN GLU LEU GLU ALA LYS GLY GLY          
SEQRES  14 A  210  GLY THR HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 A  210  ALA LYS GLU LYS ALA ARG ASP ARG GLU LYS ALA GLN GLU          
SEQRES  16 A  210  LEU LEU LYS PHE LEU GLN MET ASN GLY TYR ALA VAL THR          
SEQRES  17 A  210  ARG GLY                                                      
HET    GOL  A3001       6                                                       
HET    GOL  A3002       6                                                       
HET    GOL  A3003       6                                                       
HET    GOL  A3004       6                                                       
HET    GOL  A3005       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    5(C3 H8 O3)                                                  
FORMUL   7  HOH   *144(H2 O)                                                    
HELIX    1   1 PRO A 2748  LYS A 2750  5                                   3    
HELIX    2   2 LEU A 2751  ASN A 2773  1                                  23    
HELIX    3   3 PRO A 2793  PHE A 2797  5                                   5    
HELIX    4   4 SER A 2798  TRP A 2819  1                                  22    
HELIX    5   5 SER A 2868  GLY A 2898  1                                  31    
HELIX    6   6 PRO A 2907  LEU A 2911  5                                   5    
HELIX    7   7 THR A 2912  ASN A 2933  1                                  22    
SHEET    1   A 2 MET A2776  TYR A2777  0                                        
SHEET    2   A 2 THR A2787  HIS A2788  1  O  HIS A2788   N  MET A2776           
SHEET    1   B 2 THR A2822  LYS A2825  0                                        
SHEET    2   B 2 TYR A2935  THR A2938 -1  O  ALA A2936   N  GLU A2824           
SITE     1 AC1 10 ASP A2736  ARG A2738  LYS A2825  ALA A2826                    
SITE     2 AC1 10 ARG A2827  GLU A2828  ASN A2884  HOH A3104                    
SITE     3 AC1 10 HOH A3155  HOH A3171                                          
SITE     1 AC2  5 PRO A2748  THR A2822  ILE A2823  HOH A3172                    
SITE     2 AC2  5 HOH A3241                                                     
SITE     1 AC3  8 LEU A2785  HIS A2883  LEU A2904  GLU A2915                    
SITE     2 AC3  8 ARG A2918  ASP A2919  HOH A3114  HOH A3193                    
SITE     1 AC4  9 ASP A2736  ARG A2738  ILE A2747  TRP A2807                    
SITE     2 AC4  9 LYS A2810  LYS A2814  ARG A2827  HOH A3188                    
SITE     3 AC4  9 HOH A3213                                                     
SITE     1 AC5  8 SER A2753  ASN A2756  LYS A2757  TRP A2819                    
SITE     2 AC5  8 TRP A2821  GLN A2877  ARG A2939  HOH A3217                    
CRYST1   32.154   56.193  113.775  90.00  90.00  90.00 P 2 21 21     4          
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      0.031100  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017796  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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