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Database: PDB
Entry: 4ETV
LinkDB: 4ETV
Original site: 4ETV 
HEADER    METAL TRANSPORT                         24-APR-12   4ETV              
TITLE     CRYSTAL STRUCTURE OF MOUSE RYANODINE RECEPTOR 2 (2699-2904)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RYANODINE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RYR-2, RYR2, CARDIAC MUSCLE RYANODINE RECEPTOR, CARDIAC     
COMPND   5 MUSCLE RYANODINE RECEPTOR-CALCIUM RELEASE CHANNEL, TYPE 2 RYANODINE  
COMPND   6 RECEPTOR;                                                            
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: 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 CARDIAC, METAL TRANSPORT                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.YUCHI,K.LAU,F.VAN PETEGEM                                           
REVDAT   2   17-OCT-12 4ETV    1       JRNL                                     
REVDAT   1   13-JUN-12 4ETV    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55490                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2921                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4022                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 212                          
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2628                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 329                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : -0.79000                                             
REMARK   3    B33 (A**2) : 0.50000                                              
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): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.098         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2738 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3710 ; 1.331 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   332 ; 4.629 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;38.779 ;24.524       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   448 ;12.727 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;14.187 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   394 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2063 ; 0.007 ; 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 4ETV 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 RCSB072062.                                      
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                             : 9                                  
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) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   WITH CRYO-COOLED 1ST CRYSTAL       
REMARK 200                                   SAGITTALLY BENT 2ND CRYSTAL        
REMARK 200                                   FOLLOWED BY VERTICALLY FOCUSING    
REMARK 200                                   MIRROR                             
REMARK 200  OPTICS                         : DOUBLE CRYSTAL MONOCHROMATOR,      
REMARK 200                                   MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58410                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.14100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.940                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% PEG3350, 0.1M BICINE, PH 9, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.45000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.03500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.11000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.03500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.45000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.11000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     SER A  2696                                                      
REMARK 465     ASN A  2697                                                      
REMARK 465     ALA A  2698                                                      
REMARK 465     ASN A  2699                                                      
REMARK 465     ARG A  2802                                                      
REMARK 465     THR A  2803                                                      
REMARK 465     ARG A  2804                                                      
REMARK 465     ARG A  2805                                                      
REMARK 465     ILE A  2806                                                      
REMARK 465     SER A  2807                                                      
REMARK 465     GLN A  2808                                                      
REMARK 465     THR A  2809                                                      
REMARK 465     SER A  2810                                                      
REMARK 465     GLN A  2811                                                      
REMARK 465     VAL A  2812                                                      
REMARK 465     SER A  2813                                                      
REMARK 465     ILE A  2814                                                      
REMARK 465     ASP A  2815                                                      
REMARK 465     SER B  2696                                                      
REMARK 465     ASN B  2697                                                      
REMARK 465     ALA B  2698                                                      
REMARK 465     LYS B  2730                                                      
REMARK 465     TRP B  2731                                                      
REMARK 465     SER B  2732                                                      
REMARK 465     MSE B  2733                                                      
REMARK 465     ASP B  2734                                                      
REMARK 465     LYS B  2735                                                      
REMARK 465     LEU B  2736                                                      
REMARK 465     ALA B  2737                                                      
REMARK 465     ASN B  2738                                                      
REMARK 465     GLY B  2739                                                      
REMARK 465     TRP B  2740                                                      
REMARK 465     ILE B  2741                                                      
REMARK 465     TYR B  2742                                                      
REMARK 465     GLY B  2743                                                      
REMARK 465     GLU B  2744                                                      
REMARK 465     ILE B  2745                                                      
REMARK 465     TYR B  2746                                                      
REMARK 465     SER B  2747                                                      
REMARK 465     ASP B  2748                                                      
REMARK 465     SER B  2749                                                      
REMARK 465     SER B  2750                                                      
REMARK 465     LYS B  2751                                                      
REMARK 465     ILE B  2752                                                      
REMARK 465     GLN B  2753                                                      
REMARK 465     PRO B  2754                                                      
REMARK 465     LEU B  2755                                                      
REMARK 465     MSE B  2756                                                      
REMARK 465     LYS B  2757                                                      
REMARK 465     PRO B  2758                                                      
REMARK 465     TYR B  2759                                                      
REMARK 465     LYS B  2760                                                      
REMARK 465     LEU B  2761                                                      
REMARK 465     LEU B  2762                                                      
REMARK 465     GLU B  2793                                                      
REMARK 465     GLY B  2794                                                      
REMARK 465     ASP B  2795                                                      
REMARK 465     SER B  2796                                                      
REMARK 465     MSE B  2797                                                      
REMARK 465     ALA B  2798                                                      
REMARK 465     LEU B  2799                                                      
REMARK 465     TYR B  2800                                                      
REMARK 465     ASN B  2801                                                      
REMARK 465     ARG B  2802                                                      
REMARK 465     THR B  2803                                                      
REMARK 465     ARG B  2804                                                      
REMARK 465     ARG B  2805                                                      
REMARK 465     ILE B  2806                                                      
REMARK 465     SER B  2807                                                      
REMARK 465     GLN B  2808                                                      
REMARK 465     THR B  2809                                                      
REMARK 465     SER B  2810                                                      
REMARK 465     GLN B  2811                                                      
REMARK 465     VAL B  2812                                                      
REMARK 465     SER B  2813                                                      
REMARK 465     ILE B  2814                                                      
REMARK 465     ASP B  2815                                                      
REMARK 465     ALA B  2816                                                      
REMARK 465     ALA B  2817                                                      
REMARK 465     HIS B  2818                                                      
REMARK 465     GLY B  2819                                                      
REMARK 465     TYR B  2820                                                      
REMARK 465     SER B  2821                                                      
REMARK 465     PRO B  2822                                                      
REMARK 465     ARG B  2823                                                      
REMARK 465     ALA B  2824                                                      
REMARK 465     ILE B  2825                                                      
REMARK 465     SER B  2861                                                      
REMARK 465     LYS B  2862                                                      
REMARK 465     GLY B  2863                                                      
REMARK 465     GLY B  2864                                                      
REMARK 465     GLY B  2865                                                      
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     ARG A2823    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A2834    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A2860    CG   CD   OE1  OE2                                  
REMARK 470     ASN A2866    CG   OD1  ND2                                       
REMARK 470     ASP A2874    CG   OD1  OD2                                       
REMARK 470     GLU B2714    CG   CD   OE1  OE2                                  
REMARK 470     LYS B2715    CG   CD   CE   NZ                                   
REMARK 470     GLU B2717    CG   CD   OE1  OE2                                  
REMARK 470     LYS B2722    CG   CD   CE   NZ                                   
REMARK 470     GLU B2766    CG   CD   OE1  OE2                                  
REMARK 470     ARG B2787    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B2792    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B2854    CG   CD   CE   NZ                                   
REMARK 470     GLU B2860    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU B  2845     O    HOH B  3194              1.42            
REMARK 500   OD1  ASN A  2721     NH1  ARG A  2771              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A2818       14.50     59.32                                   
REMARK 500    ASN B2701       75.33   -118.63                                   
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 CL B 3001                 
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: 4ESU   RELATED DB: PDB                                   
REMARK 900 RYR1 S2776M                                                          
REMARK 900 RELATED ID: 4ETU   RELATED DB: PDB                                   
REMARK 900 RYR1 R2939S                                                          
DBREF  4ETV A 2699  2904  UNP    E9Q401   RYR2_MOUSE    2699   2904             
DBREF  4ETV B 2699  2904  UNP    E9Q401   RYR2_MOUSE    2699   2904             
SEQADV 4ETV SER A 2696  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ASN A 2697  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ALA A 2698  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ALA A 2879  UNP  E9Q401    LYS  2879 ENGINEERED MUTATION            
SEQADV 4ETV SER B 2696  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ASN B 2697  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ALA B 2698  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 4ETV ALA B 2879  UNP  E9Q401    LYS  2879 ENGINEERED MUTATION            
SEQRES   1 A  209  SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER          
SEQRES   2 A  209  ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN          
SEQRES   3 A  209  LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MSE ASP          
SEQRES   4 A  209  LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER          
SEQRES   5 A  209  ASP SER SER LYS ILE GLN PRO LEU MSE LYS PRO TYR LYS          
SEQRES   6 A  209  LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 A  209  ILE LYS GLU SER LEU LYS THR MSE LEU ALA TRP GLY TRP          
SEQRES   8 A  209  ARG ILE GLU ARG THR ARG GLU GLY ASP SER MSE ALA LEU          
SEQRES   9 A  209  TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL          
SEQRES  10 A  209  SER ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE          
SEQRES  11 A  209  ASP MSE SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA          
SEQRES  12 A  209  MSE ALA GLU MSE MSE ALA GLU ASN TYR HIS ASN ILE TRP          
SEQRES  13 A  209  ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY          
SEQRES  14 A  209  GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 A  209  ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP          
SEQRES  16 A  209  ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER          
SEQRES  17 A  209  ARG                                                          
SEQRES   1 B  209  SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER          
SEQRES   2 B  209  ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN          
SEQRES   3 B  209  LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MSE ASP          
SEQRES   4 B  209  LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER          
SEQRES   5 B  209  ASP SER SER LYS ILE GLN PRO LEU MSE LYS PRO TYR LYS          
SEQRES   6 B  209  LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 B  209  ILE LYS GLU SER LEU LYS THR MSE LEU ALA TRP GLY TRP          
SEQRES   8 B  209  ARG ILE GLU ARG THR ARG GLU GLY ASP SER MSE ALA LEU          
SEQRES   9 B  209  TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL          
SEQRES  10 B  209  SER ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE          
SEQRES  11 B  209  ASP MSE SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA          
SEQRES  12 B  209  MSE ALA GLU MSE MSE ALA GLU ASN TYR HIS ASN ILE TRP          
SEQRES  13 B  209  ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY          
SEQRES  14 B  209  GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 B  209  ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP          
SEQRES  16 B  209  ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER          
SEQRES  17 B  209  ARG                                                          
MODRES 4ETV MSE A 2733  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2756  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2781  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2797  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2827  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2839  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2842  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE A 2843  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE B 2781  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE B 2827  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE B 2839  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE B 2842  MET  SELENOMETHIONINE                                   
MODRES 4ETV MSE B 2843  MET  SELENOMETHIONINE                                   
HET    MSE  A2733       8                                                       
HET    MSE  A2756       8                                                       
HET    MSE  A2781       8                                                       
HET    MSE  A2797       8                                                       
HET    MSE  A2827       8                                                       
HET    MSE  A2839       8                                                       
HET    MSE  A2842       8                                                       
HET    MSE  A2843       8                                                       
HET    MSE  B2781       8                                                       
HET    MSE  B2827       8                                                       
HET    MSE  B2839       8                                                       
HET    MSE  B2842       8                                                       
HET    MSE  B2843       8                                                       
HET     CL  B3001       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    13(C5 H11 N O2 SE)                                           
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *329(H2 O)                                                    
HELIX    1   1 PRO A 2713  LYS A 2715  5                                   3    
HELIX    2   2 LEU A 2716  ASN A 2738  1                                  23    
HELIX    3   3 PRO A 2758  LEU A 2762  5                                   5    
HELIX    4   4 SER A 2763  TRP A 2784  1                                  22    
HELIX    5   5 ASP A 2795  TYR A 2800  5                                   6    
HELIX    6   6 ALA A 2816  TYR A 2820  5                                   5    
HELIX    7   7 ASP A 2826  VAL A 2830  5                                   5    
HELIX    8   8 SER A 2833  LYS A 2862  1                                  30    
HELIX    9   9 PRO A 2872  LEU A 2876  5                                   5    
HELIX   10  10 THR A 2877  GLY A 2899  1                                  23    
HELIX   11  11 PRO B 2713  LYS B 2715  5                                   3    
HELIX   12  12 LEU B 2716  ASP B 2729  1                                  14    
HELIX   13  13 GLU B 2764  TRP B 2784  1                                  21    
HELIX   14  14 SER B 2833  GLU B 2860  1                                  28    
HELIX   15  15 PRO B 2872  LEU B 2876  5                                   5    
HELIX   16  16 THR B 2877  SER B 2898  1                                  22    
SHEET    1   A 2 ARG A2787  ARG A2790  0                                        
SHEET    2   A 2 TYR A2900  SER A2903 -1  O  VAL A2901   N  GLU A2789           
SHEET    1   B 2 ARG B2787  ARG B2790  0                                        
SHEET    2   B 2 TYR B2900  SER B2903 -1  O  VAL B2901   N  GLU B2789           
LINK         C   SER A2732                 N   MSE A2733     1555   1555  1.34  
LINK         C   MSE A2733                 N   ASP A2734     1555   1555  1.34  
LINK         C   LEU A2755                 N   MSE A2756     1555   1555  1.34  
LINK         C   MSE A2756                 N   LYS A2757     1555   1555  1.33  
LINK         C   THR A2780                 N   MSE A2781     1555   1555  1.34  
LINK         C   MSE A2781                 N   LEU A2782     1555   1555  1.32  
LINK         C   SER A2796                 N   MSE A2797     1555   1555  1.33  
LINK         C   MSE A2797                 N   ALA A2798     1555   1555  1.33  
LINK         C   ASP A2826                 N   MSE A2827     1555   1555  1.32  
LINK         C   MSE A2827                 N   SER A2828     1555   1555  1.35  
LINK         C   ALA A2838                 N   MSE A2839     1555   1555  1.32  
LINK         C   MSE A2839                 N   ALA A2840     1555   1555  1.33  
LINK         C   GLU A2841                 N   MSE A2842     1555   1555  1.34  
LINK         C   MSE A2842                 N   MSE A2843     1555   1555  1.34  
LINK         C   MSE A2843                 N   ALA A2844     1555   1555  1.34  
LINK         C   THR B2780                 N   MSE B2781     1555   1555  1.34  
LINK         C   MSE B2781                 N   LEU B2782     1555   1555  1.32  
LINK         C   ASP B2826                 N   MSE B2827     1555   1555  1.33  
LINK         C   MSE B2827                 N   SER B2828     1555   1555  1.33  
LINK         C   ALA B2838                 N   MSE B2839     1555   1555  1.33  
LINK         C   MSE B2839                 N   ALA B2840     1555   1555  1.33  
LINK         C   GLU B2841                 N   MSE B2842     1555   1555  1.34  
LINK         C   MSE B2842                 N   MSE B2843     1555   1555  1.34  
LINK         C   MSE B2843                 N   ALA B2844     1555   1555  1.34  
SITE     1 AC1  2 TRP A2851  ARG B2834                                          
CRYST1   58.900   88.220   92.070  90.00  90.00  90.00 P 21 21 21    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      0.016978  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010861        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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