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Database: PDB
Entry: 6MM8
LinkDB: 6MM8
Original site: 6MM8 
HEADER    PROTEIN BINDING                         29-SEP-18   6MM8              
TITLE     CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH  
TITLE    2 RYR2 K2879A, S2813D PHOSPHOMIMETIC (2699-2904) CRYSTAL FORM 2        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: C;                                                            
COMPND   4 FRAGMENT: RESIDUES 16-351;                                           
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RYANODINE RECEPTOR 2;                                      
COMPND  10 CHAIN: D;                                                            
COMPND  11 FRAGMENT: RESIDUES 2699-2904;                                        
COMPND  12 SYNONYM: RYR2,CARDIAC MUSCLE RYANODINE RECEPTOR,CARDIAC MUSCLE       
COMPND  13 RYANODINE RECEPTOR-CALCIUM RELEASE CHANNEL,TYPE 2 RYANODINE RECEPTOR;
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 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: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: RYR2;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, COMPLEX, ION CHANNEL, ENZYME, PROTEIN BINDING                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN PETEGEM,O.HAJI-GHASSEMI                                         
REVDAT   2   08-JAN-20 6MM8    1       REMARK                                   
REVDAT   1   08-MAY-19 6MM8    0                                                
JRNL        AUTH   O.HAJI-GHASSEMI,Z.YUCHI,F.VAN PETEGEM                        
JRNL        TITL   CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH RYR2 PEPTIDE 
JRNL        TITL 2 (2799-2810)                                                  
JRNL        REF    MOL.CELL                                   2019              
JRNL        REFN                   ISSN 1097-2765                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0232                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 52992                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2798                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1957                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4372                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 503                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.08000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.23000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.137         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.132         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.189         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
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):  4642 ; 0.010 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4304 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6279 ; 1.467 ; 1.654       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10005 ; 1.402 ; 1.581       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   549 ; 6.100 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   246 ;34.366 ;22.398       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   838 ;14.936 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;20.017 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   587 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5072 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   995 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6MM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237205.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58151                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6MM7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M HEPES PH 7.5, 15% (W/V) PEG       
REMARK 280  20K, AND 25% (V/V) ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
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        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       89.82150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.93000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       89.82150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.93000            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     LYS C   319                                                      
REMARK 465     GLY C   320                                                      
REMARK 465     PRO C   321                                                      
REMARK 465     GLY C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     THR C   324                                                      
REMARK 465     SER C   325                                                      
REMARK 465     ASN C   326                                                      
REMARK 465     PHE C   327                                                      
REMARK 465     ASP C   328                                                      
REMARK 465     ASP C   329                                                      
REMARK 465     SER D  2696                                                      
REMARK 465     ASN D  2697                                                      
REMARK 465     ALA D  2698                                                      
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 C  16    CG   CD   CE   NZ                                   
REMARK 470     GLU C  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 317    CG   CD   CE   NZ                                   
REMARK 470     PHE C 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER D2750    OG                                                  
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    ILE C  46      -62.77    -91.99                                   
REMARK 500    ASP C 166       33.18   -148.69                                   
REMARK 500    LYS C 168      154.61    179.64                                   
REMARK 500    SER D2750        3.74     81.67                                   
REMARK 500    LYS D2751       66.90     60.82                                   
REMARK 500    ARG D2792     -159.07   -145.01                                   
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 PEG C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY D 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 3003                 
DBREF  6MM8 C   15   350  UNP    P05132   KAPCA_MOUSE     16    351             
DBREF  6MM8 D 2699  2904  UNP    E9Q401   RYR2_MOUSE    2699   2904             
SEQADV 6MM8 SER C   12  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM8 ASN C   13  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM8 ALA C   14  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM8 SER D 2696  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM8 ASN D 2697  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM8 ALA D 2698  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM8 ASP D 2813  UNP  E9Q401    SER  2813 ENGINEERED MUTATION            
SEQADV 6MM8 ALA D 2879  UNP  E9Q401    LYS  2879 ENGINEERED MUTATION            
SEQRES   1 C  339  SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU          
SEQRES   2 C  339  ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR          
SEQRES   3 C  339  ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY          
SEQRES   4 C  339  THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS          
SEQRES   5 C  339  GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS          
SEQRES   6 C  339  GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU          
SEQRES   7 C  339  ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE          
SEQRES   8 C  339  LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN          
SEQRES   9 C  339  LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET          
SEQRES  10 C  339  PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO          
SEQRES  11 C  339  HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE          
SEQRES  12 C  339  GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU          
SEQRES  13 C  339  LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE          
SEQRES  14 C  339  GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY          
SEQRES  15 C  339  ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA          
SEQRES  16 C  339  PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL          
SEQRES  17 C  339  ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA          
SEQRES  18 C  339  ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN          
SEQRES  19 C  339  ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO          
SEQRES  20 C  339  SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN          
SEQRES  21 C  339  LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU          
SEQRES  22 C  339  LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE          
SEQRES  23 C  339  ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL          
SEQRES  24 C  339  GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP          
SEQRES  25 C  339  THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG          
SEQRES  26 C  339  VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU          
SEQRES  27 C  339  PHE                                                          
SEQRES   1 D  209  SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER          
SEQRES   2 D  209  ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN          
SEQRES   3 D  209  LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MET ASP          
SEQRES   4 D  209  LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER          
SEQRES   5 D  209  ASP SER SER LYS ILE GLN PRO LEU MET LYS PRO TYR LYS          
SEQRES   6 D  209  LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 D  209  ILE LYS GLU SER LEU LYS THR MET LEU ALA TRP GLY TRP          
SEQRES   8 D  209  ARG ILE GLU ARG THR ARG GLU GLY ASP SER MET ALA LEU          
SEQRES   9 D  209  TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL          
SEQRES  10 D  209  ASP ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE          
SEQRES  11 D  209  ASP MET SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA          
SEQRES  12 D  209  MET ALA GLU MET MET ALA GLU ASN TYR HIS ASN ILE TRP          
SEQRES  13 D  209  ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY          
SEQRES  14 D  209  GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 D  209  ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP          
SEQRES  16 D  209  ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER          
SEQRES  17 D  209  ARG                                                          
MODRES 6MM8 TPO C  197  THR  MODIFIED RESIDUE                                   
MODRES 6MM8 SEP C  338  SER  MODIFIED RESIDUE                                   
HET    TPO  C 197      11                                                       
HET    SEP  C 338      10                                                       
HET    PEG  C 401       7                                                       
HET    ACY  C 402       4                                                       
HET    ANP  C 403      62                                                       
HET    EDO  C 404       4                                                       
HET    EDO  C 405       4                                                       
HET    EDO  C 406       4                                                       
HET    EDO  C 407       4                                                       
HET    ACY  D3001       4                                                       
HET    EDO  D3002       4                                                       
HET     CL  D3003       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     ACY ACETIC ACID                                                      
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  PEG    C4 H10 O3                                                    
FORMUL   4  ACY    2(C2 H4 O2)                                                  
FORMUL   5  ANP    C10 H17 N6 O12 P3                                            
FORMUL   6  EDO    5(C2 H6 O2)                                                  
FORMUL  12   CL    CL 1-                                                        
FORMUL  13  HOH   *503(H2 O)                                                    
HELIX    1 AA1 ALA C   14  THR C   32  1                                  19    
HELIX    2 AA2 GLN C   39  ASP C   41  5                                   3    
HELIX    3 AA3 LYS C   76  LEU C   82  1                                   7    
HELIX    4 AA4 GLN C   84  GLN C   96  1                                  13    
HELIX    5 AA5 MET C  128  GLY C  136  1                                   9    
HELIX    6 AA6 SER C  139  LEU C  160  1                                  22    
HELIX    7 AA7 LYS C  168  GLU C  170  5                                   3    
HELIX    8 AA8 THR C  201  LEU C  205  5                                   5    
HELIX    9 AA9 ALA C  206  LEU C  211  1                                   6    
HELIX   10 AB1 LYS C  217  GLY C  234  1                                  18    
HELIX   11 AB2 GLN C  242  GLY C  253  1                                  12    
HELIX   12 AB3 SER C  262  LEU C  273  1                                  12    
HELIX   13 AB4 ASP C  276  ARG C  280  5                                   5    
HELIX   14 AB5 VAL C  288  ASN C  293  1                                   6    
HELIX   15 AB6 HIS C  294  ALA C  298  5                                   5    
HELIX   16 AB7 ASP C  301  GLN C  307  1                                   7    
HELIX   17 AB8 PRO D 2713  LYS D 2715  5                                   3    
HELIX   18 AB9 LEU D 2716  ASN D 2738  1                                  23    
HELIX   19 AC1 PRO D 2758  LEU D 2762  5                                   5    
HELIX   20 AC2 SER D 2763  TRP D 2784  1                                  22    
HELIX   21 AC3 ASP D 2795  TYR D 2800  1                                   6    
HELIX   22 AC4 SER D 2810  ALA D 2817  1                                   8    
HELIX   23 AC5 ASP D 2826  VAL D 2830  5                                   5    
HELIX   24 AC6 SER D 2833  GLY D 2863  1                                  31    
HELIX   25 AC7 PRO D 2872  LEU D 2876  5                                   5    
HELIX   26 AC8 THR D 2877  SER D 2898  1                                  22    
SHEET    1 AA1 5 PHE C  43  THR C  51  0                                        
SHEET    2 AA1 5 GLY C  55  HIS C  62 -1  O  LEU C  59   N  LYS C  47           
SHEET    3 AA1 5 HIS C  68  ASP C  75 -1  O  MET C  71   N  MET C  58           
SHEET    4 AA1 5 ASN C 115  GLU C 121 -1  O  LEU C 116   N  LEU C  74           
SHEET    5 AA1 5 LEU C 106  LYS C 111 -1  N  PHE C 110   O  TYR C 117           
SHEET    1 AA2 3 GLY C 126  GLU C 127  0                                        
SHEET    2 AA2 3 LEU C 172  ILE C 174 -1  O  ILE C 174   N  GLY C 126           
SHEET    3 AA2 3 ILE C 180  VAL C 182 -1  O  GLN C 181   N  LEU C 173           
SHEET    1 AA3 2 LEU C 162  ILE C 163  0                                        
SHEET    2 AA3 2 LYS C 189  ARG C 190 -1  O  LYS C 189   N  ILE C 163           
SHEET    1 AA4 2 ARG D2787  ARG D2790  0                                        
SHEET    2 AA4 2 TYR D2900  SER D2903 -1  O  VAL D2901   N  GLU D2789           
LINK         C   TRP C 196                 N   TPO C 197     1555   1555  1.34  
LINK         C   TPO C 197                 N   LEU C 198     1555   1555  1.33  
LINK         C   VAL C 337                 N   SEP C 338     1555   1555  1.33  
LINK         C   SEP C 338                 N   ILE C 339     1555   1555  1.35  
SITE     1 AC1  9 ASN C  99  PHE C 100  PRO C 101  ARG C 308                    
SITE     2 AC1  9 HOH C 503  HOH C 645  SER D2861  LYS D2862                    
SITE     3 AC1  9 HOH D3120                                                     
SITE     1 AC2  7 ILE C 135  ARG C 137  PHE C 138  SER C 139                    
SITE     2 AC2  7 HIS C 142  EDO C 404  TRP D2784                               
SITE     1 AC3 13 GLY C  52  SER C  53  VAL C  57  ALA C  70                    
SITE     2 AC3 13 LYS C  72  GLU C 121  VAL C 123  GLU C 127                    
SITE     3 AC3 13 HOH C 518  HOH C 535  HOH C 637  HOH C 727                    
SITE     4 AC3 13 ARG D2804                                                     
SITE     1 AC4  6 HIS C 131  HIS C 142  TYR C 146  PHE C 314                    
SITE     2 AC4  6 ACY C 402  HOH C 507                                          
SITE     1 AC5  6 LYS C  72  GLU C  91  LEU C  95  VAL C 104                    
SITE     2 AC5  6 THR C 183  HOH C 614                                          
SITE     1 AC6  4 ASN C  36  ALA C  38  GLN C  42  HOH C 597                    
SITE     1 AC7  4 ALA C 298  THR C 299  THR C 300  HOH C 608                    
SITE     1 AC8  5 THR D2711  ILE D2712  LYS D2775  LYS D2779                    
SITE     2 AC8  5 HOH D3255                                                     
SITE     1 AC9  6 SER D2727  PRO D2773  ILE D2774  HOH D3114                    
SITE     2 AC9  6 HOH D3143  HOH D3160                                          
SITE     1 AD1  4 GLU C 140  TRP D2786  MET D2842  ARG D2904                    
CRYST1  179.643   67.860   58.529  90.00  92.22  90.00 C 1 2 1       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      0.005567  0.000000  0.000215        0.00000                         
SCALE2      0.000000  0.014736  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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