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Database: PDB
Entry: 6MM5
LinkDB: 6MM5
Original site: 6MM5 
HEADER    TRANSFERASE/PROTEIN BINDING             29-SEP-18   6MM5              
TITLE     CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH  
TITLE    2 RYR2 PEPTIDE (2799-2810)                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
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: C;                                                            
COMPND  11 FRAGMENT: RESIDUES 2799-2810;                                        
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                                                      
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 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090                                                
KEYWDS    KINASE, COMPLEX, ION CHANNEL, ENZYME, PROTEIN BINDING, TRANSFERASE-   
KEYWDS   2 PROTEIN BINDING COMPLEX                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN PETEGEM,O.HAJI-GHASSEMI                                         
REVDAT   2   08-JAN-20 6MM5    1       REMARK                                   
REVDAT   1   08-MAY-19 6MM5    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.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 28701                          
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) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1484                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2053                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2872                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.15000                                              
REMARK   3    B22 (A**2) : -2.48000                                             
REMARK   3    B33 (A**2) : -0.66000                                             
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): 0.158         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.149         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.575         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3008 ; 0.008 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  2763 ; 0.003 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4073 ; 1.428 ; 1.652       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6407 ; 1.415 ; 1.581       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   354 ; 6.499 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;34.815 ;22.349       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   525 ;15.413 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;22.153 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   378 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3320 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   673 ; 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 6MM5 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_1000237161.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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) : 0.97946                            
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   : 30237                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66100                            
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: 3O7L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRIMETHYLAMINE N-OXIDE, 0.1 M       
REMARK 280  TRIS-HCL, 20% (W/V) PEG MONOMETHYL ETHER 2K 25% (V/V) ETHYLENE      
REMARK 280  GLYCOL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K     
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       27.43050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.28050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.44050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.28050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.43050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.44050            
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 APPLY THE FOLLOWING TO CHAINS: E, C                                  
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 E    12                                                      
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 E 254    CG   CD   CE   NZ                                   
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
REMARK 470     LYS E 345    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG E 165       -0.72     72.11                                   
REMARK 500    ASP E 166       54.01   -141.23                                   
REMARK 500    ASP E 184       91.05     76.02                                   
REMARK 500    LEU E 273       47.42    -86.56                                   
REMARK 500    LYS E 319       55.24    -98.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 171   OD1                                                    
REMARK 620 2 ASP E 184   OD2  86.2                                              
REMARK 620 3 ANP E 402   O2B 173.1  87.0                                        
REMARK 620 4 ANP E 402   O2G  91.5 175.2  95.4                                  
REMARK 620 5 ANP E 402   O2A  89.5  95.8  90.1  88.4                            
REMARK 620 6 HOH E 519   O    88.1  83.9  92.3  91.8 177.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 2901                
DBREF  6MM5 E   15   350  UNP    P05132   KAPCA_MOUSE     16    351             
DBREF  6MM5 C 2799  2810  UNP    E9Q401   RYR2_MOUSE    2799   2810             
SEQADV 6MM5 SER E   12  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM5 ASN E   13  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM5 ALA E   14  UNP  P05132              EXPRESSION TAG                 
SEQRES   1 E  339  SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU          
SEQRES   2 E  339  ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR          
SEQRES   3 E  339  ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY          
SEQRES   4 E  339  THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS          
SEQRES   5 E  339  GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS          
SEQRES   6 E  339  GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU          
SEQRES   7 E  339  ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE          
SEQRES   8 E  339  LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN          
SEQRES   9 E  339  LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET          
SEQRES  10 E  339  PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO          
SEQRES  11 E  339  HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE          
SEQRES  12 E  339  GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU          
SEQRES  13 E  339  LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE          
SEQRES  14 E  339  GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY          
SEQRES  15 E  339  ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA          
SEQRES  16 E  339  PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL          
SEQRES  17 E  339  ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA          
SEQRES  18 E  339  ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN          
SEQRES  19 E  339  ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO          
SEQRES  20 E  339  SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN          
SEQRES  21 E  339  LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU          
SEQRES  22 E  339  LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE          
SEQRES  23 E  339  ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL          
SEQRES  24 E  339  GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP          
SEQRES  25 E  339  THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG          
SEQRES  26 E  339  VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU          
SEQRES  27 E  339  PHE                                                          
SEQRES   1 C   12  LEU TYR ASN ARG THR ARG ARG ILE SER GLN THR SER              
MODRES 6MM5 TPO E  197  THR  MODIFIED RESIDUE                                   
MODRES 6MM5 SEP E  338  SER  MODIFIED RESIDUE                                   
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET     MG  E 401       1                                                       
HET    ANP  E 402      31                                                       
HET    EDO  C2901       4                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
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   MG    MG 2+                                                        
FORMUL   4  ANP    C10 H17 N6 O12 P3                                            
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6  HOH   *214(H2 O)                                                    
HELIX    1 AA1 ASN E   13  THR E   32  1                                  20    
HELIX    2 AA2 GLN E   39  ASP E   41  5                                   3    
HELIX    3 AA3 LYS E   76  LEU E   82  1                                   7    
HELIX    4 AA4 GLN E   84  VAL E   98  1                                  15    
HELIX    5 AA5 GLU E  127  GLY E  136  1                                  10    
HELIX    6 AA6 SER E  139  LEU E  160  1                                  22    
HELIX    7 AA7 LYS E  168  GLU E  170  5                                   3    
HELIX    8 AA8 THR E  201  LEU E  205  5                                   5    
HELIX    9 AA9 ALA E  206  LEU E  211  1                                   6    
HELIX   10 AB1 LYS E  217  GLY E  234  1                                  18    
HELIX   11 AB2 GLN E  242  GLY E  253  1                                  12    
HELIX   12 AB3 SER E  262  LEU E  273  1                                  12    
HELIX   13 AB4 VAL E  288  ASN E  293  1                                   6    
HELIX   14 AB5 HIS E  294  ALA E  298  5                                   5    
HELIX   15 AB6 ASP E  301  GLN E  307  1                                   7    
SHEET    1 AA1 5 PHE E  43  GLY E  52  0                                        
SHEET    2 AA1 5 GLY E  55  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3 AA1 5 HIS E  68  ASP E  75 -1  O  ILE E  73   N  ARG E  56           
SHEET    4 AA1 5 ASN E 115  GLU E 121 -1  O  MET E 120   N  ALA E  70           
SHEET    5 AA1 5 LEU E 106  LYS E 111 -1  N  GLU E 107   O  VAL E 119           
SHEET    1 AA2 2 LEU E 162  ILE E 163  0                                        
SHEET    2 AA2 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1 AA3 2 LEU E 172  ILE E 174  0                                        
SHEET    2 AA3 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
SHEET    1 AA4 2 CYS E 199  GLY E 200  0                                        
SHEET    2 AA4 2 GLN C2808  THR C2809 -1  O  GLN C2808   N  GLY E 200           
LINK         OD1 ASN E 171                MG    MG E 401     1555   1555  2.16  
LINK         OD2 ASP E 184                MG    MG E 401     1555   1555  2.14  
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.34  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.34  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.33  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.34  
LINK        MG    MG E 401                 O2BBANP E 402     1555   1555  2.06  
LINK        MG    MG E 401                 O2GBANP E 402     1555   1555  1.97  
LINK        MG    MG E 401                 O2ABANP E 402     1555   1555  2.07  
LINK        MG    MG E 401                 O   HOH E 519     1555   1555  2.19  
SITE     1 AC1  4 ASN E 171  ASP E 184  ANP E 402  HOH E 519                    
SITE     1 AC2 29 ARG C2804  LEU E  49  THR E  51  GLY E  52                    
SITE     2 AC2 29 VAL E  57  ALA E  70  LYS E  72  VAL E 104                    
SITE     3 AC2 29 MET E 120  GLU E 121  TYR E 122  VAL E 123                    
SITE     4 AC2 29 GLU E 127  LYS E 168  GLU E 170  ASN E 171                    
SITE     5 AC2 29 LEU E 173  THR E 183  ASP E 184  PHE E 327                    
SITE     6 AC2 29  MG E 401  HOH E 507  HOH E 519  HOH E 522                    
SITE     7 AC2 29 HOH E 552  HOH E 565  HOH E 583  HOH E 619                    
SITE     8 AC2 29 HOH E 626                                                     
SITE     1 AC3  5 GLN C2808  SER C2810  HOH C3002  GLY E 200                    
SITE     2 AC3  5 PRO E 202                                                     
CRYST1   54.861   74.881   98.561  90.00  90.00  90.00 P 21 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      0.018228  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013355  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010146        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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