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Database: PDB
Entry: 6MM7
LinkDB: 6MM7
Original site: 6MM7 
HEADER    TRANSFERASE/PROTEIN BINDING             29-SEP-18   6MM7              
TITLE     CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH  
TITLE    2 RYR2 K2879A, S2813D PHOSPHOMIMETIC (2699-2904) CRYSTAL FORM 1        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, D;                                                         
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, E;                                                         
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, TRANSFERASE-   
KEYWDS   2 PROTEIN BINDING COMPLEX                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN PETEGEM,O.HAJI-GHASSEMI                                         
REVDAT   2   08-JAN-20 6MM7    1       REMARK                                   
REVDAT   1   08-MAY-19 6MM7    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) : 33.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 105173                         
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5806                            
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) : 7514                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 393                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8654                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 830                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.76000                                             
REMARK   3    B22 (A**2) : 1.93000                                              
REMARK   3    B33 (A**2) : -0.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.157         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9042 ; 0.007 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  8323 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12217 ; 1.376 ; 1.651       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19297 ; 1.294 ; 1.582       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1075 ; 6.167 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   479 ;34.147 ;22.317       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1595 ;15.014 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;20.537 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1146 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9976 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1969 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A   350                          
REMARK   3    RESIDUE RANGE :   A   401        A   405                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.290   19.108   19.803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0637 T22:   0.0279                                     
REMARK   3      T33:   0.0710 T12:   0.0146                                     
REMARK   3      T13:   0.0348 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8432 L22:   0.0186                                     
REMARK   3      L33:   0.7996 L12:   0.1199                                     
REMARK   3      L13:   0.5814 L23:   0.1045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0317 S12:   0.1153 S13:  -0.0072                       
REMARK   3      S21:   0.0076 S22:  -0.0073 S23:   0.0127                       
REMARK   3      S31:  -0.0455 S32:  -0.1013 S33:  -0.0244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  2699        C  2904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   29.757   51.560   29.698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3243 T22:   0.2079                                     
REMARK   3      T33:   0.1100 T12:  -0.0492                                     
REMARK   3      T13:  -0.0354 T23:   0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9755 L22:   1.3582                                     
REMARK   3      L33:   1.2728 L12:   0.9111                                     
REMARK   3      L13:   1.4535 L23:   1.0867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2565 S12:   0.3991 S13:   0.2475                       
REMARK   3      S21:  -0.4937 S22:   0.1329 S23:   0.1486                       
REMARK   3      S31:  -0.3197 S32:   0.0463 S33:   0.1236                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    15        D   350                          
REMARK   3    RESIDUE RANGE :   D   401        D   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.412  -13.801   68.071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0046 T22:   0.0309                                     
REMARK   3      T33:   0.0080 T12:  -0.0102                                     
REMARK   3      T13:   0.0051 T23:  -0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4090 L22:   0.1345                                     
REMARK   3      L33:   0.4721 L12:  -0.0144                                     
REMARK   3      L13:   0.4758 L23:  -0.0503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0144 S12:  -0.1930 S13:   0.0798                       
REMARK   3      S21:  -0.0060 S22:   0.0050 S23:  -0.0190                       
REMARK   3      S31:  -0.0366 S32:   0.0593 S33:  -0.0194                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E  2699        E  2904                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -36.000   18.118   58.455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2791 T22:   0.1386                                     
REMARK   3      T33:   0.1067 T12:   0.0443                                     
REMARK   3      T13:  -0.0082 T23:  -0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8953 L22:   1.6267                                     
REMARK   3      L33:   0.6113 L12:  -0.9531                                     
REMARK   3      L13:   0.8023 L23:  -0.7509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0918 S12:  -0.3217 S13:  -0.0227                       
REMARK   3      S21:   0.3883 S22:   0.1160 S23:  -0.0952                       
REMARK   3      S31:  -0.0373 S32:  -0.0108 S33:  -0.0242                       
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 : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6MM7 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_1000237199.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-18                          
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               : CLSI                               
REMARK 200  BEAMLINE                       : 08B1-1                             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111231                             
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     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
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) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79300                            
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: 6MM6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM FORMATE AND 25% (W/V)    
REMARK 280  PEG 3350; 0.05 M HEPES, AND 25% ETHYLENE GLYCOL, PH 7.5, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ASN A   326                                                      
REMARK 465     SER C  2696                                                      
REMARK 465     ASN C  2697                                                      
REMARK 465     ALA C  2698                                                      
REMARK 465     SER D    12                                                      
REMARK 465     ASN D    13                                                      
REMARK 465     ALA D    14                                                      
REMARK 465     PHE D   318                                                      
REMARK 465     LYS D   319                                                      
REMARK 465     GLY D   320                                                      
REMARK 465     PRO D   321                                                      
REMARK 465     GLY D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     THR D   324                                                      
REMARK 465     SER D   325                                                      
REMARK 465     ASN D   326                                                      
REMARK 465     PHE D   327                                                      
REMARK 465     ASP D   328                                                      
REMARK 465     ASP D   329                                                      
REMARK 465     SER E  2696                                                      
REMARK 465     ASN E  2697                                                      
REMARK 465     ALA E  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 A  16    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     PHE A  18    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A  19    CG   CD1  CD2                                       
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 327    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN C2709    CG   OD1  ND2                                       
REMARK 470     GLU C2714    CG   CD   OE1  OE2                                  
REMARK 470     ILE C2741    CG1  CG2  CD1                                       
REMARK 470     GLU C2744    CG   CD   OE1  OE2                                  
REMARK 470     ILE C2745    CG1  CG2  CD1                                       
REMARK 470     SER C2747    OG                                                  
REMARK 470     SER C2749    OG                                                  
REMARK 470     SER C2750    OG                                                  
REMARK 470     LYS C2760    CG   CD   CE   NZ                                   
REMARK 470     LYS C2765    CG   CD   CE   NZ                                   
REMARK 470     GLU C2789    CG   CD   OE1  OE2                                  
REMARK 470     LEU C2799    CG   CD1  CD2                                       
REMARK 470     LYS D  16    CG   CD   CE   NZ                                   
REMARK 470     GLU D  17    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  31    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 332    CG   CD   OE1  OE2                                  
REMARK 470     LYS E2715    CG   CD   CE   NZ                                   
REMARK 470     LYS E2730    CG   CD   CE   NZ                                   
REMARK 470     LYS E2735    CG   CD   CE   NZ                                   
REMARK 470     GLU E2744    CG   CD   OE1  OE2                                  
REMARK 470     SER E2747    OG                                                  
REMARK 470     SER E2749    OG                                                  
REMARK 470     SER E2750    OG                                                  
REMARK 470     LYS E2760    CG   CD   CE   NZ                                   
REMARK 470     LYS E2765    CG   CD   CE   NZ                                   
REMARK 470     GLU E2793    CG   CD   OE1  OE2                                  
REMARK 470     SER E2796    OG                                                  
REMARK 470     LEU E2799    CG   CD1  CD2                                       
REMARK 470     LYS E2883    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    ASN A  36       61.20     39.95                                   
REMARK 500    ASP A 166       29.46   -144.36                                   
REMARK 500    LEU A 273       46.59    -82.78                                   
REMARK 500    LYS C2751       60.59     66.83                                   
REMARK 500    SER C2796      -53.96    -28.51                                   
REMARK 500    LYS D  16      -74.65    -47.35                                   
REMARK 500    ASP D 166       30.09   -144.07                                   
REMARK 500    LEU D 273       47.24    -81.76                                   
REMARK 500    SER E2749      -70.37    -50.45                                   
REMARK 500    LYS E2751       61.71     67.59                                   
REMARK 500    SER E2796       52.08     34.94                                   
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 FMT A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 3002                
DBREF  6MM7 A   15   350  UNP    P05132   KAPCA_MOUSE     16    351             
DBREF  6MM7 C 2699  2904  UNP    E9Q401   RYR2_MOUSE    2699   2904             
DBREF  6MM7 D   15   350  UNP    P05132   KAPCA_MOUSE     16    351             
DBREF  6MM7 E 2699  2904  UNP    E9Q401   RYR2_MOUSE    2699   2904             
SEQADV 6MM7 SER A   12  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 ASN A   13  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 ALA A   14  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 SER C 2696  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ASN C 2697  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ALA C 2698  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ASP C 2813  UNP  E9Q401    SER  2813 ENGINEERED MUTATION            
SEQADV 6MM7 ALA C 2879  UNP  E9Q401    LYS  2879 ENGINEERED MUTATION            
SEQADV 6MM7 SER D   12  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 ASN D   13  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 ALA D   14  UNP  P05132              EXPRESSION TAG                 
SEQADV 6MM7 SER E 2696  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ASN E 2697  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ALA E 2698  UNP  E9Q401              EXPRESSION TAG                 
SEQADV 6MM7 ASP E 2813  UNP  E9Q401    SER  2813 ENGINEERED MUTATION            
SEQADV 6MM7 ALA E 2879  UNP  E9Q401    LYS  2879 ENGINEERED MUTATION            
SEQRES   1 A  339  SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU          
SEQRES   2 A  339  ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR          
SEQRES   3 A  339  ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY          
SEQRES   4 A  339  THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS          
SEQRES   5 A  339  GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS          
SEQRES   6 A  339  GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU          
SEQRES   7 A  339  ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE          
SEQRES   8 A  339  LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN          
SEQRES   9 A  339  LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET          
SEQRES  10 A  339  PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO          
SEQRES  11 A  339  HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE          
SEQRES  12 A  339  GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU          
SEQRES  13 A  339  LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE          
SEQRES  14 A  339  GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY          
SEQRES  15 A  339  ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA          
SEQRES  16 A  339  PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL          
SEQRES  17 A  339  ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA          
SEQRES  18 A  339  ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN          
SEQRES  19 A  339  ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO          
SEQRES  20 A  339  SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN          
SEQRES  21 A  339  LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU          
SEQRES  22 A  339  LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE          
SEQRES  23 A  339  ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL          
SEQRES  24 A  339  GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP          
SEQRES  25 A  339  THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG          
SEQRES  26 A  339  VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU          
SEQRES  27 A  339  PHE                                                          
SEQRES   1 C  209  SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER          
SEQRES   2 C  209  ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN          
SEQRES   3 C  209  LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MET ASP          
SEQRES   4 C  209  LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER          
SEQRES   5 C  209  ASP SER SER LYS ILE GLN PRO LEU MET LYS PRO TYR LYS          
SEQRES   6 C  209  LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 C  209  ILE LYS GLU SER LEU LYS THR MET LEU ALA TRP GLY TRP          
SEQRES   8 C  209  ARG ILE GLU ARG THR ARG GLU GLY ASP SER MET ALA LEU          
SEQRES   9 C  209  TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL          
SEQRES  10 C  209  ASP ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE          
SEQRES  11 C  209  ASP MET SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA          
SEQRES  12 C  209  MET ALA GLU MET MET ALA GLU ASN TYR HIS ASN ILE TRP          
SEQRES  13 C  209  ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY          
SEQRES  14 C  209  GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 C  209  ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP          
SEQRES  16 C  209  ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER          
SEQRES  17 C  209  ARG                                                          
SEQRES   1 D  339  SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU          
SEQRES   2 D  339  ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR          
SEQRES   3 D  339  ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY          
SEQRES   4 D  339  THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS          
SEQRES   5 D  339  GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS          
SEQRES   6 D  339  GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU          
SEQRES   7 D  339  ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE          
SEQRES   8 D  339  LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN          
SEQRES   9 D  339  LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET          
SEQRES  10 D  339  PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO          
SEQRES  11 D  339  HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE          
SEQRES  12 D  339  GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU          
SEQRES  13 D  339  LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE          
SEQRES  14 D  339  GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY          
SEQRES  15 D  339  ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA          
SEQRES  16 D  339  PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL          
SEQRES  17 D  339  ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA          
SEQRES  18 D  339  ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN          
SEQRES  19 D  339  ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO          
SEQRES  20 D  339  SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN          
SEQRES  21 D  339  LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU          
SEQRES  22 D  339  LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE          
SEQRES  23 D  339  ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL          
SEQRES  24 D  339  GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP          
SEQRES  25 D  339  THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG          
SEQRES  26 D  339  VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU          
SEQRES  27 D  339  PHE                                                          
SEQRES   1 E  209  SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER          
SEQRES   2 E  209  ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN          
SEQRES   3 E  209  LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MET ASP          
SEQRES   4 E  209  LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER          
SEQRES   5 E  209  ASP SER SER LYS ILE GLN PRO LEU MET LYS PRO TYR LYS          
SEQRES   6 E  209  LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO          
SEQRES   7 E  209  ILE LYS GLU SER LEU LYS THR MET LEU ALA TRP GLY TRP          
SEQRES   8 E  209  ARG ILE GLU ARG THR ARG GLU GLY ASP SER MET ALA LEU          
SEQRES   9 E  209  TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL          
SEQRES  10 E  209  ASP ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE          
SEQRES  11 E  209  ASP MET SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA          
SEQRES  12 E  209  MET ALA GLU MET MET ALA GLU ASN TYR HIS ASN ILE TRP          
SEQRES  13 E  209  ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY          
SEQRES  14 E  209  GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR          
SEQRES  15 E  209  ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP          
SEQRES  16 E  209  ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER          
SEQRES  17 E  209  ARG                                                          
MODRES 6MM7 TPO A  197  THR  MODIFIED RESIDUE                                   
MODRES 6MM7 SEP A  338  SER  MODIFIED RESIDUE                                   
MODRES 6MM7 TPO D  197  THR  MODIFIED RESIDUE                                   
MODRES 6MM7 SEP D  338  SER  MODIFIED RESIDUE                                   
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    TPO  D 197      11                                                       
HET    SEP  D 338      10                                                       
HET    FMT  A 401       3                                                       
HET    FMT  A 402       3                                                       
HET    ACY  A 403       4                                                       
HET    FMT  A 404       3                                                       
HET    FMT  A 405       3                                                       
HET    ANP  A 406      31                                                       
HET    EDO  A 407       4                                                       
HET    EDO  C3001       4                                                       
HET    FMT  D 401       3                                                       
HET    FMT  D 402       3                                                       
HET    FMT  D 403       3                                                       
HET    FMT  D 404       3                                                       
HET    ANP  D 405      31                                                       
HET     CL  D 406       1                                                       
HET    EDO  D 407       4                                                       
HET    EDO  D 408       4                                                       
HET    EDO  D 409       4                                                       
HET    EDO  D 410       4                                                       
HET     CL  E3001       1                                                       
HET    EDO  E3002       4                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     FMT FORMIC ACID                                                      
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    2(C4 H10 N O6 P)                                             
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  FMT    8(C H2 O2)                                                   
FORMUL   7  ACY    C2 H4 O2                                                     
FORMUL  10  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL  11  EDO    7(C2 H6 O2)                                                  
FORMUL  18   CL    2(CL 1-)                                                     
FORMUL  25  HOH   *830(H2 O)                                                    
HELIX    1 AA1 LYS A   16  THR A   32  1                                  17    
HELIX    2 AA2 GLN A   39  ASP A   41  5                                   3    
HELIX    3 AA3 LYS A   76  LEU A   82  1                                   7    
HELIX    4 AA4 GLN A   84  GLN A   96  1                                  13    
HELIX    5 AA5 MET A  128  GLY A  136  1                                   9    
HELIX    6 AA6 SER A  139  LEU A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  201  LEU A  205  5                                   5    
HELIX    9 AA9 ALA A  206  SER A  212  1                                   7    
HELIX   10 AB1 LYS A  217  GLY A  234  1                                  18    
HELIX   11 AB2 GLN A  242  GLY A  253  1                                  12    
HELIX   12 AB3 SER A  262  LEU A  273  1                                  12    
HELIX   13 AB4 ASP A  276  ARG A  280  5                                   5    
HELIX   14 AB5 VAL A  288  ASN A  293  1                                   6    
HELIX   15 AB6 HIS A  294  ALA A  298  5                                   5    
HELIX   16 AB7 ASP A  301  GLN A  307  1                                   7    
HELIX   17 AB8 PRO C 2713  LYS C 2715  5                                   3    
HELIX   18 AB9 LEU C 2716  ASN C 2738  1                                  23    
HELIX   19 AC1 PRO C 2758  LEU C 2762  5                                   5    
HELIX   20 AC2 SER C 2763  TRP C 2784  1                                  22    
HELIX   21 AC3 ASP C 2795  TYR C 2800  1                                   6    
HELIX   22 AC4 SER C 2810  ALA C 2817  1                                   8    
HELIX   23 AC5 SER C 2833  GLY C 2863  1                                  31    
HELIX   24 AC6 PRO C 2872  LEU C 2876  5                                   5    
HELIX   25 AC7 THR C 2877  SER C 2898  1                                  22    
HELIX   26 AC8 LYS D   16  THR D   32  1                                  17    
HELIX   27 AC9 GLN D   39  ASP D   41  5                                   3    
HELIX   28 AD1 LYS D   76  LEU D   82  1                                   7    
HELIX   29 AD2 GLN D   84  GLN D   96  1                                  13    
HELIX   30 AD3 MET D  128  GLY D  136  1                                   9    
HELIX   31 AD4 SER D  139  LEU D  160  1                                  22    
HELIX   32 AD5 LYS D  168  GLU D  170  5                                   3    
HELIX   33 AD6 THR D  201  LEU D  205  5                                   5    
HELIX   34 AD7 ALA D  206  SER D  212  1                                   7    
HELIX   35 AD8 LYS D  217  GLY D  234  1                                  18    
HELIX   36 AD9 GLN D  242  GLY D  253  1                                  12    
HELIX   37 AE1 SER D  262  LEU D  273  1                                  12    
HELIX   38 AE2 ASP D  276  ARG D  280  5                                   5    
HELIX   39 AE3 VAL D  288  ASN D  293  1                                   6    
HELIX   40 AE4 HIS D  294  ALA D  298  5                                   5    
HELIX   41 AE5 ASP D  301  GLN D  307  1                                   7    
HELIX   42 AE6 PRO E 2713  LYS E 2715  5                                   3    
HELIX   43 AE7 LEU E 2716  ASN E 2738  1                                  23    
HELIX   44 AE8 PRO E 2758  LEU E 2762  5                                   5    
HELIX   45 AE9 SER E 2763  TRP E 2784  1                                  22    
HELIX   46 AF1 SER E 2796  TYR E 2800  5                                   5    
HELIX   47 AF2 SER E 2810  ALA E 2817  1                                   8    
HELIX   48 AF3 SER E 2833  GLY E 2863  1                                  31    
HELIX   49 AF4 PRO E 2872  LEU E 2876  5                                   5    
HELIX   50 AF5 THR E 2877  SER E 2898  1                                  22    
SHEET    1 AA1 5 PHE A  43  THR A  51  0                                        
SHEET    2 AA1 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3 AA1 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4 AA1 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
SHEET    5 AA1 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1 AA2 3 GLY A 126  GLU A 127  0                                        
SHEET    2 AA2 3 LEU A 172  ILE A 174 -1  O  ILE A 174   N  GLY A 126           
SHEET    3 AA2 3 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1 AA3 2 LEU A 162  ILE A 163  0                                        
SHEET    2 AA3 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1 AA4 2 ARG C2787  ARG C2790  0                                        
SHEET    2 AA4 2 TYR C2900  SER C2903 -1  O  VAL C2901   N  GLU C2789           
SHEET    1 AA5 5 PHE D  43  THR D  51  0                                        
SHEET    2 AA5 5 ARG D  56  HIS D  62 -1  O  VAL D  57   N  GLY D  50           
SHEET    3 AA5 5 HIS D  68  ASP D  75 -1  O  MET D  71   N  MET D  58           
SHEET    4 AA5 5 ASN D 115  GLU D 121 -1  O  MET D 118   N  LYS D  72           
SHEET    5 AA5 5 LEU D 106  LYS D 111 -1  N  PHE D 108   O  VAL D 119           
SHEET    1 AA6 3 GLY D 126  GLU D 127  0                                        
SHEET    2 AA6 3 LEU D 172  ILE D 174 -1  O  ILE D 174   N  GLY D 126           
SHEET    3 AA6 3 ILE D 180  VAL D 182 -1  O  GLN D 181   N  LEU D 173           
SHEET    1 AA7 2 LEU D 162  ILE D 163  0                                        
SHEET    2 AA7 2 LYS D 189  ARG D 190 -1  O  LYS D 189   N  ILE D 163           
SHEET    1 AA8 2 ARG E2787  ARG E2790  0                                        
SHEET    2 AA8 2 TYR E2900  SER E2903 -1  O  VAL E2901   N  GLU E2789           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.34  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.34  
LINK         C   TRP D 196                 N   TPO D 197     1555   1555  1.34  
LINK         C   TPO D 197                 N   LEU D 198     1555   1555  1.33  
LINK         C   VAL D 337                 N   SEP D 338     1555   1555  1.33  
LINK         C   SEP D 338                 N   ILE D 339     1555   1555  1.34  
SITE     1 AC1  6 LYS A  83  GLN A  84  ILE A  85  GLU A  86                    
SITE     2 AC1  6 HOH A 568  HOH A 621                                          
SITE     1 AC2  2 HIS A 142  HOH E3161                                          
SITE     1 AC3  6 ARG A 144  ALA A 148  THR A 300  ILE A 305                    
SITE     2 AC3  6 HOH A 577  HOH A 647                                          
SITE     1 AC4  2 HIS A 131  TYR A 146                                          
SITE     1 AC5  3 GLY A  55  ARG A  56  ILE A  73                               
SITE     1 AC6 14 LEU A  49  THR A  51  GLY A  52  SER A  53                    
SITE     2 AC6 14 VAL A  57  ALA A  70  LYS A  72  GLU A 121                    
SITE     3 AC6 14 TYR A 122  VAL A 123  HOH A 506  HOH A 519                    
SITE     4 AC6 14 HOH A 549  HOH A 716                                          
SITE     1 AC7  5 PHE A 138  SER A 139  HIS A 142  ALA E2783                    
SITE     2 AC7  5 TRP E2784                                                     
SITE     1 AC8  5 PRO C2713  LYS C2715  LEU C2782  ARG C2787                    
SITE     2 AC8  5 ILE C2788                                                     
SITE     1 AC9  6 HIS D 158  LYS D 217  TRP D 221  GLY D 282                    
SITE     2 AC9  6 HOH D 509  HOH D 652                                          
SITE     1 AD1  5 LYS D  83  GLN D  84  ILE D  85  GLU D  86                    
SITE     2 AD1  5 HOH D 659                                                     
SITE     1 AD2  5 HIS D 131  ILE D 135  TYR D 146  PHE D 314                    
SITE     2 AD2  5 EDO D 407                                                     
SITE     1 AD3  5 THR D  37  ALA D  38  GLN D  42  HIS D  62                    
SITE     2 AD3  5 HOH D 705                                                     
SITE     1 AD4 13 LEU D  49  THR D  51  GLY D  52  SER D  53                    
SITE     2 AD4 13 VAL D  57  ALA D  70  LYS D  72  GLU D 121                    
SITE     3 AD4 13 VAL D 123  ASP D 184  HOH D 645  HOH D 718                    
SITE     4 AD4 13 HOH D 721                                                     
SITE     1 AD5  4 TRP C2786  ARG C2904  HOH C3203  GLU D 140                    
SITE     1 AD6  7 VAL C2705  ILE D 135  ARG D 137  PHE D 138                    
SITE     2 AD6  7 SER D 139  HIS D 142  FMT D 403                               
SITE     1 AD7  5 LYS D  72  GLU D  91  MET D 120  THR D 183                    
SITE     2 AD7  5 HOH D 547                                                     
SITE     1 AD8  7 ARG D 144  THR D 299  THR D 300  ILE D 305                    
SITE     2 AD8  7 VAL D 310  HOH D 504  HOH D 557                               
SITE     1 AD9  5 TYR D  69  GLU D 107  HOH D 505  HOH D 625                    
SITE     2 AD9  5 HOH E3192                                                     
SITE     1 AE1  4 GLU A 140  TRP E2786  MET E2842  ARG E2904                    
SITE     1 AE2  4 ARG E2805  ILE E2806  HOH E3112  HOH E3177                    
CRYST1   58.337   67.560  176.852  90.00  90.73  90.00 P 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      0.017142  0.000000  0.000219        0.00000                         
SCALE2      0.000000  0.014802  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005655        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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