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Database: PDB
Entry: 4I8M
LinkDB: 4I8M
Original site: 4I8M 
HEADER    METAL TRANSPORT                         03-DEC-12   4I8M              
TITLE     CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES 1-536)     
TITLE    2 DISEASE MUTANT V219I                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RYANODINE RECEPTOR 1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DISEASE HOT SPOT, RESIDUES 1-536;               
COMPND   5 SYNONYM: RYR-1, RYR1, SKELETAL MUSCLE CALCIUM RELEASE CHANNEL,       
COMPND   6 SKELETAL MUSCLE RYANODINE RECEPTOR, SKELETAL MUSCLE-TYPE RYANODINE   
COMPND   7 RECEPTOR, TYPE 1 RYANODINE RECEPTOR;                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 GENE: RYR1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA                                    
KEYWDS    CALCIUM CHANNEL, SR/ER MEMBRANE, METAL TRANSPORT                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.KIMLICKA,F.VAN PETEGEM                                              
REVDAT   2   06-MAR-13 4I8M    1       JRNL                                     
REVDAT   1   20-FEB-13 4I8M    0                                                
JRNL        AUTH   L.KIMLICKA,K.LAU,C.C.TUNG,F.VAN PETEGEM                      
JRNL        TITL   DISEASE MUTATIONS IN THE RYANODINE RECEPTOR N-TERMINAL       
JRNL        TITL 2 REGION COUPLE TO A MOBILE INTERSUBUNIT INTERFACE.            
JRNL        REF    NAT COMMUN                    V.   4  1506 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23422674                                                     
JRNL        DOI    10.1038/NCOMMS2501                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 39637                          
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) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2084                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2907                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 148                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3575                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
REMARK   3    B12 (A**2) : -0.05000                                             
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): 0.254         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.193         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.390        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3654 ; 0.005 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4968 ; 0.902 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 4.595 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;33.234 ;23.311       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   543 ;16.926 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;14.661 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   575 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2761 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2379 ; 0.222 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3745 ; 0.405 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1275 ; 0.189 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1222 ; 0.360 ; 4.500       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8540  53.2120 -10.2870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4864 T22:   0.8601                                     
REMARK   3      T33:   0.2378 T12:  -0.3126                                     
REMARK   3      T13:  -0.2169 T23:  -0.0839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9501 L22:   2.3092                                     
REMARK   3      L33:   5.4665 L12:   0.2901                                     
REMARK   3      L13:   2.9291 L23:  -0.0367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6167 S12:  -0.6685 S13:  -0.5369                       
REMARK   3      S21:   0.3245 S22:  -0.0808 S23:  -0.2974                       
REMARK   3      S31:   0.2955 S32:   0.0239 S33:  -0.5360                       
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 :   A   206        A   394                          
REMARK   3    ORIGIN FOR THE GROUP (A): -70.6850  61.6330 -25.6460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4503 T22:   0.4370                                     
REMARK   3      T33:   0.0876 T12:  -0.0498                                     
REMARK   3      T13:   0.0313 T23:  -0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3076 L22:   2.1163                                     
REMARK   3      L33:   1.2727 L12:  -0.0631                                     
REMARK   3      L13:  -0.2961 L23:  -0.2146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1817 S12:  -0.0659 S13:   0.2454                       
REMARK   3      S21:   0.1331 S22:   0.0673 S23:  -0.1606                       
REMARK   3      S31:  -0.2164 S32:  -0.0020 S33:  -0.2491                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   395        A   533                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.1890  53.7960 -41.1990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2621 T22:   0.7112                                     
REMARK   3      T33:   0.1331 T12:  -0.0914                                     
REMARK   3      T13:  -0.0297 T23:  -0.2362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7038 L22:   3.0083                                     
REMARK   3      L33:   6.0063 L12:  -0.1767                                     
REMARK   3      L13:  -1.2633 L23:   0.0022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2605 S12:   0.0901 S13:   0.0032                       
REMARK   3      S21:  -0.0116 S22:   0.2240 S23:  -0.3838                       
REMARK   3      S31:  -0.0491 S32:   0.8912 S33:  -0.4844                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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                                                           
REMARK   4                                                                      
REMARK   4 4I8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076441.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : ACCEL/BRUKER DOUBLE CRYSTAL        
REMARK 200                                   MONOCHROMATOR (DCM)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SCALA                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41721                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 2XOA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 82.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 9.0, EVAPORATION                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       84.63350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.86317            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      101.86633            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       84.63350            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       48.86317            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      101.86633            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       84.63350            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       48.86317            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      101.86633            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       84.63350            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       48.86317            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      101.86633            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       84.63350            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       48.86317            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      101.86633            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       84.63350            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       48.86317            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      101.86633            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       97.72635            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      203.73267            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       97.72635            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      203.73267            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       97.72635            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      203.73267            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       97.72635            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      203.73267            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       97.72635            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      203.73267            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       97.72635            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      203.73267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     ASN A    84                                                      
REMARK 465     THR A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     GLU A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     SER A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     SER A   126                                                      
REMARK 465     MET A   127                                                      
REMARK 465     THR A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     MET A   227                                                      
REMARK 465     ASP A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     ALA A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     ASP A   363                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     ALA A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     ARG A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLY A   370                                                      
REMARK 465     VAL A   371                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     PRO A   430                                                      
REMARK 465     PRO A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     ARG A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     ASN A   536                                                      
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     ARG A  15    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  28    CG1  CG2                                            
REMARK 470     LEU A  29    CG   CD1  CD2                                       
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     GLU A  31    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  33    CG   CD1  CD2                                       
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     VAL A  75    CG1  CG2                                            
REMARK 470     ARG A  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  78    CG   CD1  CD2                                       
REMARK 470     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     MET A  81    CG   SD   CE                                        
REMARK 470     LEU A  82    CG   CD1  CD2                                       
REMARK 470     HIS A  98    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 124    OG                                                  
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 131    CG   CD1  CD2                                       
REMARK 470     ASP A 140    CG   OD1  OD2                                       
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 155    CG   CD   CE   NZ                                   
REMARK 470     GLN A 156    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 186    OG                                                  
REMARK 470     LEU A 199    CG   CD1  CD2                                       
REMARK 470     ASP A 237    CG   OD1  OD2                                       
REMARK 470     ASP A 239    CG   OD1  OD2                                       
REMARK 470     GLN A 241    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 275    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 296    CG   OD1  OD2                                       
REMARK 470     LYS A 306    CG   CD   CE   NZ                                   
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     LYS A 328    CG   CD   CE   NZ                                   
REMARK 470     ARG A 329    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     LYS A 416    CG   CD   CE   NZ                                   
REMARK 470     LYS A 424    CG   CD   CE   NZ                                   
REMARK 470     SER A 456    OG                                                  
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 458    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 459    CG   CD1  CD2                                       
REMARK 470     GLN A 460    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 462    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     LYS A 467    CG   CD   CE   NZ                                   
REMARK 470     GLU A 509    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 513    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 516    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    SER A 207     -159.89   -116.68                                   
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 GOL A 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XOA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N-TERMINAL THREE DOMAINS OF THE             
REMARK 900 SKELETAL MUSCLE RYANODINE RECEPTOR (RYR1)                            
REMARK 900 RELATED ID: 4I7I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT L14R                                                   
REMARK 900 RELATED ID: 4I6I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-559) MUTANT R45C                                                   
REMARK 900 RELATED ID: 4I3N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT D61N                                                   
REMARK 900 RELATED ID: 4I37   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT R402G                                                  
REMARK 900 RELATED ID: 4I2S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT I404M                                                  
REMARK 900 RELATED ID: 4I1E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT G249R                                                  
REMARK 900 RELATED ID: 4I0Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 1-536) MUTANT C36R                                                   
REMARK 900 RELATED ID: 4I96   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RABBIT RYANODINE RECEPTOR 1 (RESIDUES           
REMARK 900 217-536) MUTANT V219I                                                
DBREF  4I8M A    1   536  UNP    P11716   RYR1_RABIT       1    536             
SEQADV 4I8M ILE A  219  UNP  P11716    VAL   219 ENGINEERED MUTATION            
SEQRES   1 A  536  MET GLY ASP GLY GLY GLU GLY GLU ASP GLU VAL GLN PHE          
SEQRES   2 A  536  LEU ARG THR ASP ASP GLU VAL VAL LEU GLN CYS SER ALA          
SEQRES   3 A  536  THR VAL LEU LYS GLU GLN LEU LYS LEU CYS LEU ALA ALA          
SEQRES   4 A  536  GLU GLY PHE GLY ASN ARG LEU CYS PHE LEU GLU PRO THR          
SEQRES   5 A  536  SER ASN ALA GLN ASN VAL PRO PRO ASP LEU ALA ILE CYS          
SEQRES   6 A  536  CYS PHE THR LEU GLU GLN SER LEU SER VAL ARG ALA LEU          
SEQRES   7 A  536  GLN GLU MET LEU ALA ASN THR VAL GLU ALA GLY VAL GLU          
SEQRES   8 A  536  SER SER GLN GLY GLY GLY HIS ARG THR LEU LEU TYR GLY          
SEQRES   9 A  536  HIS ALA ILE LEU LEU ARG HIS ALA HIS SER ARG MET TYR          
SEQRES  10 A  536  LEU SER CYS LEU THR THR SER ARG SER MET THR ASP LYS          
SEQRES  11 A  536  LEU ALA PHE ASP VAL GLY LEU GLN GLU ASP ALA THR GLY          
SEQRES  12 A  536  GLU ALA CYS TRP TRP THR MET HIS PRO ALA SER LYS GLN          
SEQRES  13 A  536  ARG SER GLU GLY GLU LYS VAL ARG VAL GLY ASP ASP LEU          
SEQRES  14 A  536  ILE LEU VAL SER VAL SER SER GLU ARG TYR LEU HIS LEU          
SEQRES  15 A  536  SER THR ALA SER GLY GLU LEU GLN VAL ASP ALA SER PHE          
SEQRES  16 A  536  MET GLN THR LEU TRP ASN MET ASN PRO ILE CYS SER CYS          
SEQRES  17 A  536  CYS GLU GLU GLY TYR VAL THR GLY GLY HIS ILE LEU ARG          
SEQRES  18 A  536  LEU PHE HIS GLY HIS MET ASP GLU CYS LEU THR ILE SER          
SEQRES  19 A  536  ALA ALA ASP SER ASP ASP GLN ARG ARG LEU VAL TYR TYR          
SEQRES  20 A  536  GLU GLY GLY ALA VAL CYS THR HIS ALA ARG SER LEU TRP          
SEQRES  21 A  536  ARG LEU GLU PRO LEU ARG ILE SER TRP SER GLY SER HIS          
SEQRES  22 A  536  LEU ARG TRP GLY GLN PRO LEU ARG ILE ARG HIS VAL THR          
SEQRES  23 A  536  THR GLY ARG TYR LEU ALA LEU THR GLU ASP GLN GLY LEU          
SEQRES  24 A  536  VAL VAL VAL ASP ALA CYS LYS ALA HIS THR LYS ALA THR          
SEQRES  25 A  536  SER PHE CYS PHE ARG VAL SER LYS GLU LYS LEU ASP THR          
SEQRES  26 A  536  ALA PRO LYS ARG ASP VAL GLU GLY MET GLY PRO PRO GLU          
SEQRES  27 A  536  ILE LYS TYR GLY GLU SER LEU CYS PHE VAL GLN HIS VAL          
SEQRES  28 A  536  ALA SER GLY LEU TRP LEU THR TYR ALA ALA PRO ASP PRO          
SEQRES  29 A  536  LYS ALA LEU ARG LEU GLY VAL LEU LYS LYS LYS ALA ILE          
SEQRES  30 A  536  LEU HIS GLN GLU GLY HIS MET ASP ASP ALA LEU PHE LEU          
SEQRES  31 A  536  THR ARG CYS GLN GLN GLU GLU SER GLN ALA ALA ARG MET          
SEQRES  32 A  536  ILE HIS SER THR ALA GLY LEU TYR ASN GLN PHE ILE LYS          
SEQRES  33 A  536  GLY LEU ASP SER PHE SER GLY LYS PRO ARG GLY SER GLY          
SEQRES  34 A  536  PRO PRO ALA GLY PRO ALA LEU PRO ILE GLU ALA VAL ILE          
SEQRES  35 A  536  LEU SER LEU GLN ASP LEU ILE GLY TYR PHE GLU PRO PRO          
SEQRES  36 A  536  SER GLU GLU LEU GLN HIS GLU GLU LYS GLN SER LYS LEU          
SEQRES  37 A  536  ARG SER LEU ARG ASN ARG GLN SER LEU PHE GLN GLU GLU          
SEQRES  38 A  536  GLY MET LEU SER LEU VAL LEU ASN CYS ILE ASP ARG LEU          
SEQRES  39 A  536  ASN VAL TYR THR THR ALA ALA HIS PHE ALA GLU TYR ALA          
SEQRES  40 A  536  GLY GLU GLU ALA ALA GLU SER TRP LYS GLU ILE VAL ASN          
SEQRES  41 A  536  LEU LEU TYR GLU LEU LEU ALA SER LEU ILE ARG GLY ASN          
SEQRES  42 A  536  ARG ALA ASN                                                  
HET    GOL  A 601       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    C3 H8 O3                                                     
FORMUL   3  HOH   *36(H2 O)                                                     
HELIX    1   1 ASP A   61  CYS A   65  5                                   5    
HELIX    2   2 SER A   74  ALA A   83  1                                  10    
HELIX    3   3 GLY A  250  SER A  258  5                                   9    
HELIX    4   4 ASP A  303  ALA A  307  5                                   5    
HELIX    5   5 HIS A  308  SER A  313  1                                   6    
HELIX    6   6 GLN A  394  PHE A  421  1                                  28    
HELIX    7   7 PRO A  437  GLU A  453  1                                  17    
HELIX    8   8 GLN A  460  GLU A  480  1                                  21    
HELIX    9   9 GLY A  482  VAL A  496  1                                  15    
HELIX   10  10 THR A  499  ALA A  504  1                                   6    
HELIX   11  11 GLY A  508  GLU A  513  1                                   6    
HELIX   12  12 SER A  514  ARG A  531  1                                  18    
SHEET    1   A 9 PHE A  48  PRO A  51  0                                        
SHEET    2   A 9 GLU A  31  ALA A  38 -1  N  ALA A  38   O  PHE A  48           
SHEET    3   A 9 GLU A  19  VAL A  28 -1  N  VAL A  28   O  GLU A  31           
SHEET    4   A 9 TRP A 200  CYS A 206 -1  O  ILE A 205   N  GLU A  19           
SHEET    5   A 9 ASP A 168  SER A 173 -1  N  LEU A 169   O  TRP A 200           
SHEET    6   A 9 TRP A 147  PRO A 152 -1  N  THR A 149   O  VAL A 172           
SHEET    7   A 9 ALA A 106  HIS A 111 -1  N  ILE A 107   O  TRP A 148           
SHEET    8   A 9 PHE A  67  LEU A  73 -1  N  LEU A  73   O  ALA A 106           
SHEET    9   A 9 GLU A  19  VAL A  28 -1  N  VAL A  20   O  PHE A  67           
SHEET    1   B 2 TYR A 117  CYS A 120  0                                        
SHEET    2   B 2 VAL A 135  GLN A 138 -1  O  GLY A 136   N  SER A 119           
SHEET    1   C 2 TYR A 179  SER A 183  0                                        
SHEET    2   C 2 GLN A 190  SER A 194 -1  O  GLN A 190   N  SER A 183           
SHEET    1   D 7 LEU A 280  HIS A 284  0                                        
SHEET    2   D 7 TRP A 260  PRO A 264 -1  N  GLU A 263   O  ARG A 281           
SHEET    3   D 7 ILE A 219  HIS A 224 -1  N  LEU A 220   O  TRP A 260           
SHEET    4   D 7 GLU A 229  ILE A 233 -1  O  GLU A 229   N  HIS A 224           
SHEET    5   D 7 VAL A 245  GLU A 248 -1  O  TYR A 246   N  THR A 232           
SHEET    6   D 7 LYS A 373  HIS A 379 -1  O  ALA A 376   N  VAL A 245           
SHEET    7   D 7 TRP A 356  TYR A 359 -1  N  TRP A 356   O  HIS A 379           
SHEET    1   E 4 LEU A 280  HIS A 284  0                                        
SHEET    2   E 4 TRP A 260  PRO A 264 -1  N  GLU A 263   O  ARG A 281           
SHEET    3   E 4 ILE A 219  HIS A 224 -1  N  LEU A 220   O  TRP A 260           
SHEET    4   E 4 PHE A 389  ARG A 392 -1  O  PHE A 389   N  PHE A 223           
SHEET    1   F 2 TYR A 290  THR A 294  0                                        
SHEET    2   F 2 GLY A 298  VAL A 302 -1  O  VAL A 302   N  TYR A 290           
SHEET    1   G 2 PHE A 314  ARG A 317  0                                        
SHEET    2   G 2 PHE A 347  HIS A 350 -1  O  PHE A 347   N  ARG A 317           
CISPEP   1 ALA A  185    SER A  186          0        -1.44                     
SITE     1 AC1  2 ILE A 267  SER A 268                                          
CRYST1  169.267  169.267  305.599  90.00  90.00 120.00 H 3 2        18          
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      0.005908  0.003411  0.000000        0.00000                         
SCALE2      0.000000  0.006822  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003272        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system