GenomeNet

Database: PDB
Entry: 3QR5
LinkDB: 3QR5
Original site: 3QR5 
HEADER    SIGNALING PROTEIN                       17-FEB-11   3QR5              
TITLE     STRUCTURE OF THE FIRST DOMAIN OF A CARDIAC RYANODINE RECEPTOR MUTANT  
TITLE    2 WITH EXON 3 DELETED                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARDIAC CA2+ RELEASE CHANNEL;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RYR2A DELTA-EXON3 (UNP RESIDUES 1-217 DELTA 57-91);        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RYR2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA TREFOIL, SARCOPLASMIC RETICULUM, SIGNALING PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.LOBO,F.VAN PETEGEM                                                
REVDAT   3   08-NOV-17 3QR5    1       REMARK                                   
REVDAT   2   26-JUL-17 3QR5    1       SOURCE REMARK                            
REVDAT   1   08-JUN-11 3QR5    0                                                
JRNL        AUTH   P.A.LOBO,L.KIMLICKA,C.-C.TUNG,F.VAN PETEGEM                  
JRNL        TITL   THE DELETION OF EXON 3 IN THE CARDIAC RYANODINE RECEPTOR IS  
JRNL        TITL 2 RESCUED BY BETA STRAND SWITCHING                             
JRNL        REF    STRUCTURE                                  2011              
JRNL        REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12901                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 642                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 430                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 43.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 17                           
REMARK   3   BIN FREE R VALUE                    : 0.2050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2335                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -1.38000                                             
REMARK   3    B33 (A**2) : 1.32000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.49000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.473         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.267         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.207         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.476        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2389 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3244 ; 1.435 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   298 ; 7.346 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    96 ;33.054 ;23.021       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   373 ;18.863 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;17.122 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   377 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1758 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   873 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1554 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   120 ; 0.169 ; 0.200       
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):    36 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.174 ; 0.200       
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):  1546 ; 0.730 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2390 ; 1.284 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   986 ; 1.763 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   853 ; 2.723 ; 4.500       
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  : 2                                          
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     1        A   217                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8810  10.4970  -5.7930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1000 T22:  -0.2061                                     
REMARK   3      T33:  -0.1238 T12:   0.0265                                     
REMARK   3      T13:   0.0047 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7113 L22:   6.1554                                     
REMARK   3      L33:   5.3169 L12:  -1.6718                                     
REMARK   3      L13:  -0.0081 L23:  -1.8499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1220 S12:   0.0692 S13:   0.0760                       
REMARK   3      S21:  -0.2405 S22:  -0.1810 S23:  -0.0007                       
REMARK   3      S31:  -0.2552 S32:  -0.0463 S33:   0.0591                       
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 :   B     1        B   217                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0250 -10.0610 -32.3760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1473 T22:  -0.1885                                     
REMARK   3      T33:  -0.1256 T12:  -0.0134                                     
REMARK   3      T13:  -0.0034 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6293 L22:   6.9629                                     
REMARK   3      L33:   4.5787 L12:   1.3581                                     
REMARK   3      L13:  -0.7263 L23:  -2.1547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0744 S12:  -0.1143 S13:  -0.1078                       
REMARK   3      S21:   0.3191 S22:  -0.1469 S23:  -0.1136                       
REMARK   3      S31:   0.1145 S32:   0.0075 S33:   0.0725                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QR5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
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) : 0.9729                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12917                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.5                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 32.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000                            
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 2.1.1                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15% PEG 1000. CRYSTALS FROZEN IN      
REMARK 280  25% 2-METHANE-2,4-PENTANEDIOL CRYOPROTECTANT, PH 7, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       47.68500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.10200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.68500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.10200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA 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     ILE A    11                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     PHE A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     ASN A    44                                                      
REMARK 465     THR A    87                                                      
REMARK 465     SER A    88                                                      
REMARK 465     ASN A    89                                                      
REMARK 465     SER A    90                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     GLN A    92                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     GLN A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     ASN A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     ILE B    11                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     GLY B    41                                                      
REMARK 465     PHE B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     GLU B    85                                                      
REMARK 465     SER B    86                                                      
REMARK 465     THR B    87                                                      
REMARK 465     SER B    88                                                      
REMARK 465     ASN B    89                                                      
REMARK 465     SER B    90                                                      
REMARK 465     LYS B    91                                                      
REMARK 465     GLN B    92                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     GLN B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     GLY B   109                                                      
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     GLN A  12    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  46    CG   CD1  CD2                                       
REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  95    CG1  CG2                                            
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     ARG A 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 140    OG1  CG2                                            
REMARK 470     GLU A 151    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     GLN A 168    CG   CD   OE1  NE2                                  
REMARK 470     SER A 170    OG                                                  
REMARK 470     ASP A 180    CG   OD1  OD2                                       
REMARK 470     TYR A 196    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 217    CG1  CG2  CD1                                       
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  14    CG   CD1  CD2                                       
REMARK 470     LYS B  30    CG   CD   CE   NZ                                   
REMARK 470     GLN B  33    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  44    CG   OD1  ND2                                       
REMARK 470     VAL B  93    CG1  CG2                                            
REMARK 470     ASP B  94    CG   OD1  OD2                                       
REMARK 470     VAL B  95    CG1  CG2                                            
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     ARG B 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 151    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 167    CG   CD   CE   NZ                                   
REMARK 470     GLN B 168    CG   CD   OE1  NE2                                  
REMARK 470     SER B 170    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  17       -4.28     61.65                                   
REMARK 500    ILE A  28      -96.61    -70.03                                   
REMARK 500    HIS A  29       35.21    -80.10                                   
REMARK 500    THR A 135      149.55    -34.50                                   
REMARK 500    GLN A 168       24.61    -79.26                                   
REMARK 500    ASP B  17       -2.92     69.39                                   
REMARK 500    ILE B  28      -98.33    -90.58                                   
REMARK 500    HIS B  29       44.90    -80.71                                   
REMARK 500    LYS B  30       19.73     55.72                                   
REMARK 500    GLN B 168       20.03    -76.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IM5   RELATED DB: PDB                                   
REMARK 900 WILD TYPE STRUCTURE OF THE DOMAIN                                    
DBREF  3QR5 A    1    91  UNP    Q9ERN6   Q9ERN6_MOUSE     1     56             
DBREF  3QR5 A   92   217  UNP    Q9ERN6   Q9ERN6_MOUSE    92    217             
DBREF  3QR5 B    1    91  UNP    Q9ERN6   Q9ERN6_MOUSE     1     56             
DBREF  3QR5 B   92   217  UNP    Q9ERN6   Q9ERN6_MOUSE    92    217             
SEQADV 3QR5 SER A   -2  UNP  Q9ERN6              EXPRESSION TAG                 
SEQADV 3QR5 ASN A   -1  UNP  Q9ERN6              EXPRESSION TAG                 
SEQADV 3QR5 ALA A    0  UNP  Q9ERN6              EXPRESSION TAG                 
SEQADV 3QR5 SER B   -2  UNP  Q9ERN6              EXPRESSION TAG                 
SEQADV 3QR5 ASN B   -1  UNP  Q9ERN6              EXPRESSION TAG                 
SEQADV 3QR5 ALA B    0  UNP  Q9ERN6              EXPRESSION TAG                 
SEQRES   1 A  185  SER ASN ALA MET ALA ASP ALA GLY GLU GLY GLU ASP GLU          
SEQRES   2 A  185  ILE GLN PHE LEU ARG THR ASP ASP GLU VAL VAL LEU GLN          
SEQRES   3 A  185  CYS THR ALA THR ILE HIS LYS GLU GLN GLN LYS LEU CYS          
SEQRES   4 A  185  LEU ALA ALA GLU GLY PHE GLY ASN ARG LEU CYS PHE LEU          
SEQRES   5 A  185  GLU SER THR SER ASN SER LYS GLN VAL ASP VAL GLU LYS          
SEQRES   6 A  185  TRP LYS PHE MET MET LYS THR ALA GLN GLY GLY GLY HIS          
SEQRES   7 A  185  ARG THR LEU LEU TYR GLY HIS ALA ILE LEU LEU ARG HIS          
SEQRES   8 A  185  SER TYR SER GLY MET TYR LEU CYS CYS LEU SER THR SER          
SEQRES   9 A  185  ARG SER SER THR ASP LYS LEU ALA PHE ASP VAL GLY LEU          
SEQRES  10 A  185  GLN GLU ASP THR THR GLY GLU ALA CYS TRP TRP THR ILE          
SEQRES  11 A  185  HIS PRO ALA SER LYS GLN ARG SER GLU GLY GLU LYS VAL          
SEQRES  12 A  185  ARG VAL GLY ASP ASP LEU ILE LEU VAL SER VAL SER SER          
SEQRES  13 A  185  GLU ARG TYR LEU HIS LEU SER TYR GLY ASN SER SER TRP          
SEQRES  14 A  185  HIS VAL ASP ALA ALA PHE GLN GLN THR LEU TRP SER VAL          
SEQRES  15 A  185  ALA PRO ILE                                                  
SEQRES   1 B  185  SER ASN ALA MET ALA ASP ALA GLY GLU GLY GLU ASP GLU          
SEQRES   2 B  185  ILE GLN PHE LEU ARG THR ASP ASP GLU VAL VAL LEU GLN          
SEQRES   3 B  185  CYS THR ALA THR ILE HIS LYS GLU GLN GLN LYS LEU CYS          
SEQRES   4 B  185  LEU ALA ALA GLU GLY PHE GLY ASN ARG LEU CYS PHE LEU          
SEQRES   5 B  185  GLU SER THR SER ASN SER LYS GLN VAL ASP VAL GLU LYS          
SEQRES   6 B  185  TRP LYS PHE MET MET LYS THR ALA GLN GLY GLY GLY HIS          
SEQRES   7 B  185  ARG THR LEU LEU TYR GLY HIS ALA ILE LEU LEU ARG HIS          
SEQRES   8 B  185  SER TYR SER GLY MET TYR LEU CYS CYS LEU SER THR SER          
SEQRES   9 B  185  ARG SER SER THR ASP LYS LEU ALA PHE ASP VAL GLY LEU          
SEQRES  10 B  185  GLN GLU ASP THR THR GLY GLU ALA CYS TRP TRP THR ILE          
SEQRES  11 B  185  HIS PRO ALA SER LYS GLN ARG SER GLU GLY GLU LYS VAL          
SEQRES  12 B  185  ARG VAL GLY ASP ASP LEU ILE LEU VAL SER VAL SER SER          
SEQRES  13 B  185  GLU ARG TYR LEU HIS LEU SER TYR GLY ASN SER SER TRP          
SEQRES  14 B  185  HIS VAL ASP ALA ALA PHE GLN GLN THR LEU TRP SER VAL          
SEQRES  15 B  185  ALA PRO ILE                                                  
FORMUL   3  HOH   *42(H2 O)                                                     
SHEET    1   A 7 CYS A  47  GLU A  50  0                                        
SHEET    2   A 7 GLN A  32  ALA A  39 -1  N  CYS A  36   O  GLU A  50           
SHEET    3   A 7 GLU A  19  THR A  27 -1  N  CYS A  24   O  LEU A  35           
SHEET    4   A 7 LYS A  97  MET A 101 -1  O  TRP A  98   N  VAL A  20           
SHEET    5   A 7 ALA A 118  HIS A 123 -1  O  LEU A 120   N  MET A 101           
SHEET    6   A 7 TRP A 159  PRO A 164 -1  O  TRP A 160   N  ILE A 119           
SHEET    7   A 7 LEU A 181  SER A 185 -1  O  VAL A 184   N  THR A 161           
SHEET    1   B 4 CYS A  47  GLU A  50  0                                        
SHEET    2   B 4 GLN A  32  ALA A  39 -1  N  CYS A  36   O  GLU A  50           
SHEET    3   B 4 GLU A  19  THR A  27 -1  N  CYS A  24   O  LEU A  35           
SHEET    4   B 4 SER A 213  PRO A 216 -1  O  SER A 213   N  GLN A  23           
SHEET    1   C 4 TYR A 129  CYS A 132  0                                        
SHEET    2   C 4 PHE A 145  GLN A 150 -1  O  GLY A 148   N  CYS A 131           
SHEET    3   C 4 HIS A 202  ALA A 206 -1  O  ALA A 205   N  PHE A 145           
SHEET    4   C 4 TYR A 191  SER A 195 -1  N  SER A 195   O  HIS A 202           
SHEET    1   D 7 CYS B  47  PHE B  48  0                                        
SHEET    2   D 7 GLN B  32  ALA B  38 -1  N  ALA B  38   O  CYS B  47           
SHEET    3   D 7 VAL B  20  THR B  27 -1  N  CYS B  24   O  LEU B  35           
SHEET    4   D 7 LYS B  97  MET B 101 -1  O  TRP B  98   N  VAL B  20           
SHEET    5   D 7 ALA B 118  HIS B 123 -1  O  LEU B 120   N  MET B 101           
SHEET    6   D 7 TRP B 159  PRO B 164 -1  O  TRP B 160   N  ILE B 119           
SHEET    7   D 7 LEU B 181  SER B 185 -1  O  VAL B 184   N  THR B 161           
SHEET    1   E 4 CYS B  47  PHE B  48  0                                        
SHEET    2   E 4 GLN B  32  ALA B  38 -1  N  ALA B  38   O  CYS B  47           
SHEET    3   E 4 VAL B  20  THR B  27 -1  N  CYS B  24   O  LEU B  35           
SHEET    4   E 4 SER B 213  PRO B 216 -1  O  ALA B 215   N  VAL B  21           
SHEET    1   F 4 TYR B 129  CYS B 132  0                                        
SHEET    2   F 4 PHE B 145  GLN B 150 -1  O  GLN B 150   N  TYR B 129           
SHEET    3   F 4 SER B 200  ALA B 206 -1  O  ALA B 205   N  PHE B 145           
SHEET    4   F 4 TYR B 191  GLY B 197 -1  N  SER B 195   O  HIS B 202           
SSBOND   1 CYS A  131    CYS A  158                          1555   1555  2.05  
SSBOND   2 CYS B  131    CYS B  158                          1555   1555  2.01  
CRYST1   95.370   44.204   76.606  90.00  90.98  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010485  0.000000  0.000180        0.00000                         
SCALE2      0.000000  0.022622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013056        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system