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Database: PDB
Entry: 2VAF
LinkDB: 2VAF
Original site: 2VAF 
HEADER    METAL BINDING PROTEIN                   31-AUG-07   2VAF              
TITLE     CRYSTAL STRUCTURE OF HUMAN CARDIAC CALSEQUESTRIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALSEQUESTRIN-2;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 22-399;                                           
COMPND   5 SYNONYM: CALSEQUESTRIN, CARDIAC MUSCLE ISOFORM, HUMAN CARDIAC        
COMPND   6 CALSEQUESTRIN;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    CALCIUM, GLYCOPROTEIN, POLYMORPHISM, MUSCLE PROTEIN, DISEASE          
KEYWDS   2 MUTATION, SARCOPLASMIC RETICULUM, CRYSTAL STRUCTURE HUMAN CARDIAC    
KEYWDS   3 CALSEQUESTRIN, METAL-BINDING PROTEIN, METAL BINDING PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.KIM,B.YOUN,L.KEMPER,C.CAMPBELL,H.MILTING,M.VARSANYI,C.KANG          
REVDAT   5   22-MAY-19 2VAF    1       REMARK                                   
REVDAT   4   24-FEB-09 2VAF    1       VERSN                                    
REVDAT   3   16-OCT-07 2VAF    1       JRNL                                     
REVDAT   2   02-OCT-07 2VAF    1       JRNL                                     
REVDAT   1   11-SEP-07 2VAF    0                                                
SPRSDE     11-SEP-07 2VAF      2V0Q                                             
JRNL        AUTH   E.KIM,B.YOUN,L.KEMPER,C.CAMPBELL,H.MILTING,M.VARSANYI,C.KANG 
JRNL        TITL   CHARACTERIZATION OF HUMAN CARDIAC CALSEQUESTRIN AND ITS      
JRNL        TITL 2 DELETERIOUS MUTANTS.                                         
JRNL        REF    J.MOL.BIOL.                   V. 373  1047 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17881003                                                     
JRNL        DOI    10.1016/J.JMB.2007.08.055                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 4119                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.274                           
REMARK   3   FREE R VALUE                     : 0.325                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2873                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.986                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2VAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290033658.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07812                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11522                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.5600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1SJI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 84.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 8.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       75.32500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       75.32500            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.73500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.86750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       75.32500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      170.60250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      170.60250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       75.32500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.86750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       75.32500            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      113.73500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       75.32500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      113.73500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       75.32500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      170.60250            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       56.86750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       75.32500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       56.86750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      170.60250            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       75.32500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       75.32500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      113.73500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.8 KCAL/MOL                        
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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      227.47000            
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     ASN A  1352                                                      
REMARK 465     THR A  1353                                                      
REMARK 465     GLU A  1354                                                      
REMARK 465     ASP A  1355                                                      
REMARK 465     ASP A  1356                                                      
REMARK 465     ASP A  1357                                                      
REMARK 465     GLU A  1358                                                      
REMARK 465     ASP A  1359                                                      
REMARK 465     ASP A  1360                                                      
REMARK 465     ASP A  1361                                                      
REMARK 465     ASP A  1362                                                      
REMARK 465     ASP A  1363                                                      
REMARK 465     ASP A  1364                                                      
REMARK 465     ASN A  1365                                                      
REMARK 465     SER A  1366                                                      
REMARK 465     ASP A  1367                                                      
REMARK 465     GLU A  1368                                                      
REMARK 465     GLU A  1369                                                      
REMARK 465     ASP A  1370                                                      
REMARK 465     ASN A  1371                                                      
REMARK 465     ASP A  1372                                                      
REMARK 465     ASP A  1373                                                      
REMARK 465     SER A  1374                                                      
REMARK 465     ASP A  1375                                                      
REMARK 465     ASP A  1376                                                      
REMARK 465     ASP A  1377                                                      
REMARK 465     ASP A  1378                                                      
REMARK 465     ASP A  1379                                                      
REMARK 465     GLU A  1380                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A1038   NE2   HIS A1038   CD2    -0.068                       
REMARK 500    HIS A1067   NE2   HIS A1067   CD2    -0.071                       
REMARK 500    HIS A1169   NE2   HIS A1169   CD2    -0.067                       
REMARK 500    HIS A1225   NE2   HIS A1225   CD2    -0.069                       
REMARK 500    HIS A1250   NE2   HIS A1250   CD2    -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP A1242   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TRP A1242   CB  -  CG  -  CD1 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    TRP A1242   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    TRP A1242   CG  -  CD2 -  CE3 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A1286   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    TRP A1286   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP A1299   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP A1299   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TRP A1324   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TRP A1324   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP A1342   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP A1342   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LEU A1004     -158.17    -77.47                                   
REMARK 500    ASN A1005     -152.12   -133.36                                   
REMARK 500    ASP A1013       99.53    -68.66                                   
REMARK 500    GLU A1020      -70.67    -50.99                                   
REMARK 500    PRO A1040       86.83    -65.87                                   
REMARK 500    SER A1042       76.34   -155.24                                   
REMARK 500    SER A1043     -157.26   -103.48                                   
REMARK 500    LEU A1058      -70.90    -52.35                                   
REMARK 500    GLU A1066       55.27     36.26                                   
REMARK 500    ALA A1069      -53.37   -166.36                                   
REMARK 500    VAL A1073     -104.76    112.73                                   
REMARK 500    ALA A1077     -121.84   -174.73                                   
REMARK 500    LYS A1079     -133.99     31.22                                   
REMARK 500    LYS A1085      -34.98   -177.02                                   
REMARK 500    LYS A1086        3.48    134.43                                   
REMARK 500    ASP A1090     -117.71    -86.03                                   
REMARK 500    GLU A1091     -144.93   -115.13                                   
REMARK 500    SER A1094      143.03    179.57                                   
REMARK 500    LYS A1099      -43.36     66.76                                   
REMARK 500    ASP A1101      -50.17     73.49                                   
REMARK 500    ARG A1102      -35.21   -177.52                                   
REMARK 500    THR A1103      149.66    179.63                                   
REMARK 500    PRO A1126      -92.48   -123.05                                   
REMARK 500    VAL A1127     -145.36   -120.76                                   
REMARK 500    SER A1131      -64.64   -146.68                                   
REMARK 500    SER A1132     -177.87    -64.51                                   
REMARK 500    GLU A1140       53.51    -94.02                                   
REMARK 500    GLN A1171       49.18    -83.56                                   
REMARK 500    PRO A1172     -130.93    -35.41                                   
REMARK 500    TYR A1173     -102.09   -138.79                                   
REMARK 500    ILE A1174     -139.61     42.82                                   
REMARK 500    ASP A1181      146.93     73.65                                   
REMARK 500    SER A1189       71.92     62.42                                   
REMARK 500    LYS A1191      -28.41     73.79                                   
REMARK 500    GLU A1194     -151.85   -123.83                                   
REMARK 500    PRO A1200      -90.36    -50.01                                   
REMARK 500    ASP A1203       94.31    -51.67                                   
REMARK 500    PRO A1205       88.39    -66.67                                   
REMARK 500    ASN A1210     -114.79   -108.54                                   
REMARK 500    LYS A1211     -118.75   -125.01                                   
REMARK 500    THR A1214     -167.62   -117.93                                   
REMARK 500    GLU A1215      -73.91    -47.99                                   
REMARK 500    ARG A1227      -34.17   -162.16                                   
REMARK 500    THR A1229      -82.47     47.20                                   
REMARK 500    ARG A1234     -146.59   -135.71                                   
REMARK 500    PRO A1235      -85.16    -46.21                                   
REMARK 500    ASP A1245       98.49     57.13                                   
REMARK 500    LEU A1246     -112.87   -101.27                                   
REMARK 500    ASN A1247      -47.76   -178.45                                   
REMARK 500    LYS A1257     -160.01    -71.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      80 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A 1125     PRO A 1126                   38.97                    
REMARK 500 GLN A 1171     PRO A 1172                   92.17                    
REMARK 500 ILE A 1208     PRO A 1209                 -136.10                    
REMARK 500 LYS A 1211     PRO A 1212                  147.30                    
REMARK 500 ARG A 1227     PRO A 1228                 -123.69                    
REMARK 500 LEU A 1333     PRO A 1334                  148.47                    
REMARK 500 GLU A 1344     ASP A 1345                  131.11                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A1343        -13.12                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2VAF A 1003  1380  UNP    O14958   CASQ2_HUMAN     22    399             
SEQRES   1 A  378  GLY LEU ASN PHE PRO THR TYR ASP GLY LYS ASP ARG VAL          
SEQRES   2 A  378  VAL SER LEU SER GLU LYS ASN PHE LYS GLN VAL LEU LYS          
SEQRES   3 A  378  LYS TYR ASP LEU LEU CYS LEU TYR TYR HIS GLU PRO VAL          
SEQRES   4 A  378  SER SER ASP LYS VAL THR GLN LYS GLN PHE GLN LEU LYS          
SEQRES   5 A  378  GLU ILE VAL LEU GLU LEU VAL ALA GLN VAL LEU GLU HIS          
SEQRES   6 A  378  LYS ALA ILE GLY PHE VAL MET VAL ASP ALA LYS LYS GLU          
SEQRES   7 A  378  ALA LYS LEU ALA LYS LYS LEU GLY PHE ASP GLU GLU GLY          
SEQRES   8 A  378  SER LEU TYR ILE LEU LYS GLY ASP ARG THR ILE GLU PHE          
SEQRES   9 A  378  ASP GLY GLU PHE ALA ALA ASP VAL LEU VAL GLU PHE LEU          
SEQRES  10 A  378  LEU ASP LEU ILE GLU ASP PRO VAL GLU ILE ILE SER SER          
SEQRES  11 A  378  LYS LEU GLU VAL GLN ALA PHE GLU ARG ILE GLU ASP TYR          
SEQRES  12 A  378  ILE LYS LEU ILE GLY PHE PHE LYS SER GLU ASP SER GLU          
SEQRES  13 A  378  TYR TYR LYS ALA PHE GLU GLU ALA ALA GLU HIS PHE GLN          
SEQRES  14 A  378  PRO TYR ILE LYS PHE PHE ALA THR PHE ASP LYS GLY VAL          
SEQRES  15 A  378  ALA LYS LYS LEU SER LEU LYS MET ASN GLU VAL ASP PHE          
SEQRES  16 A  378  TYR GLU PRO PHE MET ASP GLU PRO ILE ALA ILE PRO ASN          
SEQRES  17 A  378  LYS PRO TYR THR GLU GLU GLU LEU VAL GLU PHE VAL LYS          
SEQRES  18 A  378  GLU HIS GLN ARG PRO THR LEU ARG ARG LEU ARG PRO GLU          
SEQRES  19 A  378  GLU MET PHE GLU THR TRP GLU ASP ASP LEU ASN GLY ILE          
SEQRES  20 A  378  HIS ILE VAL ALA PHE ALA GLU LYS SER ASP PRO ASP GLY          
SEQRES  21 A  378  TYR GLU PHE LEU GLU ILE LEU LYS GLN VAL ALA ARG ASP          
SEQRES  22 A  378  ASN THR ASP ASN PRO ASP LEU SER ILE LEU TRP ILE ASP          
SEQRES  23 A  378  PRO ASP ASP PHE PRO LEU LEU VAL ALA TYR TRP GLU LYS          
SEQRES  24 A  378  THR PHE LYS ILE ASP LEU PHE ARG PRO GLN ILE GLY VAL          
SEQRES  25 A  378  VAL ASN VAL THR ASP ALA ASP SER VAL TRP MET GLU ILE          
SEQRES  26 A  378  PRO ASP ASP ASP ASP LEU PRO THR ALA GLU GLU LEU GLU          
SEQRES  27 A  378  ASP TRP ILE GLU ASP VAL LEU SER GLY LYS ILE ASN THR          
SEQRES  28 A  378  GLU ASP ASP ASP GLU ASP ASP ASP ASP ASP ASP ASN SER          
SEQRES  29 A  378  ASP GLU GLU ASP ASN ASP ASP SER ASP ASP ASP ASP ASP          
SEQRES  30 A  378  GLU                                                          
HELIX    1   1 SER A 1019  TYR A 1030  1                                  12    
HELIX    2   2 VAL A 1046  GLU A 1066  1                                  21    
HELIX    3   3 LYS A 1078  LYS A 1085  1                                   8    
HELIX    4   4 ALA A 1111  ILE A 1123  1                                  13    
HELIX    5   5 SER A 1132  GLU A 1140  1                                   9    
HELIX    6   6 SER A 1157  PHE A 1170  1                                  14    
HELIX    7   7 ASP A 1181  SER A 1189  1                                   9    
HELIX    8   8 THR A 1214  GLN A 1226  1                                  13    
HELIX    9   9 GLU A 1236  ASP A 1244  1                                   9    
HELIX   10  10 ASP A 1259  ASN A 1276  1                                  18    
HELIX   11  11 PHE A 1292  PHE A 1303  1                                  12    
HELIX   12  12 THR A 1335  GLU A 1344  1                                  10    
SHEET    1  AA 5 VAL A1016  LEU A1018  0                                        
SHEET    2  AA 5 ILE A1070  VAL A1075  1  O  PHE A1072   N  VAL A1016           
SHEET    3  AA 5 LEU A1032  TYR A1037  1  O  LEU A1032   N  GLY A1071           
SHEET    4  AA 5 LEU A1095  LEU A1098 -1  O  TYR A1096   N  LEU A1035           
SHEET    5  AA 5 THR A1103  ILE A1104 -1  O  ILE A1104   N  ILE A1097           
SHEET    1  AB 5 GLU A1128  ILE A1130  0                                        
SHEET    2  AB 5 PHE A1177  THR A1179  1  O  ALA A1178   N  ILE A1130           
SHEET    3  AB 5 LYS A1147  PHE A1151  1  O  LEU A1148   N  PHE A1177           
SHEET    4  AB 5 VAL A1195  TYR A1198 -1  O  ASP A1196   N  ILE A1149           
SHEET    5  AB 5 PRO A1205  ILE A1208 -1  O  ILE A1206   N  PHE A1197           
SHEET    1  AC 5 LEU A1230  ARG A1232  0                                        
SHEET    2  AC 5 ILE A1284  ILE A1287  1  O  ILE A1284   N  ARG A1231           
SHEET    3  AC 5 ILE A1249  PHE A1254  1  O  ILE A1251   N  LEU A1285           
SHEET    4  AC 5 GLN A1311  ASN A1316 -1  O  GLN A1311   N  PHE A1254           
SHEET    5  AC 5 SER A1322  VAL A1323 -1  O  VAL A1323   N  VAL A1314           
CISPEP   1 PHE A 1006    PRO A 1007          0       -12.37                     
CISPEP   2 ILE A 1327    PRO A 1328          0        13.22                     
CRYST1  150.650  150.650  227.470  90.00  90.00  90.00 I 41 2 2     16          
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      0.006638  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006638  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004396        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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