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Database: PDB
Entry: 4Y1T
LinkDB: 4Y1T
Original site: 4Y1T 
HEADER    IMMUNE SYSTEM                           09-FEB-15   4Y1T              
TITLE     STRUCTURAL BASIS FOR CA2+-MEDIATED INTERACTION OF THE PERFORIN C2     
TITLE    2 DOMAIN WITH LIPID MEMBRANES                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PERFORIN-1;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C2 DOMAIN (UNP RESIDUES 410-535);                          
COMPND   5 SYNONYM: P1,CYTOLYSIN,LYMPHOCYTE PORE-FORMING PROTEIN;               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRF1, PFP;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10F`;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCOMB3X                                   
KEYWDS    PERFORIN, C2 DOMAIN, CALCIUM BINDING, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.CONROY,H.YAGI,J.C.WHISSTOCK,R.S.NORTON                            
REVDAT   3   28-OCT-15 4Y1T    1       JRNL                                     
REVDAT   2   09-SEP-15 4Y1T    1       JRNL                                     
REVDAT   1   02-SEP-15 4Y1T    0                                                
JRNL        AUTH   H.YAGI,P.J.CONROY,E.W.LEUNG,R.H.LAW,J.A.TRAPANI,             
JRNL        AUTH 2 I.VOSKOBOINIK,J.C.WHISSTOCK,R.S.NORTON                       
JRNL        TITL   STRUCTURAL BASIS FOR CA2+-MEDIATED INTERACTION OF THE        
JRNL        TITL 2 PERFORIN C2 DOMAIN WITH LIPID MEMBRANES.                     
JRNL        REF    J.BIOL.CHEM.                  V. 290 25213 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26306037                                                     
JRNL        DOI    10.1074/JBC.M115.668384                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 5114                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.340                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 273                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.3882 -  3.3584    1.00     2508   118  0.1656 0.2054        
REMARK   3     2  3.3584 -  2.6657    0.99     2333   155  0.1738 0.2274        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.120           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002            991                                  
REMARK   3   ANGLE     :  0.648           1345                                  
REMARK   3   CHIRALITY :  0.025            145                                  
REMARK   3   PLANARITY :  0.003            179                                  
REMARK   3   DIHEDRAL  : 10.161            339                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y1T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206706.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.953697                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA, XSCALE                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5115                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.666                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.388                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.2500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18200                            
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: 3NSJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 0.2 M         
REMARK 280  CALCIUM CHLORIDE DIHYDRATE AND 14% V/V POLYETHYLENE GLYCOL 400,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+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        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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       22.50450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.91400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.95950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       22.50450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.91400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.95950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       22.50450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       29.91400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.95950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       22.50450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       29.91400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.95950            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 708  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 721  LIES ON A SPECIAL POSITION.                          
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     GLY A   536                                                      
REMARK 465     GLN A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     GLY A   539                                                      
REMARK 465     GLN A   540                                                      
REMARK 465     HIS A   541                                                      
REMARK 465     HIS A   542                                                      
REMARK 465     HIS A   543                                                      
REMARK 465     HIS A   544                                                      
REMARK 465     HIS A   545                                                      
REMARK 465     HIS A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     ALA A   548                                                      
REMARK 465     TYR A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     TYR A   551                                                      
REMARK 465     ASP A   552                                                      
REMARK 465     VAL A   553                                                      
REMARK 465     PRO A   554                                                      
REMARK 465     ASP A   555                                                      
REMARK 465     TYR A   556                                                      
REMARK 465     ALA A   557                                                      
REMARK 465     SER A   558                                                      
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 411    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 515    CZ   NH1  NH2                                       
REMARK 470     HIS A 527    CG   ND1  CD2  CE1  NE2                             
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 435       76.02   -113.27                                   
REMARK 500    GLU A 467     -146.52     59.58                                   
REMARK 500    ALA A 488     -101.92     62.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 428   O                                                      
REMARK 620 2 ASP A 429   OD1  77.4                                              
REMARK 620 3 ASP A 483   OD2  86.2  76.6                                        
REMARK 620 4 ASP A 485   OD1 148.6  74.3  74.1                                  
REMARK 620 5 ASP A 485   OD2 160.2 122.3  99.3  50.2                            
REMARK 620 6 ASP A 491   OD2  86.8 159.7  89.9 116.8  74.3                      
REMARK 620 7 HOH A 723   O   104.1  77.1 148.8  82.8  80.9 119.6                
REMARK 620 8 HOH A 752   O    73.9 110.8 156.1 129.4  95.5  76.2  52.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 429   OD1                                                    
REMARK 620 2 ASP A 429   OD2  52.2                                              
REMARK 620 3 ASP A 435   OD2 119.7  67.7                                        
REMARK 620 4 ASP A 483   OD1  90.8  94.9  90.0                                  
REMARK 620 5 ASP A 483   OD2  73.3 115.2 139.0  49.5                            
REMARK 620 6 ALA A 484   O   161.0 144.4  78.3  95.4  97.2                      
REMARK 620 7 ASP A 485   OD1  74.7 115.8 146.3 121.7  72.4  86.9                
REMARK 620 8 HOH A 705   O    94.1  76.6  74.8 164.5 146.0  84.8  73.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 429   OD2                                                    
REMARK 620 2 THR A 432   OG1  78.9                                              
REMARK 620 3 ALA A 433   O    88.1  92.5                                        
REMARK 620 4 ASP A 435   OD1 113.5 167.5  87.0                                  
REMARK 620 5 ASP A 435   OD2  70.2 139.7 111.3  51.0                            
REMARK 620 6 ASN A 454   OD1 164.3  87.7  84.3  79.8 125.4                      
REMARK 620 7 GLU A 467   OE2  92.6 171.2  85.0  21.0  35.9 100.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 485   OD2                                                    
REMARK 620 2 ASP A 489   O    90.3                                              
REMARK 620 3 ASP A 491   OD1  93.2  97.7                                        
REMARK 620 4 HOH A 718   O    77.0 166.4  87.8                                  
REMARK 620 5 HOH A 707   O    81.3  85.5 173.7  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 488   O                                                      
REMARK 620 2 ASP A 490   OD1  71.4                                              
REMARK 620 3 HOH A 761   O   146.0  92.3                                        
REMARK 620 4 HOH A 714   O   148.7  83.3  50.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 605                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Y1S   RELATED DB: PDB                                   
DBREF  4Y1T A  410   535  UNP    P10820   PERF_MOUSE     410    535             
SEQADV 4Y1T ALA A  427  UNP  P10820    TRP   427 ENGINEERED MUTATION            
SEQADV 4Y1T ALA A  430  UNP  P10820    TYR   430 ENGINEERED MUTATION            
SEQADV 4Y1T ALA A  486  UNP  P10820    TYR   486 ENGINEERED MUTATION            
SEQADV 4Y1T ALA A  488  UNP  P10820    TRP   488 ENGINEERED MUTATION            
SEQADV 4Y1T GLY A  536  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T GLN A  537  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T ALA A  538  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T GLY A  539  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T GLN A  540  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  541  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  542  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  543  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  544  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  545  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T HIS A  546  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T GLY A  547  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T ALA A  548  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T TYR A  549  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T PRO A  550  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T TYR A  551  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T ASP A  552  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T VAL A  553  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T PRO A  554  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T ASP A  555  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T TYR A  556  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T ALA A  557  UNP  P10820              EXPRESSION TAG                 
SEQADV 4Y1T SER A  558  UNP  P10820              EXPRESSION TAG                 
SEQRES   1 A  149  GLN ARG GLY LEU ALA HIS LEU VAL VAL SER ASN PHE ARG          
SEQRES   2 A  149  ALA GLU HIS LEU ALA GLY ASP ALA THR THR ALA THR ASP          
SEQRES   3 A  149  ALA TYR LEU LYS VAL PHE PHE GLY GLY GLN GLU PHE ARG          
SEQRES   4 A  149  THR GLY VAL VAL TRP ASN ASN ASN ASN PRO ARG TRP THR          
SEQRES   5 A  149  ASP LYS MET ASP PHE GLU ASN VAL LEU LEU SER THR GLY          
SEQRES   6 A  149  GLY PRO LEU ARG VAL GLN VAL TRP ASP ALA ASP ALA GLY          
SEQRES   7 A  149  ALA ASP ASP ASP LEU LEU GLY SER CYS ASP ARG SER PRO          
SEQRES   8 A  149  HIS SER GLY PHE HIS GLU VAL THR CYS GLU LEU ASN HIS          
SEQRES   9 A  149  GLY ARG VAL LYS PHE SER TYR HIS ALA LYS CYS LEU PRO          
SEQRES  10 A  149  HIS LEU THR GLY GLY THR CYS LEU GLU GLY GLN ALA GLY          
SEQRES  11 A  149  GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR PRO TYR ASP          
SEQRES  12 A  149  VAL PRO ASP TYR ALA SER                                      
HET     CA  A 601       1                                                       
HET     CA  A 602       1                                                       
HET     CA  A 603       1                                                       
HET     CA  A 604       1                                                       
HET     CA  A 605       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    5(CA 2+)                                                     
FORMUL   7  HOH   *63(H2 O)                                                     
SHEET    1 AA1 3 ARG A 459  TRP A 460  0                                        
SHEET    2 AA1 3 LEU A 413  GLU A 424 -1  N  PHE A 421   O  TRP A 460           
SHEET    3 AA1 3 MET A 464  LEU A 470 -1  O  MET A 464   N  VAL A 418           
SHEET    1 AA2 4 ARG A 459  TRP A 460  0                                        
SHEET    2 AA2 4 LEU A 413  GLU A 424 -1  N  PHE A 421   O  TRP A 460           
SHEET    3 AA2 4 ARG A 515  CYS A 524 -1  O  LYS A 517   N  ARG A 422           
SHEET    4 AA2 4 GLY A 503  GLU A 510 -1  N  VAL A 507   O  PHE A 518           
SHEET    1 AA3 4 GLN A 445  ARG A 448  0                                        
SHEET    2 AA3 4 ALA A 436  PHE A 442 -1  N  PHE A 442   O  GLN A 445           
SHEET    3 AA3 4 LEU A 477  ASP A 483 -1  O  ARG A 478   N  PHE A 441           
SHEET    4 AA3 4 ASP A 491  ARG A 498 -1  O  ARG A 498   N  LEU A 477           
SSBOND   1 CYS A  496    CYS A  509                          1555   1555  2.03  
SSBOND   2 CYS A  524    CYS A  533                          1555   1555  2.03  
LINK         O   GLY A 428                CA    CA A 604     1555   1555  2.41  
LINK         OD1 ASP A 429                CA    CA A 601     1555   1555  2.42  
LINK         OD1 ASP A 429                CA    CA A 604     1555   1555  2.39  
LINK         OD2 ASP A 429                CA    CA A 603     1555   1555  2.41  
LINK         OD2 ASP A 429                CA    CA A 601     1555   1555  2.56  
LINK         OG1 THR A 432                CA    CA A 603     1555   1555  2.52  
LINK         O   ALA A 433                CA    CA A 603     1555   1555  2.37  
LINK         OD1 ASP A 435                CA    CA A 603     1555   1555  2.57  
LINK         OD2 ASP A 435                CA    CA A 603     1555   1555  2.53  
LINK         OD2 ASP A 435                CA    CA A 601     1555   1555  2.55  
LINK         OD1 ASN A 454                CA    CA A 603     1555   1555  2.41  
LINK         OD1 ASP A 483                CA    CA A 601     1555   1555  2.64  
LINK         OD2 ASP A 483                CA    CA A 601     1555   1555  2.61  
LINK         OD2 ASP A 483                CA    CA A 604     1555   1555  2.46  
LINK         O   ALA A 484                CA    CA A 601     1555   1555  2.61  
LINK         OD1 ASP A 485                CA    CA A 601     1555   1555  2.51  
LINK         OD1 ASP A 485                CA    CA A 604     1555   1555  2.56  
LINK         OD2 ASP A 485                CA    CA A 604     1555   1555  2.61  
LINK         OD2 ASP A 485                CA    CA A 602     1555   1555  2.35  
LINK         O   ALA A 488                CA    CA A 605     1555   1555  2.42  
LINK         O   ASP A 489                CA    CA A 602     1555   1555  2.88  
LINK         OD1 ASP A 490                CA    CA A 605     1555   1555  2.75  
LINK         OD1 ASP A 491                CA    CA A 602     1555   1555  2.41  
LINK         OD2 ASP A 491                CA    CA A 604     1555   1555  2.35  
LINK        CA    CA A 602                 O   HOH A 718     1555   1555  2.45  
LINK        CA    CA A 604                 O   HOH A 723     1555   1555  2.72  
LINK        CA    CA A 604                 O   HOH A 752     1555   1555  2.46  
LINK        CA    CA A 605                 O   HOH A 761     1555   1555  2.47  
LINK        CA    CA A 605                 O   HOH A 714     1555   1555  2.99  
LINK         OE2 GLU A 467                CA    CA A 603     1555   7444  2.38  
LINK        CA    CA A 601                 O   HOH A 705     1555   7454  2.46  
LINK        CA    CA A 602                 O   HOH A 707     1555   7454  2.48  
SITE     1 AC1  7 ASP A 429  ASP A 435  ASP A 483  ALA A 484                    
SITE     2 AC1  7 ASP A 485   CA A 604  HOH A 705                               
SITE     1 AC2  5 ASP A 485  ASP A 489  ASP A 491  HOH A 707                    
SITE     2 AC2  5 HOH A 718                                                     
SITE     1 AC3  6 ASP A 429  THR A 432  ALA A 433  ASP A 435                    
SITE     2 AC3  6 ASN A 454  GLU A 467                                          
SITE     1 AC4  8 GLY A 428  ASP A 429  ASP A 483  ASP A 485                    
SITE     2 AC4  8 ASP A 491   CA A 601  HOH A 723  HOH A 752                    
SITE     1 AC5  5 ASP A 485  ALA A 488  ASP A 490  HOH A 714                    
SITE     2 AC5  5 HOH A 761                                                     
CRYST1   45.009   59.828  125.919  90.00  90.00  90.00 I 2 2 2       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      0.022218  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016715  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007942        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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