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Database: PDB
Entry: 2ZBD
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Original site: 2ZBD 
HEADER    HYDROLASE                               20-OCT-07   2ZBD              
TITLE     CRYSTAL STRUCTURE OF THE SR CALCIUM PUMP WITH BOUND ALUMINIUM         
TITLE    2 FLUORIDE, ADP AND CALCIUM                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CALCIUM PUMP 1, SERCA1, SR CA(2+)-ATPASE 1, CALCIUM-        
COMPND   5 TRANSPORTING ATPASE SARCOPLASMIC RETICULUM TYPE, FAST TWITCH SKELETAL
COMPND   6 MUSCLE ISOFORM, ENDOPLASMIC RETICULUM CLASS 1/2 CA(2+) ATPASE;       
COMPND   7 EC: 3.6.3.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 TISSUE: SKELETAL MUSCLE (WHITE)                                      
KEYWDS    MEMBRANE PROTEIN, P-TYPE ATPASE, HAD FOLD, ALTERNATIVE SPLICING, ATP- 
KEYWDS   2 BINDING, CALCIUM, CALCIUM TRANSPORT, ENDOPLASMIC RETICULUM,          
KEYWDS   3 HYDROLASE, ION TRANSPORT, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-      
KEYWDS   4 BINDING, PHOSPHORYLATION, SARCOPLASMIC RETICULUM, TRANSMEMBRANE,     
KEYWDS   5 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TOYOSHIMA,H.NOMURA,T.TSUDA,H.OGAWA,Y.NORIMATSU                      
REVDAT   3   01-NOV-23 2ZBD    1       REMARK LINK                              
REVDAT   2   24-FEB-09 2ZBD    1       VERSN                                    
REVDAT   1   20-NOV-07 2ZBD    0                                                
SPRSDE     20-NOV-07 2ZBD      2Z9R                                             
JRNL        AUTH   C.TOYOSHIMA,H.NOMURA,T.TSUDA                                 
JRNL        TITL   LUMENAL GATING MECHANISM REVEALED IN CALCIUM PUMP CRYSTAL    
JRNL        TITL 2 STRUCTURES WITH PHOSPHATE ANALOGUES                          
JRNL        REF    NATURE                        V. 432   361 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15448704                                                     
JRNL        DOI    10.1038/NATURE02981                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.TOYOSHIMA,M.NAKASAKO,H.NOMURA,H.OGAWA                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CALCIUM PUMP OF SARCOPLASMIC        
REMARK   1  TITL 2 RETICULUM AT 2.6 A RESOLUTION                                
REMARK   1  REF    NATURE                        V. 405   647 2000              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   10864315                                                     
REMARK   1  DOI    10.1038/35015017                                             
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.TOYOSHIMA,H.NOMURA                                         
REMARK   1  TITL   STRUCTURAL CHANGES IN THE CALCIUM PUMP ACCOMPANYING THE      
REMARK   1  TITL 2 DISSOCIATION OF CALCIUM                                      
REMARK   1  REF    NATURE                        V. 418   605 2002              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   12167852                                                     
REMARK   1  DOI    10.1038/NATURE00944                                          
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.TOYOSHIMA,T.MIZUTANI                                       
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CALCIUM PUMP WITH A BOUND ATP       
REMARK   1  TITL 2 ANALOGUE                                                     
REMARK   1  REF    NATURE                        V. 430   529 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15229613                                                     
REMARK   1  DOI    10.1038/NATURE02680                                          
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   K.OBARA,N.MIYASHITA,C.XU,I.TOYOSHIMA,Y.SUGITA,G.INESI,       
REMARK   1  AUTH 2 C.TOYOSHIMA                                                  
REMARK   1  TITL   STRUCTURAL ROLE OF COUNTERTRANSPORT REVEALED IN CA(2+) PUMP  
REMARK   1  TITL 2 CRYSTAL STRUCTURE IN THE ABSENCE OF CA(2+)                   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 102 14489 2005              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   16150713                                                     
REMARK   1  DOI    10.1073/PNAS.0506222102                                      
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.TAKAHASHI,Y.KONDOU,C.TOYOSHIMA                             
REMARK   1  TITL   INTERDOMAIN COMMUNICATION IN CALCIUM PUMP AS REVEALED IN THE 
REMARK   1  TITL 2 CRYSTAL STRUCTURES WITH TRANSMEMBRANE INHIBITORS             
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 104  5800 2007              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   17389383                                                     
REMARK   1  DOI    10.1073/PNAS.0700979104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 58265                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3093                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2663                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7674                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.73000                                             
REMARK   3    B22 (A**2) : 12.10000                                             
REMARK   3    B33 (A**2) : -11.31000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.97000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.328         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.246         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.182        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7954 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10770 ; 1.010 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   993 ; 4.722 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   319 ;35.696 ;24.357       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1382 ;16.348 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;16.924 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1245 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5816 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3774 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5525 ; 0.293 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   271 ; 0.118 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     8 ; 0.096 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.094 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.109 ; 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):  5112 ; 0.407 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8013 ; 0.607 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3216 ; 0.602 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2757 ; 0.969 ; 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  : 6                                          
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    45        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.0212  16.1036   7.2371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0241 T22:   0.4233                                     
REMARK   3      T33:  -0.2472 T12:   0.1112                                     
REMARK   3      T13:   0.0008 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2821 L22:   1.2492                                     
REMARK   3      L33:  16.4936 L12:   1.5200                                     
REMARK   3      L13:   8.8305 L23:   1.5349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5975 S12:   0.6130 S13:  -0.7648                       
REMARK   3      S21:   0.0124 S22:   0.3864 S23:  -0.1034                       
REMARK   3      S31:   1.8220 S32:   0.5476 S33:  -0.9839                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   238        A   329                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.8679  21.8503   6.9987              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1306 T22:   0.7229                                     
REMARK   3      T33:  -0.3599 T12:  -0.0636                                     
REMARK   3      T13:   0.0193 T23:   0.1502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7046 L22:   1.0569                                     
REMARK   3      L33:  11.2157 L12:   0.3513                                     
REMARK   3      L13:   5.3166 L23:   1.2923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3819 S12:   0.5868 S13:  -0.4131                       
REMARK   3      S21:   0.1382 S22:   0.2142 S23:   0.0584                       
REMARK   3      S31:   1.1708 S32:  -0.5869 S33:  -0.5961                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   751        A   994                          
REMARK   3    RESIDUE RANGE :   A   995        A   996                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.4507  38.7967  -0.5729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0667 T22:   0.6939                                     
REMARK   3      T33:  -0.5413 T12:   0.1655                                     
REMARK   3      T13:   0.0230 T23:   0.2485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2195 L22:   1.5629                                     
REMARK   3      L33:   9.1425 L12:   0.0803                                     
REMARK   3      L13:   0.9615 L23:   1.0822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1994 S12:   0.5720 S13:   0.0627                       
REMARK   3      S21:  -0.1741 S22:   0.1194 S23:   0.1065                       
REMARK   3      S31:  -1.1526 S32:  -0.7670 S33:   0.0801                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    44                          
REMARK   3    RESIDUE RANGE :   A   123        A   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.3975   3.9435  52.0783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0902 T22:  -0.2485                                     
REMARK   3      T33:   0.3358 T12:   0.2261                                     
REMARK   3      T13:  -0.2175 T23:  -0.2091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6627 L22:   1.5749                                     
REMARK   3      L33:   2.7531 L12:  -0.0754                                     
REMARK   3      L13:   0.1395 L23:  -0.2840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4793 S12:   0.6641 S13:  -0.8461                       
REMARK   3      S21:  -0.2493 S22:  -0.3380 S23:   0.3404                       
REMARK   3      S31:   0.5943 S32:   0.2922 S33:  -0.1413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   330        A   364                          
REMARK   3    RESIDUE RANGE :   A   601        A   750                          
REMARK   3    RESIDUE RANGE :   A   998        A   998                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6244  34.5452  48.1159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0316 T22:  -0.2831                                     
REMARK   3      T33:   0.0285 T12:   0.1360                                     
REMARK   3      T13:   0.0663 T23:   0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2287 L22:   0.0414                                     
REMARK   3      L33:   4.7331 L12:   0.2219                                     
REMARK   3      L13:   0.7829 L23:  -0.2157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2315 S12:   0.4822 S13:   0.0737                       
REMARK   3      S21:   0.1510 S22:  -0.1677 S23:   0.0268                       
REMARK   3      S31:  -0.3579 S32:  -0.0254 S33:  -0.0639                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   365        A   600                          
REMARK   3    RESIDUE RANGE :   A   997        A   997                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.0994  27.9923  73.0619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0221 T22:  -0.2449                                     
REMARK   3      T33:   0.0421 T12:  -0.1764                                     
REMARK   3      T13:  -0.0168 T23:   0.0865                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0833 L22:   0.5097                                     
REMARK   3      L33:   2.5019 L12:  -0.3684                                     
REMARK   3      L13:   0.1176 L23:   0.3327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2570 S12:  -0.3002 S13:  -0.1844                       
REMARK   3      S21:   0.0241 S22:  -0.2313 S23:  -0.0568                       
REMARK   3      S31:  -0.1103 S32:   0.2369 S33:  -0.0257                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000027757.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.10                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : ROTATED-INCLINED DOUBLE- CRYSTAL   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61807                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1WPE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PH 6.10, MICRODIALYSIS,         
REMARK 280  TEMPERATURE 283K                                                    
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       81.45000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       81.45000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   351    AL    ALF A   998              1.86            
REMARK 500  AL    ALF A   998     O3B  ADP A  1002              1.96            
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    LYS A  47      -93.80    -77.51                                   
REMARK 500    LEU A  49       42.30   -100.71                                   
REMARK 500    GLU A  82      -76.06    -59.69                                   
REMARK 500    GLU A  83       58.52    -93.74                                   
REMARK 500    VAL A 155      128.74    -36.98                                   
REMARK 500    LEU A 180      -71.29   -108.17                                   
REMARK 500    GLN A 238      -64.43   -125.05                                   
REMARK 500    ALA A 240       52.32    -93.55                                   
REMARK 500    THR A 388     -166.48    -79.33                                   
REMARK 500    PRO A 391       38.44    -71.55                                   
REMARK 500    LYS A 502       44.04     72.54                                   
REMARK 500    SER A 503      -64.35   -135.39                                   
REMARK 500    SER A 504      -70.06   -110.73                                   
REMARK 500    VAL A 508      -77.69    -66.25                                   
REMARK 500    THR A 558       63.26     37.57                                   
REMARK 500    GLU A 588       55.48   -105.55                                   
REMARK 500    ASP A 601       85.77   -152.94                                   
REMARK 500    MET A 857      -88.74   -100.00                                   
REMARK 500    ALA A 859      102.21    -56.09                                   
REMARK 500    HIS A 872       78.02   -116.94                                   
REMARK 500    MET A 874       36.29    -87.38                                   
REMARK 500    CYS A 888       39.50    -90.87                                   
REMARK 500    GLU A 889        6.74   -154.32                                   
REMARK 500    LEU A 992     -101.18    -77.46                                   
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 996  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 304   O                                                      
REMARK 620 2 ALA A 305   O    80.9                                              
REMARK 620 3 ILE A 307   O    92.6 112.9                                        
REMARK 620 4 GLU A 309   OE1 111.5 166.0  74.0                                  
REMARK 620 5 GLU A 309   OE2  64.0 141.8  84.7  48.3                            
REMARK 620 6 ASN A 796   OD1  75.6  86.2 156.0  90.6  71.3                      
REMARK 620 7 ASP A 800   OD2 153.2  77.1 109.9  89.2 130.4  87.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 351   OD2                                                    
REMARK 620 2 THR A 353   O    84.6                                              
REMARK 620 3 ASP A 703   OD1  73.3  88.2                                        
REMARK 620 4 HOH A1038   O    85.3 165.4  78.8                                  
REMARK 620 5 HOH A1041   O   163.2  78.7 107.4 111.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 995  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 768   OD1                                                    
REMARK 620 2 GLU A 771   OE2  87.4                                              
REMARK 620 3 THR A 799   OG1 162.5  98.8                                        
REMARK 620 4 ASP A 800   OD1  84.9 144.3  80.6                                  
REMARK 620 5 GLU A 908   OE2 125.3  77.0  72.2 134.3                            
REMARK 620 6 HOH A1014   O    81.3  71.4  85.2  73.0 137.6                      
REMARK 620 7 HOH A1015   O   101.1 142.1  84.1  73.6  67.9 146.1                
REMARK 620 N                    1     2     3     4     5     6                 
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 995                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 996                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 1012                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SU4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND CALCIUM                                  
REMARK 900 RELATED ID: 1IWO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT CALCIUM                                     
REMARK 900 RELATED ID: 1VFP   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND AMPPCP AND CALCIUM                       
REMARK 900 RELATED ID: 1WPG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND MAGNESIUM FLUORIDE AND THAPSIGARGIN IN   
REMARK 900 THE ABSENCE OF CALCIUM                                               
REMARK 900 RELATED ID: 2AGV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND BHQ AND THAPSIGARGIN IN THE ABSENCE OF   
REMARK 900 CALCIUM                                                              
REMARK 900 RELATED ID: 2DQS   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND AMPPCP IN THE ABSENCE OF CALCIUM         
REMARK 900 RELATED ID: 2EAR   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND TG                                       
REMARK 900 RELATED ID: 2EAS   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND CPA                                      
REMARK 900 RELATED ID: 2EAT   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND CPA AND TG                               
REMARK 900 RELATED ID: 2EAU   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND CPA IN THE PRESENCE OF CURCUMIN          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE C-TERMINAL RESIDUES IN UNP ENTRY P04191                          
REMARK 999 ARE FROM 994 TO 1001, DPEDERRK.                                      
REMARK 999 IN ISOFORM SERCA1A, THERE IS ONLY ONE C-TERMINAL                     
REMARK 999 RESIDUE 994 GLY.                                                     
DBREF  2ZBD A    1   993  UNP    P04191   AT2A1_RABIT      1    993             
SEQADV 2ZBD GLY A  994  UNP  P04191              SEE REMARK 999                 
SEQRES   1 A  995  ACE MET GLU ALA ALA HIS SER LYS SER THR GLU GLU CYS          
SEQRES   2 A  995  LEU ALA TYR PHE GLY VAL SER GLU THR THR GLY LEU THR          
SEQRES   3 A  995  PRO ASP GLN VAL LYS ARG HIS LEU GLU LYS TYR GLY HIS          
SEQRES   4 A  995  ASN GLU LEU PRO ALA GLU GLU GLY LYS SER LEU TRP GLU          
SEQRES   5 A  995  LEU VAL ILE GLU GLN PHE GLU ASP LEU LEU VAL ARG ILE          
SEQRES   6 A  995  LEU LEU LEU ALA ALA CYS ILE SER PHE VAL LEU ALA TRP          
SEQRES   7 A  995  PHE GLU GLU GLY GLU GLU THR ILE THR ALA PHE VAL GLU          
SEQRES   8 A  995  PRO PHE VAL ILE LEU LEU ILE LEU ILE ALA ASN ALA ILE          
SEQRES   9 A  995  VAL GLY VAL TRP GLN GLU ARG ASN ALA GLU ASN ALA ILE          
SEQRES  10 A  995  GLU ALA LEU LYS GLU TYR GLU PRO GLU MET GLY LYS VAL          
SEQRES  11 A  995  TYR ARG ALA ASP ARG LYS SER VAL GLN ARG ILE LYS ALA          
SEQRES  12 A  995  ARG ASP ILE VAL PRO GLY ASP ILE VAL GLU VAL ALA VAL          
SEQRES  13 A  995  GLY ASP LYS VAL PRO ALA ASP ILE ARG ILE LEU SER ILE          
SEQRES  14 A  995  LYS SER THR THR LEU ARG VAL ASP GLN SER ILE LEU THR          
SEQRES  15 A  995  GLY GLU SER VAL SER VAL ILE LYS HIS THR GLU PRO VAL          
SEQRES  16 A  995  PRO ASP PRO ARG ALA VAL ASN GLN ASP LYS LYS ASN MET          
SEQRES  17 A  995  LEU PHE SER GLY THR ASN ILE ALA ALA GLY LYS ALA LEU          
SEQRES  18 A  995  GLY ILE VAL ALA THR THR GLY VAL SER THR GLU ILE GLY          
SEQRES  19 A  995  LYS ILE ARG ASP GLN MET ALA ALA THR GLU GLN ASP LYS          
SEQRES  20 A  995  THR PRO LEU GLN GLN LYS LEU ASP GLU PHE GLY GLU GLN          
SEQRES  21 A  995  LEU SER LYS VAL ILE SER LEU ILE CYS VAL ALA VAL TRP          
SEQRES  22 A  995  LEU ILE ASN ILE GLY HIS PHE ASN ASP PRO VAL HIS GLY          
SEQRES  23 A  995  GLY SER TRP ILE ARG GLY ALA ILE TYR TYR PHE LYS ILE          
SEQRES  24 A  995  ALA VAL ALA LEU ALA VAL ALA ALA ILE PRO GLU GLY LEU          
SEQRES  25 A  995  PRO ALA VAL ILE THR THR CYS LEU ALA LEU GLY THR ARG          
SEQRES  26 A  995  ARG MET ALA LYS LYS ASN ALA ILE VAL ARG SER LEU PRO          
SEQRES  27 A  995  SER VAL GLU THR LEU GLY CYS THR SER VAL ILE CYS SER          
SEQRES  28 A  995  ASP LYS THR GLY THR LEU THR THR ASN GLN MET SER VAL          
SEQRES  29 A  995  CYS LYS MET PHE ILE ILE ASP LYS VAL ASP GLY ASP PHE          
SEQRES  30 A  995  CYS SER LEU ASN GLU PHE SER ILE THR GLY SER THR TYR          
SEQRES  31 A  995  ALA PRO GLU GLY GLU VAL LEU LYS ASN ASP LYS PRO ILE          
SEQRES  32 A  995  ARG SER GLY GLN PHE ASP GLY LEU VAL GLU LEU ALA THR          
SEQRES  33 A  995  ILE CYS ALA LEU CYS ASN ASP SER SER LEU ASP PHE ASN          
SEQRES  34 A  995  GLU THR LYS GLY VAL TYR GLU LYS VAL GLY GLU ALA THR          
SEQRES  35 A  995  GLU THR ALA LEU THR THR LEU VAL GLU LYS MET ASN VAL          
SEQRES  36 A  995  PHE ASN THR GLU VAL ARG ASN LEU SER LYS VAL GLU ARG          
SEQRES  37 A  995  ALA ASN ALA CYS ASN SER VAL ILE ARG GLN LEU MET LYS          
SEQRES  38 A  995  LYS GLU PHE THR LEU GLU PHE SER ARG ASP ARG LYS SER          
SEQRES  39 A  995  MET SER VAL TYR CYS SER PRO ALA LYS SER SER ARG ALA          
SEQRES  40 A  995  ALA VAL GLY ASN LYS MET PHE VAL LYS GLY ALA PRO GLU          
SEQRES  41 A  995  GLY VAL ILE ASP ARG CYS ASN TYR VAL ARG VAL GLY THR          
SEQRES  42 A  995  THR ARG VAL PRO MET THR GLY PRO VAL LYS GLU LYS ILE          
SEQRES  43 A  995  LEU SER VAL ILE LYS GLU TRP GLY THR GLY ARG ASP THR          
SEQRES  44 A  995  LEU ARG CYS LEU ALA LEU ALA THR ARG ASP THR PRO PRO          
SEQRES  45 A  995  LYS ARG GLU GLU MET VAL LEU ASP ASP SER SER ARG PHE          
SEQRES  46 A  995  MET GLU TYR GLU THR ASP LEU THR PHE VAL GLY VAL VAL          
SEQRES  47 A  995  GLY MET LEU ASP PRO PRO ARG LYS GLU VAL MET GLY SER          
SEQRES  48 A  995  ILE GLN LEU CYS ARG ASP ALA GLY ILE ARG VAL ILE MET          
SEQRES  49 A  995  ILE THR GLY ASP ASN LYS GLY THR ALA ILE ALA ILE CYS          
SEQRES  50 A  995  ARG ARG ILE GLY ILE PHE GLY GLU ASN GLU GLU VAL ALA          
SEQRES  51 A  995  ASP ARG ALA TYR THR GLY ARG GLU PHE ASP ASP LEU PRO          
SEQRES  52 A  995  LEU ALA GLU GLN ARG GLU ALA CYS ARG ARG ALA CYS CYS          
SEQRES  53 A  995  PHE ALA ARG VAL GLU PRO SER HIS LYS SER LYS ILE VAL          
SEQRES  54 A  995  GLU TYR LEU GLN SER TYR ASP GLU ILE THR ALA MET THR          
SEQRES  55 A  995  GLY ASP GLY VAL ASN ASP ALA PRO ALA LEU LYS LYS ALA          
SEQRES  56 A  995  GLU ILE GLY ILE ALA MET GLY SER GLY THR ALA VAL ALA          
SEQRES  57 A  995  LYS THR ALA SER GLU MET VAL LEU ALA ASP ASP ASN PHE          
SEQRES  58 A  995  SER THR ILE VAL ALA ALA VAL GLU GLU GLY ARG ALA ILE          
SEQRES  59 A  995  TYR ASN ASN MET LYS GLN PHE ILE ARG TYR LEU ILE SER          
SEQRES  60 A  995  SER ASN VAL GLY GLU VAL VAL CYS ILE PHE LEU THR ALA          
SEQRES  61 A  995  ALA LEU GLY LEU PRO GLU ALA LEU ILE PRO VAL GLN LEU          
SEQRES  62 A  995  LEU TRP VAL ASN LEU VAL THR ASP GLY LEU PRO ALA THR          
SEQRES  63 A  995  ALA LEU GLY PHE ASN PRO PRO ASP LEU ASP ILE MET ASP          
SEQRES  64 A  995  ARG PRO PRO ARG SER PRO LYS GLU PRO LEU ILE SER GLY          
SEQRES  65 A  995  TRP LEU PHE PHE ARG TYR MET ALA ILE GLY GLY TYR VAL          
SEQRES  66 A  995  GLY ALA ALA THR VAL GLY ALA ALA ALA TRP TRP PHE MET          
SEQRES  67 A  995  TYR ALA GLU ASP GLY PRO GLY VAL THR TYR HIS GLN LEU          
SEQRES  68 A  995  THR HIS PHE MET GLN CYS THR GLU ASP HIS PRO HIS PHE          
SEQRES  69 A  995  GLU GLY LEU ASP CYS GLU ILE PHE GLU ALA PRO GLU PRO          
SEQRES  70 A  995  MET THR MET ALA LEU SER VAL LEU VAL THR ILE GLU MET          
SEQRES  71 A  995  CYS ASN ALA LEU ASN SER LEU SER GLU ASN GLN SER LEU          
SEQRES  72 A  995  MET ARG MET PRO PRO TRP VAL ASN ILE TRP LEU LEU GLY          
SEQRES  73 A  995  SER ILE CYS LEU SER MET SER LEU HIS PHE LEU ILE LEU          
SEQRES  74 A  995  TYR VAL ASP PRO LEU PRO MET ILE PHE LYS LEU LYS ALA          
SEQRES  75 A  995  LEU ASP LEU THR GLN TRP LEU MET VAL LEU LYS ILE SER          
SEQRES  76 A  995  LEU PRO VAL ILE GLY LEU ASP GLU ILE LEU LYS PHE ILE          
SEQRES  77 A  995  ALA ARG ASN TYR LEU GLU GLY                                  
HET    ACE  A   0       3                                                       
HET     CA  A 995       1                                                       
HET     CA  A 996       1                                                       
HET     MG  A 997       1                                                       
HET    ALF  A 998       5                                                       
HET     MG  A1001       1                                                       
HET    ADP  A1002      27                                                       
HET    PC1  A1011      54                                                       
HET    PC1  A1012      54                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  ALF    AL F4 1-                                                     
FORMUL   7  ADP    C10 H15 N5 O10 P2                                            
FORMUL   8  PC1    2(C44 H88 N O8 P)                                            
FORMUL  10  HOH   *98(H2 O)                                                     
HELIX    1   1 SER A    8  GLY A   17  1                                  10    
HELIX    2   2 THR A   25  GLY A   37  1                                  13    
HELIX    3   3 LEU A   49  LEU A   49  1                                   1    
HELIX    4   4 TRP A   50  PHE A   57  1                                   8    
HELIX    5   5 ASP A   59  LEU A   75  1                                  17    
HELIX    6   6 GLU A   80  GLU A   82  5                                   3    
HELIX    7   7 GLU A   83  GLU A  123  1                                  41    
HELIX    8   8 ARG A  143  ILE A  145  5                                   3    
HELIX    9   9 GLN A  177  GLY A  182  1                                   6    
HELIX   10  10 THR A  226  THR A  230  5                                   5    
HELIX   11  11 THR A  247  LEU A  273  1                                  27    
HELIX   12  12 ASN A  275  PHE A  279  5                                   5    
HELIX   13  13 ILE A  289  ILE A  307  1                                  19    
HELIX   14  14 GLY A  310  LYS A  329  1                                  20    
HELIX   15  15 PRO A  337  THR A  345  1                                   9    
HELIX   16  16 ARG A  403  GLN A  406  5                                   4    
HELIX   17  17 PHE A  407  CYS A  420  1                                  14    
HELIX   18  18 GLU A  439  MET A  452  1                                  14    
HELIX   19  19 SER A  463  ALA A  468  1                                   6    
HELIX   20  20 ASN A  469  GLN A  477  1                                   9    
HELIX   21  21 SER A  504  VAL A  508  5                                   5    
HELIX   22  22 ALA A  517  ARG A  524  1                                   8    
HELIX   23  23 THR A  538  GLY A  555  1                                  18    
HELIX   24  24 LYS A  572  MET A  576  5                                   5    
HELIX   25  25 ARG A  583  GLU A  588  1                                   6    
HELIX   26  26 GLU A  606  ALA A  617  1                                  12    
HELIX   27  27 ASN A  628  ILE A  639  1                                  12    
HELIX   28  28 GLY A  655  ASP A  660  1                                   6    
HELIX   29  29 PRO A  662  ALA A  673  1                                  12    
HELIX   30  30 GLU A  680  SER A  693  1                                  14    
HELIX   31  31 GLY A  704  ASN A  706  5                                   3    
HELIX   32  32 ASP A  707  ALA A  714  1                                   8    
HELIX   33  33 THR A  724  ALA A  730  1                                   7    
HELIX   34  34 PHE A  740  GLY A  782  1                                  43    
HELIX   35  35 ILE A  788  ASP A  800  1                                  13    
HELIX   36  36 GLY A  801  ALA A  806  1                                   6    
HELIX   37  37 LEU A  807  ASN A  810  5                                   4    
HELIX   38  38 SER A  830  MET A  857  1                                  28    
HELIX   39  39 GLU A  889  GLU A  892  5                                   4    
HELIX   40  40 ALA A  893  SER A  915  1                                  23    
HELIX   41  41 PRO A  926  VAL A  929  5                                   4    
HELIX   42  42 ASN A  930  VAL A  950  1                                  21    
HELIX   43  43 PRO A  952  PHE A  957  1                                   6    
HELIX   44  44 THR A  965  LEU A  975  1                                  11    
HELIX   45  45 LEU A  975  ASN A  990  1                                  16    
SHEET    1   A 6 GLN A 138  LYS A 141  0                                        
SHEET    2   A 6 MET A 126  TYR A 130 -1  N  VAL A 129   O  GLN A 138           
SHEET    3   A 6 ILE A 150  ALA A 154 -1  O  ILE A 150   N  TYR A 130           
SHEET    4   A 6 LYS A 218  THR A 225 -1  O  ALA A 219   N  VAL A 153           
SHEET    5   A 6 ASP A 162  ILE A 168 -1  N  SER A 167   O  LEU A 220           
SHEET    6   A 6 MET A 207  LEU A 208 -1  O  LEU A 208   N  ILE A 163           
SHEET    1   B 3 VAL A 187  ILE A 188  0                                        
SHEET    2   B 3 ARG A 174  ASP A 176 -1  N  VAL A 175   O  VAL A 187           
SHEET    3   B 3 ASN A 213  ALA A 216 -1  O  ASN A 213   N  ASP A 176           
SHEET    1   C 8 ALA A 331  VAL A 333  0                                        
SHEET    2   C 8 MET A 733  LEU A 735 -1  O  VAL A 734   N  ILE A 332           
SHEET    3   C 8 ILE A 716  MET A 720  1  N  ALA A 719   O  LEU A 735           
SHEET    4   C 8 THR A 698  GLY A 702  1  N  MET A 700   O  ILE A 718           
SHEET    5   C 8 VAL A 347  SER A 350  1  N  CYS A 349   O  ALA A 699           
SHEET    6   C 8 ARG A 620  ILE A 624  1  O  ARG A 620   N  ILE A 348           
SHEET    7   C 8 CYS A 675  ALA A 677  1  O  PHE A 676   N  MET A 623           
SHEET    8   C 8 ALA A 652  THR A 654  1  N  TYR A 653   O  ALA A 677           
SHEET    1   D 9 LYS A 400  PRO A 401  0                                        
SHEET    2   D 9 VAL A 395  LYS A 397 -1  N  LYS A 397   O  LYS A 400           
SHEET    3   D 9 PHE A 376  ILE A 384 -1  N  SER A 383   O  LEU A 396           
SHEET    4   D 9 SER A 362  ASP A 373 -1  N  ASP A 373   O  PHE A 376           
SHEET    5   D 9 LEU A 591  LEU A 600 -1  O  GLY A 598   N  LYS A 365           
SHEET    6   D 9 ARG A 560  ARG A 567 -1  N  LEU A 564   O  GLY A 595           
SHEET    7   D 9 LYS A 511  GLY A 516 -1  N  VAL A 514   O  ALA A 565           
SHEET    8   D 9 SER A 493  PRO A 500 -1  N  CYS A 498   O  LYS A 511           
SHEET    9   D 9 MET A 479  SER A 488 -1  N  LEU A 485   O  SER A 495           
SHEET    1   E 7 LYS A 400  PRO A 401  0                                        
SHEET    2   E 7 VAL A 395  LYS A 397 -1  N  LYS A 397   O  LYS A 400           
SHEET    3   E 7 PHE A 376  ILE A 384 -1  N  SER A 383   O  LEU A 396           
SHEET    4   E 7 SER A 362  ASP A 373 -1  N  ASP A 373   O  PHE A 376           
SHEET    5   E 7 LEU A 591  LEU A 600 -1  O  GLY A 598   N  LYS A 365           
SHEET    6   E 7 CYS A 525  VAL A 530  1  N  ARG A 529   O  PHE A 593           
SHEET    7   E 7 THR A 533  PRO A 536 -1  O  VAL A 535   N  VAL A 528           
SHEET    1   F 2 SER A 424  ASN A 428  0                                        
SHEET    2   F 2 VAL A 433  VAL A 437 -1  O  GLU A 435   N  ASP A 426           
SSBOND   1 CYS A  876    CYS A  888                          1555   1555  2.04  
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.34  
LINK         O   VAL A 304                CA    CA A 996     1555   1555  2.63  
LINK         O   ALA A 305                CA    CA A 996     1555   1555  2.59  
LINK         O   ILE A 307                CA    CA A 996     1555   1555  2.28  
LINK         OE1 GLU A 309                CA    CA A 996     1555   1555  2.71  
LINK         OE2 GLU A 309                CA    CA A 996     1555   1555  2.64  
LINK         OD2 ASP A 351                MG    MG A1001     1555   1555  2.43  
LINK         O   THR A 353                MG    MG A1001     1555   1555  2.18  
LINK         OD1 ASP A 703                MG    MG A1001     1555   1555  2.12  
LINK         OD1 ASN A 768                CA    CA A 995     1555   1555  2.37  
LINK         OE2 GLU A 771                CA    CA A 995     1555   1555  2.37  
LINK         OD1 ASN A 796                CA    CA A 996     1555   1555  2.25  
LINK         OG1 THR A 799                CA    CA A 995     1555   1555  2.56  
LINK         OD1 ASP A 800                CA    CA A 995     1555   1555  2.30  
LINK         OD2 ASP A 800                CA    CA A 996     1555   1555  2.34  
LINK         OE2 GLU A 908                CA    CA A 995     1555   1555  2.45  
LINK        CA    CA A 995                 O   HOH A1014     1555   1555  2.37  
LINK        CA    CA A 995                 O   HOH A1015     1555   1555  2.43  
LINK        MG    MG A 997                 O1B ADP A1002     1555   1555  2.13  
LINK        MG    MG A1001                 O   HOH A1038     1555   1555  2.01  
LINK        MG    MG A1001                 O   HOH A1041     1555   1555  2.05  
SITE     1 AC1  7 ASN A 768  GLU A 771  THR A 799  ASP A 800                    
SITE     2 AC1  7 GLU A 908  HOH A1014  HOH A1015                               
SITE     1 AC2  6 VAL A 304  ALA A 305  ILE A 307  GLU A 309                    
SITE     2 AC2  6 ASN A 796  ASP A 800                                          
SITE     1 AC3  5 ALF A 998  ADP A1002  HOH A1041  HOH A1046                    
SITE     2 AC3  5 HOH A1059                                                     
SITE     1 AC4 12 ASP A 351  LYS A 352  THR A 353  THR A 625                    
SITE     2 AC4 12 GLY A 626  LYS A 684  ASN A 706   MG A 997                    
SITE     3 AC4 12  MG A1001  ADP A1002  HOH A1038  HOH A1041                    
SITE     1 AC5  6 ASP A 351  THR A 353  ASP A 703  ALF A 998                    
SITE     2 AC5  6 HOH A1038  HOH A1041                                          
SITE     1 AC6 20 THR A 353  GLU A 439  GLU A 442  PHE A 487                    
SITE     2 AC6 20 ARG A 489  MET A 494  LYS A 515  GLY A 516                    
SITE     3 AC6 20 ALA A 517  ARG A 560  THR A 625  GLY A 626                    
SITE     4 AC6 20 ASP A 627  ARG A 678   MG A 997  ALF A 998                    
SITE     5 AC6 20 HOH A1046  HOH A1059  HOH A1062  HOH A1077                    
SITE     1 AC7  8 VAL A 104  GLN A 108  ARG A 324  PHE A 809                    
SITE     2 AC7  8 TRP A 932  SER A 936  LEU A 946  VAL A 950                    
SITE     1 AC8  3 SER A 830  GLY A 831  PHE A 834                               
CRYST1  162.900   75.100  152.100  90.00 109.30  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006139  0.000000  0.002150        0.00000                         
SCALE2      0.000000  0.013316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006966        0.00000                         
HETATM    1  C   ACE A   0      88.089  -5.513  48.527  1.00 87.18           C  
HETATM    2  O   ACE A   0      89.047  -6.110  49.064  1.00 87.38           O  
HETATM    3  CH3 ACE A   0      88.140  -5.128  47.070  1.00 87.33           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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