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Database: PDB
Entry: 3DVE
LinkDB: 3DVE
Original site: 3DVE 
HEADER    MEMBRANE PROTEIN                        18-JUL-08   3DVE              
TITLE     CRYSTAL STRUCTURE OF CA2+/CAM-CAV2.2 IQ DOMAIN COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 1855-1875;                                    
COMPND  10 SYNONYM: VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV2.2, CALCIUM 
COMPND  11 CHANNEL, L TYPE, ALPHA-1 POLYPEPTIDE ISOFORM 5, BRAIN CALCIUM CHANNEL
COMPND  12 III, BIII;                                                           
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE   6 CAM3, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEGST;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  14 ORGANISM_COMMON: RABBIT;                                             
SOURCE  15 ORGANISM_TAXID: 9986;                                                
SOURCE  16 GENE: CACNA1B, CACH5, CACNL1A5;                                      
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET28B-HMT                                
KEYWDS    CALMODULIN, CALCIUM CHANNEL, IQ DOMAIN, INACTIVATION, FACILITATION,   
KEYWDS   2 CALCIUM-DEPENDENT, VOLTAGE-GATED, MEMBRANE PROTEIN                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,D.L.MINOR       
REVDAT   5   21-FEB-24 3DVE    1       REMARK SEQADV                            
REVDAT   4   25-OCT-17 3DVE    1       REMARK                                   
REVDAT   3   13-JUL-11 3DVE    1       VERSN                                    
REVDAT   2   24-FEB-09 3DVE    1       VERSN                                    
REVDAT   1   04-NOV-08 3DVE    0                                                
JRNL        AUTH   E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,       
JRNL        AUTH 2 D.L.MINOR                                                    
JRNL        TITL   STRUCTURES OF CA(V)2 CA(2+)/CAM-IQ DOMAIN COMPLEXES REVEAL   
JRNL        TITL 2 BINDING MODES THAT UNDERLIE CALCIUM-DEPENDENT INACTIVATION   
JRNL        TITL 3 AND FACILITATION.                                            
JRNL        REF    STRUCTURE                     V.  16  1455 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18940602                                                     
JRNL        DOI    10.1016/J.STR.2008.07.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 7757                           
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 358                             
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 483                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 26                           
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1254                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 78                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54000                                             
REMARK   3    B22 (A**2) : -0.54000                                             
REMARK   3    B33 (A**2) : 0.81000                                              
REMARK   3    B12 (A**2) : -0.27000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.419         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.279         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.012        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1308 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1764 ; 1.379 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   171 ; 5.544 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    71 ;30.037 ;25.915       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   239 ;15.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.382 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   194 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1007 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   814 ; 0.746 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1300 ; 1.482 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   494 ; 2.455 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   458 ; 4.176 ; 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  : 5                                          
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     5        A    39                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7196  20.6417  17.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0186 T22:  -0.0055                                     
REMARK   3      T33:   0.0019 T12:   0.0086                                     
REMARK   3      T13:  -0.0125 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3889 L22:   1.7307                                     
REMARK   3      L33:   5.4858 L12:   0.7706                                     
REMARK   3      L13:  -0.1603 L23:  -1.3689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0257 S12:   0.0292 S13:  -0.0141                       
REMARK   3      S21:   0.0594 S22:   0.0574 S23:  -0.1817                       
REMARK   3      S31:   0.3461 S32:  -0.0803 S33:  -0.0831                       
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    45        A    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0867  30.0799  20.6052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0033 T22:   0.0377                                     
REMARK   3      T33:  -0.0067 T12:   0.0283                                     
REMARK   3      T13:   0.0490 T23:   0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5289 L22:   0.2334                                     
REMARK   3      L33:   4.4454 L12:   0.1978                                     
REMARK   3      L13:  -0.2142 L23:  -0.9137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0728 S12:  -0.0671 S13:   0.1195                       
REMARK   3      S21:   0.1980 S22:   0.0981 S23:   0.1884                       
REMARK   3      S31:  -0.2667 S32:  -0.2962 S33:  -0.1709                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    82        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0742  13.0818   2.6398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0223 T22:  -0.0606                                     
REMARK   3      T33:   0.0109 T12:   0.0023                                     
REMARK   3      T13:  -0.0084 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7570 L22:   2.7359                                     
REMARK   3      L33:   2.5546 L12:   0.5765                                     
REMARK   3      L13:   0.0939 L23:  -0.9576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1330 S12:   0.1703 S13:   0.4022                       
REMARK   3      S21:  -0.0066 S22:   0.0311 S23:   0.0091                       
REMARK   3      S31:  -0.1615 S32:  -0.0157 S33:   0.1019                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   118        A   146                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0353   5.2078   9.4638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0006 T22:  -0.0263                                     
REMARK   3      T33:  -0.0077 T12:   0.0134                                     
REMARK   3      T13:  -0.0129 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0619 L22:   0.7985                                     
REMARK   3      L33:   2.9551 L12:   0.8654                                     
REMARK   3      L13:   0.8152 L23:  -0.8785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:  -0.1132 S13:   0.0316                       
REMARK   3      S21:   0.1962 S22:  -0.0598 S23:  -0.0653                       
REMARK   3      S31:  -0.0692 S32:  -0.0629 S33:   0.0823                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1853        B  1875                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9883  23.6503  11.7206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0515 T22:  -0.0023                                     
REMARK   3      T33:  -0.0010 T12:  -0.0037                                     
REMARK   3      T13:   0.0123 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8540 L22:   9.6907                                     
REMARK   3      L33:   1.1267 L12:  -1.9378                                     
REMARK   3      L13:   0.9517 L23:  -2.3508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0455 S12:   0.0571 S13:   0.0884                       
REMARK   3      S21:   0.0072 S22:  -0.0618 S23:  -0.0355                       
REMARK   3      S31:   0.0564 S32:  -0.0038 S33:   0.0163                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3DVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048536.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7844                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 15.00                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 25-30 % PEG 2000 MME,    
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.88400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      229.76800            
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      172.32600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      287.21000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.44200            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      114.88400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      229.76800            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      287.21000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      172.32600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       57.44200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8430 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
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     LEU A   4    CG   CD1  CD2                                       
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 115    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     HIS B1853    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B1873    OG                                                  
REMARK 470     ARG B1874    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1875    CG   OD1  OD2                                       
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  56       74.92    -69.21                                   
REMARK 500    GLU A  83      -33.58    -38.84                                   
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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  83.1                                              
REMARK 620 3 ASP A  24   OD2  89.4  76.8                                        
REMARK 620 4 THR A  26   O    91.0 152.3  76.1                                  
REMARK 620 5 GLU A  31   OE1 105.2 129.3 150.7  78.3                            
REMARK 620 6 GLU A  31   OE2  93.8  79.2 155.1 128.3  50.8                      
REMARK 620 7 HOH A 524   O   166.2  83.1  86.7 100.9  84.3  84.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD2                                                    
REMARK 620 2 ASP A  58   OD2  76.9                                              
REMARK 620 3 ASN A  60   OD1  91.3  79.3                                        
REMARK 620 4 THR A  62   O    92.8 157.3  80.8                                  
REMARK 620 5 GLU A  67   OE1 109.9 127.3 148.4  75.1                            
REMARK 620 6 GLU A  67   OE2  86.7  78.5 157.6 121.5  51.0                      
REMARK 620 7 HOH A 543   O   162.0  85.5  81.9 102.4  83.6  93.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD2                                                    
REMARK 620 2 ASP A  95   OD1  87.4                                              
REMARK 620 3 ASN A  97   OD1  88.8  83.7                                        
REMARK 620 4 TYR A  99   O    86.7 161.3  78.5                                  
REMARK 620 5 GLU A 104   OE1  97.7  80.5 162.6 117.9                            
REMARK 620 6 GLU A 104   OE2 101.8 130.2 144.2  68.4  50.0                      
REMARK 620 7 HOH A 535   O   170.1  85.9  83.2  97.4  88.5  88.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD2                                                    
REMARK 620 2 ASP A 131   OD1  80.2                                              
REMARK 620 3 ASP A 133   OD2  96.7  80.4                                        
REMARK 620 4 GLN A 135   O    90.4 158.8  81.9                                  
REMARK 620 5 GLU A 140   OE1 112.7 123.2 144.1  77.9                            
REMARK 620 6 GLU A 140   OE2  82.9  76.7 156.8 121.2  52.6                      
REMARK 620 7 HOH A 509   O   167.7  87.5  80.5 101.0  74.6  94.9                
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DVJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DVK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DVM   RELATED DB: PDB                                   
DBREF  3DVE A    1   148  UNP    P62158   CALM_HUMAN       2    149             
DBREF  3DVE B 1855  1875  UNP    Q05152   CAC1B_RABIT   1855   1875             
SEQADV 3DVE HIS B 1853  UNP  Q05152              EXPRESSION TAG                 
SEQADV 3DVE MET B 1854  UNP  Q05152              EXPRESSION TAG                 
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   23  HIS MET GLY LYS VAL TYR ALA ALA LEU MET ILE PHE ASP          
SEQRES   2 B   23  PHE TYR LYS GLN ASN LYS THR SER ARG ASP                      
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     NI  A 505       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7   NI    NI 2+                                                        
FORMUL   8  HOH   *78(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 ASP A   64  LYS A   77  1                                  14    
HELIX    5   5 GLU A   82  ASP A   93  1                                  12    
HELIX    6   6 SER A  101  LEU A  112  1                                  12    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  MET A  145  1                                   8    
HELIX    9   9 MET B 1854  ASN B 1870  1                                  17    
SHEET    1   A 2 TYR A  99  ILE A 100  0                                        
SHEET    2   A 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 501     1555   1555  2.22  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.42  
LINK         OD2 ASP A  24                CA    CA A 501     1555   1555  2.44  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.26  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.59  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.49  
LINK         OD2 ASP A  56                CA    CA A 502     1555   1555  2.23  
LINK         OD2 ASP A  58                CA    CA A 502     1555   1555  2.42  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.33  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.52  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.46  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.55  
LINK         OD2 ASP A  93                CA    CA A 503     1555   1555  2.11  
LINK         OD1 ASP A  95                CA    CA A 503     1555   1555  2.35  
LINK         OD1 ASN A  97                CA    CA A 503     1555   1555  2.39  
LINK         O   TYR A  99                CA    CA A 503     1555   1555  2.32  
LINK         OE1 GLU A 104                CA    CA A 503     1555   1555  2.44  
LINK         OE2 GLU A 104                CA    CA A 503     1555   1555  2.69  
LINK         OD2 ASP A 129                CA    CA A 504     1555   1555  2.39  
LINK         OD1 ASP A 131                CA    CA A 504     1555   1555  2.38  
LINK         OD2 ASP A 133                CA    CA A 504     1555   1555  2.37  
LINK         O   GLN A 135                CA    CA A 504     1555   1555  2.44  
LINK         OE1 GLU A 140                CA    CA A 504     1555   1555  2.50  
LINK         OE2 GLU A 140                CA    CA A 504     1555   1555  2.47  
LINK        CA    CA A 501                 O   HOH A 524     1555   1555  2.40  
LINK        CA    CA A 502                 O   HOH A 543     1555   1555  2.25  
LINK        CA    CA A 503                 O   HOH A 535     1555   1555  2.51  
LINK        CA    CA A 504                 O   HOH A 509     1555   1555  2.41  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 524                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 543                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 535                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 509                                          
CRYST1   40.303   40.303  344.652  90.00  90.00 120.00 P 61 2 2     12          
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      0.024812  0.014325  0.000000        0.00000                         
SCALE2      0.000000  0.028650  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002901        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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