GenomeNet

Database: PDB
Entry: 5HIT
LinkDB: 5HIT
Original site: 5HIT 
HEADER    SIGNALING PROTEIN                       12-JAN-16   5HIT              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF CA2+-CALMODULIN AND A C-TERMINAL EAG1   
TITLE    2 CHANNEL FRAGMENT                                                     
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: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 1;      
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 727-743;                                      
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: CALM, CAM, RCJMB04_24E7;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7-7;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: KCNH1;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRSF DUET-1                               
KEYWDS    CALMODULIN, POTASSIUM CHANNEL, SIGNALING PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.MARQUES-CARVALHO,J.H.MORAIS-CABRAL                                
REVDAT   4   19-OCT-16 5HIT    1       JRNL                                     
REVDAT   3   28-SEP-16 5HIT    1       JRNL                                     
REVDAT   2   21-SEP-16 5HIT    1       JRNL                                     
REVDAT   1   14-SEP-16 5HIT    0                                                
JRNL        AUTH   M.J.MARQUES-CARVALHO,J.OPPERMANN,E.MUNOZ,A.S.FERNANDES,      
JRNL        AUTH 2 G.GABANT,M.CADENE,S.H.HEINEMANN,R.SCHONHERR,                 
JRNL        AUTH 3 J.H.MORAIS-CABRAL                                            
JRNL        TITL   MOLECULAR INSIGHTS INTO THE MECHANISM OF CALMODULIN          
JRNL        TITL 2 INHIBITION OF THE EAG1 POTASSIUM CHANNEL.                    
JRNL        REF    STRUCTURE                     V.  24  1742 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27618660                                                     
JRNL        DOI    10.1016/J.STR.2016.07.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.170                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 5814                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1017                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.8397 -  5.4495    0.98     1371   147  0.1938 0.2380        
REMARK   3     2  5.4495 -  4.3264    0.98     1396   130  0.1834 0.2541        
REMARK   3     3  4.3264 -  3.7798    0.99     1393   146  0.1618 0.2443        
REMARK   3     4  3.7798 -  3.4343    0.99     1373   165  0.1991 0.2723        
REMARK   3     5  3.4343 -  3.1882    0.99     1367   156  0.2501 0.3314        
REMARK   3     6  3.1882 -  3.0003    0.99     1375   149  0.2789 0.2947        
REMARK   3     7  3.0003 -  2.8500    0.99     1419   124  0.3113 0.3883        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           1276                                  
REMARK   3   ANGLE     :  0.443           1749                                  
REMARK   3   CHIRALITY :  0.032            192                                  
REMARK   3   PLANARITY :  0.002            229                                  
REMARK   3   DIHEDRAL  : 10.120            471                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 64 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1796  27.2328 -25.0988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1491 T22:   0.1135                                     
REMARK   3      T33:   0.1253 T12:   0.3822                                     
REMARK   3      T13:   0.0543 T23:  -0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0123 L22:   0.0060                                     
REMARK   3      L33:  -0.0007 L12:  -0.0007                                     
REMARK   3      L13:  -0.0007 L23:  -0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:  -0.0304 S13:  -0.0385                       
REMARK   3      S21:  -0.0014 S22:  -0.0274 S23:  -0.0199                       
REMARK   3      S31:   0.0149 S32:   0.0225 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  67.5887  23.4322  -9.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1464 T22:   0.0943                                     
REMARK   3      T33:   0.2149 T12:   0.2857                                     
REMARK   3      T13:  -0.1561 T23:   0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0083 L22:  -0.0085                                     
REMARK   3      L33:  -0.0053 L12:  -0.0134                                     
REMARK   3      L13:   0.0132 L23:  -0.0055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.0320 S13:   0.0143                       
REMARK   3      S21:   0.0272 S22:  -0.0170 S23:   0.0158                       
REMARK   3      S31:  -0.0288 S32:   0.0372 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  78.6222  10.4666   5.0750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2742 T22:   0.1360                                     
REMARK   3      T33:   0.2316 T12:   0.0470                                     
REMARK   3      T13:  -0.0040 T23:  -0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0047 L22:   0.0067                                     
REMARK   3      L33:   0.0029 L12:   0.0003                                     
REMARK   3      L13:  -0.0006 L23:  -0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0090 S12:  -0.0176 S13:  -0.0511                       
REMARK   3      S21:  -0.0181 S22:   0.0613 S23:  -0.0311                       
REMARK   3      S31:   0.0380 S32:   0.0291 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 727 THROUGH 735 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  64.2953  21.1396   7.7757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3425 T22:   0.4777                                     
REMARK   3      T33:   0.3443 T12:   0.0536                                     
REMARK   3      T13:  -0.0142 T23:  -0.0855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0021 L22:  -0.0002                                     
REMARK   3      L33:   0.0033 L12:   0.0001                                     
REMARK   3      L13:   0.0000 L23:  -0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:  -0.0063 S13:   0.0030                       
REMARK   3      S21:   0.0071 S22:   0.0002 S23:   0.0102                       
REMARK   3      S31:   0.0044 S32:  -0.0071 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 736 THROUGH 743 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  65.5392  12.1339   2.9435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3485 T22:   0.3493                                     
REMARK   3      T33:   0.4079 T12:  -0.1433                                     
REMARK   3      T13:  -0.0360 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0006 L22:   0.0003                                     
REMARK   3      L33:  -0.0005 L12:   0.0007                                     
REMARK   3      L13:   0.0008 L23:  -0.0006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0128 S12:   0.0025 S13:   0.0013                       
REMARK   3      S21:   0.0033 S22:  -0.0069 S23:   0.0014                       
REMARK   3      S31:  -0.0108 S32:   0.0013 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217090.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MICROFOCUS BEAM                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5817                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61300                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 1CFD, 3OXQ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DI-AMMONIUM CITRATE, PEG 3350, PH 5.0,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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       36.92750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.92750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       26.81200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.56850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.81200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.56850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       36.92750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.81200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       60.56850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       36.92750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.81200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       60.56850            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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    57                                                      
REMARK 465     ASP A    58                                                      
REMARK 465     GLY A    59                                                      
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     GLU A  54    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  56    CG   OD1  OD2                                       
REMARK 470     ASN A  60    CG   OD1  ND2                                       
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     MET A 109    CG   SD   CE                                        
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 123    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
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   OD2  ASP A   133     O    HOH A   301              2.00            
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    ASN A  42       80.10   -153.18                                   
REMARK 500    THR A  44     -169.07   -107.91                                   
REMARK 500    GLN B 742       69.58    -66.01                                   
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 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  78.6                                              
REMARK 620 3 ASN A  97   OD1  73.0  82.7                                        
REMARK 620 4 TYR A  99   O    75.7 153.3  83.0                                  
REMARK 620 5 GLU A 104   OE1  97.8  59.2 141.9 131.6                            
REMARK 620 6 GLU A 104   OE2 115.3 114.8 161.4  83.2  55.9                      
REMARK 620 7 HOH A 307   O   149.0  79.5  82.7 120.7  89.6  93.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  96.4                                              
REMARK 620 3 ASP A 133   OD1  69.9 102.1                                        
REMARK 620 4 ASP A 133   OD2 125.3  88.5  55.9                                  
REMARK 620 5 GLN A 135   O    75.2 159.4  57.4  81.6                            
REMARK 620 6 GLU A 140   OE1  90.8 114.5 140.3 135.7  84.7                      
REMARK 620 7 GLU A 140   OE2  98.6  59.3 157.9 129.0 139.8  55.3                
REMARK 620 8 HOH A 301   O   174.8  82.2 105.5  49.8 104.6  94.3  84.9          
REMARK 620 N                    1     2     3     4     5     6     7           
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202                  
DBREF  5HIT A    1   147  UNP    P62149   CALM_CHICK       2    148             
DBREF  5HIT B  727   743  UNP    Q3USQ9   Q3USQ9_MOUSE   727    743             
SEQRES   1 A  147  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  147  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  147  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  147  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  147  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  147  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  147  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  147  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  147  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  147  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  147  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  147  MET MET THR ALA                                              
SEQRES   1 B   17  ALA PRO LEU ILE LEU PRO PRO ASP HIS PRO VAL ARG ARG          
SEQRES   2 B   17  LEU PHE GLN ARG                                              
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *10(H2 O)                                                     
HELIX    1 AA1 THR A    5  LEU A   18  1                                  14    
HELIX    2 AA2 THR A   28  LEU A   39  1                                  12    
HELIX    3 AA3 THR A   44  VAL A   55  1                                  12    
HELIX    4 AA4 PHE A   65  ASP A   93  1                                  29    
HELIX    5 AA5 SER A  101  LEU A  112  1                                  12    
HELIX    6 AA6 THR A  117  ASP A  129  1                                  13    
HELIX    7 AA7 ASN A  137  ALA A  147  1                                  11    
HELIX    8 AA8 HIS B  735  GLN B  742  1                                   8    
SHEET    1 AA1 2 THR A  26  ILE A  27  0                                        
SHEET    2 AA1 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
LINK         OD1 ASP A  93                CA    CA A 201     1555   1555  2.35  
LINK         OD1 ASP A  95                CA    CA A 201     1555   1555  2.31  
LINK         OD1 ASN A  97                CA    CA A 201     1555   1555  2.35  
LINK         O   TYR A  99                CA    CA A 201     1555   1555  2.26  
LINK         OE1 GLU A 104                CA    CA A 201     1555   1555  2.35  
LINK         OE2 GLU A 104                CA    CA A 201     1555   1555  2.34  
LINK         OD1 ASP A 129                CA    CA A 202     1555   1555  2.31  
LINK         OD1 ASP A 131                CA    CA A 202     1555   1555  2.31  
LINK         OD1 ASP A 133                CA    CA A 202     1555   1555  2.32  
LINK         OD2 ASP A 133                CA    CA A 202     1555   1555  2.35  
LINK         O   GLN A 135                CA    CA A 202     1555   1555  2.41  
LINK         OE1 GLU A 140                CA    CA A 202     1555   1555  2.34  
LINK         OE2 GLU A 140                CA    CA A 202     1555   1555  2.39  
LINK        CA    CA A 201                 O   HOH A 307     1555   1555  2.39  
LINK        CA    CA A 202                 O   HOH A 301     1555   1555  2.40  
SITE     1 AC1  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC1  6 GLU A 104  HOH A 307                                          
SITE     1 AC2  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC2  6 GLU A 140  HOH A 301                                          
CRYST1   53.624  121.137   73.855  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018648  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008255  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system