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Database: PDB
Entry: 4Q5U
LinkDB: 4Q5U
Original site: 4Q5U 
HEADER    CALCIUM BINDING PROTEIN/PROTEIN BINDING 17-APR-14   4Q5U              
TITLE     STRUCTURE OF CALMODULIN BOUND TO ITS RECOGNITION SITE FROM CALCINEURIN
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: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT  
COMPND   8 ALPHA ISOFORM;                                                       
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: CALMODULIN-BINDING DOMAIN (UNP RESIDUES 391-414);          
COMPND  11 SYNONYM: CAM-PRP CATALYTIC SUBUNIT, CALMODULIN-DEPENDENT CALCINEURIN 
COMPND  12 A SUBUNIT ALPHA ISOFORM;                                             
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: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PETCAMI;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    EF HAND, CALCIUM BINDING PROTEIN-PROTEIN BINDING COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GUO,T.B.DUNLAP,T.P.CREAMER,C.W.VANDER KOOI                          
REVDAT   3   20-SEP-23 4Q5U    1       REMARK LINK                              
REVDAT   2   01-OCT-14 4Q5U    1       JRNL                                     
REVDAT   1   03-SEP-14 4Q5U    0                                                
JRNL        AUTH   T.B.DUNLAP,H.F.GUO,E.C.COOK,E.HOLBROOK,J.RUMI-MASANTE,       
JRNL        AUTH 2 T.E.LESTER,C.L.COLBERT,C.W.VANDER KOOI,T.P.CREAMER           
JRNL        TITL   STOICHIOMETRY OF THE CALCINEURIN REGULATORY                  
JRNL        TITL 2 DOMAIN-CALMODULIN COMPLEX.                                   
JRNL        REF    BIOCHEMISTRY                  V.  53  5779 2014              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   25144868                                                     
JRNL        DOI    10.1021/BI5004734                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15779                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 801                             
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 19.1211 -  3.5364    1.00     2871   152  0.1914 0.2354        
REMARK   3     2  3.5364 -  2.8098    1.00     2749   151  0.2281 0.2295        
REMARK   3     3  2.8098 -  2.4555    1.00     2714   142  0.2314 0.2724        
REMARK   3     4  2.4555 -  2.2313    0.93     2531   145  0.2364 0.2608        
REMARK   3     5  2.2313 -  2.0716    0.82     2211   111  0.2472 0.2966        
REMARK   3     6  2.0716 -  1.9500    0.70     1902   100  0.2711 0.3420        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           1352                                  
REMARK   3   ANGLE     :  0.972           1810                                  
REMARK   3   CHIRALITY :  0.070            200                                  
REMARK   3   PLANARITY :  0.004            244                                  
REMARK   3   DIHEDRAL  : 14.430            524                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 3:73)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7736  10.2143   6.8774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4581 T22:   0.4150                                     
REMARK   3      T33:   0.4407 T12:   0.0503                                     
REMARK   3      T13:  -0.0565 T23:   0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8011 L22:   8.3605                                     
REMARK   3      L33:   4.4845 L12:  -0.6887                                     
REMARK   3      L13:  -2.5826 L23:   2.7268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1732 S12:  -0.0153 S13:  -0.2597                       
REMARK   3      S21:  -0.1124 S22:  -0.0515 S23:   0.0840                       
REMARK   3      S31:   0.4012 S32:   0.0583 S33:   0.3139                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 74:97)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2153  22.8885  -4.3999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5042 T22:   0.4474                                     
REMARK   3      T33:   0.5069 T12:   0.0595                                     
REMARK   3      T13:  -0.1119 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6530 L22:   2.7600                                     
REMARK   3      L33:   9.3238 L12:   0.0406                                     
REMARK   3      L13:  -0.2818 L23:  -0.3199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2090 S12:   0.2182 S13:  -0.2068                       
REMARK   3      S21:   0.0644 S22:  -0.3618 S23:   0.1089                       
REMARK   3      S31:   0.9835 S32:  -0.3170 S33:   0.1975                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 98:147)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2582  28.1702  -1.9114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3862 T22:   0.7742                                     
REMARK   3      T33:   0.9206 T12:  -0.0185                                     
REMARK   3      T13:  -0.0914 T23:   0.1001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4794 L22:   4.9089                                     
REMARK   3      L33:   3.3430 L12:   0.1059                                     
REMARK   3      L13:  -0.3538 L23:  -3.9252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0861 S12:  -0.1467 S13:   0.5988                       
REMARK   3      S21:   0.2157 S22:  -0.8049 S23:  -1.3760                       
REMARK   3      S31:  -0.4058 S32:   1.7490 S33:   0.7322                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 391:414)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8319  17.7501  -0.2849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4668 T22:   0.4221                                     
REMARK   3      T33:   0.4269 T12:   0.0160                                     
REMARK   3      T13:  -0.1025 T23:   0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9890 L22:   7.8130                                     
REMARK   3      L33:   7.1995 L12:  -2.2740                                     
REMARK   3      L13:  -1.8630 L23:   1.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0810 S12:   0.4257 S13:  -0.0722                       
REMARK   3      S21:  -0.3109 S22:  -0.2869 S23:  -0.1353                       
REMARK   3      S31:   0.2894 S32:   0.0088 S33:   0.0776                       
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 4Q5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085641.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15779                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: PDB ENTRY 2W73                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3:1 10 MG/ML PROTEIN TO MOTHER LIQUOR    
REMARK 280  (24% PEG1000, 20% GLYCEROL), FINAL VOLUME 200 NL, PH 7.5, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                         
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       19.72400            
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       19.72400            
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       52.74950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.51650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.74950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.51650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       19.72400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.74950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.51650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       19.72400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.74950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.51650            
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: 3280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9050 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 340  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A   148                                                      
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 115       69.26   -116.33                                   
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  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  72.7                                              
REMARK 620 3 ASP A  24   OD1  83.8  79.0                                        
REMARK 620 4 THR A  26   O    83.7 153.6  87.0                                  
REMARK 620 5 GLU A  31   OE2  92.1  69.2 147.6 124.6                            
REMARK 620 6 GLU A  31   OE1 107.9 122.9 157.1  75.2  53.7                      
REMARK 620 7 HOH A 370   O   162.1  90.8  86.3 110.6  88.3  86.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  69.5                                              
REMARK 620 3 ASN A  60   OD1  86.8  80.1                                        
REMARK 620 4 THR A  62   O    83.0 147.7  81.9                                  
REMARK 620 5 GLU A  67   OE2  96.9 115.0 164.9  84.1                            
REMARK 620 6 GLU A  67   OE1  76.5  64.8 144.5 125.7  50.3                      
REMARK 620 7 HOH A 339   O   141.5  72.8  93.9 135.2  92.2  81.2                
REMARK 620 8 HOH A 369   O   148.4 125.1  70.6  72.3  99.8 134.2  64.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  74.7                                              
REMARK 620 3 ASN A  97   OD1  87.3  75.0                                        
REMARK 620 4 TYR A  99   O    94.9 157.6  84.8                                  
REMARK 620 5 GLU A 104   OE1  93.9  74.8 148.3 126.4                            
REMARK 620 6 GLU A 104   OE2 101.2 126.9 157.8  74.1  52.3                      
REMARK 620 7 HOH A 341   O   161.7  87.2  85.4 101.1  83.8  91.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  81.3                                              
REMARK 620 3 ASP A 133   OD1  85.0  80.5                                        
REMARK 620 4 GLN A 135   O    85.4 155.0  77.3                                  
REMARK 620 5 GLU A 140   OE2  94.2  74.8 155.1 127.5                            
REMARK 620 6 GLU A 140   OE1 115.9 126.7 146.2  78.2  55.0                      
REMARK 620 7 HOH A 327   O   158.4  83.2  77.7 103.0  96.2  85.4                
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204                  
DBREF  4Q5U A    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4Q5U C  391   414  UNP    Q08209   PP2BA_HUMAN    391    414             
SEQRES   1 A  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 C   24  ALA ARG LYS GLU VAL ILE ARG ASN LYS ILE ARG ALA ILE          
SEQRES   2 C   24  GLY LYS MET ALA ARG VAL PHE SER VAL LEU ARG                  
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *100(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 PHE A   65  ALA A   73  1                                   9    
HELIX    5   5 LYS A   77  ASP A   93  1                                  17    
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  THR A  146  1                                   9    
HELIX    9   9 ARG C  392  ARG C  414  1                                  23    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 TYR A  99  ILE A 100  0                                        
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 201     1555   1555  2.29  
LINK         OD1 ASP A  22                CA    CA A 201     1555   1555  2.35  
LINK         OD1 ASP A  24                CA    CA A 201     1555   1555  2.27  
LINK         O   THR A  26                CA    CA A 201     1555   1555  2.30  
LINK         OE2 GLU A  31                CA    CA A 201     1555   1555  2.44  
LINK         OE1 GLU A  31                CA    CA A 201     1555   1555  2.45  
LINK         OD1 ASP A  56                CA    CA A 204     1555   1555  2.35  
LINK         OD1 ASP A  58                CA    CA A 204     1555   1555  2.55  
LINK         OD1 ASN A  60                CA    CA A 204     1555   1555  2.35  
LINK         O   THR A  62                CA    CA A 204     1555   1555  2.35  
LINK         OE2 GLU A  67                CA    CA A 204     1555   1555  2.49  
LINK         OE1 GLU A  67                CA    CA A 204     1555   1555  2.66  
LINK         OD1 ASP A  93                CA    CA A 202     1555   1555  2.37  
LINK         OD1 ASP A  95                CA    CA A 202     1555   1555  2.36  
LINK         OD1 ASN A  97                CA    CA A 202     1555   1555  2.37  
LINK         O   TYR A  99                CA    CA A 202     1555   1555  2.21  
LINK         OE1 GLU A 104                CA    CA A 202     1555   1555  2.45  
LINK         OE2 GLU A 104                CA    CA A 202     1555   1555  2.53  
LINK         OD1 ASP A 129                CA    CA A 203     1555   1555  2.39  
LINK         OD1 ASP A 131                CA    CA A 203     1555   1555  2.30  
LINK         OD1 ASP A 133                CA    CA A 203     1555   1555  2.37  
LINK         O   GLN A 135                CA    CA A 203     1555   1555  2.27  
LINK         OE2 GLU A 140                CA    CA A 203     1555   1555  2.33  
LINK         OE1 GLU A 140                CA    CA A 203     1555   1555  2.43  
LINK        CA    CA A 201                 O   HOH A 370     1555   1555  2.19  
LINK        CA    CA A 202                 O   HOH A 341     1555   1555  2.46  
LINK        CA    CA A 203                 O   HOH A 327     1555   1555  2.35  
LINK        CA    CA A 204                 O   HOH A 339     1555   1555  2.40  
LINK        CA    CA A 204                 O   HOH A 369     1555   1555  2.52  
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 370                                          
SITE     1 AC2  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC2  6 GLU A 104  HOH A 341                                          
SITE     1 AC3  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC3  6 GLU A 140  HOH A 327                                          
SITE     1 AC4  7 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC4  7 GLU A  67  HOH A 339  HOH A 369                               
CRYST1  105.499  111.033   39.448  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      0.009479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009006  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025350        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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