GenomeNet

Database: PDB
Entry: 2K0E
LinkDB: 2K0E
Original site: 2K0E 
HEADER    METAL BINDING PROTEIN                   02-FEB-08   2K0E              
TITLE     A COUPLED EQUILIBRIUM SHIFT MECHANISM IN CALMODULIN-MEDIATED SIGNAL   
TITLE    2 TRANSDUCTION                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: AR58                                       
KEYWDS    EF HANDS, ENSEMBLE, HELIX BUNDLE, CALCIUM BINDING, METAL BINDING      
KEYWDS   2 PROTEIN                                                              
EXPDTA    SOLUTION NMR                                                          
NUMMDL    160                                                                   
AUTHOR    J.GSPONER,J.CHRISTODOULOU,A.CAVALLI,J.M.BUI,B.RICHTER,C.M.DOBSON,     
AUTHOR   2 M.VENDRUSCOLO                                                        
REVDAT   3   16-MAR-22 2K0E    1       REMARK                                   
REVDAT   2   24-FEB-09 2K0E    1       VERSN                                    
REVDAT   1   10-JUN-08 2K0E    0                                                
JRNL        AUTH   J.GSPONER,J.CHRISTODOULOU,A.CAVALLI,J.M.BUI,B.RICHTER,       
JRNL        AUTH 2 C.M.DOBSON,M.VENDRUSCOLO                                     
JRNL        TITL   A COUPLED EQUILIBRIUM SHIFT MECHANISM IN CALMODULIN-MEDIATED 
JRNL        TITL 2 SIGNAL TRANSDUCTION                                          
JRNL        REF    STRUCTURE                     V.  16   736 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18462678                                                     
JRNL        DOI    10.1016/J.STR.2008.02.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CHARMM C30                                           
REMARK   3   AUTHORS     : B.R.BROOKS, R.E.BRUCCOLERI,                          
REMARK   3                 B.D.OLAFSON,D.J.STATES, S.SWAMINATHAN, M.KARLPLUS    
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PROGRAM : CHARMM C30 AUTHORS :            
REMARK   3  B.R.BROOKS, R.E.BRUCCOLERI, B.D.OLAFSON,D.J.STATES,                 
REMARK   3  S.SWAMINATHAN, M.KARLPLUS                                           
REMARK   4                                                                      
REMARK   4 2K0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000100517.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : 0.5 MM CALMODULIN                  
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : CHARMM                             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 160                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 160                                
REMARK 210 CONFORMERS, SELECTION CRITERIA  : ALL CALCULATED STRUCTURES          
REMARK 210                                   SUBMITTED                          
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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    24     HG1  THR A    26              1.60            
REMARK 500   O    VAL A   142     HG1  THR A   146              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  1 ASP A  22   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500  1 THR A  62   CA  -  CB  -  CG2 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500  1 ASP A  80   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500  1 ASP A  80   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500  1 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  1 PHE A  89   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  1 PHE A  89   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  1 ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500  1 LEU A 112   O   -  C   -  N   ANGL. DEV. = -10.5 DEGREES          
REMARK 500  1 ASP A 118   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  1 GLU A 120   O   -  C   -  N   ANGL. DEV. = -10.1 DEGREES          
REMARK 500  1 VAL A 121   CA  -  CB  -  CG2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500  1 ARG A 126   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ASP A 129   O   -  C   -  N   ANGL. DEV. =  -9.9 DEGREES          
REMARK 500  1 ASP A 131   CB  -  CG  -  OD1 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500  1 TYR A 138   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500  1 GLU A 140   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500  2 PHE A  19   CB  -  CG  -  CD1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  2 THR A  26   CA  -  CB  -  CG2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500  2 ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500  2 MET A  72   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500  2 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  2 ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500  2 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500  2 MET A 109   CG  -  SD  -  CE  ANGL. DEV. = -15.0 DEGREES          
REMARK 500  2 MET A 145   CG  -  SD  -  CE  ANGL. DEV. = -11.3 DEGREES          
REMARK 500  3 ASP A   2   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500  3 PHE A  12   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  3 PHE A  16   CB  -  CG  -  CD2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500  3 PHE A  16   CB  -  CG  -  CD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500  3 PHE A  19   CB  -  CG  -  CD2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500  3 PHE A  19   CB  -  CG  -  CD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500  3 GLY A  25   O   -  C   -  N   ANGL. DEV. = -10.2 DEGREES          
REMARK 500  3 THR A  26   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES          
REMARK 500  3 GLU A  31   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500  3 ASP A  64   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500  3 ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500  3 PHE A  68   CB  -  CG  -  CD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500  3 PHE A  68   CB  -  CG  -  CD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500  3 ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500  3 ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500  3 ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500  3 TYR A  99   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500  3 TYR A  99   CD1 -  CG  -  CD2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500  3 TYR A  99   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500  3 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  3 ASP A 129   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500  3 VAL A 136   CB  -  CA  -  C   ANGL. DEV. =  13.4 DEGREES          
REMARK 500  3 PHE A 141   CB  -  CG  -  CD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  3 MET A 145   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    2628 ANGLE DEVIATIONS.                             
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  1 ASP A  24     -141.95    -93.04                                   
REMARK 500  1 ASN A  42       70.57   -161.45                                   
REMARK 500  1 LYS A  75      -74.17    -62.92                                   
REMARK 500  1 ASP A  78      -71.06    -57.51                                   
REMARK 500  1 SER A  81      -57.71     81.62                                   
REMARK 500  1 GLU A  82      -32.64    105.08                                   
REMARK 500  3 ASP A  20      107.61    -54.67                                   
REMARK 500  3 ASN A  42       64.41   -150.36                                   
REMARK 500  3 ASP A  93       87.86    -65.03                                   
REMARK 500  3 ASP A 129      106.96    -55.06                                   
REMARK 500  5 ASN A  42       69.15   -159.75                                   
REMARK 500  5 THR A  79       35.05    -88.20                                   
REMARK 500  5 ASP A  80      -47.99   -152.85                                   
REMARK 500  5 ASP A 131     -103.20    -99.84                                   
REMARK 500  6 ASP A   2     -143.62   -102.72                                   
REMARK 500  6 SER A  81      101.83     -4.17                                   
REMARK 500  6 ASP A  95      -84.96    -80.07                                   
REMARK 500  6 THR A 146      -78.95    -56.67                                   
REMARK 500  7 ASP A  64     -155.60    -89.43                                   
REMARK 500  7 THR A  79       51.41    -91.90                                   
REMARK 500  7 ASP A  80      -42.79   -150.16                                   
REMARK 500  8 SER A  81     -139.41     53.58                                   
REMARK 500  8 ILE A 130      -70.84   -104.79                                   
REMARK 500  8 ASP A 131       23.90    -74.00                                   
REMARK 500  8 THR A 146      -71.12    -65.84                                   
REMARK 500  8 ALA A 147      134.17     79.62                                   
REMARK 500  9 ASP A  80      -66.34   -175.70                                   
REMARK 500  9 ASN A 137     -165.70   -104.83                                   
REMARK 500 10 ASP A  20      107.86    -56.98                                   
REMARK 500 10 ASN A  42       57.87   -142.86                                   
REMARK 500 10 SER A  81     -162.42     55.58                                   
REMARK 500 10 ILE A  85      -56.92   -127.78                                   
REMARK 500 10 ALA A 128      -73.98    -67.12                                   
REMARK 500 10 ILE A 130      -63.38   -102.16                                   
REMARK 500 11 ASP A  56       95.39    -62.96                                   
REMARK 500 11 MET A  76      -58.10     63.39                                   
REMARK 500 11 ASP A  78     -131.84   -111.70                                   
REMARK 500 11 THR A  79       83.88    -69.77                                   
REMARK 500 11 ASP A  80      -40.30   -163.85                                   
REMARK 500 11 THR A 146      -71.10    -55.03                                   
REMARK 500 12 LYS A  21      -71.38    -57.86                                   
REMARK 500 12 ASP A  56       93.67    -68.54                                   
REMARK 500 12 THR A  79       49.43    -88.78                                   
REMARK 500 12 ASP A  80       83.90   -150.02                                   
REMARK 500 12 SER A  81     -154.84     58.01                                   
REMARK 500 12 ILE A 130      -67.16    -90.28                                   
REMARK 500 13 MET A  76       63.51   -103.82                                   
REMARK 500 13 ALA A 147      -67.20    -21.03                                   
REMARK 500 14 THR A  28     -169.77   -102.22                                   
REMARK 500 14 ASP A  56       93.67    -69.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     542 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A   32     GLY A   33          2       144.35                    
REMARK 500 SER A   81     GLU A   82          2      -146.88                    
REMARK 500 SER A   81     GLU A   82          4      -140.39                    
REMARK 500 ALA A  128     ASP A  129         10      -144.87                    
REMARK 500 ASN A   42     PRO A   43         17      -148.91                    
REMARK 500 SER A   81     GLU A   82         20      -145.01                    
REMARK 500 ALA A  128     ASP A  129         27      -143.35                    
REMARK 500 GLN A  135     VAL A  136         31      -148.88                    
REMARK 500 ASN A   42     PRO A   43         33       141.69                    
REMARK 500 ASP A  131     GLY A  132         34       143.45                    
REMARK 500 ASN A   42     PRO A   43         44       147.42                    
REMARK 500 PRO A   43     THR A   44         50       149.40                    
REMARK 500 SER A   81     GLU A   82         54      -149.83                    
REMARK 500 ASP A   78     THR A   79         58      -145.66                    
REMARK 500 ASP A  131     GLY A  132         58       146.44                    
REMARK 500 SER A   81     GLU A   82         65      -146.36                    
REMARK 500 GLY A  132     ASP A  133         67      -147.52                    
REMARK 500 SER A   81     GLU A   82         68       148.28                    
REMARK 500 GLU A  120     VAL A  121         71       146.27                    
REMARK 500 MET A   76     LYS A   77         76       149.00                    
REMARK 500 MET A  109     THR A  110         79       149.86                    
REMARK 500 PRO A   43     THR A   44         80       149.64                    
REMARK 500 ASN A   42     PRO A   43        106       149.58                    
REMARK 500 ALA A  147     LYS A  148        116       143.36                    
REMARK 500 ALA A  128     ASP A  129        117      -149.34                    
REMARK 500 SER A   81     GLU A   82        119      -141.64                    
REMARK 500 ASN A   42     PRO A   43        122       149.63                    
REMARK 500 GLU A   82     GLU A   83        126      -148.35                    
REMARK 500 THR A  146     ALA A  147        129      -145.12                    
REMARK 500 ASP A  131     GLY A  132        158       147.84                    
REMARK 500 ASP A   80     SER A   81        159      -142.26                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 PHE A  12         0.08    SIDE CHAIN                              
REMARK 500  1 ARG A 106         0.10    SIDE CHAIN                              
REMARK 500  1 ARG A 126         0.10    SIDE CHAIN                              
REMARK 500  3 PHE A  19         0.10    SIDE CHAIN                              
REMARK 500  3 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500  3 ARG A 106         0.09    SIDE CHAIN                              
REMARK 500  4 ARG A 106         0.10    SIDE CHAIN                              
REMARK 500  4 TYR A 138         0.17    SIDE CHAIN                              
REMARK 500  6 PHE A  68         0.08    SIDE CHAIN                              
REMARK 500  6 ARG A  86         0.08    SIDE CHAIN                              
REMARK 500  7 ARG A  86         0.10    SIDE CHAIN                              
REMARK 500  7 TYR A 138         0.13    SIDE CHAIN                              
REMARK 500  8 PHE A  16         0.09    SIDE CHAIN                              
REMARK 500  8 ARG A  74         0.10    SIDE CHAIN                              
REMARK 500  8 PHE A  89         0.07    SIDE CHAIN                              
REMARK 500  8 ARG A 106         0.09    SIDE CHAIN                              
REMARK 500  9 ARG A  86         0.11    SIDE CHAIN                              
REMARK 500  9 ARG A 126         0.14    SIDE CHAIN                              
REMARK 500  9 TYR A 138         0.08    SIDE CHAIN                              
REMARK 500 10 PHE A  19         0.07    SIDE CHAIN                              
REMARK 500 10 PHE A  68         0.11    SIDE CHAIN                              
REMARK 500 10 PHE A  92         0.07    SIDE CHAIN                              
REMARK 500 10 ARG A 126         0.13    SIDE CHAIN                              
REMARK 500 10 TYR A 138         0.07    SIDE CHAIN                              
REMARK 500 11 ARG A  37         0.09    SIDE CHAIN                              
REMARK 500 11 TYR A  99         0.12    SIDE CHAIN                              
REMARK 500 11 ARG A 106         0.18    SIDE CHAIN                              
REMARK 500 11 TYR A 138         0.07    SIDE CHAIN                              
REMARK 500 12 ARG A  74         0.09    SIDE CHAIN                              
REMARK 500 12 ARG A  86         0.12    SIDE CHAIN                              
REMARK 500 12 ARG A  90         0.15    SIDE CHAIN                              
REMARK 500 12 TYR A  99         0.09    SIDE CHAIN                              
REMARK 500 12 ARG A 106         0.09    SIDE CHAIN                              
REMARK 500 12 PHE A 141         0.11    SIDE CHAIN                              
REMARK 500 13 PHE A  16         0.08    SIDE CHAIN                              
REMARK 500 13 ARG A  37         0.10    SIDE CHAIN                              
REMARK 500 13 TYR A  99         0.09    SIDE CHAIN                              
REMARK 500 14 ARG A 106         0.09    SIDE CHAIN                              
REMARK 500 15 PHE A  12         0.07    SIDE CHAIN                              
REMARK 500 15 ARG A 126         0.09    SIDE CHAIN                              
REMARK 500 15 TYR A 138         0.08    SIDE CHAIN                              
REMARK 500 16 ARG A  86         0.12    SIDE CHAIN                              
REMARK 500 16 ARG A 106         0.13    SIDE CHAIN                              
REMARK 500 17 ARG A  86         0.09    SIDE CHAIN                              
REMARK 500 17 ARG A  90         0.08    SIDE CHAIN                              
REMARK 500 17 TYR A 138         0.10    SIDE CHAIN                              
REMARK 500 18 PHE A  19         0.12    SIDE CHAIN                              
REMARK 500 18 ARG A  37         0.10    SIDE CHAIN                              
REMARK 500 18 ARG A 126         0.07    SIDE CHAIN                              
REMARK 500 18 PHE A 141         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     454 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500  6 ALA A  15        -10.57                                           
REMARK 500 16 ASP A  50        -10.69                                           
REMARK 500 23 LYS A  75        -10.72                                           
REMARK 500 29 ILE A 125        -10.37                                           
REMARK 500 35 ALA A 102        -11.74                                           
REMARK 500 42 GLU A 127        -10.43                                           
REMARK 500 44 LYS A  75        -10.84                                           
REMARK 500 45 GLU A  84        -10.57                                           
REMARK 500 46 ILE A 100        -10.12                                           
REMARK 500 50 MET A 124        -10.08                                           
REMARK 500 56 VAL A 108        -13.26                                           
REMARK 500 59 MET A  36        -10.19                                           
REMARK 500 67 GLY A 132         10.49                                           
REMARK 500 84 GLY A  33         10.74                                           
REMARK 500 84 VAL A 136        -10.89                                           
REMARK 500 19 TYR A  99        -11.56                                           
REMARK 500 26 LEU A  32        -11.48                                           
REMARK 500 50 MET A 144        -10.11                                           
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 151  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  20   OD2  50.3                                              
REMARK 620 3 ASP A  22   OD2  93.5 143.8                                        
REMARK 620 4 ASP A  24   OD1  71.4  75.4  94.5                                  
REMARK 620 5 THR A  26   O   110.2  61.4 152.4  80.4                            
REMARK 620 6 GLU A  31   OE1 115.9  99.5  97.1 165.7  85.4                      
REMARK 620 7 GLU A  31   OE2  71.8  90.7  75.4 141.0 124.7  51.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 152  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  56   OD2  52.0                                              
REMARK 620 3 ASP A  58   OD2  79.5 123.2                                        
REMARK 620 4 ASN A  60   OD1  92.6  70.7  86.1                                  
REMARK 620 5 THR A  62   O   123.7  72.2 149.3  74.0                            
REMARK 620 6 ASP A  64   OD1 157.7 150.2  82.0  98.4  78.2                      
REMARK 620 7 GLU A  67   OE1  98.1  97.4 119.2 153.9  80.2  80.3                
REMARK 620 8 GLU A  67   OE2  68.2 107.0  73.3 153.7 131.2  94.7  51.1          
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 153  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  85.9                                              
REMARK 620 3 TYR A  99   O    70.7 149.2                                        
REMARK 620 4 GLU A 104   OE1 109.8 121.6  85.9                                  
REMARK 620 5 GLU A 104   OE2  77.6  79.6 113.0  52.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 154  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  84.4                                              
REMARK 620 3 ASP A 133   OD1  78.8  82.0                                        
REMARK 620 4 GLN A 135   O    98.8 154.8  74.2                                  
REMARK 620 5 GLU A 140   OE1 108.5 124.5 152.5  78.4                            
REMARK 620 6 GLU A 140   OE2  79.3  78.4 151.8 126.8  53.4                      
REMARK 620 N                    1     2     3     4     5                       
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 151                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 153                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 154                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J7O   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN N-TERMINAL DOMAIN           
REMARK 900 RELATED ID: 1J7P   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN C-TERMINAL DOMAIN           
REMARK 900 RELATED ID: 2K0F   RELATED DB: PDB                                   
DBREF  2K0E A    1   148  UNP    P62158   CALM_HUMAN       2    149             
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                                          
HET     CA  A 151       1                                                       
HET     CA  A 152       1                                                       
HET     CA  A 153       1                                                       
HET     CA  A 154       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    4(CA 2+)                                                     
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  THR A   79  1                                  16    
HELIX    5   5 GLU A   82  ASP A   93  1                                  12    
HELIX    6   6 ALA A  102  GLY A  113  1                                  12    
HELIX    7   7 THR A  117  GLU A  127  1                                  11    
HELIX    8   8 ASN A  137  LYS A  148  1                                  12    
SHEET    1   A 2 ILE A 100  SER A 101  0                                        
SHEET    2   A 2 GLN A 135  VAL A 136 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 151     1555   1555  2.66  
LINK         OD2 ASP A  20                CA    CA A 151     1555   1555  2.46  
LINK         OD2 ASP A  22                CA    CA A 151     1555   1555  2.56  
LINK         OD1 ASP A  24                CA    CA A 151     1555   1555  2.35  
LINK         O   THR A  26                CA    CA A 151     1555   1555  2.49  
LINK         OE1 GLU A  31                CA    CA A 151     1555   1555  2.60  
LINK         OE2 GLU A  31                CA    CA A 151     1555   1555  2.58  
LINK         OD1 ASP A  56                CA    CA A 152     1555   1555  2.52  
LINK         OD2 ASP A  56                CA    CA A 152     1555   1555  2.53  
LINK         OD2 ASP A  58                CA    CA A 152     1555   1555  2.40  
LINK         OD1 ASN A  60                CA    CA A 152     1555   1555  2.57  
LINK         O   THR A  62                CA    CA A 152     1555   1555  2.48  
LINK         OD1 ASP A  64                CA    CA A 152     1555   1555  2.47  
LINK         OE1 GLU A  67                CA    CA A 152     1555   1555  2.42  
LINK         OE2 GLU A  67                CA    CA A 152     1555   1555  2.64  
LINK         OD1 ASP A  93                CA    CA A 153     1555   1555  2.37  
LINK         OD1 ASP A  95                CA    CA A 153     1555   1555  2.41  
LINK         O   TYR A  99                CA    CA A 153     1555   1555  2.58  
LINK         OE1 GLU A 104                CA    CA A 153     1555   1555  2.45  
LINK         OE2 GLU A 104                CA    CA A 153     1555   1555  2.54  
LINK         OD1 ASP A 129                CA    CA A 154     1555   1555  2.44  
LINK         OD1 ASP A 131                CA    CA A 154     1555   1555  2.47  
LINK         OD1 ASP A 133                CA    CA A 154     1555   1555  2.33  
LINK         O   GLN A 135                CA    CA A 154     1555   1555  2.67  
LINK         OE1 GLU A 140                CA    CA A 154     1555   1555  2.36  
LINK         OE2 GLU A 140                CA    CA A 154     1555   1555  2.39  
SITE     1 AC1  3 ASP A  20  LYS A  21  ASP A  22                               
SITE     1 AC2  4 ILE A  52  ASP A  56  ASP A  58  ILE A  63                    
SITE     1 AC3  6 ASP A  93  LYS A  94  ASP A  95  TYR A  99                    
SITE     2 AC3  6 SER A 101  GLU A 104                                          
SITE     1 AC4  3 TYR A  99  ILE A 125  ASP A 129                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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