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Database: PDB
Entry: 4BYA
LinkDB: 4BYA
Original site: 4BYA 
HEADER    METAL BINDING PROTEIN                   18-JUL-13   4BYA              
TITLE     CALMODULIN, C-TERMINAL DOMAIN, M144H MUTANT                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN, C-TERMINAL DOMAIN, M144H MUTANT;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 76-144;                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: BANTAM, CHICKENS;                                   
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEXP5-NT/TOPO                             
KEYWDS    CALMODULIN, METAL BINDING PROTEIN                                     
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    Y.S.MOROZ,Y.WU,N.A.J.VAN NULAND,I.V.KORENDOVYCH                       
REVDAT   3   16-DEC-15 4BYA    1       JRNL   MASTER                            
REVDAT   2   25-NOV-15 4BYA    1       JRNL                                     
REVDAT   1   18-JUN-14 4BYA    0                                                
JRNL        AUTH   Y.S.MOROZ,T.T.DUNSTON,O.V.MAKHLYNETS,O.V.MOROZ,Y.WU,         
JRNL        AUTH 2 J.H.YOON,A.B.OLSEN,J.M.MCLAUGHLIN,K.L.MACK,P.M.GOSAVI,       
JRNL        AUTH 3 N.A.J.VAN NULAND,I.V.KORENDOVYCH                             
JRNL        TITL   NEW TRICKS FOR OLD PROTEINS: SINGLE MUTATIONS IN A           
JRNL        TITL 2 NONENZYMATIC PROTEIN GIVE RISE TO VARIOUS ENZYMATIC          
JRNL        TITL 3 ACTIVITIES.                                                  
JRNL        REF    J.AM.CHEM.SOC.                V. 137 14905 2015              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   26555770                                                     
JRNL        DOI    10.1021/JACS.5B07812                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57722.                                       
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303.0                              
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 100 MM                             
REMARK 210  PRESSURE                       : 1.0 ATM                            
REMARK 210  SAMPLE CONTENTS                : 1.1 MM [U-100% 13C; U-100% 15N]    
REMARK 210                                   CCAMM144H, 95% H2O/5% D2O          
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC, 2D 1H-13C          
REMARK 210                                   HSQC, 3D HBHA(CO)NH, 3D            
REMARK 210                                   HNCACB, 3D CBCA(CO)NH, 3D          
REMARK 210                                   HNCO, 3D HCCH-TOCSY, 3D            
REMARK 210                                   N15-NOESY, 3D C13-NOESY            
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600                                
REMARK 210  SPECTROMETER MODEL             : UNITYINOVA                         
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA, NMRPIPE, CNS, XPLOR,        
REMARK 210                                    CARA                              
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST ENERGY  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NONE                                                         
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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: 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 SER A   8     -161.32     53.26                                   
REMARK 500  2 THR A   6       92.24     66.32                                   
REMARK 500  2 ASP A   7     -112.76   -113.52                                   
REMARK 500  2 SER A   8      -96.22   -148.16                                   
REMARK 500  3 ASP A   7      -57.44   -145.16                                   
REMARK 500  4 LEU A   2      -79.22     67.45                                   
REMARK 500  4 LYS A   4       73.67     57.72                                   
REMARK 500  4 LYS A  42       84.87     61.38                                   
REMARK 500  4 ALA A  74      -86.74    -92.21                                   
REMARK 500  5 ASP A   5      -23.19     74.93                                   
REMARK 500  6 ASP A   5      -71.57    -88.41                                   
REMARK 500  6 THR A   6      103.26     49.16                                   
REMARK 500  6 LYS A  42       81.96     57.86                                   
REMARK 500  7 LYS A   4      -37.83     79.60                                   
REMARK 500  7 ASP A   7       93.51    -64.06                                   
REMARK 500  7 SER A   8     -169.89   -169.30                                   
REMARK 500  8 SER A   8     -156.16   -155.03                                   
REMARK 500  8 LYS A  42       80.88     40.59                                   
REMARK 500  9 LYS A   4      -78.38    -60.22                                   
REMARK 500  9 ASP A   5      -65.33    168.36                                   
REMARK 500  9 THR A   6     -159.28   -121.79                                   
REMARK 500  9 SER A   8     -167.61   -109.86                                   
REMARK 500  9 LYS A  42       77.17     59.12                                   
REMARK 500 10 ASP A   5      -59.48   -124.42                                   
REMARK 500 10 THR A   6       75.60     51.19                                   
REMARK 500 10 ASP A   7      -50.60   -134.06                                   
REMARK 500 11 LYS A  42       85.96     61.67                                   
REMARK 500 11 ALA A  74     -164.17   -104.84                                   
REMARK 500 12 THR A   6     -112.46   -104.15                                   
REMARK 500 12 LYS A  42       86.81     56.68                                   
REMARK 500 13 LYS A   4       99.29     64.94                                   
REMARK 500 13 LYS A  42       78.80     58.60                                   
REMARK 500 14 ASN A  64     -179.30    -65.25                                   
REMARK 500 15 ASP A   5      -75.05    -64.03                                   
REMARK 500 16 LYS A   4     -171.50     63.25                                   
REMARK 500 16 SER A   8     -121.81     68.19                                   
REMARK 500 16 LYS A  42       90.31     59.43                                   
REMARK 500 17 LEU A   2       81.91     60.00                                   
REMARK 500 17 LYS A   4       86.23     53.86                                   
REMARK 500 17 ASP A   7      -87.57    -89.31                                   
REMARK 500 17 LYS A  42       76.41   -104.60                                   
REMARK 500 17 ALA A  74     -163.35   -116.34                                   
REMARK 500 18 LYS A   4      -81.24   -114.05                                   
REMARK 500 18 ASP A   5      -25.59     72.10                                   
REMARK 500 18 ASP A   7      -61.59   -103.79                                   
REMARK 500 18 LYS A  42       81.64     62.11                                   
REMARK 500 18 ALA A  74     -160.38   -105.81                                   
REMARK 500 19 LEU A   2       81.16   -159.30                                   
REMARK 500 19 MET A   3      -27.57     74.07                                   
REMARK 500 20 THR A   6       75.52     49.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
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                           1  CA A  76  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  78.4                                              
REMARK 620 3 ASP A  22   OD2 111.0  50.8                                        
REMARK 620 4 ASN A  24   OD1 101.8  73.9 104.0                                  
REMARK 620 5 TYR A  26   O   115.7 146.2 132.8  73.2                            
REMARK 620 6 GLU A  31   OE1  76.4 103.9  75.1 177.4 109.2                      
REMARK 620 7 GLU A  31   OE2 129.7 125.9  75.1 125.9  70.5  56.4                
REMARK 620 8 ASP A  20   OD2  50.4 112.0 160.0  76.6  66.9 103.3 121.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  CA A  77  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  56   OD2  50.5                                              
REMARK 620 3 ASP A  58   OD1 116.9  69.9                                        
REMARK 620 4 ASP A  60   OD1  94.2  75.4  88.6                                  
REMARK 620 5 ASP A  60   OD2 143.7 115.0  75.2  50.4                            
REMARK 620 6 GLN A  62   O    67.1 101.9 155.4  66.7  88.3                      
REMARK 620 7 ASP A  58   OD2 143.7 116.6  50.1 116.5  71.4 141.0                
REMARK 620 8 GLU A  67   OE1  82.6 125.4 125.5 143.2 119.6  78.5  83.2          
REMARK 620 9 GLU A  67   OE2  74.5  84.2  81.5 159.4 141.5 121.6  70.1  53.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
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  76                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A  77                 
DBREF  4BYA A    3    71  UNP    F2Z4K8   F2Z4K8_CHICK    76    144             
SEQADV 4BYA SER A    1  UNP  F2Z4K8              EXPRESSION TAG                 
SEQADV 4BYA LEU A    2  UNP  F2Z4K8              EXPRESSION TAG                 
SEQADV 4BYA HIS A   71  UNP  F2Z4K8    MET   144 ENGINEERED MUTATION            
SEQADV 4BYA MET A   72  UNP  F2Z4K8              EXPRESSION TAG                 
SEQADV 4BYA THR A   73  UNP  F2Z4K8              EXPRESSION TAG                 
SEQADV 4BYA ALA A   74  UNP  F2Z4K8              EXPRESSION TAG                 
SEQADV 4BYA LYS A   75  UNP  F2Z4K8              EXPRESSION TAG                 
SEQRES   1 A   75  SER LEU MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG          
SEQRES   2 A   75  GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR          
SEQRES   3 A   75  ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU          
SEQRES   4 A   75  GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE          
SEQRES   5 A   75  ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR          
SEQRES   6 A   75  GLU GLU PHE VAL GLN HIS MET THR ALA LYS                      
HET     CA  A  76       1                                                       
HET     CA  A  77       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    2(CA 2+)                                                     
HELIX    1   1 GLU A    9  ASP A   20  1                                  12    
HELIX    2   2 SER A   28  GLY A   40  1                                  13    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 ASN A   64  LYS A   75  1                                  12    
LINK        CA    CA A  76                 OD1 ASP A  20     1555   1555  2.29  
LINK        CA    CA A  76                 OD1 ASP A  22     1555   1555  2.25  
LINK        CA    CA A  76                 OD2 ASP A  22     1555   1555  2.66  
LINK        CA    CA A  76                 OD1 ASN A  24     1555   1555  2.30  
LINK        CA    CA A  76                 O   TYR A  26     1555   1555  2.43  
LINK        CA    CA A  76                 OE1 GLU A  31     1555   1555  2.25  
LINK        CA    CA A  76                 OE2 GLU A  31     1555   1555  2.32  
LINK        CA    CA A  76                 OD2 ASP A  20     1555   1555  2.64  
LINK        CA    CA A  77                 OD2 ASP A  56     1555   1555  2.65  
LINK        CA    CA A  77                 OD1 ASP A  58     1555   1555  2.23  
LINK        CA    CA A  77                 OD1 ASP A  60     1555   1555  2.24  
LINK        CA    CA A  77                 OD2 ASP A  60     1555   1555  2.66  
LINK        CA    CA A  77                 O   GLN A  62     1555   1555  2.66  
LINK        CA    CA A  77                 OD2 ASP A  58     1555   1555  2.69  
LINK        CA    CA A  77                 OE1 GLU A  67     1555   1555  2.25  
LINK        CA    CA A  77                 OE2 GLU A  67     1555   1555  2.50  
LINK        CA    CA A  77                 OD1 ASP A  56     1555   1555  2.29  
SITE     1 AC1  5 ASP A  20  ASP A  22  ASN A  24  TYR A  26                    
SITE     2 AC1  5 GLU A  31                                                     
SITE     1 AC2  6 ASP A  56  ASP A  58  ASP A  60  GLN A  62                    
SITE     2 AC2  6 ASN A  64  GLU A  67                                          
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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