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Database: PDB
Entry: 2KUG
LinkDB: 2KUG
Original site: 2KUG 
HEADER    METAL BINDING PROTEIN                   17-FEB-10   2KUG              
TITLE     HALOTHANE BINDS TO DRUGGABLE SITES IN CALCIUM-CALMODULIN: SOLUTION    
TITLE    2 STRUCTURE OF HALOTHANE-CAM N-TERMINAL DOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN EF-HANDS 1 AND 2;                        
COMPND   5 SYNONYM: CAM;                                                        
COMPND   6 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: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3,      
SOURCE   6 CAMB, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET 15B                                    
KEYWDS    CALMODULIN, CALCIUM BINDING, VOLATILE ANESTHETIC, HALOTHANE,          
KEYWDS   2 CYTOSKELETON, ISOPEPTIDE BOND, METHYLATION, PHOSPHOPROTEIN, METAL    
KEYWDS   3 BINDING PROTEIN                                                      
EXPDTA    SOLUTION NMR                                                          
NUMMDL    5                                                                     
AUTHOR    N.JURANIC,S.MACURA,M.V.SIMEONOV,K.A.JONES,A.R.PENHEITER,T.J.HOCK,     
AUTHOR   2 J.H.STREIFF                                                          
REVDAT   3   05-FEB-20 2KUG    1       REMARK                                   
REVDAT   2   11-DEC-13 2KUG    1       JRNL   VERSN                             
REVDAT   1   09-MAR-10 2KUG    0                                                
JRNL        AUTH   N.O.JURANIC,K.A.JONES,A.R.PENHEITER,T.J.HOCK,J.H.STREIFF     
JRNL        TITL   HALOTHANE BINDS TO DRUGGABLE SITES IN THE [CA2+]4-CALMODULIN 
JRNL        TITL 2 (CAM) COMPLEX, BUT DOES NOT INHIBIT [CA2+]4-CAM ACTIVATION   
JRNL        TITL 3 OF KINASE.                                                   
JRNL        REF    J. SERB. CHEM. SOC.           V.  78  1655 2013              
JRNL        REFN                   ISSN 0352-5139                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR MSI XPLOR 3.843, X-PLOR MSI XPLOR 3.843       
REMARK   3   AUTHORS     : BRUNGER (X-PLOR), BRUNGER (X-PLOR)                   
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 100 STEP STEEPEST DESCENT - FINAL         
REMARK   3  REFINEMENT                                                          
REMARK   4                                                                      
REMARK   4 2KUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000101586.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.2                                
REMARK 210  IONIC STRENGTH                 : 0.1                                
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 2 MM [U-99% 13C; U-99% 15N]        
REMARK 210  CALMODULIN, 20 MM CALCIUM ION, 20 MM N-{[2-({[1-(4-                 
REMARK 210  CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]        
REMARK 210  ACETYL}-2-PHENYLETHYLAMINE, 95% H2O/5% D2O; 2 MM [U-99% 15N]        
REMARK 210  CALMODULIN, 20 MM CALCIUM ION, 20 MM N-{[2-({[1-(4-                 
REMARK 210  CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]        
REMARK 210  ACETYL}-2-PHENYLETHYLAMINE, 95% H2O/5% D2O                          
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D HNCO; 3D HNCA; 3D HNCACB; 3D    
REMARK 210                                   HBHA(CO)NH; 3D H(CCO)NH; 3D HCCH-  
REMARK 210                                   TOCSY; 3D 1H-15N NOESY; 3D 1H-     
REMARK 210                                   13C NOESY; 3D HNHA; 3D HCCH-COSY   
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ; 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : SIMULATED ANNEALING, CHARMM22      
REMARK 210                                   ENERGY MINIMIZATION                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 5                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
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: 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 LYS A  75       84.74    -69.91                                   
REMARK 500  2 LYS A  75       94.35    -64.43                                   
REMARK 500  4 LYS A  75       90.71    -67.55                                   
REMARK 500  5 LYS A  75       94.48    -64.38                                   
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 990  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  26   O                                                      
REMARK 620 2 ASP A  24   OD2  87.2                                              
REMARK 620 3 GLU A  31   OE2 133.2 139.5                                        
REMARK 620 4 GLU A  31   OE1  82.8 169.8  50.5                                  
REMARK 620 5 ASP A  22   OD2 154.8  81.4  60.7 108.6                            
REMARK 620 6 ASP A  20   OD1  76.8  94.1  93.8  85.7  81.6                      
REMARK 620 7 ASP A  24   OD1  61.9  46.3 142.4 128.7  94.5  52.4                
REMARK 620 8 ASP A  22   OD1 112.3  64.7  92.4 121.3  42.5  48.5  54.1          
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 991  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  62   O                                                      
REMARK 620 2 ASP A  58   OD1 119.1                                              
REMARK 620 3 GLU A  67   OE1  76.9 120.5                                        
REMARK 620 4 ASP A  58   OD2 154.7  50.0 128.2                                  
REMARK 620 5 GLU A  67   OE2 114.5  74.0  49.6  85.9                            
REMARK 620 6 ASP A  56   OD1  68.2  56.2  88.0 106.1  74.3                      
REMARK 620 7 ASN A  60   OD1  78.4  62.2 152.0  76.6 134.2  70.6                
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 990                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 991                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HLT A 149                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2KUH   RELATED DB: PDB                                   
REMARK 900 CAM O-TERMINAL DOMAIN STRUCTURE OF THE SAME COMPLEX                  
REMARK 900 RELATED ID: 16764   RELATED DB: BMRB                                 
DBREF  2KUG A    1    76  UNP    P62158   CALM_HUMAN       2     77             
SEQRES   1 A   76  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A   76  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A   76  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A   76  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A   76  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A   76  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET                  
HET     CA  A 990       1                                                       
HET     CA  A 991       1                                                       
HET    HLT  A 149       8                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     HLT 2-BROMO-2-CHLORO-1,1,1-TRIFLUOROETHANE                           
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  HLT    C2 H BR CL F3                                                
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  VAL A   55  1                                  12    
HELIX    4   4 ASP A   64  LYS A   75  1                                  12    
LINK         O   THR A  26                CA    CA A 990     1555   1555  2.45  
LINK         O   THR A  62                CA    CA A 991     1555   1555  2.45  
LINK         OD2 ASP A  24                CA    CA A 990     1555   1555  2.50  
LINK         OD1 ASP A  58                CA    CA A 991     1555   1555  2.53  
LINK         OE2 GLU A  31                CA    CA A 990     1555   1555  2.53  
LINK         OE1 GLU A  31                CA    CA A 990     1555   1555  2.55  
LINK         OE1 GLU A  67                CA    CA A 991     1555   1555  2.57  
LINK         OD2 ASP A  22                CA    CA A 990     1555   1555  2.57  
LINK         OD2 ASP A  58                CA    CA A 991     1555   1555  2.58  
LINK         OE2 GLU A  67                CA    CA A 991     1555   1555  2.59  
LINK         OD1 ASP A  56                CA    CA A 991     1555   1555  2.61  
LINK         OD1 ASN A  60                CA    CA A 991     1555   1555  2.62  
LINK         OD1 ASP A  20                CA    CA A 990     1555   1555  2.72  
LINK         OD1 ASP A  24                CA    CA A 990     1555   1555  2.90  
LINK         OD1 ASP A  22                CA    CA A 990     1555   1555  3.15  
SITE     1 AC1  5 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  5 GLU A  31                                                     
SITE     1 AC2  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  5 GLU A  67                                                     
SITE     1 AC3  3 MET A  36  MET A  51  MET A  71                               
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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