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Database: PDB
Entry: 2LL7
LinkDB: 2LL7
Original site: 2LL7 
HEADER    OXIDOREDUCTASE                          29-OCT-11   2LL7              
TITLE     SOLUTION NMR STRUCTURE OF CAM BOUND TO THE ENOS CAM BINDING DOMAIN    
TITLE    2 PEPTIDE                                                              
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: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;                        
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: CALMODULIN-BINDING REGION RESIDUES 493-509;                
COMPND  10 SYNONYM: CONSTITUTIVE NOS, CNOS, EC-NOS, ENDOTHELIAL NOS, ENOS, NOS  
COMPND  11 TYPE III, NOSIII;                                                    
COMPND  12 EC: 1.14.13.39;                                                      
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: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET9DCAM;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: NOS3;                                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    M.PIAZZA,K.FUTREGA,D.E.SPRATT,J.G.GUILLEMETTE,T.DIECKMANN             
REVDAT   2   14-JUN-23 2LL7    1       REMARK                                   
REVDAT   1   16-MAY-12 2LL7    0                                                
JRNL        AUTH   M.PIAZZA,K.FUTREGA,D.E.SPRATT,T.DIECKMANN,J.G.GUILLEMETTE    
JRNL        TITL   STRUCTURE AND DYNAMICS OF CALMODULIN (CAM) BOUND TO NITRIC   
JRNL        TITL 2 OXIDE SYNTHASE PEPTIDES: EFFECTS OF A PHOSPHOMIMETIC CAM     
JRNL        TITL 3 MUTATION.                                                    
JRNL        REF    BIOCHEMISTRY                  V.  51  3651 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   22486744                                                     
JRNL        DOI    10.1021/BI300327Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNSSOLVE, CNSSOLVE                                   
REMARK   3   AUTHORS     : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ         
REMARK   3                 (CNSSOLVE), BRUNGER, ADAMS, CLORE, GROS, NILGES      
REMARK   3                 AND READ (CNSSOLVE)                                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2LL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000102517.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 6.0                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.0 MM [U-99% 13C; U-99% 15N]      
REMARK 210                                   PROTEIN_1, 1.0 MM PROTEIN_2, 100   
REMARK 210                                   MM POTASSIUM CHLORIDE, 10 MM       
REMARK 210                                   CALCIUM CHLORIDE, 0.2 MM SODIUM    
REMARK 210                                   AZIDE, 90% H2O/10% D2O             
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D CBCA(CO)NH;     
REMARK 210                                   3D HNCA; 3D HCCH-TOCSY; 3D 1H-     
REMARK 210                                   15N NOESY; 3D 1H-13C NOESY         
REMARK 210                                   ALIPHATIC                          
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : DGSA-DISTANCE GEOMETRY SIMULATED   
REMARK 210                                   ANNEALING                          
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 20                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   O    VAL A   121     H    MET A   124              1.58            
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  56       70.00     36.94                                   
REMARK 500  1 THR A  79     -100.26   -149.40                                   
REMARK 500  1 ASP A  80      104.92   -177.03                                   
REMARK 500  1 ASP A 122      -18.65    -43.72                                   
REMARK 500  1 LYS B 150      -41.71   -150.86                                   
REMARK 500  1 THR B 151      -53.99   -153.36                                   
REMARK 500  2 ASP A  56       69.22     28.45                                   
REMARK 500  2 THR A  79      -57.98     56.62                                   
REMARK 500  2 ASP A 118      -16.67    -47.31                                   
REMARK 500  2 ASN A 137     -165.89   -110.00                                   
REMARK 500  2 LYS B 150       50.57     79.29                                   
REMARK 500  2 THR B 151      -62.09   -154.51                                   
REMARK 500  2 PHE B 152      -31.67   -153.88                                   
REMARK 500  2 SER B 164       31.72    -95.50                                   
REMARK 500  3 ASP A   2      126.44     62.97                                   
REMARK 500  3 ASP A  56       70.83     36.80                                   
REMARK 500  3 THR A  79     -106.14   -149.14                                   
REMARK 500  3 ASP A  80       99.22   -160.27                                   
REMARK 500  3 LYS A 115     -136.46    -68.96                                   
REMARK 500  3 LEU A 116      132.91    -31.46                                   
REMARK 500  3 ARG A 126      -14.95    -47.14                                   
REMARK 500  3 ALA A 147       76.18   -105.22                                   
REMARK 500  3 LYS B 150      -39.84   -149.16                                   
REMARK 500  3 THR B 151      -49.54   -157.23                                   
REMARK 500  4 ASP A   2      131.57     63.62                                   
REMARK 500  4 ARG A  37      -19.76    -45.76                                   
REMARK 500  4 GLN A  41      127.14   -175.35                                   
REMARK 500  4 ASN A  42      -53.21   -130.04                                   
REMARK 500  4 ASP A  56       69.82     35.92                                   
REMARK 500  4 THR A  79      -96.67   -147.73                                   
REMARK 500  4 ASP A  80      105.39   -176.69                                   
REMARK 500  4 LYS A 115     -138.34    -54.53                                   
REMARK 500  4 LEU A 116      166.71    -40.30                                   
REMARK 500  4 ASP A 118      -17.75    -40.08                                   
REMARK 500  4 ASP A 129       93.59    -61.63                                   
REMARK 500  4 LYS B 150      -37.33   -156.21                                   
REMARK 500  5 GLU A   6      -17.48    -49.78                                   
REMARK 500  5 THR A  79     -104.50   -142.53                                   
REMARK 500  5 LYS A 115     -137.01    -75.11                                   
REMARK 500  5 LEU A 116      145.39    -33.95                                   
REMARK 500  5 ASP A 118      -16.85    -38.64                                   
REMARK 500  5 ALA A 128       44.18   -149.46                                   
REMARK 500  5 ASP A 129      103.63    -59.62                                   
REMARK 500  5 ALA A 147       74.43   -104.29                                   
REMARK 500  5 THR B 151      -33.29     89.28                                   
REMARK 500  5 PHE B 152       22.44   -173.88                                   
REMARK 500  6 ASP A  56       69.54     26.31                                   
REMARK 500  6 ASP A  64     -162.06   -119.69                                   
REMARK 500  6 THR A  79     -108.61   -157.29                                   
REMARK 500  6 ASP A  80      101.53   -167.59                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     173 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2LL6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 18028   RELATED DB: BMRB                                 
DBREF  2LL7 A    1   148  UNP    P62158   CALM_HUMAN       2    149             
DBREF  2LL7 B  149   165  UNP    P29474   NOS3_HUMAN     493    509             
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                                          
SEQRES   1 B   17  LYS LYS THR PHE LYS GLU VAL ALA ASN ALA VAL LYS ILE          
SEQRES   2 B   17  SER ALA SER LEU                                              
HELIX    1   1 THR A    5  GLU A   14  1                                  10    
HELIX    2   2 ALA A   15  ASP A   20  1                                   6    
HELIX    3   3 GLU A   31  GLY A   40  1                                  10    
HELIX    4   4 THR A   44  ASP A   50  1                                   7    
HELIX    5   5 ASP A   64  LEU A   69  1                                   6    
HELIX    6   6 LEU A   69  ARG A   74  1                                   6    
HELIX    7   7 SER A   81  ARG A   86  1                                   6    
HELIX    8   8 ARG A   86  ASP A   93  1                                   8    
HELIX    9   9 ALA A  102  THR A  110  1                                   9    
HELIX   10  10 ASN A  111  GLY A  113  5                                   3    
HELIX   11  11 GLU A  119  ALA A  128  5                                  10    
HELIX   12  12 ASN A  137  MET A  145  1                                   9    
HELIX   13  13 PHE B  152  SER B  162  1                                  11    
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           
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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