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Database: PDB
Entry: 2ENZ
LinkDB: 2ENZ
Original site: 2ENZ 
HEADER    TRANSFERASE                             28-MAR-07   2ENZ              
TITLE     SOLUTION STRUCTURE OF THE SECOND C1 DOMAIN FROM HUMAN                 
TITLE    2 PROTEIN KINASE C THETA                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE C THETA TYPE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C1 DOMAIN, PHORBOL-ESTER/DAG-TYPE 2;                       
COMPND   5 SYNONYM: NPKC-THETA;                                                 
COMPND   6 EC: 2.7.11.13;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: P060227-08;                               
SOURCE   7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS                           
KEYWDS    ZINC BINDING, DAG/PE-BINDING PROTEIN, DIACYLGLYCEROL,                 
KEYWDS   2 PHORBOL ESTER, TCR, T-CELL, PKC, STRUCTURAL GENOMICS,                
KEYWDS   3 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND                   
KEYWDS   4 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS            
KEYWDS   5 INITIATIVE, RSGI, TRANSFERASE                                        
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL                     
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
REVDAT   2   24-FEB-09 2ENZ    1       VERSN                                    
REVDAT   1   01-APR-08 2ENZ    0                                                
JRNL        AUTH   T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA                             
JRNL        TITL   SOLUTION STRUCTURE OF THE SECOND C1 DOMAIN FROM              
JRNL        TITL 2 HUMAN PROTEIN KINASE C THETA                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 2.1                                            
REMARK   3   AUTHORS     : GUNTERT, P.                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ENZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026893.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 293                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 120MM                              
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.08MM UNIFORMLY 13C,15N-          
REMARK 210                                   LABELED PROTEIN; 20MM TRISHCL;     
REMARK 210                                   100MM NACL; 1MM DTT; 0.02%         
REMARK 210                                   NAN3; 0.05MM ZNCL2; 1MM IDA;       
REMARK 210                                   10% D2O, 90% H2O                   
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY, 3D_        
REMARK 210                                   15N-SEPARATED_NOESY                
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ, 800 MHZ                   
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR 6.1C, NMRPIPE 20020425,       
REMARK 210                                   NMRVIEW 5.0.4, KUJIRA 0.9822,      
REMARK 210                                   CYANA 2.1                          
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS, TARGET       
REMARK 210                                   FUNCTION                           
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 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 ARG A 233       69.27    -69.99                                   
REMARK 500  1 LEU A 255      -56.82   -124.19                                   
REMARK 500  1 ARG A 257       43.36   -109.02                                   
REMARK 500  1 GLN A 258       86.68    -52.44                                   
REMARK 500  1 ALA A 264      -74.14    -96.57                                   
REMARK 500  1 ASN A 279       41.56    -94.43                                   
REMARK 500  2 LYS A 227       64.18   -105.47                                   
REMARK 500  2 ARG A 233       72.46    -69.96                                   
REMARK 500  2 SER A 241      147.15     62.22                                   
REMARK 500  2 CYS A 245      109.06    -53.32                                   
REMARK 500  2 HIS A 247      -67.05    -93.14                                   
REMARK 500  2 LEU A 255      -72.58   -125.57                                   
REMARK 500  2 ARG A 257       41.89   -104.30                                   
REMARK 500  2 HIS A 270     -175.24    -52.63                                   
REMARK 500  2 ASN A 279       45.74    -95.63                                   
REMARK 500  3 SER A 225      114.39    -39.62                                   
REMARK 500  3 ARG A 233       70.12    -69.39                                   
REMARK 500  3 HIS A 247      -71.64   -119.33                                   
REMARK 500  3 LEU A 251      157.80    -47.76                                   
REMARK 500  3 LEU A 255      -74.84   -102.63                                   
REMARK 500  3 GLN A 258       43.30     34.32                                   
REMARK 500  3 ALA A 264      -71.58   -101.65                                   
REMARK 500  3 HIS A 270     -174.92    -52.19                                   
REMARK 500  4 ASP A 229      102.73    -40.84                                   
REMARK 500  4 ARG A 233       72.64    -66.43                                   
REMARK 500  4 LEU A 251      168.37    -44.70                                   
REMARK 500  4 ALA A 264      -71.39   -112.67                                   
REMARK 500  4 HIS A 270     -175.28    -51.58                                   
REMARK 500  4 ASN A 279       34.63    -88.35                                   
REMARK 500  5 ASP A 229      114.68    -37.47                                   
REMARK 500  5 ARG A 233       69.58    -69.69                                   
REMARK 500  5 CYS A 245      101.48    -56.81                                   
REMARK 500  5 HIS A 247      -70.82    -82.67                                   
REMARK 500  5 LEU A 251      178.32    -59.28                                   
REMARK 500  5 LEU A 255      -64.72   -108.41                                   
REMARK 500  5 GLN A 258       38.67     35.84                                   
REMARK 500  5 HIS A 270     -177.91    -58.77                                   
REMARK 500  5 ILE A 283      -89.12    -72.66                                   
REMARK 500  6 ARG A 233       74.39    -63.63                                   
REMARK 500  6 LYS A 240      -62.23   -130.81                                   
REMARK 500  6 HIS A 247      -67.15   -121.76                                   
REMARK 500  6 ARG A 272      -63.29    -93.87                                   
REMARK 500  7 ILE A 228       76.20   -107.67                                   
REMARK 500  7 SER A 241      144.35    -39.00                                   
REMARK 500  7 HIS A 247      -70.09    -87.23                                   
REMARK 500  7 TRP A 253      130.92   -173.23                                   
REMARK 500  7 ALA A 256      -34.43    -37.61                                   
REMARK 500  7 ARG A 257       36.51    -86.65                                   
REMARK 500  7 GLN A 258      -74.29    -41.28                                   
REMARK 500  7 HIS A 270      179.06    -51.64                                   
REMARK 500  7 CYS A 273      -27.76    -39.29                                   
REMARK 500  7 ILE A 283      -77.86    -83.45                                   
REMARK 500  8 SER A 241      153.23    -39.09                                   
REMARK 500  8 HIS A 247      -67.79    -97.65                                   
REMARK 500  8 LEU A 252      172.16    -46.24                                   
REMARK 500  8 TRP A 253      133.35   -173.74                                   
REMARK 500  8 LEU A 255      -74.50    -90.67                                   
REMARK 500  8 GLN A 258      114.81    -36.48                                   
REMARK 500  8 ALA A 264      -60.20    -93.93                                   
REMARK 500  8 HIS A 270      172.15    -48.56                                   
REMARK 500  8 ILE A 283      -79.58    -90.66                                   
REMARK 500  9 HIS A 247      -72.07   -117.80                                   
REMARK 500  9 ARG A 257       26.20     45.22                                   
REMARK 500  9 GLN A 258      104.19    -42.03                                   
REMARK 500  9 ALA A 264      -60.71   -107.42                                   
REMARK 500  9 HIS A 270     -175.75    -51.28                                   
REMARK 500  9 ASN A 279       48.22    -95.13                                   
REMARK 500 10 SER A 224       76.48   -107.46                                   
REMARK 500 10 SER A 225       76.33   -103.62                                   
REMARK 500 10 HIS A 247      -68.13   -127.98                                   
REMARK 500 10 LEU A 255      -70.42   -116.79                                   
REMARK 500 10 ALA A 256      -64.17   -100.92                                   
REMARK 500 10 HIS A 270     -178.85    -50.93                                   
REMARK 500 10 ASN A 279       30.79    -86.64                                   
REMARK 500 10 LEU A 280       67.56   -103.34                                   
REMARK 500 11 CYS A 245      128.91    -39.69                                   
REMARK 500 11 HIS A 247      -71.22   -113.75                                   
REMARK 500 11 LEU A 251     -179.52    -63.90                                   
REMARK 500 11 LEU A 252      124.84   -171.04                                   
REMARK 500 11 ARG A 257       47.94    -78.61                                   
REMARK 500 11 HIS A 270     -178.71    -64.52                                   
REMARK 500 12 ASP A 229      114.32   -162.66                                   
REMARK 500 12 SER A 241      151.08    -44.22                                   
REMARK 500 12 HIS A 247      -68.40   -120.93                                   
REMARK 500 12 ALA A 256      -64.33   -105.15                                   
REMARK 500 12 HIS A 270     -175.88    -65.87                                   
REMARK 500 12 ALA A 278      173.33    -47.84                                   
REMARK 500 12 ASN A 279       46.57    -99.90                                   
REMARK 500 13 SER A 221      129.55    -39.64                                   
REMARK 500 13 PRO A 242       77.87    -69.71                                   
REMARK 500 13 HIS A 247      -73.02   -110.94                                   
REMARK 500 13 LEU A 251      126.16    -34.58                                   
REMARK 500 13 TRP A 253      -74.66    -34.64                                   
REMARK 500 13 GLN A 258       94.16    -36.04                                   
REMARK 500 13 ALA A 264      -74.52   -102.90                                   
REMARK 500 13 HIS A 270     -174.94    -54.92                                   
REMARK 500 14 PRO A 242       78.82    -69.75                                   
REMARK 500 14 HIS A 247      -70.28   -101.56                                   
REMARK 500 14 TRP A 253       94.17    -39.12                                   
REMARK 500 14 ALA A 256       47.54     71.81                                   
REMARK 500 14 ARG A 257       50.49     74.89                                   
REMARK 500 14 ASN A 279       50.67    -94.42                                   
REMARK 500 14 LEU A 280       73.55   -118.56                                   
REMARK 500 15 HIS A 247      -73.25   -110.03                                   
REMARK 500 15 LEU A 251      146.35    -34.78                                   
REMARK 500 15 GLN A 258       93.46    -37.84                                   
REMARK 500 15 HIS A 270     -175.82    -59.04                                   
REMARK 500 15 LEU A 280       79.48   -108.90                                   
REMARK 500 16 PRO A 242       88.57    -69.72                                   
REMARK 500 16 ALA A 256      144.18   -172.80                                   
REMARK 500 16 ALA A 264      -67.39   -106.54                                   
REMARK 500 17 SER A 241      146.71   -176.10                                   
REMARK 500 17 PRO A 242       87.04    -69.64                                   
REMARK 500 17 HIS A 247      -70.64   -110.64                                   
REMARK 500 17 LEU A 255      179.96    -56.37                                   
REMARK 500 17 ALA A 264      -73.17    -76.29                                   
REMARK 500 17 ASN A 279       41.36    -83.22                                   
REMARK 500 18 SER A 221      -72.42    -83.26                                   
REMARK 500 18 PRO A 242       92.83    -69.79                                   
REMARK 500 18 CYS A 245      140.76    -39.35                                   
REMARK 500 18 HIS A 247      -66.87   -123.56                                   
REMARK 500 18 TRP A 253      129.70   -173.52                                   
REMARK 500 18 ALA A 256      -35.64    -39.08                                   
REMARK 500 18 ARG A 257       57.61    -93.56                                   
REMARK 500 18 ALA A 264      -65.10   -102.40                                   
REMARK 500 18 HIS A 270     -176.45    -67.54                                   
REMARK 500 18 ASN A 279       50.95   -104.12                                   
REMARK 500 19 SER A 241      150.78    -36.34                                   
REMARK 500 19 HIS A 247      -73.22   -119.13                                   
REMARK 500 19 LEU A 255      -70.09   -125.75                                   
REMARK 500 19 ARG A 257       26.19     44.88                                   
REMARK 500 19 GLN A 258      108.30    -54.20                                   
REMARK 500 19 ALA A 264      -71.32    -83.86                                   
REMARK 500 19 LEU A 280       65.79   -106.83                                   
REMARK 500 20 HIS A 247      -70.81   -110.89                                   
REMARK 500 20 ARG A 257       44.98     36.15                                   
REMARK 500 20 ASN A 279       50.58    -98.25                                   
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  ZN A 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 232   ND1                                                    
REMARK 620 2 CYS A 262   SG  117.9                                              
REMARK 620 3 CYS A 265   SG  107.0 104.5                                        
REMARK 620 4 CYS A 281   SG  112.1 107.3 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 245   SG                                                     
REMARK 620 2 CYS A 248   SG  103.6                                              
REMARK 620 3 HIS A 270   ND1 109.4 105.5                                        
REMARK 620 4 CYS A 273   SG  111.6 109.0 116.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400                  
DBREF  2ENZ A  227   284  UNP    Q04759   KPCT_HUMAN     227    284             
SEQADV 2ENZ GLY A  220  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ SER A  221  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ SER A  222  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ GLY A  223  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ SER A  224  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ SER A  225  UNP  Q04759              EXPRESSION TAG                 
SEQADV 2ENZ GLY A  226  UNP  Q04759              EXPRESSION TAG                 
SEQRES   1 A   65  GLY SER SER GLY SER SER GLY LYS ILE ASP MET PRO HIS          
SEQRES   2 A   65  ARG PHE LYS VAL TYR ASN TYR LYS SER PRO THR PHE CYS          
SEQRES   3 A   65  GLU HIS CYS GLY THR LEU LEU TRP GLY LEU ALA ARG GLN          
SEQRES   4 A   65  GLY LEU LYS CYS ASP ALA CYS GLY MET ASN VAL HIS HIS          
SEQRES   5 A   65  ARG CYS GLN THR LYS VAL ALA ASN LEU CYS GLY ILE ASN          
HET     ZN  A 300       1                                                       
HET     ZN  A 400       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
SHEET    1   A 3 PHE A 234  VAL A 236  0                                        
SHEET    2   A 3 LEU A 260  CYS A 262 -1  O  LYS A 261   N  LYS A 235           
SHEET    3   A 3 ASN A 268  VAL A 269 -1  O  VAL A 269   N  LEU A 260           
LINK         ND1 HIS A 232                ZN    ZN A 300     1555   1555  2.05  
LINK         SG  CYS A 245                ZN    ZN A 400     1555   1555  2.35  
LINK         SG  CYS A 248                ZN    ZN A 400     1555   1555  2.35  
LINK         SG  CYS A 262                ZN    ZN A 300     1555   1555  2.27  
LINK         SG  CYS A 265                ZN    ZN A 300     1555   1555  2.35  
LINK         ND1 HIS A 270                ZN    ZN A 400     1555   1555  2.05  
LINK         SG  CYS A 273                ZN    ZN A 400     1555   1555  2.29  
LINK         SG  CYS A 281                ZN    ZN A 300     1555   1555  2.26  
SITE     1 AC1  3 PRO A 231  HIS A 232  ARG A 233                               
SITE     1 AC2  3 CYS A 245  HIS A 247  HIS A 270                               
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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