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Database: PDB
Entry: 2JT4
LinkDB: 2JT4
Original site: 2JT4 
HEADER    SIGNALING PROTEIN                       18-JUL-07   2JT4              
TITLE     SOLUTION STRUCTURE OF THE SLA1 SH3-3-UBIQUITIN COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOSKELETON ASSEMBLY CONTROL PROTEIN SLA1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: UBIQUITIN;                                                 
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: SH3 DOMAIN SEQUENCE DATABASE RESIDUES 350-420;             
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: SLA1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET30;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  12 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  13 ORGANISM_TAXID: 4932;                                                
SOURCE  14 GENE: UBI1, RPL40A;                                                  
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PET3A                                      
KEYWDS    ENDOCYTOSIS, MONOUBIQUITIN SIGNALING, UBIQUITIN-BINDING               
KEYWDS   2 MOTIF, SH3, UBIQUITIN, ACTIN-BINDING, CYTOPLASM,                     
KEYWDS   3 CYTOSKELETON, PHOSPHORYLATION, SH3 DOMAIN, DNA DAMAGE, DNA           
KEYWDS   4 REPAIR, NUCLEUS, UBL CONJUGATION, SIGNALING PROTEIN                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    Y.HE,I.RADHAKRISHNAN                                                  
REVDAT   2   24-FEB-09 2JT4    1       VERSN                                    
REVDAT   1   25-SEP-07 2JT4    0                                                
JRNL        AUTH   Y.HE,L.HICKE,I.RADHAKRISHNAN                                 
JRNL        TITL   STRUCTURAL BASIS FOR UBIQUITIN RECOGNITION BY SH3            
JRNL        TITL 2 DOMAINS                                                      
JRNL        REF    J.MOL.BIOL.                   V. 373   190 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17765920                                                     
JRNL        DOI    10.1016/J.JMB.2007.07.074                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : ARIA, CNS                                            
REMARK   3   AUTHORS     : LINGE, O'DONOGHUE AND NILGES (ARIA), BRUNGER,        
REMARK   3                 ADAMS, CLORE, GROS, NILGES AND READ (CNS)            
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2JT4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB100256.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 318                                
REMARK 210  PH                             : 6                                  
REMARK 210  IONIC STRENGTH                 : 20                                 
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.9 MM [U-98% 13C; U-98% 15N]      
REMARK 210                                   SH3, 0.9 MM UBIQUITIN, 90%         
REMARK 210                                   H2O/10% D2O; 0.9 MM [U-98%         
REMARK 210                                   13C; U-98% 15N] UBIQUITIN, 0.9     
REMARK 210                                   MM SH3, 90% H2O/10% D2O; 0.9       
REMARK 210                                   MM [U-98% 13C; U-98% 15N] SH3,     
REMARK 210                                   0.9 MM UBIQUITIN, 100% D2O;        
REMARK 210                                   0.9 MM [U-98% 13C; U-98% 15N]      
REMARK 210                                   UBIQUITIN, 0.9 MM SH3, 100% D2O    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D HNCACB, 3D C(CO)NH-TOCSY,       
REMARK 210                                   3D HNCO, 3D H(CCO)NH-TOCSY, 3D     
REMARK 210                                   15N-EDITED NOESY, 3D HCCH-         
REMARK 210                                   COSY, 3D HCCH-TOCSY, 3D 13C-       
REMARK 210                                   EDITED NOESY, 3D 13C-FILTERED,     
REMARK 210                                   13C-EDITED NOESY, 2D 15N,13C-      
REMARK 210                                   DOUBLE-HALF-FILTERED NOESY         
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR, FELIX, NMRVIEW, ARIA,        
REMARK 210                                   CNS                                
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS,            
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 80                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT ENERGIES, RESTRAINT      
REMARK 210                                   VIOLATIONS AND RMS DEVIATIONS      
REMARK 210                                   FROM IDEAL COVALENT GEOMETRY       
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  65      -42.86     70.14                                   
REMARK 500  1 ASP A  66      -71.73    -49.33                                   
REMARK 500  2 SER A   5      -64.10   -100.10                                   
REMARK 500  2 SER A  50      -62.47   -149.93                                   
REMARK 500  2 ARG A  65      -23.53     73.75                                   
REMARK 500  2 ASP A  66      138.06     71.92                                   
REMARK 500  2 LYS A  67       29.24   -159.37                                   
REMARK 500  2 VAL B  17     -157.98   -127.17                                   
REMARK 500  2 LEU B  73       23.32    -78.01                                   
REMARK 500  3 SER A   3       86.46     63.16                                   
REMARK 500  3 SER A  39      -89.88   -106.30                                   
REMARK 500  3 LYS A  40      -55.04    165.17                                   
REMARK 500  3 ARG A  65      -71.33    -56.48                                   
REMARK 500  3 ASP A  66        4.85   -151.48                                   
REMARK 500  3 HIS A  69     -174.62     63.71                                   
REMARK 500  3 LYS B  33      -72.73    -77.98                                   
REMARK 500  4 SER A   3     -166.72     65.41                                   
REMARK 500  4 GLU A  18      -33.97   -130.87                                   
REMARK 500  4 ASP A  41      -63.44   -120.71                                   
REMARK 500  4 ARG A  65      -64.24   -103.99                                   
REMARK 500  4 LYS B  33      -60.92   -107.82                                   
REMARK 500  4 ALA B  46       17.22     58.53                                   
REMARK 500  4 ARG B  74       80.71     43.93                                   
REMARK 500  5 LYS A   4       83.13     64.69                                   
REMARK 500  5 LYS A   6     -167.30     62.74                                   
REMARK 500  5 ASP A  49      -70.73    -62.84                                   
REMARK 500  5 ARG A  65      -54.58   -163.91                                   
REMARK 500  5 ASP A  66     -173.16   -170.47                                   
REMARK 500  5 THR A  70       93.90     49.16                                   
REMARK 500  5 LYS B  33      -63.05    -92.68                                   
REMARK 500  5 ASN B  60       71.69     58.86                                   
REMARK 500  5 LEU B  73       90.76    -67.48                                   
REMARK 500  6 ALA A   2      -44.65   -136.10                                   
REMARK 500  6 SER A   3       85.99     51.58                                   
REMARK 500  6 LYS A   4       89.42     63.47                                   
REMARK 500  6 LYS A  37       27.27   -141.71                                   
REMARK 500  6 LYS A  40      -69.45     70.17                                   
REMARK 500  6 ASP A  66      -87.99     65.84                                   
REMARK 500  6 LYS A  67       -7.47   -147.22                                   
REMARK 500  6 LYS A  68      115.99     69.45                                   
REMARK 500  7 LYS A   4      -75.27   -142.20                                   
REMARK 500  7 SER A   5      -49.56   -145.77                                   
REMARK 500  7 GLU A  18      -41.28   -141.62                                   
REMARK 500  7 ARG A  65      -82.15   -140.68                                   
REMARK 500  7 ASN B  60       90.92     63.27                                   
REMARK 500  8 ALA A   2       94.76     63.31                                   
REMARK 500  8 LEU A  34      -78.27    -76.37                                   
REMARK 500  8 LYS A  37      -62.72    -94.51                                   
REMARK 500  8 VAL A  64       49.48    -82.47                                   
REMARK 500  8 LYS A  68       94.33     63.21                                   
REMARK 500  8 HIS A  69      -79.66   -163.45                                   
REMARK 500  8 THR A  70       76.20     48.86                                   
REMARK 500  8 ALA B  46       19.49     59.37                                   
REMARK 500  8 ARG B  74      -66.54     67.63                                   
REMARK 500  9 LYS A  37       21.74   -148.20                                   
REMARK 500  9 LYS A  40      -64.96     67.23                                   
REMARK 500  9 ARG A  65      -89.93   -141.40                                   
REMARK 500  9 ASP A  66     -158.84   -146.38                                   
REMARK 500  9 LYS A  67      -51.49     77.97                                   
REMARK 500  9 LYS B  33      -70.07    -82.72                                   
REMARK 500 10 ASP A  49      -71.62    -62.85                                   
REMARK 500 10 ARG A  65       76.46   -169.48                                   
REMARK 500 10 LYS A  67       76.83     52.15                                   
REMARK 500 10 LYS B  33      -64.89    -90.64                                   
REMARK 500 10 PRO B  37      121.44    -37.37                                   
REMARK 500 11 ALA A   2      177.40     63.75                                   
REMARK 500 11 LEU A  34      -77.16    -94.07                                   
REMARK 500 11 ASP A  41      -71.46   -140.70                                   
REMARK 500 11 ARG A  65      -86.47    -99.88                                   
REMARK 500 11 LYS A  67      100.86     66.59                                   
REMARK 500 11 THR A  70      -98.26     46.60                                   
REMARK 500 11 GLU B  51      -85.48    -68.95                                   
REMARK 500 11 ASP B  52      -58.66   -179.07                                   
REMARK 500 11 LEU B  73       86.68     55.60                                   
REMARK 500 12 SER A   3      168.17     78.12                                   
REMARK 500 12 LYS A   4      -75.16   -173.47                                   
REMARK 500 12 LYS A   6      148.56     71.27                                   
REMARK 500 12 ARG A  65      -26.73    160.25                                   
REMARK 500 12 ASP A  66       -0.38     79.19                                   
REMARK 500 12 THR A  70      -21.72   -169.62                                   
REMARK 500 12 LEU B  73       26.42    -73.95                                   
REMARK 500 12 ARG B  74      103.91     64.00                                   
REMARK 500 13 ALA A   2      100.82     68.21                                   
REMARK 500 13 ASP A  41      -52.82   -127.95                                   
REMARK 500 13 ARG A  65      -65.08   -133.16                                   
REMARK 500 13 ASP A  66      116.23    171.19                                   
REMARK 500 13 LYS A  67      177.41     59.25                                   
REMARK 500 13 ASN B  60       68.50     64.89                                   
REMARK 500 14 SER A   3       35.66    -81.11                                   
REMARK 500 14 SER A  39      -81.07   -125.00                                   
REMARK 500 14 LYS A  40      -54.67   -175.79                                   
REMARK 500 14 GLN B  41       99.71    -68.09                                   
REMARK 500 14 LEU B  73       30.14    -82.98                                   
REMARK 500 15 SER A   3      172.58     65.82                                   
REMARK 500 15 LYS A   4      -48.41   -131.20                                   
REMARK 500 15 SER A   5      -57.51   -139.89                                   
REMARK 500 15 ASP A  66      -61.89   -160.12                                   
REMARK 500 15 ASN B  60       76.96     60.28                                   
REMARK 500 15 ARG B  74      -67.57     65.68                                   
REMARK 500 16 SER A   5      138.87     73.56                                   
REMARK 500 16 ASP A  66      -84.23    178.68                                   
REMARK 500 16 LYS A  67       95.01   -163.55                                   
REMARK 500 16 LYS B  33      -69.37    -91.02                                   
REMARK 500 16 LEU B  73       85.76     63.02                                   
REMARK 500 17 LEU A  34      -74.16    -98.16                                   
REMARK 500 17 ASP A  36      -58.17   -122.00                                   
REMARK 500 17 ASP A  66      -37.80     72.13                                   
REMARK 500 17 LYS B  33      -77.48    -74.38                                   
REMARK 500 17 ASN B  60       67.98     60.91                                   
REMARK 500 17 ARG B  74       87.49     58.41                                   
REMARK 500 18 LYS A   4       34.48    -97.35                                   
REMARK 500 18 SER A   5       90.58     48.05                                   
REMARK 500 18 LEU A  34      -74.73    -80.02                                   
REMARK 500 18 ASP A  36      -62.85   -128.53                                   
REMARK 500 18 ASP A  41      -51.67   -124.89                                   
REMARK 500 18 ASP A  66      -12.72   -166.11                                   
REMARK 500 18 LYS A  67      161.19     76.65                                   
REMARK 500 18 HIS A  69      -90.00   -127.39                                   
REMARK 500 18 ALA B  46       18.47     58.69                                   
REMARK 500 19 SER A   3      108.87     68.83                                   
REMARK 500 19 LYS A   4      108.34     70.67                                   
REMARK 500 19 LEU A  34      -76.50    -92.52                                   
REMARK 500 19 ASP A  66      100.22     67.47                                   
REMARK 500 19 LYS A  67       77.00     68.13                                   
REMARK 500 19 LEU B  73      100.33    -55.05                                   
REMARK 500 20 ALA A   2      119.94   -161.86                                   
REMARK 500 20 LYS A   4       81.17     59.61                                   
REMARK 500 20 LYS A   6       35.50    -89.82                                   
REMARK 500 20 LYS A   7      133.28     64.39                                   
REMARK 500 20 ARG A  65      -50.38   -164.00                                   
REMARK 500 20 HIS A  69       33.21    -86.11                                   
REMARK 500 20 ARG B  74      -69.18     71.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR                                         
REMARK 650 THE AUTHORS STATE THAT THESE RECORDS REFLECT CONSENSUS               
REMARK 650 START AND END RESIDUES IN THE 20 NMR MODELS.                         
REMARK 650                                                                      
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR                                         
REMARK 700 THE AUTHORS STATE THAT THESE RECORDS REFLECT CONSENSUS               
REMARK 700 START AND END RESIDUES IN THE 20 NMR MODELS.                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UBQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Z9Z   RELATED DB: PDB                                   
DBREF  2JT4 A    1    71  UNP    P32790   SLA1_YEAST     350    420             
DBREF  2JT4 B    1    76  UNP    P61864   UBIQ_YEAST       1     76             
SEQRES   1 A   71  MET ALA SER LYS SER LYS LYS ARG GLY ILE VAL GLN TYR          
SEQRES   2 A   71  ASP PHE MET ALA GLU SER GLN ASP GLU LEU THR ILE LYS          
SEQRES   3 A   71  SER GLY ASP LYS VAL TYR ILE LEU ASP ASP LYS LYS SER          
SEQRES   4 A   71  LYS ASP TRP TRP MET CYS GLN LEU VAL ASP SER GLY LYS          
SEQRES   5 A   71  SER GLY LEU VAL PRO ALA GLN PHE ILE GLU PRO VAL ARG          
SEQRES   6 A   71  ASP LYS LYS HIS THR GLU                                      
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 B   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HELIX    1   1 ILE B   23  LYS B   33  1                                  11    
SHEET    1   A 5 SER A  53  PRO A  57  0                                        
SHEET    2   A 5 TRP A  42  LEU A  47 -1  N  TRP A  43   O  VAL A  56           
SHEET    3   A 5 LYS A  30  ASP A  35 -1  N  TYR A  32   O  GLN A  46           
SHEET    4   A 5 LYS A   7  VAL A  11 -1  N  LYS A   7   O  ILE A  33           
SHEET    5   A 5 ILE A  61  PRO A  63 -1  O  GLU A  62   N  ILE A  10           
SHEET    1   B 5 THR B  12  GLU B  16  0                                        
SHEET    2   B 5 GLN B   2  THR B   7 -1  N  ILE B   3   O  LEU B  15           
SHEET    3   B 5 THR B  66  LEU B  71  1  O  LEU B  67   N  LYS B   6           
SHEET    4   B 5 GLN B  41  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5   B 5 LYS B  48  LEU B  50 -1  O  LYS B  48   N  PHE B  45           
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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