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Database: PDB
Entry: 1A0N
LinkDB: 1A0N
Original site: 1A0N 
HEADER    COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE)    05-DEC-97   1A0N              
TITLE     NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE                   
TITLE    2 TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L             
TITLE    3 CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-          
TITLE    4 KINASE, FAMILY OF 25 STRUCTURES                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRO-PRO-ARG-PRO-LEU-PRO-VAL-ALA-PRO-GLY-SER-SER-           
COMPND   3 LYS-THR;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: P85 SUBUNIT OF PI3-KINASE, RESIDUES 91 - 104;              
COMPND   6 SYNONYM: P2L;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FYN;                                                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: SH3 DOMAIN, RESIDUES 82 - 148;                             
COMPND  12 EC: 2.7.1.112;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 MOL_ID: 2;                                                           
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE), SH3 DOMAIN,                     
KEYWDS   2 POLYPROLINE-BINDING                                                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    25                                                                    
AUTHOR    D.A.RENZONI,D.J.R.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,C.ROSSI,          
AUTHOR   2 M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY                              
REVDAT   2   24-FEB-09 1A0N    1       VERSN                                    
REVDAT   1   25-FEB-98 1A0N    0                                                
JRNL        AUTH   D.A.RENZONI,D.J.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,           
JRNL        AUTH 2 C.ROSSI,M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY              
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF             
JRNL        TITL 2 THE INTERACTION OF THE SH3 DOMAIN FROM FYN WITH              
JRNL        TITL 3 THE PROLINE-RICH BINDING SITE ON THE P85 SUBUNIT             
JRNL        TITL 4 OF PI3-KINASE.                                               
JRNL        REF    BIOCHEMISTRY                  V.  35 15646 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8961927                                                      
JRNL        DOI    10.1021/BI9620969                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.J.MORTON,D.J.PUGH,E.L.BROWN,J.D.KAHMANN,                   
REMARK   1  AUTH 2 D.A.RENZONI,I.D.CAMPBELL                                     
REMARK   1  TITL   SOLUTION STRUCTURE AND PEPTIDE BINDING OF THE SH3            
REMARK   1  TITL 2 DOMAIN FROM HUMAN FYN                                        
REMARK   1  REF    STRUCTURE                     V.   4   705 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A0N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 25                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-25                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     GLY B    83                                                      
REMARK 465     ASP B   152                                                      
REMARK 465     SER B   153                                                      
REMARK 465     ILE B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     GLU B   158                                                      
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 PRO A  94        0.87    -66.47                                   
REMARK 500  1 LEU A  95       96.47    -33.95                                   
REMARK 500  1 PRO A  99     -162.01    -61.04                                   
REMARK 500  1 SER A 102     -162.93     42.88                                   
REMARK 500  1 THR B  85       59.33   -156.27                                   
REMARK 500  1 ASP B 110      173.98    -57.78                                   
REMARK 500  1 PRO B 150      109.88    -58.77                                   
REMARK 500  2 ARG A  93       83.43   -173.89                                   
REMARK 500  2 LEU A  95      133.16    -22.80                                   
REMARK 500  2 VAL A  97       34.05    -93.75                                   
REMARK 500  2 ALA A  98      168.23     54.77                                   
REMARK 500  2 SER A 101       44.13    -92.28                                   
REMARK 500  2 SER A 102       93.11   -177.68                                   
REMARK 500  2 THR B  85       64.04   -158.19                                   
REMARK 500  2 ASP B 128       24.63     48.84                                   
REMARK 500  2 THR B 136      -64.12   -109.02                                   
REMARK 500  3 ARG A  93       75.20   -159.13                                   
REMARK 500  3 LEU A  95      143.04     74.13                                   
REMARK 500  3 SER A 101      -76.23     77.41                                   
REMARK 500  3 SER A 102      136.37     64.29                                   
REMARK 500  3 LYS A 103      -52.63   -121.58                                   
REMARK 500  3 ALA B 105       91.18    -68.32                                   
REMARK 500  3 SER B 125      -38.73   -161.09                                   
REMARK 500  4 PRO A  92       83.27    -61.96                                   
REMARK 500  4 ARG A  93       57.80   -146.81                                   
REMARK 500  4 PRO A  94      105.60    -59.28                                   
REMARK 500  4 LEU A  95      150.19    -45.02                                   
REMARK 500  4 SER A 101      108.67     61.29                                   
REMARK 500  4 ALA B 105      108.00    -42.34                                   
REMARK 500  4 SER B 125       36.42   -172.13                                   
REMARK 500  4 GLU B 126       44.67   -140.05                                   
REMARK 500  4 THR B 136      -72.66    -91.24                                   
REMARK 500  5 PRO A  92       82.36    -62.53                                   
REMARK 500  5 ARG A  93       86.69     40.87                                   
REMARK 500  5 LEU A  95       98.34     65.40                                   
REMARK 500  5 PRO A  96     -164.73    -63.04                                   
REMARK 500  5 SER A 101     -154.30     60.27                                   
REMARK 500  5 SER B 125      -72.08   -143.01                                   
REMARK 500  6 LEU A  95      101.07     62.49                                   
REMARK 500  6 PRO A  96     -165.80    -60.78                                   
REMARK 500  6 PRO A  99     -157.55    -60.99                                   
REMARK 500  6 SER A 102      -50.67   -123.47                                   
REMARK 500  6 THR B  85       73.64   -161.15                                   
REMARK 500  6 PHE B 113     -166.93   -169.23                                   
REMARK 500  6 SER B 125      -68.76   -101.63                                   
REMARK 500  7 ARG A  93       97.49   -177.56                                   
REMARK 500  7 LEU A  95      156.26    -47.21                                   
REMARK 500  7 SER A 101       69.31     61.09                                   
REMARK 500  7 THR B  85       75.52   -166.13                                   
REMARK 500  7 THR B 107     -168.57   -160.31                                   
REMARK 500  7 ASP B 109      -63.33    -95.23                                   
REMARK 500  7 ASP B 110     -174.91    -63.08                                   
REMARK 500  7 GLU B 126       45.97   -107.80                                   
REMARK 500  8 PRO A  92      -78.93    -60.64                                   
REMARK 500  8 PRO A  94      -78.98    -60.58                                   
REMARK 500  8 LEU A  95      105.44     62.87                                   
REMARK 500  8 VAL A  97      129.88     62.35                                   
REMARK 500  8 PRO A  99     -172.27    -60.85                                   
REMARK 500  8 SER B 124       40.59   -148.68                                   
REMARK 500  8 THR B 137      -73.95    -83.94                                   
REMARK 500  9 PRO A  94       90.80    -62.56                                   
REMARK 500  9 PRO A  96     -178.62    -60.96                                   
REMARK 500  9 PRO A  99      -73.42    -61.25                                   
REMARK 500  9 SER A 102       71.33    178.09                                   
REMARK 500  9 THR B  85       74.21   -150.79                                   
REMARK 500  9 SER B 124      -85.88   -169.02                                   
REMARK 500  9 SER B 125       23.10     48.31                                   
REMARK 500  9 ASP B 128      -61.44   -145.16                                   
REMARK 500 10 PRO A  94       81.90    -62.26                                   
REMARK 500 10 SER A 101      -42.15   -144.60                                   
REMARK 500 10 GLU B 104       74.24   -101.44                                   
REMARK 500 10 ASP B 109      -75.09   -104.60                                   
REMARK 500 10 ASP B 110      172.62    -46.96                                   
REMARK 500 11 PRO A  94      -79.66    -59.97                                   
REMARK 500 11 LEU A  95      104.50     60.06                                   
REMARK 500 11 SER A 101      138.21   -175.73                                   
REMARK 500 11 THR B  85       80.85   -158.61                                   
REMARK 500 11 SER B 124       63.66   -114.24                                   
REMARK 500 11 SER B 125       28.02   -152.24                                   
REMARK 500 12 PRO A  92     -162.78    -61.56                                   
REMARK 500 12 LEU A  95      157.81    -46.23                                   
REMARK 500 12 PRO A  96     -155.17    -60.59                                   
REMARK 500 12 PRO A  99     -152.73    -61.47                                   
REMARK 500 12 SER A 101      126.51    172.97                                   
REMARK 500 12 ASP B 110      170.50    -56.53                                   
REMARK 500 12 SER B 125       35.08    -90.08                                   
REMARK 500 12 GLU B 126     -161.98   -108.58                                   
REMARK 500 13 LEU A  95      100.59     62.62                                   
REMARK 500 13 ALA A  98      171.45     57.30                                   
REMARK 500 13 THR B  85       88.28   -158.37                                   
REMARK 500 13 SER B 124       56.23   -163.39                                   
REMARK 500 13 SER B 125       15.54   -144.24                                   
REMARK 500 13 GLU B 126       40.94   -106.85                                   
REMARK 500 14 LEU A  95      110.66     63.54                                   
REMARK 500 14 SER A 101      -76.76   -153.99                                   
REMARK 500 14 ASP B 128      -36.72   -145.93                                   
REMARK 500 15 PRO A  92     -160.23    -59.89                                   
REMARK 500 15 LEU A  95      155.66     72.89                                   
REMARK 500 15 SER A 102      139.41     67.78                                   
REMARK 500 15 LYS A 103      151.07     69.95                                   
REMARK 500 15 PHE B 113     -178.04   -172.92                                   
REMARK 500 15 GLU B 126     -178.53    -50.83                                   
REMARK 500 16 PRO A  94      -78.03    -60.58                                   
REMARK 500 16 LEU A  95      101.22     63.02                                   
REMARK 500 16 ALA A  98      161.50    -45.31                                   
REMARK 500 16 PRO A  99       98.71    -60.96                                   
REMARK 500 16 PHE B 113     -168.72   -174.24                                   
REMARK 500 16 SER B 125      -78.72    -96.51                                   
REMARK 500 16 THR B 136      -70.10    -89.56                                   
REMARK 500 17 PRO A  94      -70.61    -57.98                                   
REMARK 500 17 LEU A  95      114.98     59.15                                   
REMARK 500 17 PRO A  99       84.94    -60.75                                   
REMARK 500 17 THR B  85       86.65   -158.92                                   
REMARK 500 17 PHE B 113     -169.83    174.94                                   
REMARK 500 17 SER B 124       59.92   -141.60                                   
REMARK 500 17 SER B 125       22.39   -143.57                                   
REMARK 500 17 THR B 136      -64.35    -97.39                                   
REMARK 500 18 PRO A  94       85.37    -61.98                                   
REMARK 500 18 LEU A  95      155.27    -40.05                                   
REMARK 500 18 PRO A  96     -178.53    -59.65                                   
REMARK 500 18 ALA A  98      146.73     76.65                                   
REMARK 500 18 ALA B 105      106.56    -54.31                                   
REMARK 500 18 SER B 124       30.77   -152.08                                   
REMARK 500 18 THR B 136      -68.60   -100.09                                   
REMARK 500 19 LEU A  95       93.58     57.11                                   
REMARK 500 19 VAL A  97     -119.03     70.71                                   
REMARK 500 19 SER A 101      102.02   -179.40                                   
REMARK 500 19 ASP B 109      -72.26    -99.45                                   
REMARK 500 19 ASP B 110      166.74    -47.02                                   
REMARK 500 19 PHE B 113     -178.45   -174.90                                   
REMARK 500 19 SER B 124      -99.16   -111.21                                   
REMARK 500 19 SER B 125       28.71     39.38                                   
REMARK 500 19 ASP B 128      -23.62    166.41                                   
REMARK 500 19 THR B 136      -61.54    -98.58                                   
REMARK 500 20 PRO A  92     -176.83    -60.38                                   
REMARK 500 20 LEU A  95      153.87     76.31                                   
REMARK 500 20 THR B  85       50.52   -159.46                                   
REMARK 500 20 ALA B 105      100.44    -51.71                                   
REMARK 500 20 SER B 124       64.56   -161.39                                   
REMARK 500 20 THR B 136      -63.04   -109.04                                   
REMARK 500 21 ARG A  93       69.84     39.59                                   
REMARK 500 21 LEU A  95      111.20     58.45                                   
REMARK 500 21 PRO A  96     -163.00    -58.45                                   
REMARK 500 21 PRO A  99      106.81    -59.85                                   
REMARK 500 21 SER A 101       30.65    -94.72                                   
REMARK 500 21 SER A 102      -93.67     49.18                                   
REMARK 500 21 THR B  85       64.21   -166.44                                   
REMARK 500 21 PHE B 113     -172.73   -175.29                                   
REMARK 500 21 SER B 124       80.58   -154.34                                   
REMARK 500 21 GLU B 126     -164.11    -56.35                                   
REMARK 500 22 PRO A  94      -71.56    -60.24                                   
REMARK 500 22 LEU A  95      102.94     53.72                                   
REMARK 500 22 ALA A  98       92.61     63.38                                   
REMARK 500 22 PRO A  99     -164.11    -61.09                                   
REMARK 500 22 THR B  85       62.48   -119.06                                   
REMARK 500 22 SER B 124       92.30   -171.77                                   
REMARK 500 22 SER B 125      -36.83   -173.96                                   
REMARK 500 22 GLU B 126       58.20   -110.42                                   
REMARK 500 22 THR B 136      -70.33    -91.08                                   
REMARK 500 23 PRO A  92     -154.29    -61.19                                   
REMARK 500 23 LEU A  95      112.49    -38.98                                   
REMARK 500 23 SER A 101       64.08   -160.81                                   
REMARK 500 23 SER A 102      120.98     61.60                                   
REMARK 500 23 SER B 125      -51.80   -134.98                                   
REMARK 500 24 ARG A  93      166.16     62.96                                   
REMARK 500 24 LEU A  95      103.29     58.96                                   
REMARK 500 24 SER A 101      177.63    -59.75                                   
REMARK 500 24 TYR B 103      119.44   -166.19                                   
REMARK 500 25 PRO A  92     -178.37    -60.53                                   
REMARK 500 25 ARG A  93       81.22   -167.48                                   
REMARK 500 25 LEU A  95      104.06     60.02                                   
REMARK 500 25 VAL A  97      124.81     60.29                                   
REMARK 500 25 SER A 101      178.38    177.47                                   
REMARK 500 25 SER A 102       89.19     62.97                                   
REMARK 500 25 LYS A 103       70.70     44.95                                   
REMARK 500 25 THR B  85       59.50   -146.03                                   
REMARK 500 25 PHE B 113     -177.85   -176.68                                   
REMARK 500 25 ASP B 128      -37.59   -142.41                                   
REMARK 500 25 SER B 134      109.98    -57.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 ARG A  93         0.30    SIDE_CHAIN                              
REMARK 500  1 ARG B 106         0.31    SIDE_CHAIN                              
REMARK 500  1 ARG B 133         0.31    SIDE_CHAIN                              
REMARK 500  2 ARG A  93         0.30    SIDE_CHAIN                              
REMARK 500  2 ARG B 106         0.25    SIDE_CHAIN                              
REMARK 500  2 ARG B 133         0.29    SIDE_CHAIN                              
REMARK 500  3 ARG A  93         0.24    SIDE_CHAIN                              
REMARK 500  3 ARG B 106         0.24    SIDE_CHAIN                              
REMARK 500  3 ARG B 133         0.25    SIDE_CHAIN                              
REMARK 500  4 ARG A  93         0.27    SIDE_CHAIN                              
REMARK 500  4 ARG B 106         0.28    SIDE_CHAIN                              
REMARK 500  4 ARG B 133         0.30    SIDE_CHAIN                              
REMARK 500  5 ARG A  93         0.22    SIDE_CHAIN                              
REMARK 500  5 ARG B 106         0.29    SIDE_CHAIN                              
REMARK 500  5 ARG B 133         0.24    SIDE_CHAIN                              
REMARK 500  6 ARG B 106         0.32    SIDE_CHAIN                              
REMARK 500  6 ARG B 133         0.32    SIDE_CHAIN                              
REMARK 500  7 ARG A  93         0.30    SIDE_CHAIN                              
REMARK 500  7 ARG B 106         0.20    SIDE_CHAIN                              
REMARK 500  7 ARG B 133         0.10    SIDE_CHAIN                              
REMARK 500  8 ARG A  93         0.22    SIDE_CHAIN                              
REMARK 500  8 ARG B 106         0.26    SIDE_CHAIN                              
REMARK 500  8 ARG B 133         0.32    SIDE_CHAIN                              
REMARK 500  9 ARG A  93         0.19    SIDE_CHAIN                              
REMARK 500  9 ARG B 106         0.29    SIDE_CHAIN                              
REMARK 500  9 ARG B 133         0.22    SIDE_CHAIN                              
REMARK 500 10 ARG A  93         0.22    SIDE_CHAIN                              
REMARK 500 10 ARG B 106         0.23    SIDE_CHAIN                              
REMARK 500 10 ARG B 133         0.30    SIDE_CHAIN                              
REMARK 500 11 ARG A  93         0.29    SIDE_CHAIN                              
REMARK 500 11 ARG B 106         0.31    SIDE_CHAIN                              
REMARK 500 11 ARG B 133         0.30    SIDE_CHAIN                              
REMARK 500 12 ARG A  93         0.24    SIDE_CHAIN                              
REMARK 500 12 ARG B 133         0.28    SIDE_CHAIN                              
REMARK 500 13 ARG A  93         0.29    SIDE_CHAIN                              
REMARK 500 13 ARG B 106         0.24    SIDE_CHAIN                              
REMARK 500 14 ARG A  93         0.20    SIDE_CHAIN                              
REMARK 500 14 ARG B 106         0.28    SIDE_CHAIN                              
REMARK 500 14 ARG B 133         0.31    SIDE_CHAIN                              
REMARK 500 15 ARG A  93         0.19    SIDE_CHAIN                              
REMARK 500 15 ARG B 106         0.31    SIDE_CHAIN                              
REMARK 500 15 ARG B 133         0.14    SIDE_CHAIN                              
REMARK 500 16 ARG A  93         0.22    SIDE_CHAIN                              
REMARK 500 16 ARG B 106         0.31    SIDE_CHAIN                              
REMARK 500 16 ARG B 133         0.18    SIDE_CHAIN                              
REMARK 500 17 ARG A  93         0.23    SIDE_CHAIN                              
REMARK 500 17 ARG B 106         0.10    SIDE_CHAIN                              
REMARK 500 17 ARG B 133         0.28    SIDE_CHAIN                              
REMARK 500 18 ARG B 106         0.23    SIDE_CHAIN                              
REMARK 500 18 ARG B 133         0.18    SIDE_CHAIN                              
REMARK 500 19 ARG A  93         0.13    SIDE_CHAIN                              
REMARK 500 19 ARG B 106         0.25    SIDE_CHAIN                              
REMARK 500 19 ARG B 133         0.28    SIDE_CHAIN                              
REMARK 500 20 ARG A  93         0.19    SIDE_CHAIN                              
REMARK 500 20 ARG B 106         0.31    SIDE_CHAIN                              
REMARK 500 20 ARG B 133         0.15    SIDE_CHAIN                              
REMARK 500 21 ARG A  93         0.27    SIDE_CHAIN                              
REMARK 500 21 ARG B 106         0.09    SIDE_CHAIN                              
REMARK 500 21 ARG B 133         0.24    SIDE_CHAIN                              
REMARK 500 22 ARG A  93         0.31    SIDE_CHAIN                              
REMARK 500 22 ARG B 106         0.30    SIDE_CHAIN                              
REMARK 500 22 ARG B 133         0.19    SIDE_CHAIN                              
REMARK 500 23 ARG A  93         0.20    SIDE_CHAIN                              
REMARK 500 23 ARG B 106         0.18    SIDE_CHAIN                              
REMARK 500 23 ARG B 133         0.32    SIDE_CHAIN                              
REMARK 500 24 ARG A  93         0.31    SIDE_CHAIN                              
REMARK 500 24 ARG B 106         0.29    SIDE_CHAIN                              
REMARK 500 24 ARG B 133         0.29    SIDE_CHAIN                              
REMARK 500 25 ARG B 106         0.20    SIDE_CHAIN                              
REMARK 500 25 ARG B 133         0.31    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1A0N A   91   104  UNP    P27986   P85A_HUMAN      91    104             
DBREF  1A0N B   80   158  UNP    P06241   FYN_HUMAN       79    147             
SEQADV 1A0N SER B   81  UNP  P06241    GLY    80 CONFLICT                       
SEQRES   1 A   14  PRO PRO ARG PRO LEU PRO VAL ALA PRO GLY SER SER LYS          
SEQRES   2 A   14  THR                                                          
SEQRES   1 B   69  GLY SER THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 B   69  TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS          
SEQRES   3 B   69  GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP          
SEQRES   4 B   69  TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY          
SEQRES   5 B   69  TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER ILE          
SEQRES   6 B   69  GLN ALA GLU GLU                                              
HELIX    1   1 SER B  145  TYR B  147  5                                   3    
SHEET    1   A 5 VAL B 148  PRO B 150  0                                        
SHEET    2   A 5 LEU B  86  ALA B  89 -1  N  VAL B  88   O  ALA B 149           
SHEET    3   A 5 LYS B 118  ASN B 123 -1  N  PHE B 119   O  PHE B  87           
SHEET    4   A 5 TRP B 129  ARG B 133 -1  N  ARG B 133   O  GLN B 120           
SHEET    5   A 5 THR B 140  PRO B 144 -1  N  ILE B 143   O  TRP B 130           
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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