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Database: PDB
Entry: 1PKT
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Original site: 1PKT 
HEADER    PHOSPHOTRANSFERASE                      07-MAR-94   1PKT              
TITLE     STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN;
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.1.137;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    PHOSPHOTRANSFERASE                                                    
EXPDTA    SOLUTION NMR                                                          
NUMMDL    30                                                                    
AUTHOR    S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,S.L.SCHREIBER        
REVDAT   3   29-NOV-17 1PKT    1       REMARK HELIX                             
REVDAT   2   24-FEB-09 1PKT    1       VERSN                                    
REVDAT   1   31-MAY-94 1PKT    0                                                
JRNL        AUTH   S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,            
JRNL        AUTH 2 S.L.SCHREIBER                                                
JRNL        TITL   STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3     
JRNL        TITL 2 FAMILY.                                                      
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  72   945 1993              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   7681364                                                      
JRNL        DOI    10.1016/0092-8674(93)90582-B                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,            
REMARK   1  AUTH 2 S.L.SCHREIBER                                                
REMARK   1  TITL   1H AND 15N ASSIGNMENTS AND SECONDARY STRUCTURE OF THE PI3L   
REMARK   1  TITL 2 SH3 DOMAIN                                                   
REMARK   1  REF    FEBS LETT.                    V. 324    93 1993              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PKT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000175716.                                   
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   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 30                                 
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 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 1-30                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500  1 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500  2 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500  3 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500  4 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500  4 TRP A  55   CG    TRP A  55   CD2    -0.102                       
REMARK 500  5 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500  5 TRP A  55   CG    TRP A  55   CD2    -0.102                       
REMARK 500  6 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500  7 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500  8 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500  9 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 10 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 11 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500 12 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 13 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 14 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 15 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 16 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 17 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 18 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500 19 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500 19 TRP A  55   CG    TRP A  55   CD2    -0.102                       
REMARK 500 20 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 21 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 22 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 23 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 24 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 25 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 26 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500 27 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 28 HIS A  25   CG    HIS A  25   ND1    -0.101                       
REMARK 500 29 HIS A  25   CG    HIS A  25   ND1    -0.100                       
REMARK 500 30 HIS A  25   CG    HIS A  25   ND1    -0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  1 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  1 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  1 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500  1 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500  2 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  2 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500  2 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500  2 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500  3 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  3 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  3 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500  3 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500  4 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  4 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  4 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500  4 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500  5 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  5 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500  5 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500  5 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500  6 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  6 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  6 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500  6 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500  7 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  7 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500  7 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500  7 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500  8 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  8 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  8 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500  8 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500  9 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  9 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  9 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500  9 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500 10 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500 10 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500 10 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500 10 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500 11 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500 11 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500 11 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500 11 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500 12 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500 12 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500 12 TRP A  55   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500 12 TRP A  55   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500 13 TRP A  55   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500 13 TRP A  55   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     120 ANGLE DEVIATIONS.                             
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 LYS A  16       95.71    153.68                                   
REMARK 500  1 GLU A  19       25.85    -74.38                                   
REMARK 500  1 GLU A  20       13.98   -149.05                                   
REMARK 500  1 ASP A  23      109.68    -49.15                                   
REMARK 500  1 ARG A  49       75.80   -119.14                                   
REMARK 500  1 GLU A  52       50.48   -114.12                                   
REMARK 500  1 ILE A  53      -45.71   -134.91                                   
REMARK 500  2 TYR A  12     -169.02   -129.75                                   
REMARK 500  2 TYR A  14      118.17   -173.42                                   
REMARK 500  2 LYS A  16      109.26    -42.70                                   
REMARK 500  2 LYS A  34       53.84    -90.47                                   
REMARK 500  2 PHE A  42     -172.76    -59.94                                   
REMARK 500  2 GLU A  52       47.06    -98.64                                   
REMARK 500  2 ILE A  53      -42.21   -146.89                                   
REMARK 500  3 ALA A  10       85.36    -61.94                                   
REMARK 500  3 TYR A  14      115.58    179.75                                   
REMARK 500  3 LYS A  16       93.23    -39.69                                   
REMARK 500  3 PHE A  42     -168.32    -67.26                                   
REMARK 500  3 GLU A  52       51.53   -113.75                                   
REMARK 500  3 ILE A  53      -39.58   -141.49                                   
REMARK 500  3 TYR A  76      113.39    -37.56                                   
REMARK 500  4 TYR A  12     -158.72   -128.18                                   
REMARK 500  4 TYR A  14      113.79   -171.49                                   
REMARK 500  4 LYS A  16       93.16    -55.08                                   
REMARK 500  4 ASN A  33     -165.68    -61.22                                   
REMARK 500  4 LYS A  34      -70.98    -89.08                                   
REMARK 500  4 PHE A  42     -168.13    -67.21                                   
REMARK 500  4 GLU A  52       34.06    -99.28                                   
REMARK 500  4 GLU A  75       87.15   -154.84                                   
REMARK 500  5 LYS A  16       88.87    -55.80                                   
REMARK 500  5 ASN A  33     -171.97    -56.21                                   
REMARK 500  5 PHE A  42     -168.28    -69.66                                   
REMARK 500  5 THR A  62      -79.76    -41.26                                   
REMARK 500  5 TYR A  76      110.58    -37.67                                   
REMARK 500  6 ALA A  10       99.12    -66.02                                   
REMARK 500  6 TYR A  12     -163.59   -127.94                                   
REMARK 500  6 LYS A  16       92.13     64.19                                   
REMARK 500  6 GLU A  17      -80.06    -86.02                                   
REMARK 500  6 ASN A  33      178.48    -47.79                                   
REMARK 500  6 LYS A  34      -71.31    -87.40                                   
REMARK 500  6 PHE A  42     -168.92    -53.81                                   
REMARK 500  6 GLU A  52       43.92    -90.70                                   
REMARK 500  6 ILE A  53      -40.19   -136.68                                   
REMARK 500  6 TYR A  76      115.78    -37.75                                   
REMARK 500  6 ILE A  77       28.47   -149.37                                   
REMARK 500  7 ALA A  10      103.31    -44.92                                   
REMARK 500  7 GLU A  17      -84.26    -68.23                                   
REMARK 500  7 LEU A  26      151.07    -42.81                                   
REMARK 500  7 PHE A  42     -168.42    -55.75                                   
REMARK 500  7 ASP A  44       95.77    -57.80                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     246 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PKS   RELATED DB: PDB                                   
DBREF  1PKT A    1    79  UNP    P27986   P85A_HUMAN       1     79             
SEQRES   1 A   79  MET SER ALA GLU GLY TYR GLN TYR ARG ALA LEU TYR ASP          
SEQRES   2 A   79  TYR LYS LYS GLU ARG GLU GLU ASP ILE ASP LEU HIS LEU          
SEQRES   3 A   79  GLY ASP ILE LEU THR VAL ASN LYS GLY SER LEU VAL ALA          
SEQRES   4 A   79  LEU GLY PHE SER ASP GLY GLN GLU ALA ARG PRO GLU GLU          
SEQRES   5 A   79  ILE GLY TRP LEU ASN GLY TYR ASN GLU THR THR GLY GLU          
SEQRES   6 A   79  ARG GLY ASP PHE PRO GLY THR TYR VAL GLU TYR ILE GLY          
SEQRES   7 A   79  ARG                                                          
HELIX    1  H1 LYS A   34  ALA A   39  1RIGHT-HANDED ALPHA HELIX           6    
HELIX    2  H2 GLN A   46  ARG A   49  1RIGHT-HANDED 3=10= HELIX           4    
HELIX    3  H3 PRO A   50  ILE A   53  1RIGHT-HANDED 3=10= HELIX           4    
HELIX    4  H4 GLY A   71  VAL A   74  1RIGHT-HANDED 3=10= HELIX           4    
SHEET    1  S1 5 GLU A  65  PRO A  70  0                                        
SHEET    2  S1 5 TRP A  55  ASN A  60 -1  N  GLY A  58   O  GLY A  67           
SHEET    3  S1 5 ASP A  28  VAL A  32 -1  N  THR A  31   O  TYR A  59           
SHEET    4  S1 5 TYR A   6  LEU A  11 -1  N  TYR A   8   O  LEU A  30           
SHEET    5  S1 5 VAL A  74  GLY A  78 -1  N  GLU A  75   O  ARG A   9           
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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