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Database: PDB
Entry: 1GK5
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Original site: 1GK5 
HEADER    GROWTH FACTOR                           08-AUG-01   1GK5              
TITLE     SOLUTION STRUCTURE THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH FACTOR      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRO-EPIDERMAL GROWTH FACTOR,PROTRANSFORMING GROWTH FACTOR  
COMPND   3 ALPHA;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 977-1018,UNP RESIDUES 83-89;                  
COMPND   6 SYNONYM: EGF;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: THE PROTEIN IS A CHIMERA OF EPIDERMAL GROWTH FACTOR   
COMPND   9 RESIDUES 977-1018 AND HUMAN TRANSFORMING GROWTH FACTOR ALPHA RESIDUES
COMPND  10 83-89,THE PROTEIN IS A CHIMERA OF EPIDERMAL GROWTH FACTOR RESIDUES   
COMPND  11 977-1018 AND HUMAN TRANSFORMING GROWTH FACTOR ALPHA RESIDUES 83-89   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE, HUMAN;                                 
SOURCE   4 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE   5 GENE: EGF, TGFA;                                                     
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PPIC9                                      
KEYWDS    GROWTH FACTOR, EGF GROWTH FACTOR, CHIMERIC                            
EXPDTA    SOLUTION NMR                                                          
NUMMDL    10                                                                    
AUTHOR    S.G.CHAMBERLIN,L.BRENNAN,S.M.PUDDICOMBE,D.E.DAVIES,D.L.TURNER         
REVDAT   3   28-MAR-18 1GK5    1       COMPND SOURCE DBREF                      
REVDAT   2   24-FEB-09 1GK5    1       VERSN                                    
REVDAT   1   08-AUG-02 1GK5    0                                                
JRNL        AUTH   S.CHAMBERLIN,L.BRENNAN,S.PUDDICOMBE,D.DAVIES,D.TURNER        
JRNL        TITL   SOLUTION STRUCTURE OF THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH 
JRNL        TITL 2 FACTOR.                                                      
JRNL        REF    EUR.J.BIOCHEM.                V. 268  6247 2001              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   11733021                                                     
JRNL        DOI    10.1046/J.0014-2956.2001.02581.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.M.PUDDICOMBE,L.WOOD,S.G.CHAMBERLIN,D.E.DAVIES              
REMARK   1  TITL   THE INTERACTION OF AN EPIDERMAL GROWTH FACTOR/ TRANSFORMING  
REMARK   1  TITL 2 GROWTH FACTOR ALPHA TAIL CHIMERA WITH THE HUMAN EPIDERMAL    
REMARK   1  TITL 3 GROWTH FACTOR RECEPTOR REVEALS UNEXPECTED COMPLEXITIES       
REMARK   1  REF    J.BIOL.CHEM.                  V. 271 30392 1996              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   8940002                                                      
REMARK   1  DOI    10.1074/JBC.271.48.30392                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : INDYANA                                              
REMARK   3   AUTHORS     : BRENNAN L, TURNER DL, MESSIAS AM, TEODORO ML,        
REMARK   3                 LEGALL J, SANTOS H, XAVIER AX.                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GK5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290008426.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 3.0                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D-1H-NOESY 2D-1H-TOCSY 2D-1H      
REMARK 210                                   -COSY                              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ                            
REMARK 210  SPECTROMETER MODEL             : VXR500                             
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : INDYANA                            
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS WITH        
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LEAST RESTRAINT VIOLATION          
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HG   SER A    25     H    LEU A    26              1.03            
REMARK 500   HG   SER A    28     H    TYR A    29              1.30            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 ASP A  11       65.22     77.15                                   
REMARK 500  1 ASN A  16       86.28     45.49                                   
REMARK 500  1 SER A  25      -83.33    -63.67                                   
REMARK 500  1 SER A  38      -32.19   -152.19                                   
REMARK 500  1 CYS A  42       27.72     43.93                                   
REMARK 500  1 ASP A  46       53.20   -113.21                                   
REMARK 500  2 TYR A   3      -42.21   -169.46                                   
REMARK 500  2 CYS A   6      170.04    -55.13                                   
REMARK 500  2 ASP A  11       57.97     77.77                                   
REMARK 500  2 ASN A  16       85.72     44.63                                   
REMARK 500  2 SER A  25      -83.17    -62.03                                   
REMARK 500  2 SER A  38      -23.20   -151.19                                   
REMARK 500  2 CYS A  42       28.13     46.54                                   
REMARK 500  2 ASP A  46       54.11   -109.52                                   
REMARK 500  3 ASP A  11       65.38     77.15                                   
REMARK 500  3 ASN A  16       85.58     44.20                                   
REMARK 500  3 SER A  25      -82.39    -64.25                                   
REMARK 500  3 SER A  38      -34.13   -148.50                                   
REMARK 500  3 ASP A  40      119.63    -38.65                                   
REMARK 500  3 CYS A  42       29.21     44.84                                   
REMARK 500  3 HIS A  44       94.57    -55.93                                   
REMARK 500  4 SER A   2      -26.04   -171.23                                   
REMARK 500  4 TYR A   3       60.99   -169.96                                   
REMARK 500  4 ASP A  11       83.45     77.09                                   
REMARK 500  4 ASN A  16       84.64     43.85                                   
REMARK 500  4 SER A  25      -81.75    -67.42                                   
REMARK 500  4 ASP A  46       52.04   -146.56                                   
REMARK 500  4 LEU A  48      -61.03   -147.85                                   
REMARK 500  5 SER A   2      -22.73    175.37                                   
REMARK 500  5 ASP A  11       57.38     76.86                                   
REMARK 500  5 ASN A  16       86.91     45.87                                   
REMARK 500  5 SER A  25      -83.11    -62.31                                   
REMARK 500  5 SER A  38     -154.03   -139.35                                   
REMARK 500  5 CYS A  42       22.63     42.42                                   
REMARK 500  5 HIS A  44       91.95    -56.56                                   
REMARK 500  5 ASP A  46       52.40   -140.89                                   
REMARK 500  6 ASP A  11       64.31     77.34                                   
REMARK 500  6 ASN A  16       89.12     49.33                                   
REMARK 500  6 MET A  21       97.48   -166.33                                   
REMARK 500  6 SER A  25      -76.42    -66.00                                   
REMARK 500  6 SER A  38     -157.53   -143.40                                   
REMARK 500  6 ASP A  40      108.43    -58.21                                   
REMARK 500  6 HIS A  44       96.18    -65.55                                   
REMARK 500  6 ASP A  46       53.09   -143.03                                   
REMARK 500  6 LEU A  47       28.64    -77.42                                   
REMARK 500  6 LEU A  48       96.67     62.13                                   
REMARK 500  7 SER A   2       27.85   -171.79                                   
REMARK 500  7 ASP A  11       56.63     77.10                                   
REMARK 500  7 ASN A  16       86.39     46.73                                   
REMARK 500  7 SER A  25      -83.25    -64.16                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5120   RELATED DB: BMRB                                  
DBREF  1GK5 A    1    42  UNP    P01132   EGF_MOUSE      977   1018             
DBREF  1GK5 A   43    49  UNP    P01135   TGFA_HUMAN      83     89             
SEQRES   1 A   49  ASN SER TYR PRO GLY CYS PRO SER SER TYR ASP GLY TYR          
SEQRES   2 A   49  CYS LEU ASN GLY GLY VAL CYS MET HIS ILE GLU SER LEU          
SEQRES   3 A   49  ASP SER TYR THR CYS ASN CYS VAL ILE GLY TYR SER GLY          
SEQRES   4 A   49  ASP ARG CYS GLU HIS ALA ASP LEU LEU ALA                      
HELIX    1   1 GLY A   39  GLU A   43  5                                   5    
SHEET    1  AA 2 VAL A  19  ILE A  23  0                                        
SHEET    2  AA 2 SER A  28  ASN A  32 -1  O  SER A  28   N  ILE A  23           
SSBOND   1 CYS A    6    CYS A   20                          1555   1555  2.01  
SSBOND   2 CYS A   14    CYS A   31                          1555   1555  2.02  
SSBOND   3 CYS A   33    CYS A   42                          1555   1555  2.02  
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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