HEADER    MEMBRANE PROTEIN                        02-JUN-03   1PJD              
TITLE     STRUCTURE AND TOPOLOGY OF A PEPTIDE SEGMENT OF THE 6TH TRANSMEMBRANE  
TITLE    2 DOMAIN OF THE SACCHAROMYCES CEREVISIAE ALPHA-FACTOR RECEPTOR IN      
TITLE    3 PHOSPHOLIPID BILAYERS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHEROMONE ALPHA FACTOR RECEPTOR;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN A PORTION OF THE    
SOURCE   4 6TH TRANSMEMBRANE DOMAIN OF THE ALPHA FACTOR RECEPTOR OF             
SOURCE   5 SACCHAROMYCES CEREVISIAE. 15N SELECTIVELY LABELED FMOC-LEU, -ALA, -  
SOURCE   6 PHE, -VAL, -ILE WERE USED.                                           
KEYWDS    ALPHA HELIX, MEMBRANE PROTEIN                                         
EXPDTA    SOLID-STATE NMR                                                       
AUTHOR    K.G.VALENTINE,S.-F.LIU,F.M.MARASSI,G.VEGLIA,A.A.NEVZOROV,S.J.OPELLA,  
AUTHOR   2 F.-X.DING,S.-H.WANG,B.ARSHAVA,J.M.BECKER,F.NAIDER                    
REVDAT   3   27-OCT-21 1PJD    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 1PJD    1       VERSN                                    
REVDAT   1   16-SEP-03 1PJD    0                                                
JRNL        AUTH   K.G.VALENTINE,S.-F.LIU,F.M.MARASSI,G.VEGLIA,S.J.OPELLA,      
JRNL        AUTH 2 F.-X.DING,S.-H.WANG,B.ARSHAVA,J.M.BECKER,F.NAIDER            
JRNL        TITL   STRUCTURE AND TOPOLOGY OF A PEPTIDE SEGMENT OF THE 6TH       
JRNL        TITL 2 TRANSMEMBRANE DOMAIN OF THE SACCHAROMYCES CEREVISIAE         
JRNL        TITL 3 ALPHA-FACTOR RECEPTOR IN PHOSPHOLIPID BILAYERS               
JRNL        REF    BIOPOLYMERS                   V.  59   243 2001              
JRNL        REFN                   ISSN 0006-3525                               
JRNL        PMID   11473349                                                     
JRNL        DOI    10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H  
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : FELIX 97, SRUCTURAL FITTING 1.0                      
REMARK   3   AUTHORS     : ACCELRYS (FELIX), NEVZOROV, OPELLA (SRUCTURAL        
REMARK   3                 FITTING)                                             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS STRUCTURE WAS CALCULATED BY USING    
REMARK   3  A STRUCTURAL FITTING ALGORITHM THAT FINDS TORSION ANGLES BETWEEN    
REMARK   3  CONSECUTIVE RESIDUES BASED ON THEIR NMR FREQUENCIES.                
REMARK   4                                                                      
REMARK   4 1PJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019358.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 278                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : ALIGNED SAMPLE ON GLASS PLATES     
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : PISEMA                             
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : MAGNEX                             
REMARK 210  SPECTROMETER MANUFACTURER      : HOME-BUILT                         
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : SRUCTURAL FITTING 1.0              
REMARK 210   METHOD USED                   : DIRECT STRUCTURAL FITTING OF 2D    
REMARK 210                                   SOLID-STATE NMR SPECTRA            
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: PISEMA: POLARIZATION INVERSION SPIN EXCHANGE AT THE MAGIC    
REMARK 210  ANGLE                                                               
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID-             
REMARK 215 STATE NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE               
REMARK 215 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES            
REMARK 215 ON THESE RECORDS ARE MEANINGLESS.                                    
REMARK 217                                                                      
REMARK 217 SOLID STATE NMR STUDY                                                
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID              
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT           
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 217 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     RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     LYS A    18                                                      
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   O    LEU A    13     H    SER A    16              1.55            
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    VAL A   6      -31.46    -35.12                                   
REMARK 500    ILE A   9      -31.11    -35.21                                   
REMARK 500    ALA A  14      -18.93    -45.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1PJD A    1    18  UNP    P06842   STE2_YEAST     252    269             
SEQADV 1PJD ALA A    1  UNP  P06842    CYS   252 ENGINEERED MUTATION            
SEQRES   1 A   18  ALA GLN SER LEU LEU VAL PRO SER ILE ILE PHE ILE LEU          
SEQRES   2 A   18  ALA TYR SER LEU LYS                                          
HELIX    1   1 LEU A    4  ALA A   14  1                                  11    
HELIX    2   2 TYR A   15  LEU A   17  5                                   3    
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                         
ATOM      1  CA  SER A   3      -0.072   2.021 -11.518  1.00  0.00           C  
ATOM      2  C   SER A   3      -0.967   1.292 -10.529  1.00  0.00           C  
ATOM      3  O   SER A   3      -1.677   1.915  -9.743  1.00  0.00           O  
ATOM      4  N   LEU A   4      -0.920  -0.036 -10.582  1.00  0.00           N  
ATOM      5  CA  LEU A   4      -1.719  -0.880  -9.699  1.00  0.00           C  
ATOM      6  C   LEU A   4      -0.913  -1.284  -8.475  1.00  0.00           C  
ATOM      7  O   LEU A   4      -1.396  -1.206  -7.348  1.00  0.00           O  
ATOM      8  H   LEU A   4      -0.314  -0.487 -11.253  1.00  0.00           H  
ATOM      9  N   LEU A   5       0.321  -1.716  -8.717  1.00  0.00           N  
ATOM     10  CA  LEU A   5       1.222  -2.141  -7.649  1.00  0.00           C  
ATOM     11  C   LEU A   5       1.590  -0.962  -6.763  1.00  0.00           C  
ATOM     12  O   LEU A   5       1.184  -0.893  -5.605  1.00  0.00           O  
ATOM     13  H   LEU A   5       0.657  -1.756  -9.669  1.00  0.00           H  
ATOM     14  N   VAL A   6       2.364  -0.039  -7.326  1.00  0.00           N  
ATOM     15  CA  VAL A   6       2.806   1.153  -6.607  1.00  0.00           C  
ATOM     16  C   VAL A   6       1.721   1.633  -5.656  1.00  0.00           C  
ATOM     17  O   VAL A   6       2.009   2.192  -4.601  1.00  0.00           O  
ATOM     18  H   VAL A   6       2.662  -0.157  -8.284  1.00  0.00           H  
ATOM     19  N   PRO A   7       0.471   1.405  -6.048  1.00  0.00           N  
ATOM     20  CA  PRO A   7      -0.683   1.805  -5.248  1.00  0.00           C  
ATOM     21  C   PRO A   7      -0.946   0.789  -4.149  1.00  0.00           C  
ATOM     22  O   PRO A   7      -1.213   1.151  -3.006  1.00  0.00           O  
ATOM     23  N   SER A   8      -0.868  -0.488  -4.515  1.00  0.00           N  
ATOM     24  CA  SER A   8      -1.094  -1.584  -3.578  1.00  0.00           C  
ATOM     25  C   SER A   8      -0.175  -1.453  -2.374  1.00  0.00           C  
ATOM     26  O   SER A   8      -0.633  -1.291  -1.245  1.00  0.00           O  
ATOM     27  H   SER A   8      -0.645  -0.719  -5.473  1.00  0.00           H  
ATOM     28  N   ILE A   9       1.127  -1.525  -2.636  1.00  0.00           N  
ATOM     29  CA  ILE A   9       2.140  -1.418  -1.590  1.00  0.00           C  
ATOM     30  C   ILE A   9       1.696  -0.437  -0.517  1.00  0.00           C  
ATOM     31  O   ILE A   9       2.040  -0.584   0.653  1.00  0.00           O  
ATOM     32  H   ILE A   9       1.436  -1.657  -3.588  1.00  0.00           H  
ATOM     33  N   ILE A  10       0.927   0.564  -0.936  1.00  0.00           N  
ATOM     34  CA  ILE A  10       0.418   1.589  -0.030  1.00  0.00           C  
ATOM     35  C   ILE A  10      -0.576   0.987   0.950  1.00  0.00           C  
ATOM     36  O   ILE A  10      -0.356   0.998   2.159  1.00  0.00           O  
ATOM     37  H   ILE A  10       0.679   0.626  -1.913  1.00  0.00           H  
ATOM     38  N   PHE A  11      -1.671   0.462   0.408  1.00  0.00           N  
ATOM     39  CA  PHE A  11      -2.721  -0.154   1.213  1.00  0.00           C  
ATOM     40  C   PHE A  11      -2.116  -0.955   2.355  1.00  0.00           C  
ATOM     41  O   PHE A  11      -2.432  -0.729   3.521  1.00  0.00           O  
ATOM     42  H   PHE A  11      -1.791   0.485  -0.595  1.00  0.00           H  
ATOM     43  N   ILE A  12      -1.242  -1.893   1.998  1.00  0.00           N  
ATOM     44  CA  ILE A  12      -0.573  -2.747   2.975  1.00  0.00           C  
ATOM     45  C   ILE A  12       0.142  -1.904   4.019  1.00  0.00           C  
ATOM     46  O   ILE A  12       0.240  -2.289   5.182  1.00  0.00           O  
ATOM     47  H   ILE A  12      -1.026  -2.027   1.020  1.00  0.00           H  
ATOM     48  N   LEU A  13       0.638  -0.749   3.583  1.00  0.00           N  
ATOM     49  CA  LEU A  13       1.352   0.174   4.460  1.00  0.00           C  
ATOM     50  C   LEU A  13       0.470   0.589   5.627  1.00  0.00           C  
ATOM     51  O   LEU A  13       0.956   0.844   6.726  1.00  0.00           O  
ATOM     52  H   LEU A  13       0.522  -0.492   2.613  1.00  0.00           H  
ATOM     53  N   ALA A  14      -0.833   0.651   5.369  1.00  0.00           N  
ATOM     54  CA  ALA A  14      -1.812   1.034   6.382  1.00  0.00           C  
ATOM     55  C   ALA A  14      -1.537   0.307   7.689  1.00  0.00           C  
ATOM     56  O   ALA A  14      -2.002   0.719   8.750  1.00  0.00           O  
ATOM     57  H   ALA A  14      -1.168   0.428   4.442  1.00  0.00           H  
ATOM     58  N   TYR A  15      -0.776  -0.779   7.593  1.00  0.00           N  
ATOM     59  CA  TYR A  15      -0.421  -1.588   8.756  1.00  0.00           C  
ATOM     60  C   TYR A  15       0.454  -0.792   9.710  1.00  0.00           C  
ATOM     61  O   TYR A  15       0.618  -1.161  10.871  1.00  0.00           O  
ATOM     62  H   TYR A  15      -0.427  -1.064   6.689  1.00  0.00           H  
ATOM     63  N   SER A  16       1.011   0.304   9.201  1.00  0.00           N  
ATOM     64  CA  SER A  16       1.878   1.176   9.988  1.00  0.00           C  
ATOM     65  C   SER A  16       1.059   1.989  10.977  1.00  0.00           C  
ATOM     66  O   SER A  16       1.485   2.226  12.105  1.00  0.00           O  
ATOM     67  H   SER A  16       0.833   0.551   8.238  1.00  0.00           H  
ATOM     68  N   LEU A  17      -0.123   2.410  10.535  1.00  0.00           N  
ATOM     69  CA  LEU A  17      -1.028   3.202  11.363  1.00  0.00           C  
ATOM     70  H   LEU A  17      -0.415   2.179   9.596  1.00  0.00           H  
TER      71      LEU A  17                                                      
MASTER      113    0    0    2    0    0    0    6   57    1    0    2          
END