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Database: PDB
Entry: 2AKI
LinkDB: 2AKI
Original site: 2AKI 
HEADER    PROTEIN TRANSPORT                       03-AUG-05   2AKI              
TITLE     NORMAL MODE-BASED FLEXIBLE FITTED COORDINATES OF A TRANSLOCATING      
TITLE    2 SECYEG PROTEIN-CONDUCTING CHANNEL INTO THE CRYO-EM MAP OF A SECYEG-  
TITLE    3 NASCENT CHAIN-70S RIBOSOME COMPLEX FROM E. COLI                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN-EXPORT MEMBRANE PROTEIN SECG;                      
COMPND   3 CHAIN: X, A;                                                         
COMPND   4 SYNONYM: PREPROTEIN TRANSLOCASE BAND 1 SUBUNIT, P12;                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PREPROTEIN TRANSLOCASE SECY SUBUNIT;                       
COMPND   8 CHAIN: Y, B;                                                         
COMPND   9 FRAGMENT: PLUG TMH 2A OMITTED;                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PREPROTEIN TRANSLOCASE SECE SUBUNIT;                       
COMPND  14 CHAIN: Z, C;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SECG;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 GENE: SECY, PRLA;                                                    
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 562;                                                 
SOURCE  16 GENE: SECE, PRLG;                                                    
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN TRANSPORT, TRANSLOCATION, TRANSMEMBRANE, TRANSPORT            
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN X, Y, Z, A, B, C                                 
AUTHOR    K.MITRA,C.SCHAFFITZEL,T.SHAIKH,F.TAMA,S.JENNI,C.L.BROOKS III,N.BAN,   
AUTHOR   2 J.FRANK                                                              
REVDAT   4   14-FEB-24 2AKI    1       REMARK                                   
REVDAT   3   18-JUL-18 2AKI    1       REMARK                                   
REVDAT   2   24-FEB-09 2AKI    1       VERSN                                    
REVDAT   1   15-NOV-05 2AKI    0                                                
JRNL        AUTH   K.MITRA,C.SCHAFFITZEL,T.SHAIKH,F.TAMA,S.JENNI,C.L.BROOKS,    
JRNL        AUTH 2 N.BAN,J.FRANK                                                
JRNL        TITL   STRUCTURE OF THE E. COLI PROTEIN-CONDUCTING CHANNEL BOUND TO 
JRNL        TITL 2 A TRANSLATING RIBOSOME.                                      
JRNL        REF    NATURE                        V. 438   318 2005              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   16292303                                                     
JRNL        DOI    10.1038/NATURE04133                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.   14.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RSR2000, SPIDER                           
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : CORRELATION COEFFICIENT, R-FACTOR   
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--NORMAL MODE-BASED FLEXIBLE FITTING       
REMARK   3  REFINEMENT PROTOCOL--NORMAL MODE-BASED FLEXIBLE FITTING, REAL       
REMARK   3  SPACE REFINEMENT                                                    
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 14.90                          
REMARK   3   NUMBER OF PARTICLES               : 53325                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: THE RESOLUTION IS BASED ON FSC AT 0.5 CUT-OFF         
REMARK   4                                                                      
REMARK   4 2AKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034001.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : PROTEIN-CONDUCTING CHANNEL;       
REMARK 245                                    PROTEIN TRANSLOCASE ACTIVITY;     
REMARK 245                                    PROTEIN TRANSLOCASE ACTIVITY;     
REMARK 245                                    PROTEIN TRANSLOCASE ACTIVITY      
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : NULL                              
REMARK 245   SAMPLE DETAILS                 : DIMER OF SECYEG HETEROTRIMER;     
REMARK 245  DIMER OF SECYEG HETEROTRIMER; DIMER OF SECYEG HETEROTRIMER          
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 09-MAR-04                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 93.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F30                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4300.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.26                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1100.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 39000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 39000                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y, Z, A, B, C                      
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-1143   RELATED DB: EMDB                              
REMARK 900 CRYO-EM MAP OF THE E. COLI PROTEIN-CONDUCTING CHANNEL BOUND TO A     
REMARK 900 TRANSLATING RIBOSOME                                                 
REMARK 900 RELATED ID: 2AKH   RELATED DB: PDB                                   
REMARK 900 NORMAL MODE-BASED FLEXIBLE FITTED COORDINATES OF A NON-              
REMARK 900 TRANSLOCATING SECYEG PROTEIN-CONDUCTING CHANNEL INTO THE CRYO-EM     
REMARK 900 MAP OF A SECYEG-NASCENT CHAIN-70S RIBOSOME COMPLEX FROM E. COLI      
DBREF  2AKI X    1    77  UNP    P33582   SECG_ECOLI       1     77             
DBREF  2AKI A    1    77  UNP    P33582   SECG_ECOLI       1     77             
DBREF  2AKI Y    1    39  UNP    P03844   SECY_ECOLI       1     39             
DBREF  2AKI Y   76   436  UNP    P03844   SECY_ECOLI      76    436             
DBREF  2AKI B    1   400  UNP    P03844   SECY_ECOLI       1    436             
DBREF  2AKI B   76   436  UNP    P03844   SECY_ECOLI      76    436             
DBREF  2AKI Z   17   127  UNP    P16920   SECE_ECOLI      17    127             
DBREF  2AKI C   17   127  UNP    P16920   SECE_ECOLI      17    127             
SEQRES   1 X   77  MET TYR GLU ALA LEU LEU VAL VAL PHE LEU ILE VAL ALA          
SEQRES   2 X   77  ILE GLY LEU VAL GLY LEU ILE MET LEU GLN GLN GLY LYS          
SEQRES   3 X   77  GLY ALA ASP MET GLY ALA SER PHE GLY ALA GLY ALA SER          
SEQRES   4 X   77  ALA THR LEU PHE GLY SER SER GLY SER GLY ASN PHE MET          
SEQRES   5 X   77  THR ARG MET THR ALA LEU LEU ALA THR LEU PHE PHE ILE          
SEQRES   6 X   77  ILE SER LEU VAL LEU GLY ASN ILE ASN SER ASN LYS              
SEQRES   1 Y  400  MET ALA LYS GLN PRO GLY LEU ASP PHE GLN SER ALA LYS          
SEQRES   2 Y  400  GLY GLY LEU GLY GLU LEU LYS ARG ARG LEU LEU PHE VAL          
SEQRES   3 Y  400  ILE GLY ALA LEU ILE VAL PHE ARG ILE GLY SER PHE ILE          
SEQRES   4 Y  400  SER ILE PHE ALA LEU GLY ILE MET PRO TYR ILE SER ALA          
SEQRES   5 Y  400  SER ILE ILE ILE GLN LEU LEU THR VAL VAL HIS PRO THR          
SEQRES   6 Y  400  LEU ALA GLU ILE LYS LYS GLU GLY GLU SER GLY ARG ARG          
SEQRES   7 Y  400  LYS ILE SER GLN TYR THR ARG TYR GLY THR LEU VAL LEU          
SEQRES   8 Y  400  ALA ILE PHE GLN SER ILE GLY ILE ALA THR GLY LEU PRO          
SEQRES   9 Y  400  ASN MET PRO GLY MET GLN GLY LEU VAL ILE ASN PRO GLY          
SEQRES  10 Y  400  PHE ALA PHE TYR PHE THR ALA VAL VAL SER LEU VAL THR          
SEQRES  11 Y  400  GLY THR MET PHE LEU MET TRP LEU GLY GLU GLN ILE THR          
SEQRES  12 Y  400  GLU ARG GLY ILE GLY ASN GLY ILE SER ILE ILE ILE PHE          
SEQRES  13 Y  400  ALA GLY ILE VAL ALA GLY LEU PRO PRO ALA ILE ALA HIS          
SEQRES  14 Y  400  THR ILE GLU GLN ALA ARG GLN GLY ASP LEU HIS PHE LEU          
SEQRES  15 Y  400  VAL LEU LEU LEU VAL ALA VAL LEU VAL PHE ALA VAL THR          
SEQRES  16 Y  400  PHE PHE VAL VAL PHE VAL GLU ARG GLY GLN ARG ARG ILE          
SEQRES  17 Y  400  VAL VAL ASN TYR ALA LYS ARG GLN GLN GLY ARG ARG VAL          
SEQRES  18 Y  400  TYR ALA ALA GLN SER THR HIS LEU PRO LEU LYS VAL ASN          
SEQRES  19 Y  400  MET ALA GLY VAL ILE PRO ALA ILE PHE ALA SER SER ILE          
SEQRES  20 Y  400  ILE LEU PHE PRO ALA THR ILE ALA SER TRP PHE GLY GLY          
SEQRES  21 Y  400  GLY THR GLY TRP ASN TRP LEU THR THR ILE SER LEU TYR          
SEQRES  22 Y  400  LEU GLN PRO GLY GLN PRO LEU TYR VAL LEU LEU TYR ALA          
SEQRES  23 Y  400  SER ALA ILE ILE PHE PHE CYS PHE PHE TYR THR ALA LEU          
SEQRES  24 Y  400  VAL PHE ASN PRO ARG GLU THR ALA ASP ASN LEU LYS LYS          
SEQRES  25 Y  400  SER GLY ALA PHE VAL PRO GLY ILE ARG PRO GLY GLU GLN          
SEQRES  26 Y  400  THR ALA LYS TYR ILE ASP LYS VAL MET THR ARG LEU THR          
SEQRES  27 Y  400  LEU VAL GLY ALA LEU TYR ILE THR PHE ILE CYS LEU ILE          
SEQRES  28 Y  400  PRO GLU PHE MET ARG ASP ALA MET LYS VAL PRO PHE TYR          
SEQRES  29 Y  400  PHE GLY GLY THR SER LEU LEU ILE VAL VAL VAL VAL ILE          
SEQRES  30 Y  400  MET ASP PHE MET ALA GLN VAL GLN THR LEU MET MET SER          
SEQRES  31 Y  400  SER GLN TYR GLU SER ALA LEU LYS LYS ALA                      
SEQRES   1 Z  111  MET LYS TRP VAL VAL VAL VAL ALA LEU LEU LEU VAL ALA          
SEQRES   2 Z  111  ILE VAL GLY ASN TYR LEU TYR ARG ASP ILE MET LEU PRO          
SEQRES   3 Z  111  LEU ARG ALA LEU ALA VAL VAL ILE LEU ILE ALA ALA ALA          
SEQRES   4 Z  111  GLY GLY VAL ALA LEU LEU THR THR LYS GLY LYS ALA THR          
SEQRES   5 Z  111  VAL ALA PHE ALA ARG GLU ALA ARG THR GLU VAL ARG LYS          
SEQRES   6 Z  111  VAL ILE TRP PRO THR ARG GLN GLU THR LEU HIS THR THR          
SEQRES   7 Z  111  LEU ILE VAL ALA ALA VAL THR ALA VAL MET SER LEU ILE          
SEQRES   8 Z  111  LEU TRP GLY LEU ASP GLY ILE LEU VAL ARG LEU VAL SER          
SEQRES   9 Z  111  PHE ILE THR GLY LEU ARG PHE                                  
SEQRES   1 A   77  MET TYR GLU ALA LEU LEU VAL VAL PHE LEU ILE VAL ALA          
SEQRES   2 A   77  ILE GLY LEU VAL GLY LEU ILE MET LEU GLN GLN GLY LYS          
SEQRES   3 A   77  GLY ALA ASP MET GLY ALA SER PHE GLY ALA GLY ALA SER          
SEQRES   4 A   77  ALA THR LEU PHE GLY SER SER GLY SER GLY ASN PHE MET          
SEQRES   5 A   77  THR ARG MET THR ALA LEU LEU ALA THR LEU PHE PHE ILE          
SEQRES   6 A   77  ILE SER LEU VAL LEU GLY ASN ILE ASN SER ASN LYS              
SEQRES   1 B  400  MET ALA LYS GLN PRO GLY LEU ASP PHE GLN SER ALA LYS          
SEQRES   2 B  400  GLY GLY LEU GLY GLU LEU LYS ARG ARG LEU LEU PHE VAL          
SEQRES   3 B  400  ILE GLY ALA LEU ILE VAL PHE ARG ILE GLY SER PHE ILE          
SEQRES   4 B  400  SER ILE PHE ALA LEU GLY ILE MET PRO TYR ILE SER ALA          
SEQRES   5 B  400  SER ILE ILE ILE GLN LEU LEU THR VAL VAL HIS PRO THR          
SEQRES   6 B  400  LEU ALA GLU ILE LYS LYS GLU GLY GLU SER GLY ARG ARG          
SEQRES   7 B  400  LYS ILE SER GLN TYR THR ARG TYR GLY THR LEU VAL LEU          
SEQRES   8 B  400  ALA ILE PHE GLN SER ILE GLY ILE ALA THR GLY LEU PRO          
SEQRES   9 B  400  ASN MET PRO GLY MET GLN GLY LEU VAL ILE ASN PRO GLY          
SEQRES  10 B  400  PHE ALA PHE TYR PHE THR ALA VAL VAL SER LEU VAL THR          
SEQRES  11 B  400  GLY THR MET PHE LEU MET TRP LEU GLY GLU GLN ILE THR          
SEQRES  12 B  400  GLU ARG GLY ILE GLY ASN GLY ILE SER ILE ILE ILE PHE          
SEQRES  13 B  400  ALA GLY ILE VAL ALA GLY LEU PRO PRO ALA ILE ALA HIS          
SEQRES  14 B  400  THR ILE GLU GLN ALA ARG GLN GLY ASP LEU HIS PHE LEU          
SEQRES  15 B  400  VAL LEU LEU LEU VAL ALA VAL LEU VAL PHE ALA VAL THR          
SEQRES  16 B  400  PHE PHE VAL VAL PHE VAL GLU ARG GLY GLN ARG ARG ILE          
SEQRES  17 B  400  VAL VAL ASN TYR ALA LYS ARG GLN GLN GLY ARG ARG VAL          
SEQRES  18 B  400  TYR ALA ALA GLN SER THR HIS LEU PRO LEU LYS VAL ASN          
SEQRES  19 B  400  MET ALA GLY VAL ILE PRO ALA ILE PHE ALA SER SER ILE          
SEQRES  20 B  400  ILE LEU PHE PRO ALA THR ILE ALA SER TRP PHE GLY GLY          
SEQRES  21 B  400  GLY THR GLY TRP ASN TRP LEU THR THR ILE SER LEU TYR          
SEQRES  22 B  400  LEU GLN PRO GLY GLN PRO LEU TYR VAL LEU LEU TYR ALA          
SEQRES  23 B  400  SER ALA ILE ILE PHE PHE CYS PHE PHE TYR THR ALA LEU          
SEQRES  24 B  400  VAL PHE ASN PRO ARG GLU THR ALA ASP ASN LEU LYS LYS          
SEQRES  25 B  400  SER GLY ALA PHE VAL PRO GLY ILE ARG PRO GLY GLU GLN          
SEQRES  26 B  400  THR ALA LYS TYR ILE ASP LYS VAL MET THR ARG LEU THR          
SEQRES  27 B  400  LEU VAL GLY ALA LEU TYR ILE THR PHE ILE CYS LEU ILE          
SEQRES  28 B  400  PRO GLU PHE MET ARG ASP ALA MET LYS VAL PRO PHE TYR          
SEQRES  29 B  400  PHE GLY GLY THR SER LEU LEU ILE VAL VAL VAL VAL ILE          
SEQRES  30 B  400  MET ASP PHE MET ALA GLN VAL GLN THR LEU MET MET SER          
SEQRES  31 B  400  SER GLN TYR GLU SER ALA LEU LYS LYS ALA                      
SEQRES   1 C  111  MET LYS TRP VAL VAL VAL VAL ALA LEU LEU LEU VAL ALA          
SEQRES   2 C  111  ILE VAL GLY ASN TYR LEU TYR ARG ASP ILE MET LEU PRO          
SEQRES   3 C  111  LEU ARG ALA LEU ALA VAL VAL ILE LEU ILE ALA ALA ALA          
SEQRES   4 C  111  GLY GLY VAL ALA LEU LEU THR THR LYS GLY LYS ALA THR          
SEQRES   5 C  111  VAL ALA PHE ALA ARG GLU ALA ARG THR GLU VAL ARG LYS          
SEQRES   6 C  111  VAL ILE TRP PRO THR ARG GLN GLU THR LEU HIS THR THR          
SEQRES   7 C  111  LEU ILE VAL ALA ALA VAL THR ALA VAL MET SER LEU ILE          
SEQRES   8 C  111  LEU TRP GLY LEU ASP GLY ILE LEU VAL ARG LEU VAL SER          
SEQRES   9 C  111  PHE ILE THR GLY LEU ARG PHE                                  
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 LINES ARE NOT SHOWN.)
END                                                                             
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