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Database: PDB
Entry: 2PM9
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Original site: 2PM9 
HEADER    PROTEIN TRANSPORT                       20-APR-07   2PM9              
TITLE     CRYSTAL STRUCTURE OF YEAST SEC13/31 VERTEX ELEMENT OF THE COPII       
TITLE    2 VESICULAR COAT                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC31;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-411;                                            
COMPND   5 SYNONYM: PROTEIN WEB1;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC13;                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: WEB1, SEC31;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HI5 INSECT CELLS;                                 
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   9 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  10 ORGANISM_TAXID: 4932;                                                
SOURCE  11 GENE: SEC13, ANU3;                                                   
SOURCE  12 EXPRESSION_SYSTEM: HI5 INSECT CELLS                                  
KEYWDS    BETA PROPELLER, PROTEIN TRANSPORT                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GOLDBERG,S.FATH,J.D.MANCIAS,X.BI                                    
REVDAT   6   21-FEB-24 2PM9    1       REMARK                                   
REVDAT   5   20-OCT-21 2PM9    1       SEQADV                                   
REVDAT   4   18-OCT-17 2PM9    1       REMARK                                   
REVDAT   3   24-FEB-09 2PM9    1       VERSN                                    
REVDAT   2   17-JUL-07 2PM9    1       JRNL                                     
REVDAT   1   03-JUL-07 2PM9    0                                                
JRNL        AUTH   S.FATH,J.D.MANCIAS,X.BI,J.GOLDBERG                           
JRNL        TITL   STRUCTURE AND ORGANIZATION OF COAT PROTEINS IN THE COPII     
JRNL        TITL 2 CAGE.                                                        
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 129  1325 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17604721                                                     
JRNL        DOI    10.1016/J.CELL.2007.05.036                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 18996                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 959                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 19                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.36                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 651                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4040                       
REMARK   3   BIN FREE R VALUE                    : 0.5240                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 35                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5168                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.92600                                            
REMARK   3    B22 (A**2) : -10.92600                                            
REMARK   3    B33 (A**2) : 21.85100                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.636                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.025 ; 3.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.842 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.972 ; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.460 ; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 28.75                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042532.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20444                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE, RESOLVE 2.01                                   
REMARK 200 STARTING MODEL: YEAST SEC13                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.1M TRI-SODIUM CITRATE,    
REMARK 280  10MM MANGANESE CHLORIDE, PH 7.2, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.93300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.89950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       14.96650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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 300 REMARK: THE BIOLOGICAL ASSEMBLY UNIT INVOLVES THIS STRUCTURE OF THE  
REMARK 300 SEC13/31 VERTEX ELEMENT TOGETHER WITH THE SEC13/31 EDGE ELEMENT.     
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLN A   340                                                      
REMARK 465     GLU A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     GLU A   343                                                      
REMARK 465     THR A   344                                                      
REMARK 465     LYS A   345                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     GLN A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     GLU A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     ASP A   352                                                      
REMARK 465     PHE A   353                                                      
REMARK 465     TRP A   354                                                      
REMARK 465     ASN A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     VAL A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     GLY A   411                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLU B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     ASN B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     THR B   167                                                      
REMARK 465     LYS B   168                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     VAL B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     GLN B   297                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
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    VAL A   368     N    HIS A   370              2.02            
REMARK 500   O    ASN A    73     N    LYS A    75              2.11            
REMARK 500   O    HIS A    72     ND2  ASN A    74              2.16            
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    PRO A 313   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
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    PHE A   7     -143.45   -150.96                                   
REMARK 500    ARG A   9     -161.75    -69.63                                   
REMARK 500    THR A  10      122.09     -7.78                                   
REMARK 500    ALA A  11      152.42    172.35                                   
REMARK 500    SER A  16     -145.38    -75.23                                   
REMARK 500    HIS A  17       23.59   -153.85                                   
REMARK 500    ASP A  33     -161.33    -55.51                                   
REMARK 500    THR A  38      -61.55   -136.41                                   
REMARK 500    LEU A  42       36.44     71.69                                   
REMARK 500    LEU A  48      -68.74    -98.87                                   
REMARK 500    ALA A  49      150.19    -17.24                                   
REMARK 500    ASP A  51       23.37     45.74                                   
REMARK 500    SER A  52       50.45     26.12                                   
REMARK 500    ALA A  57      116.64   -165.11                                   
REMARK 500    LEU A  59       69.63   -168.53                                   
REMARK 500    GLN A  60      135.41    -27.47                                   
REMARK 500    ASP A  62      -72.17    -61.99                                   
REMARK 500    HIS A  72       76.66    -65.61                                   
REMARK 500    ASN A  73       -9.73     64.75                                   
REMARK 500    ASN A  74       32.77    -54.09                                   
REMARK 500    LYS A  75       56.06     37.71                                   
REMARK 500    SER A  90      -59.34   -121.44                                   
REMARK 500    THR A  91      106.49     64.14                                   
REMARK 500    GLU A  93      106.16     94.43                                   
REMARK 500    ALA A  94      134.11    -29.22                                   
REMARK 500    ASN A  95      -13.67     85.45                                   
REMARK 500    ALA A  97      122.03   -174.83                                   
REMARK 500    MET A 101     -139.73    -98.74                                   
REMARK 500    SER A 105       37.53   -173.41                                   
REMARK 500    ASN A 106        7.33    -67.86                                   
REMARK 500    SER A 109       68.73     23.71                                   
REMARK 500    SER A 110      111.28    160.73                                   
REMARK 500    LYS A 112      -63.80   -103.89                                   
REMARK 500    ASP A 121        0.88    -55.12                                   
REMARK 500    GLU A 143      -90.69    -37.63                                   
REMARK 500    SER A 146      -54.63    -14.24                                   
REMARK 500    ASN A 147       27.26    163.97                                   
REMARK 500    TYR A 148      135.33    -27.98                                   
REMARK 500    GLN A 155      149.43    178.46                                   
REMARK 500    SER A 156      -97.89     58.47                                   
REMARK 500    SER A 159      -72.40    172.79                                   
REMARK 500    VAL A 160        9.42   -160.17                                   
REMARK 500    LYS A 193       71.50     35.67                                   
REMARK 500    LYS A 194      153.46    160.60                                   
REMARK 500    SER A 200      110.20   -166.93                                   
REMARK 500    THR A 202        0.53   -158.47                                   
REMARK 500    PRO A 204      -14.18    -35.36                                   
REMARK 500    PRO A 219        2.36    -67.53                                   
REMARK 500    LYS A 220      -47.77   -144.60                                   
REMARK 500    SER A 231      133.23    -36.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PM6   RELATED DB: PDB                                   
REMARK 900 EDGE ELEMENT OF THE SEC13/31 COMPLEX, NATIVE PROTEIN                 
REMARK 900 RELATED ID: 2PM7   RELATED DB: PDB                                   
REMARK 900 EDGE ELEMENT OF THE SEC13/31 COMPLEX, SELENOMETHIONINE PROTEIN       
DBREF  2PM9 A    1   411  UNP    P38968   WEB1_YEAST       1    411             
DBREF  2PM9 B    1   297  UNP    Q04491   SEC13_YEAST      1    297             
SEQADV 2PM9 GLY A   -4  UNP  P38968              CLONING ARTIFACT               
SEQADV 2PM9 ALA A   -3  UNP  P38968              CLONING ARTIFACT               
SEQADV 2PM9 MET A   -2  UNP  P38968              CLONING ARTIFACT               
SEQADV 2PM9 GLY A   -1  UNP  P38968              CLONING ARTIFACT               
SEQADV 2PM9 SER A    0  UNP  P38968              CLONING ARTIFACT               
SEQADV 2PM9 MET B   11  UNP  Q04491    LEU    11 ENGINEERED MUTATION            
SEQADV 2PM9 MET B   17  UNP  Q04491    LEU    17 ENGINEERED MUTATION            
SEQADV 2PM9 MET B   24  UNP  Q04491    LEU    24 ENGINEERED MUTATION            
SEQADV 2PM9 MET B   80  UNP  Q04491    LEU    80 ENGINEERED MUTATION            
SEQADV 2PM9 MET B  115  UNP  Q04491    LEU   115 ENGINEERED MUTATION            
SEQADV 2PM9 MET B  222  UNP  Q04491    LEU   222 ENGINEERED MUTATION            
SEQRES   1 A  416  GLY ALA MET GLY SER MET VAL LYS LEU ALA GLU PHE SER          
SEQRES   2 A  416  ARG THR ALA THR PHE ALA TRP SER HIS ASP LYS ILE PRO          
SEQRES   3 A  416  LEU LEU VAL SER GLY THR VAL SER GLY THR VAL ASP ALA          
SEQRES   4 A  416  ASN PHE SER THR ASP SER SER LEU GLU LEU TRP SER LEU          
SEQRES   5 A  416  LEU ALA ALA ASP SER GLU LYS PRO ILE ALA SER LEU GLN          
SEQRES   6 A  416  VAL ASP SER LYS PHE ASN ASP LEU ASP TRP SER HIS ASN          
SEQRES   7 A  416  ASN LYS ILE ILE ALA GLY ALA LEU ASP ASN GLY SER LEU          
SEQRES   8 A  416  GLU LEU TYR SER THR ASN GLU ALA ASN ASN ALA ILE ASN          
SEQRES   9 A  416  SER MET ALA ARG PHE SER ASN HIS SER SER SER VAL LYS          
SEQRES  10 A  416  THR VAL LYS PHE ASN ALA LYS GLN ASP ASN VAL LEU ALA          
SEQRES  11 A  416  SER GLY GLY ASN ASN GLY GLU ILE PHE ILE TRP ASP MET          
SEQRES  12 A  416  ASN LYS CYS THR GLU SER PRO SER ASN TYR THR PRO LEU          
SEQRES  13 A  416  THR PRO GLY GLN SER MET SER SER VAL ASP GLU VAL ILE          
SEQRES  14 A  416  SER LEU ALA TRP ASN GLN SER LEU ALA HIS VAL PHE ALA          
SEQRES  15 A  416  SER ALA GLY SER SER ASN PHE ALA SER ILE TRP ASP LEU          
SEQRES  16 A  416  LYS ALA LYS LYS GLU VAL ILE HIS LEU SER TYR THR SER          
SEQRES  17 A  416  PRO ASN SER GLY ILE LYS GLN GLN LEU SER VAL VAL GLU          
SEQRES  18 A  416  TRP HIS PRO LYS ASN SER THR ARG VAL ALA THR ALA THR          
SEQRES  19 A  416  GLY SER ASP ASN ASP PRO SER ILE LEU ILE TRP ASP LEU          
SEQRES  20 A  416  ARG ASN ALA ASN THR PRO LEU GLN THR LEU ASN GLN GLY          
SEQRES  21 A  416  HIS GLN LYS GLY ILE LEU SER LEU ASP TRP CYS HIS GLN          
SEQRES  22 A  416  ASP GLU HIS LEU LEU LEU SER SER GLY ARG ASP ASN THR          
SEQRES  23 A  416  VAL LEU LEU TRP ASN PRO GLU SER ALA GLU GLN LEU SER          
SEQRES  24 A  416  GLN PHE PRO ALA ARG GLY ASN TRP CYS PHE LYS THR LYS          
SEQRES  25 A  416  PHE ALA PRO GLU ALA PRO ASP LEU PHE ALA CYS ALA SER          
SEQRES  26 A  416  PHE ASP ASN LYS ILE GLU VAL GLN THR LEU GLN ASN LEU          
SEQRES  27 A  416  THR ASN THR LEU ASP GLU GLN GLU THR GLU THR LYS GLN          
SEQRES  28 A  416  GLN GLU SER GLU THR ASP PHE TRP ASN ASN VAL SER ARG          
SEQRES  29 A  416  GLU GLU SER LYS GLU LYS PRO SER VAL PHE HIS LEU GLN          
SEQRES  30 A  416  ALA PRO THR TRP TYR GLY GLU PRO SER PRO ALA ALA HIS          
SEQRES  31 A  416  TRP ALA PHE GLY GLY LYS LEU VAL GLN ILE THR PRO ASP          
SEQRES  32 A  416  GLY LYS GLY VAL SER ILE THR ASN PRO LYS ILE SER GLY          
SEQRES   1 B  297  MET VAL VAL ILE ALA ASN ALA HIS ASN GLU MET ILE HIS          
SEQRES   2 B  297  ASP ALA VAL MET ASP TYR TYR GLY LYS ARG MET ALA THR          
SEQRES   3 B  297  CYS SER SER ASP LYS THR ILE LYS ILE PHE GLU VAL GLU          
SEQRES   4 B  297  GLY GLU THR HIS LYS LEU ILE ASP THR LEU THR GLY HIS          
SEQRES   5 B  297  GLU GLY PRO VAL TRP ARG VAL ASP TRP ALA HIS PRO LYS          
SEQRES   6 B  297  PHE GLY THR ILE LEU ALA SER CYS SER TYR ASP GLY LYS          
SEQRES   7 B  297  VAL MET ILE TRP LYS GLU GLU ASN GLY ARG TRP SER GLN          
SEQRES   8 B  297  ILE ALA VAL HIS ALA VAL HIS SER ALA SER VAL ASN SER          
SEQRES   9 B  297  VAL GLN TRP ALA PRO HIS GLU TYR GLY PRO MET LEU LEU          
SEQRES  10 B  297  VAL ALA SER SER ASP GLY LYS VAL SER VAL VAL GLU PHE          
SEQRES  11 B  297  LYS GLU ASN GLY THR THR SER PRO ILE ILE ILE ASP ALA          
SEQRES  12 B  297  HIS ALA ILE GLY VAL ASN SER ALA SER TRP ALA PRO ALA          
SEQRES  13 B  297  THR ILE GLU GLU ASP GLY GLU HIS ASN GLY THR LYS GLU          
SEQRES  14 B  297  SER ARG LYS PHE VAL THR GLY GLY ALA ASP ASN LEU VAL          
SEQRES  15 B  297  LYS ILE TRP LYS TYR ASN SER ASP ALA GLN THR TYR VAL          
SEQRES  16 B  297  LEU GLU SER THR LEU GLU GLY HIS SER ASP TRP VAL ARG          
SEQRES  17 B  297  ASP VAL ALA TRP SER PRO THR VAL LEU LEU ARG SER TYR          
SEQRES  18 B  297  MET ALA SER VAL SER GLN ASP ARG THR CYS ILE ILE TRP          
SEQRES  19 B  297  THR GLN ASP ASN GLU GLN GLY PRO TRP LYS LYS THR LEU          
SEQRES  20 B  297  LEU LYS GLU GLU LYS PHE PRO ASP VAL LEU TRP ARG ALA          
SEQRES  21 B  297  SER TRP SER LEU SER GLY ASN VAL LEU ALA LEU SER GLY          
SEQRES  22 B  297  GLY ASP ASN LYS VAL THR LEU TRP LYS GLU ASN LEU GLU          
SEQRES  23 B  297  GLY LYS TRP GLU PRO ALA GLY GLU VAL HIS GLN                  
FORMUL   3  HOH   *28(H2 O)                                                     
HELIX    1   1 ALA A   49  GLU A   53  5                                   5    
HELIX    2   2 HIS B   63  GLY B   67  5                                   5    
HELIX    3   3 GLU B   85  ARG B   88  5                                   4    
SHEET    1   A 4 GLU A   6  ARG A   9  0                                        
SHEET    2   A 4 LYS A 324  THR A 329 -1  O  ILE A 325   N  SER A   8           
SHEET    3   A 4 LEU A 315  CYS A 318 -1  N  PHE A 316   O  GLN A 328           
SHEET    4   A 4 THR A 306  PHE A 308 -1  N  LYS A 307   O  ALA A 317           
SHEET    1   B 2 LEU A  22  SER A  25  0                                        
SHEET    2   B 2 GLU A  43  SER A  46 -1  O  GLU A  43   N  SER A  25           
SHEET    1   C 4 PHE A  65  TRP A  70  0                                        
SHEET    2   C 4 ILE A  77  LEU A  81 -1  O  ALA A  80   N  ASN A  66           
SHEET    3   C 4 LEU A  86  TYR A  89 -1  O  GLU A  87   N  GLY A  79           
SHEET    4   C 4 SER A 100  ARG A 103 -1  O  ALA A 102   N  LEU A  88           
SHEET    1   D 3 THR A 113  PHE A 116  0                                        
SHEET    2   D 3 LEU A 124  GLY A 127 -1  O  ALA A 125   N  LYS A 115           
SHEET    3   D 3 ILE A 133  PHE A 134 -1  O  PHE A 134   N  SER A 126           
SHEET    1   E 4 SER A 165  TRP A 168  0                                        
SHEET    2   E 4 VAL A 175  ALA A 179 -1  O  ALA A 177   N  ALA A 167           
SHEET    3   E 4 ALA A 185  ASP A 189 -1  O  TRP A 188   N  PHE A 176           
SHEET    4   E 4 LYS A 194  LEU A 199 -1  O  VAL A 196   N  ILE A 187           
SHEET    1   F 3 LEU A 212  TRP A 217  0                                        
SHEET    2   F 3 ARG A 224  THR A 229 -1  O  ALA A 226   N  GLU A 216           
SHEET    3   F 3 ILE A 239  ASP A 241 -1  O  TRP A 240   N  VAL A 225           
SHEET    1   G 4 ILE A 260  TRP A 265  0                                        
SHEET    2   G 4 LEU A 273  GLY A 277 -1  O  LEU A 274   N  ASP A 264           
SHEET    3   G 4 THR A 281  TRP A 285 -1  O  LEU A 283   N  SER A 275           
SHEET    4   G 4 GLN A 292  PRO A 297 -1  O  PHE A 296   N  VAL A 282           
SHEET    1   H 2 HIS A 385  ALA A 387  0                                        
SHEET    2   H 2 LYS A 391  VAL A 393 -1  O  VAL A 393   N  HIS A 385           
SHEET    1   I 4 ILE B  12  ALA B  15  0                                        
SHEET    2   I 4 ALA B  25  SER B  28 -1  O  CYS B  27   N  HIS B  13           
SHEET    3   I 4 THR B  32  GLU B  39 -1  O  LYS B  34   N  THR B  26           
SHEET    4   I 4 THR B  42  THR B  50 -1  N  THR B  42   O  GLU B  39           
SHEET    1   J 4 VAL B  56  TRP B  61  0                                        
SHEET    2   J 4 ILE B  69  SER B  74 -1  O  CYS B  73   N  TRP B  57           
SHEET    3   J 4 VAL B  79  LYS B  83 -1  O  MET B  80   N  SER B  72           
SHEET    4   J 4 SER B  90  HIS B  95 -1  O  HIS B  95   N  VAL B  79           
SHEET    1   K 4 VAL B 102  TRP B 107  0                                        
SHEET    2   K 4 MET B 115  SER B 120 -1  O  LEU B 117   N  GLN B 106           
SHEET    3   K 4 LYS B 124  GLU B 129 -1  O  SER B 126   N  VAL B 118           
SHEET    4   K 4 ILE B 139  ASP B 142 -1  O  ILE B 139   N  VAL B 127           
SHEET    1   L 4 VAL B 148  SER B 150  0                                        
SHEET    2   L 4 LYS B 172  GLY B 177 -1  O  GLY B 176   N  ASN B 149           
SHEET    3   L 4 VAL B 182  LYS B 186 -1  O  LYS B 183   N  THR B 175           
SHEET    4   L 4 VAL B 195  LEU B 196 -1  O  VAL B 195   N  LYS B 186           
SHEET    1   M 3 ASP B 209  TRP B 212  0                                        
SHEET    2   M 3 SER B 220  SER B 226 -1  O  VAL B 225   N  ASP B 209           
SHEET    3   M 3 THR B 230  CYS B 231 -1  O  THR B 230   N  SER B 226           
SHEET    1   N 3 ASP B 209  TRP B 212  0                                        
SHEET    2   N 3 SER B 220  SER B 226 -1  O  VAL B 225   N  ASP B 209           
SHEET    3   N 3 TRP B 234  GLN B 236 -1  O  GLN B 236   N  SER B 220           
SHEET    1   O 3 ARG B 259  TRP B 262  0                                        
SHEET    2   O 3 LEU B 269  SER B 272 -1  O  ALA B 270   N  SER B 261           
SHEET    3   O 3 VAL B 278  TRP B 281 -1  O  TRP B 281   N  LEU B 269           
CRYST1  155.163  155.163   59.866  90.00  90.00  90.00 P 43          4          
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      0.006445  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006445  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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