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Database: PDB
Entry: 1AVF
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HEADER    ASPARTYL PROTEASE                       16-SEP-97   1AVF              
TITLE     ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GASTRICSIN;                                                
COMPND   3 CHAIN: P, Q;                                                         
COMPND   4 SYNONYM: PEPSINOGEN C;                                               
COMPND   5 EC: 3.4.23.3;                                                        
COMPND   6 OTHER_DETAILS: ASPARTIC PROTEINASE ACTIVATION INTERMEDIATE;          
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GASTRICSIN;                                                
COMPND   9 CHAIN: A, J;                                                         
COMPND  10 SYNONYM: PEPSINOGEN C;                                               
COMPND  11 EC: 3.4.23.3;                                                        
COMPND  12 OTHER_DETAILS: ASPARTIC PROTEINASE ACTIVATION INTERMEDIATE           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: STOMACH;                                                      
SOURCE   6 TISSUE: GASTRIC MUCOSA;                                              
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 ORGAN: STOMACH;                                                      
SOURCE  12 TISSUE: GASTRIC MUCOSA                                               
KEYWDS    ASPARTYL PROTEASE, GASTRICSIN, ASPARTIC PROTEINASE, INTERMEDIATE,     
KEYWDS   2 ACTIVATION, ACID                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.R.KHAN,M.M.CHERNEY,N.I.TARASOVA,M.N.G.JAMES                         
REVDAT   3   02-AUG-23 1AVF    1       REMARK LINK                              
REVDAT   2   24-FEB-09 1AVF    1       VERSN                                    
REVDAT   1   25-FEB-98 1AVF    0                                                
JRNL        AUTH   A.R.KHAN,M.M.CHERNEY,N.I.TARASOVA,M.N.JAMES                  
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF ACTIVATION 'INTERMEDIATE 2'   
JRNL        TITL 2 ON THE PATHWAY TO HUMAN GASTRICSIN.                          
JRNL        REF    NAT.STRUCT.BIOL.              V.   4  1010 1997              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9406551                                                      
JRNL        DOI    10.1038/NSB1297-1010                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34523                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : R-FREE                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3407                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 813                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 90                           
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            : 5218                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 467                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.690                           
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) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; 10.0                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; 1.0                  
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171305.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GOBEL MIRRORS                      
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34523                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.04500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HTR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED IN 4M NA        
REMARK 280  FORMATE, 100 MM BIS-TRIS-PROPANE, PH 7.8.                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.13000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.13000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.20500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, J                                  
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     LEU P    22                                                      
REMARK 465     LEU P    23                                                      
REMARK 465     GLY P    24                                                      
REMARK 465     GLU P    25                                                      
REMARK 465     PHE P    26                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLN A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     LEU Q    23                                                      
REMARK 465     GLY Q    24                                                      
REMARK 465     GLU Q    25                                                      
REMARK 465     PHE Q    26                                                      
REMARK 465     SER J     1                                                      
REMARK 465     GLN J   158                                                      
REMARK 465     GLN J   159                                                      
REMARK 465     GLY J   160                                                      
REMARK 465     SER J   161                                                      
REMARK 465     SER J   162                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   2    CG1  CG2                                            
REMARK 470     THR A   3    OG1  CG2                                            
REMARK 470     TYR A  75    CA   C    O    CB   CG   CD1  CD2                   
REMARK 470     TYR A  75    CE1  CE2  CZ   OH                                   
REMARK 470     SER A  79    OG                                                  
REMARK 470     ASN A 157    CA   C    O    CB   CG   OD1  ND2                   
REMARK 470     ASN A 281    CG   OD1  ND2                                       
REMARK 470     VAL J   2    CG1  CG2                                            
REMARK 470     THR J   3    OG1  CG2                                            
REMARK 470     GLN J  74    CG   CD   OE1  NE2                                  
REMARK 470     ASN J 157    CA   C    O    CB   CG   OD1  ND2                   
REMARK 470     ASN J 281    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   475     O    HOH A   485     2556     0.11            
REMARK 500   O    HOH A   341     O    HOH A   457     2556     0.46            
REMARK 500   O    HOH J   475     O    HOH J   519     4445     0.47            
REMARK 500   C    LEU J   257     O    HOH J   530     4455     0.72            
REMARK 500   O    HOH A   444     O    HOH A   538     2556     0.75            
REMARK 500   O    ASP A   242     O    HOH A   539     4556     0.76            
REMARK 500   CA   LEU J   257     O    HOH J   530     4455     0.80            
REMARK 500   N    GLN A   142     O    HOH A   529     2556     0.87            
REMARK 500   C    ASP A   242     O    HOH A   539     4556     0.93            
REMARK 500   CB   THR A   177     O    HOH A   545     4546     1.35            
REMARK 500   CA   GLN A   255     O    HOH A   544     4546     1.36            
REMARK 500   CA   GLN A   142     O    HOH A   529     2556     1.38            
REMARK 500   CD1  TYR J    44     O    HOH A   516     1545     1.42            
REMARK 500   O    ASP J   242     O    HOH J   524     4445     1.42            
REMARK 500   N    GLU A   243     O    HOH A   539     4556     1.51            
REMARK 500   C    VAL A   141     O    HOH A   529     2556     1.53            
REMARK 500   N    GLY J   144     O    HOH A   524     2556     1.66            
REMARK 500   O    LEU J   257     O    HOH J   530     4455     1.67            
REMARK 500   N    ASN A   256     O    HOH A   530     4546     1.69            
REMARK 500   N    PRO J   258     O    HOH J   530     4455     1.82            
REMARK 500   O    HOH A   550     O    HOH Q    89     2556     1.82            
REMARK 500   O    GLN J   142     O    HOH A   524     2556     1.82            
REMARK 500   N    LEU J   257     O    HOH J   530     4455     1.84            
REMARK 500   O    HOH A   459     O    HOH A   555     4546     1.88            
REMARK 500   O    ASN J   256     O    HOH J   502     4455     1.89            
REMARK 500   N    GLN A   255     O    HOH A   530     4546     1.90            
REMARK 500   C    GLN J   142     O    HOH A   524     2556     1.92            
REMARK 500   CB   LEU J   257     O    HOH J   530     4455     1.93            
REMARK 500   CA   GLU A   243     O    HOH A   539     4556     1.97            
REMARK 500   O    HOH A   350     O    HOH A   509     4546     1.98            
REMARK 500   C    GLU J   143     O    HOH A   524     2556     2.01            
REMARK 500   N    GLN A   255     O    HOH A   544     4546     2.03            
REMARK 500   O    HOH A   451     O    HOH A   530     4546     2.08            
REMARK 500   O    SER A   253     O    HOH A   530     4546     2.08            
REMARK 500   N    ASP J   242     O    HOH J   524     4445     2.09            
REMARK 500   CG2  THR A   177     O    HOH A   545     4546     2.09            
REMARK 500   CB   GLN A   255     O    HOH A   510     4546     2.10            
REMARK 500   O    HOH J   392     O    HOH J   525     4445     2.13            
REMARK 500   CE1  TYR J    44     O    HOH A   516     1545     2.14            
REMARK 500   O    HOH A   350     O    HOH A   555     4546     2.15            
REMARK 500   CA   THR A   177     O    HOH A   545     4546     2.16            
REMARK 500   O    VAL A   141     O    HOH A   529     2556     2.17            
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 J   6   C   -  N   -  CA  ANGL. DEV. =   9.3 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    THR A   3       21.91   -145.45                                   
REMARK 500    THR A  51      -18.12    -48.31                                   
REMARK 500    GLN A  92     -126.98     53.46                                   
REMARK 500    LEU A 189      -80.32   -147.66                                   
REMARK 500    ILE A 254      -59.37    -28.22                                   
REMARK 500    ASN A 281      103.51    168.68                                   
REMARK 500    THR J   3       16.19   -148.37                                   
REMARK 500    ALA J  13      -13.37   -142.25                                   
REMARK 500    THR J  51      -26.43    -39.59                                   
REMARK 500    THR J  66      145.07   -176.54                                   
REMARK 500    GLN J  74     -127.13     60.73                                   
REMARK 500    TYR J  75      147.02    -23.09                                   
REMARK 500    SER J  77       33.60     74.96                                   
REMARK 500    GLN J  92     -125.19     52.30                                   
REMARK 500    ASP J 131       19.33     53.21                                   
REMARK 500    GLU J 188       91.83    -69.06                                   
REMARK 500    LEU J 189      -75.93   -153.01                                   
REMARK 500    ASN J 281      104.81     81.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 330  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 275   OG                                                     
REMARK 620 2 SER A 311   OG   71.2                                              
REMARK 620 3 HOH A 332   O    93.0 157.9                                        
REMARK 620 4 HOH A 335   O   155.5  93.6  95.6                                  
REMARK 620 5 HOH A 342   O   106.6  88.4 111.3  91.5                            
REMARK 620 6 HOH A 471   O    81.4  77.9  84.7  76.6 161.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 330                  
DBREF  1AVF P    1    26  UNP    P20142   PEPC_HUMAN      17     42             
DBREF  1AVF A    1   329  UNP    P20142   PEPC_HUMAN      60    388             
DBREF  1AVF Q    1    26  UNP    P20142   PEPC_HUMAN      17     42             
DBREF  1AVF J    1   329  UNP    P20142   PEPC_HUMAN      60    388             
SEQRES   1 P   26  ALA VAL VAL LYS VAL PRO LEU LYS LYS PHE LYS SER ILE          
SEQRES   2 P   26  ARG GLU THR MET LYS GLU LYS GLY LEU LEU GLY GLU PHE          
SEQRES   1 A  329  SER VAL THR TYR GLU PRO MET ALA TYR MET ASP ALA ALA          
SEQRES   2 A  329  TYR PHE GLY GLU ILE SER ILE GLY THR PRO PRO GLN ASN          
SEQRES   3 A  329  PHE LEU VAL LEU PHE ASP THR GLY SER SER ASN LEU TRP          
SEQRES   4 A  329  VAL PRO SER VAL TYR CYS GLN SER GLN ALA CYS THR SER          
SEQRES   5 A  329  HIS SER ARG PHE ASN PRO SER GLU SER SER THR TYR SER          
SEQRES   6 A  329  THR ASN GLY GLN THR PHE SER LEU GLN TYR GLY SER GLY          
SEQRES   7 A  329  SER LEU THR GLY PHE PHE GLY TYR ASP THR LEU THR VAL          
SEQRES   8 A  329  GLN SER ILE GLN VAL PRO ASN GLN GLU PHE GLY LEU SER          
SEQRES   9 A  329  GLU ASN GLU PRO GLY THR ASN PHE VAL TYR ALA GLN PHE          
SEQRES  10 A  329  ASP GLY ILE MET GLY LEU ALA TYR PRO ALA LEU SER VAL          
SEQRES  11 A  329  ASP GLU ALA THR THR ALA MET GLN GLY MET VAL GLN GLU          
SEQRES  12 A  329  GLY ALA LEU THR SER PRO VAL PHE SER VAL TYR LEU SER          
SEQRES  13 A  329  ASN GLN GLN GLY SER SER GLY GLY ALA VAL VAL PHE GLY          
SEQRES  14 A  329  GLY VAL ASP SER SER LEU TYR THR GLY GLN ILE TYR TRP          
SEQRES  15 A  329  ALA PRO VAL THR GLN GLU LEU TYR TRP GLN ILE GLY ILE          
SEQRES  16 A  329  GLU GLU PHE LEU ILE GLY GLY GLN ALA SER GLY TRP CYS          
SEQRES  17 A  329  SER GLU GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER          
SEQRES  18 A  329  LEU LEU THR VAL PRO GLN GLN TYR MET SER ALA LEU LEU          
SEQRES  19 A  329  GLN ALA THR GLY ALA GLN GLU ASP GLU TYR GLY GLN PHE          
SEQRES  20 A  329  LEU VAL ASN CYS ASN SER ILE GLN ASN LEU PRO SER LEU          
SEQRES  21 A  329  THR PHE ILE ILE ASN GLY VAL GLU PHE PRO LEU PRO PRO          
SEQRES  22 A  329  SER SER TYR ILE LEU SER ASN ASN GLY TYR CYS THR VAL          
SEQRES  23 A  329  GLY VAL GLU PRO THR TYR LEU SER SER GLN ASN GLY GLN          
SEQRES  24 A  329  PRO LEU TRP ILE LEU GLY ASP VAL PHE LEU ARG SER TYR          
SEQRES  25 A  329  TYR SER VAL TYR ASP LEU GLY ASN ASN ARG VAL GLY PHE          
SEQRES  26 A  329  ALA THR ALA ALA                                              
SEQRES   1 Q   26  ALA VAL VAL LYS VAL PRO LEU LYS LYS PHE LYS SER ILE          
SEQRES   2 Q   26  ARG GLU THR MET LYS GLU LYS GLY LEU LEU GLY GLU PHE          
SEQRES   1 J  329  SER VAL THR TYR GLU PRO MET ALA TYR MET ASP ALA ALA          
SEQRES   2 J  329  TYR PHE GLY GLU ILE SER ILE GLY THR PRO PRO GLN ASN          
SEQRES   3 J  329  PHE LEU VAL LEU PHE ASP THR GLY SER SER ASN LEU TRP          
SEQRES   4 J  329  VAL PRO SER VAL TYR CYS GLN SER GLN ALA CYS THR SER          
SEQRES   5 J  329  HIS SER ARG PHE ASN PRO SER GLU SER SER THR TYR SER          
SEQRES   6 J  329  THR ASN GLY GLN THR PHE SER LEU GLN TYR GLY SER GLY          
SEQRES   7 J  329  SER LEU THR GLY PHE PHE GLY TYR ASP THR LEU THR VAL          
SEQRES   8 J  329  GLN SER ILE GLN VAL PRO ASN GLN GLU PHE GLY LEU SER          
SEQRES   9 J  329  GLU ASN GLU PRO GLY THR ASN PHE VAL TYR ALA GLN PHE          
SEQRES  10 J  329  ASP GLY ILE MET GLY LEU ALA TYR PRO ALA LEU SER VAL          
SEQRES  11 J  329  ASP GLU ALA THR THR ALA MET GLN GLY MET VAL GLN GLU          
SEQRES  12 J  329  GLY ALA LEU THR SER PRO VAL PHE SER VAL TYR LEU SER          
SEQRES  13 J  329  ASN GLN GLN GLY SER SER GLY GLY ALA VAL VAL PHE GLY          
SEQRES  14 J  329  GLY VAL ASP SER SER LEU TYR THR GLY GLN ILE TYR TRP          
SEQRES  15 J  329  ALA PRO VAL THR GLN GLU LEU TYR TRP GLN ILE GLY ILE          
SEQRES  16 J  329  GLU GLU PHE LEU ILE GLY GLY GLN ALA SER GLY TRP CYS          
SEQRES  17 J  329  SER GLU GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER          
SEQRES  18 J  329  LEU LEU THR VAL PRO GLN GLN TYR MET SER ALA LEU LEU          
SEQRES  19 J  329  GLN ALA THR GLY ALA GLN GLU ASP GLU TYR GLY GLN PHE          
SEQRES  20 J  329  LEU VAL ASN CYS ASN SER ILE GLN ASN LEU PRO SER LEU          
SEQRES  21 J  329  THR PHE ILE ILE ASN GLY VAL GLU PHE PRO LEU PRO PRO          
SEQRES  22 J  329  SER SER TYR ILE LEU SER ASN ASN GLY TYR CYS THR VAL          
SEQRES  23 J  329  GLY VAL GLU PRO THR TYR LEU SER SER GLN ASN GLY GLN          
SEQRES  24 J  329  PRO LEU TRP ILE LEU GLY ASP VAL PHE LEU ARG SER TYR          
SEQRES  25 J  329  TYR SER VAL TYR ASP LEU GLY ASN ASN ARG VAL GLY PHE          
SEQRES  26 J  329  ALA THR ALA ALA                                              
HET     NA  A 330       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *467(H2 O)                                                    
HELIX    1   1 ILE P   13  GLU P   19  1                                   7    
HELIX    2   2 GLN A   48  THR A   51  1                                   4    
HELIX    3   3 PRO A   58  GLU A   60  5                                   3    
HELIX    4   4 THR A  110  TYR A  114  5                                   5    
HELIX    5   5 PRO A  126  LEU A  128  5                                   3    
HELIX    6   6 VAL A  130  GLU A  132  5                                   3    
HELIX    7   7 ALA A  136  GLU A  143  1                                   8    
HELIX    8   8 GLN A  227  ALA A  236  5                                  10    
HELIX    9   9 ILE A  254  ASN A  256  5                                   3    
HELIX   10  10 PRO A  273  TYR A  276  1                                   4    
HELIX   11  11 ASP A  306  LEU A  309  1                                   4    
HELIX   12  12 ILE Q   13  LYS Q   20  1                                   8    
HELIX   13  13 GLN J   48  THR J   51  1                                   4    
HELIX   14  14 PRO J   58  GLU J   60  5                                   3    
HELIX   15  15 THR J  110  TYR J  114  5                                   5    
HELIX   16  16 PRO J  126  LEU J  128  5                                   3    
HELIX   17  17 VAL J  130  GLU J  132  5                                   3    
HELIX   18  18 ALA J  136  GLN J  142  1                                   7    
HELIX   19  19 SER J  173  LEU J  175  5                                   3    
HELIX   20  20 GLN J  227  THR J  237  5                                  11    
HELIX   21  21 CYS J  251  ASN J  256  5                                   6    
HELIX   22  22 PRO J  273  TYR J  276  1                                   4    
HELIX   23  23 ASP J  306  LEU J  309  1                                   4    
SHEET    1   A 3 PHE A  15  ILE A  20  0                                        
SHEET    2   A 3 GLN A  25  ASP A  32 -1  N  VAL A  29   O  GLY A  16           
SHEET    3   A 3 GLY A 119  GLY A 122  1  N  GLY A 119   O  LEU A  30           
SHEET    1   B 4 TRP A  39  PRO A  41  0                                        
SHEET    2   B 4 GLN A  99  SER A 104  1  N  GLY A 102   O  VAL A  40           
SHEET    3   B 4 LEU A  80  ASP A  87 -1  N  ASP A  87   O  GLN A  99           
SHEET    4   B 4 THR A  70  LEU A  73 -1  N  LEU A  73   O  LEU A  80           
SHEET    1   C 2 LEU A  89  VAL A  91  0                                        
SHEET    2   C 2 ILE A  94  VAL A  96 -1  N  VAL A  96   O  LEU A  89           
SHEET    1   D 5 ALA A 165  PHE A 168  0                                        
SHEET    2   D 5 VAL A 150  TYR A 154 -1  N  TYR A 154   O  ALA A 165           
SHEET    3   D 5 TYR A 312  ASP A 317 -1  N  TYR A 316   O  PHE A 151           
SHEET    4   D 5 ARG A 322  THR A 327 -1  N  ALA A 326   O  TYR A 313           
SHEET    5   D 5 TYR A 181  PRO A 184 -1  N  ALA A 183   O  VAL A 323           
SHEET    1   E 3 GLN A 192  ILE A 195  0                                        
SHEET    2   E 3 CYS A 212  VAL A 216 -1  N  ALA A 214   O  ILE A 193           
SHEET    3   E 3 LEU A 301  LEU A 304  1  N  TRP A 302   O  GLN A 213           
SHEET    1   F 3 GLU A 197  ILE A 200  0                                        
SHEET    2   F 3 LEU A 260  ILE A 264 -1  N  ILE A 263   O  GLU A 197           
SHEET    3   F 3 VAL A 267  PHE A 269 -1  N  PHE A 269   O  PHE A 262           
SHEET    1   G 2 LEU A 223  PRO A 226  0                                        
SHEET    2   G 2 VAL A 288  THR A 291  1  N  GLU A 289   O  LEU A 223           
SHEET    1   H 2 ILE A 277  SER A 279  0                                        
SHEET    2   H 2 CYS A 284  VAL A 286 -1  N  THR A 285   O  LEU A 278           
SHEET    1   I 3 GLY J  16  ILE J  20  0                                        
SHEET    2   I 3 GLN J  25  ASP J  32 -1  N  VAL J  29   O  GLY J  16           
SHEET    3   I 3 GLY J 119  GLY J 122  1  N  GLY J 119   O  LEU J  30           
SHEET    1   J 4 TRP J  39  PRO J  41  0                                        
SHEET    2   J 4 GLN J  99  SER J 104  1  N  GLY J 102   O  VAL J  40           
SHEET    3   J 4 THR J  81  ASP J  87 -1  N  ASP J  87   O  GLN J  99           
SHEET    4   J 4 THR J  70  SER J  72 -1  N  PHE J  71   O  GLY J  82           
SHEET    1   K 2 LEU J  89  VAL J  91  0                                        
SHEET    2   K 2 ILE J  94  VAL J  96 -1  N  VAL J  96   O  LEU J  89           
SHEET    1   L 5 ALA J 165  PHE J 168  0                                        
SHEET    2   L 5 VAL J 150  TYR J 154 -1  N  TYR J 154   O  ALA J 165           
SHEET    3   L 5 TYR J 312  ASP J 317 -1  N  TYR J 316   O  PHE J 151           
SHEET    4   L 5 ARG J 322  THR J 327 -1  N  ALA J 326   O  TYR J 313           
SHEET    5   L 5 TYR J 181  PRO J 184 -1  N  ALA J 183   O  VAL J 323           
SHEET    1   M 3 GLN J 192  ILE J 195  0                                        
SHEET    2   M 3 CYS J 212  VAL J 216 -1  N  ALA J 214   O  ILE J 193           
SHEET    3   M 3 PRO J 300  LEU J 304  1  N  PRO J 300   O  GLN J 213           
SHEET    1   N 3 GLU J 197  ILE J 200  0                                        
SHEET    2   N 3 LEU J 260  ILE J 264 -1  N  ILE J 263   O  GLU J 197           
SHEET    3   N 3 VAL J 267  LEU J 271 -1  N  LEU J 271   O  LEU J 260           
SHEET    1   O 2 LEU J 223  PRO J 226  0                                        
SHEET    2   O 2 VAL J 288  THR J 291  1  N  GLU J 289   O  LEU J 223           
SHEET    1   P 2 ILE J 277  SER J 279  0                                        
SHEET    2   P 2 CYS J 284  VAL J 286 -1  N  THR J 285   O  LEU J 278           
SSBOND   1 CYS A   45    CYS A   50                          1555   1555  2.02  
SSBOND   2 CYS A  208    CYS A  212                          1555   1555  2.03  
SSBOND   3 CYS A  251    CYS A  284                          1555   1555  2.03  
SSBOND   4 CYS J   45    CYS J   50                          1555   1555  2.02  
SSBOND   5 CYS J  208    CYS J  212                          1555   1555  2.03  
SSBOND   6 CYS J  251    CYS J  284                          1555   1555  2.02  
LINK         OG  SER A 275                NA    NA A 330     1555   1555  2.36  
LINK         OG  SER A 311                NA    NA A 330     1555   1555  2.52  
LINK        NA    NA A 330                 O   HOH A 332     1555   1555  2.37  
LINK        NA    NA A 330                 O   HOH A 335     1555   1555  2.62  
LINK        NA    NA A 330                 O   HOH A 342     1555   1555  2.27  
LINK        NA    NA A 330                 O   HOH A 471     1555   1555  2.34  
CISPEP   1 THR A   22    PRO A   23          0        -0.11                     
CISPEP   2 THR J   22    PRO J   23          0        -0.03                     
SITE     1 AC1  6 SER A 275  SER A 311  HOH A 332  HOH A 335                    
SITE     2 AC1  6 HOH A 342  HOH A 471                                          
CRYST1  156.260   50.410  125.180  90.00 117.62  90.00 C 1 2 1       8          
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      0.006400  0.000000  0.003348        0.00000                         
SCALE2      0.000000  0.019837  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009016        0.00000                         
MTRIX1   1  0.199420  0.013420 -0.979820       13.14116    1                    
MTRIX2   1  0.018600 -0.999780 -0.009910      -14.41568    1                    
MTRIX3   1 -0.979740 -0.016250 -0.199630       20.86819    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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