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Database: PDB
Entry: 1FQ3
LinkDB: 1FQ3
Original site: 1FQ3 
HEADER    HYDROLASE                               03-SEP-00   1FQ3              
TITLE     CRYSTAL STRUCTURE OF HUMAN GRANZYME B                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GRANZYME B;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.21.79;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS SYSTEM                    
KEYWDS    CHYMOTRYPSIN-LIKE SERINE PROTEINASE, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ESTEBANEZ-PERPINA,P.FUENTES-PRIOR,D.BELORGEY,H.RUBIN,W.BODE         
REVDAT   3   13-JUL-11 1FQ3    1       VERSN                                    
REVDAT   2   24-FEB-09 1FQ3    1       VERSN                                    
REVDAT   1   31-JAN-01 1FQ3    0                                                
JRNL        AUTH   E.ESTEBANEZ-PERPINA,P.FUENTES-PRIOR,D.BELORGEY,M.BRAUN,      
JRNL        AUTH 2 R.KIEFERSAUER,K.MASKOS,R.HUBER,H.RUBIN,W.BODE                
JRNL        TITL   CRYSTAL STRUCTURE OF THE CASPASE ACTIVATOR HUMAN GRANZYME B, 
JRNL        TITL 2 A PROTEINASE HIGHLY SPECIFIC FOR AN ASP-P1 RESIDUE.          
JRNL        REF    BIOL.CHEM.                    V. 381  1203 2000              
JRNL        REFN                   ISSN 1431-6730                               
JRNL        PMID   11209755                                                     
JRNL        DOI    10.1515/BC.2000.148                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 32.500                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 3582                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.51                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FQ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011806.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 289                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11275                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.19900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 15.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: CATHEPSIN G                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, AMMONIUM SULFATE, VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 290K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       20.87000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.76000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.15500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.76000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.87000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.15500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMER CONSTRUCTED FROM CHAIN A AND CHAIN B NOT RELATED BY A  
REMARK 300 TWO-FOLD SYMMETRY                                                    
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 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ARG A  244                                                       
REMARK 475     TYR A  245                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   23   CG   CD   CE   NZ                                   
REMARK 480     HIS A   25   CG   ND1  CD2  CE1  NE2                             
REMARK 480     MET A   34   CG   SD   CE                                        
REMARK 480     TRP A   36   CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 480     TRP A   36   CZ3  CH2                                            
REMARK 480     GLN A   37A  CG   CD   OE1  NE2                                  
REMARK 480     LYS A   37B  CG   CD   CE   NZ                                   
REMARK 480     LYS A   40   CG   CD   CE   NZ                                   
REMARK 480     LYS A   86   CE   NZ                                             
REMARK 480     ARG A  114   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG A  116   CZ   NH1  NH2                                       
REMARK 480     ASN A  126   CB   CG   OD1  ND2                                  
REMARK 480     LYS A  127   CB   CG   CD   CE   NZ                              
REMARK 480     LYS A  131   CD   CE   NZ                                        
REMARK 480     HIS A  151   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU A  164   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG A  166   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  167   CD   CE   NZ                                        
REMARK 480     ASP A  170A  CB   CG   OD1  OD2                                  
REMARK 480     LEU A  171   CA                                                  
REMARK 480     ARG A  172   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     HIS A  173   CG   ND1  CD2  CE1  NE2                             
REMARK 480     SER A  177   OG                                                  
REMARK 480     GLU A  186   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  188   CG   CD   CE   NZ                                   
REMARK 480     LYS A  188A  CD   CE   NZ                                        
REMARK 480     LYS A  192   CG   CD   CE   NZ                                   
REMARK 480     LYS A  203   CG   CD   CE   NZ                                   
REMARK 480     ARG A  217   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     CYS A  228   SG                                                  
REMARK 480     LYS A  230   NZ                                                  
REMARK 480     LYS A  239   CG   CD   CE   NZ                                   
REMARK 480     LYS A  243   CD   CE   NZ                                        
REMARK 480     LYS B   23   CE   NZ                                             
REMARK 480     ASP B   37   CG   OD1  OD2                                       
REMARK 480     GLN B   37A  CG   CD   OE1  NE2                                  
REMARK 480     LYS B   37B  CB   CG   CD   CE   NZ                              
REMARK 480     LYS B   40   CG   CD   CE   NZ                                   
REMARK 480     GLU B   75   CG   CD   OE1  OE2                                  
REMARK 480     GLN B   76   CD   OE1  NE2                                       
REMARK 480     LYS B  111   CD   CE   NZ                                        
REMARK 480     LYS B  113   CD   CE   NZ                                        
REMARK 480     HIS B  151   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS B  159   CE   NZ                                             
REMARK 480     GLU B  164   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG B  166   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  167   CG   CD   CE   NZ                                   
REMARK 480     ARG B  172   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     HIS B  173   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     LYS B  188   CG   CD   CE   NZ                                   
REMARK 480     LYS B  192   CG   CD   CE   NZ                                   
REMARK 480     LYS B  203   CG   CD   CE   NZ                                   
REMARK 480     LYS B  239   CD   CE   NZ                                        
REMARK 480     LYS B  240   CG   CD   CE   NZ                                   
REMARK 480     LYS B  243   CD   CE   NZ                                        
REMARK 480     ARG B  244   NE   CZ   NH1  NH2                                  
REMARK 480     TYR B  245   C    O    CB   CG   CD1  CD2  CE1                   
REMARK 480     TYR B  245   CE2  CZ   OH   OXT                                  
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    SER A  38   N   -  CA  -  C   ANGL. DEV. =  17.9 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    HIS A  25       49.23     36.72                                   
REMARK 500    MET A  34      109.61   -166.68                                   
REMARK 500    GLN A  37A     155.72     73.89                                   
REMARK 500    LYS A  37B     -42.35    -12.07                                   
REMARK 500    GLN A  48      137.65   -175.45                                   
REMARK 500    ASP A  49      -37.16    -27.31                                   
REMARK 500    HIS A  57        8.28    -68.77                                   
REMARK 500    PRO A  96     -174.81    -53.77                                   
REMARK 500    LYS A  97       17.99     52.55                                   
REMARK 500    ASN A  98      -28.43   -168.24                                   
REMARK 500    SER A 100     -115.64    -42.19                                   
REMARK 500    ASP A 102       82.02    -65.47                                   
REMARK 500    LEU A 105       95.84   -165.33                                   
REMARK 500    SER A 125      139.55     62.70                                   
REMARK 500    ASN A 126     -157.66     75.91                                   
REMARK 500    ALA A 145      156.27     63.41                                   
REMARK 500    LYS A 149      130.81   -176.70                                   
REMARK 500    HIS A 151       95.39    -22.71                                   
REMARK 500    LEU A 155     -176.27    -60.24                                   
REMARK 500    GLN A 156      109.64   -168.64                                   
REMARK 500    VAL A 158      144.66   -179.59                                   
REMARK 500    VAL A 162       84.72    -66.13                                   
REMARK 500    GLN A 163      174.46    -55.04                                   
REMARK 500    GLU A 169      -16.92    -47.34                                   
REMARK 500    ASP A 170A     -37.86     76.67                                   
REMARK 500    LEU A 171       44.51    -76.79                                   
REMARK 500    ARG A 172      -60.75    -16.63                                   
REMARK 500    THR A 178      -24.83    -34.24                                   
REMARK 500    LYS A 203       56.15     88.02                                   
REMARK 500    GLN A 210      -12.68     52.14                                   
REMARK 500    SER A 214      -88.15   -104.92                                   
REMARK 500    ARG A 217      140.01    -29.94                                   
REMARK 500    MET A 242       13.54    -54.44                                   
REMARK 500    LYS A 243      -76.22   -152.43                                   
REMARK 500    HIS B  25       50.12     37.06                                   
REMARK 500    GLN B  37A     132.73     49.49                                   
REMARK 500    LYS B  37B      56.35     21.52                                   
REMARK 500    SER B  38      133.14    161.71                                   
REMARK 500    GLN B  48      138.41   -176.81                                   
REMARK 500    ASP B  49      -41.60    -23.75                                   
REMARK 500    HIS B  57       10.28    -68.71                                   
REMARK 500    HIS B  71      -50.97   -120.29                                   
REMARK 500    ASN B  72       79.52   -116.58                                   
REMARK 500    ILE B  73        5.58    -53.32                                   
REMARK 500    GLN B  76       95.44    -46.58                                   
REMARK 500    LYS B  97      -38.81     76.94                                   
REMARK 500    PHE B  99       23.57     41.15                                   
REMARK 500    ASP B 102       75.67    -69.16                                   
REMARK 500    LEU B 105       94.30   -168.94                                   
REMARK 500    PRO B 124       84.73    -64.72                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  32         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A  38        22.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 900                 
DBREF  1FQ3 A   16   245  UNP    P10144   GRAB_HUMAN      21    247             
DBREF  1FQ3 B   16   245  UNP    P10144   GRAB_HUMAN      21    247             
SEQRES   1 A  227  ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO          
SEQRES   2 A  227  TYR MET ALA TYR LEU MET ILE TRP ASP GLN LYS SER LEU          
SEQRES   3 A  227  LYS ARG CYS GLY GLY PHE LEU ILE GLN ASP ASP PHE VAL          
SEQRES   4 A  227  LEU THR ALA ALA HIS CYS TRP GLY SER SER ILE ASN VAL          
SEQRES   5 A  227  THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU PRO THR          
SEQRES   6 A  227  GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO          
SEQRES   7 A  227  ALA TYR ASN PRO LYS ASN PHE SER ASN ASP ILE MET LEU          
SEQRES   8 A  227  LEU GLN LEU GLU ARG LYS ALA LYS ARG THR ARG ALA VAL          
SEQRES   9 A  227  GLN PRO LEU ARG LEU PRO SER ASN LYS ALA GLN VAL LYS          
SEQRES  10 A  227  PRO GLY GLN THR CYS SER VAL ALA GLY TRP GLY GLN THR          
SEQRES  11 A  227  ALA PRO LEU GLY LYS HIS SER HIS THR LEU GLN GLU VAL          
SEQRES  12 A  227  LYS MET THR VAL GLN GLU ASP ARG LYS CYS GLU SER ASP          
SEQRES  13 A  227  LEU ARG HIS TYR TYR ASP SER THR ILE GLU LEU CYS VAL          
SEQRES  14 A  227  GLY ASP PRO GLU ILE LYS LYS THR SER PHE LYS GLY ASP          
SEQRES  15 A  227  SER GLY GLY PRO LEU VAL CYS ASN LYS VAL ALA GLN GLY          
SEQRES  16 A  227  ILE VAL SER TYR GLY ARG ASN ASN GLY MET PRO PRO ARG          
SEQRES  17 A  227  ALA CYS THR LYS VAL SER SER PHE VAL HIS TRP ILE LYS          
SEQRES  18 A  227  LYS THR MET LYS ARG TYR                                      
SEQRES   1 B  227  ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO          
SEQRES   2 B  227  TYR MET ALA TYR LEU MET ILE TRP ASP GLN LYS SER LEU          
SEQRES   3 B  227  LYS ARG CYS GLY GLY PHE LEU ILE GLN ASP ASP PHE VAL          
SEQRES   4 B  227  LEU THR ALA ALA HIS CYS TRP GLY SER SER ILE ASN VAL          
SEQRES   5 B  227  THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU PRO THR          
SEQRES   6 B  227  GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO          
SEQRES   7 B  227  ALA TYR ASN PRO LYS ASN PHE SER ASN ASP ILE MET LEU          
SEQRES   8 B  227  LEU GLN LEU GLU ARG LYS ALA LYS ARG THR ARG ALA VAL          
SEQRES   9 B  227  GLN PRO LEU ARG LEU PRO SER ASN LYS ALA GLN VAL LYS          
SEQRES  10 B  227  PRO GLY GLN THR CYS SER VAL ALA GLY TRP GLY GLN THR          
SEQRES  11 B  227  ALA PRO LEU GLY LYS HIS SER HIS THR LEU GLN GLU VAL          
SEQRES  12 B  227  LYS MET THR VAL GLN GLU ASP ARG LYS CYS GLU SER ASP          
SEQRES  13 B  227  LEU ARG HIS TYR TYR ASP SER THR ILE GLU LEU CYS VAL          
SEQRES  14 B  227  GLY ASP PRO GLU ILE LYS LYS THR SER PHE LYS GLY ASP          
SEQRES  15 B  227  SER GLY GLY PRO LEU VAL CYS ASN LYS VAL ALA GLN GLY          
SEQRES  16 B  227  ILE VAL SER TYR GLY ARG ASN ASN GLY MET PRO PRO ARG          
SEQRES  17 B  227  ALA CYS THR LYS VAL SER SER PHE VAL HIS TRP ILE LYS          
SEQRES  18 B  227  LYS THR MET LYS ARG TYR                                      
MODRES 1FQ3 ASN B   65  ASN  GLYCOSYLATION SITE                                 
MODRES 1FQ3 ASN A   65  ASN  GLYCOSYLATION SITE                                 
HET    NDG  A 600      14                                                       
HET    NAG  A 601      14                                                       
HET    BMA  A 602      11                                                       
HET    NDG  B 700      14                                                       
HET    NAG  B 701      14                                                       
HET    BMA  B 702      11                                                       
HET    SO4  A 800       5                                                       
HET    SO4  B 900       5                                                       
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  NDG    2(C8 H15 N O6)                                               
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   5  SO4    2(O4 S 2-)                                                   
HELIX    1   1 ALA A   55  TRP A   59  5                                   5    
HELIX    2   2 GLU A  164  GLU A  169  1                                   6    
HELIX    3   3 LYS A  230  MET A  242  1                                  13    
HELIX    4   4 ALA B   55  TRP B   59  5                                   5    
HELIX    5   5 GLU B  164  LEU B  171  1                                   9    
HELIX    6   6 LYS B  230  MET B  242  1                                  13    
SHEET    1   A 9 SER A  38  LYS A  40  0                                        
SHEET    2   A 9 ILE A  35  ASP A  37 -1  N  ILE A  35   O  LYS A  40           
SHEET    3   A 9 SER A  63  LEU A  68 -1  N  SER A  63   O  TRP A  36           
SHEET    4   A 9 MET A  30  TYR A  32 -1  O  TYR A  32   N  THR A  67           
SHEET    5   A 9 GLY A  43  GLN A  48 -1  O  GLY A  44   N  ALA A  31           
SHEET    6   A 9 PHE A  51  THR A  54 -1  N  PHE A  51   O  GLN A  48           
SHEET    7   A 9 MET A 104  LEU A 108 -1  N  MET A 104   O  THR A  54           
SHEET    8   A 9 GLN A  81  PRO A  88 -1  N  LYS A  86   O  GLN A 107           
SHEET    9   A 9 SER A  63  LEU A  68 -1  O  ILE A  64   N  VAL A  85           
SHEET    1   B 2 THR A 135  SER A 137  0                                        
SHEET    2   B 2 LYS A 159  THR A 161 -1  N  MET A 160   O  CYS A 136           
SHEET    1   C 3 GLU A 180  LEU A 181  0                                        
SHEET    2   C 3 CYS A 228  THR A 229 -1  N  CYS A 228   O  LEU A 181           
SHEET    3   C 3 ILE A 212  VAL A 213 -1  N  ILE A 212   O  THR A 229           
SHEET    1   D 7 MET B 104  LEU B 108  0                                        
SHEET    2   D 7 GLN B  81  PRO B  88 -1  N  LYS B  86   O  GLN B 107           
SHEET    3   D 7 ILE B  64  LEU B  68 -1  O  ILE B  64   N  VAL B  85           
SHEET    4   D 7 MET B  30  TRP B  36 -1  N  TYR B  32   O  THR B  67           
SHEET    5   D 7 LEU B  39  GLN B  48 -1  O  LYS B  40   N  ILE B  35           
SHEET    6   D 7 PHE B  51  THR B  54 -1  O  PHE B  51   N  GLN B  48           
SHEET    7   D 7 MET B 104  LEU B 108 -1  N  MET B 104   O  THR B  54           
SHEET    1   E 6 LYS B 159  THR B 161  0                                        
SHEET    2   E 6 THR B 135  VAL B 138 -1  O  CYS B 136   N  MET B 160           
SHEET    3   E 6 PRO B 198  VAL B 200 -1  O  VAL B 200   N  SER B 137           
SHEET    4   E 6 ALA B 209  TYR B 215 -1  N  GLN B 210   O  LEU B 199           
SHEET    5   E 6 ALA B 227  THR B 229 -1  O  ALA B 227   N  SER B 214           
SHEET    6   E 6 GLU B 180  LEU B 181 -1  O  LEU B 181   N  CYS B 228           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   2 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   3 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   4 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   5 CYS B  136    CYS B  201                          1555   1555  2.02  
SSBOND   6 CYS B  168    CYS B  182                          1555   1555  2.02  
LINK         O4  NDG B 700                 C1  NAG B 701     1555   1555  1.41  
LINK         C1  NAG A 601                 O4  NDG A 600     1555   1555  1.42  
LINK         C1  BMA B 702                 O4  NAG B 701     1555   1555  1.45  
LINK         C1  BMA A 602                 O4  NAG A 601     1555   1555  1.47  
LINK         C1  NDG B 700                 ND2 ASN B  65     1555   1555  1.56  
LINK         C1  NDG A 600                 ND2 ASN A  65     1555   1555  1.57  
CISPEP   1 PRO A  224A   PRO A  225          0        -0.12                     
CISPEP   2 PRO B  224A   PRO B  225          0        -0.45                     
SITE     1 AC1  8 MET A  34  ASN A  65  PHE A  82  NAG A 601                    
SITE     2 AC1  8 TRP B  36  SER B  63  NDG B 700  NAG B 701                    
SITE     1 AC2  5 NDG A 600  BMA A 602  TRP B  36  NDG B 700                    
SITE     2 AC2  5 NAG B 701                                                     
SITE     1 AC3  1 NAG A 601                                                     
SITE     1 AC4  7 NDG A 600  NAG A 601  MET B  34  SER B  63                    
SITE     2 AC4  7 ASN B  65  PHE B  82  NAG B 701                               
SITE     1 AC5  6 GLU A 109  ARG A 110  NDG A 600  NAG A 601                    
SITE     2 AC5  6 NDG B 700  BMA B 702                                          
SITE     1 AC6  1 NAG B 701                                                     
SITE     1 AC7  4 HIS A  57  LYS A 192  GLY A 193  SER A 195                    
SITE     1 AC8  2 LYS B 192  SER B 195                                          
CRYST1   41.740  114.310  135.520  90.00  90.00  90.00 P 21 21 21    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      0.023958  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007379        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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