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Database: PDB
Entry: 2B8O
LinkDB: 2B8O
Original site: 2B8O 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-OCT-05   2B8O              
TITLE     CRYSTAL STRUCTURE OF GLU-GLY-ARG-CHLOROMETHYL KETONE-FACTOR           
TITLE    2 VIIA/SOLUBLE TISSUE FACTOR COMPLEX                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII LIGHT CHAIN;                        
COMPND   3 CHAIN: L;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: COAGULATION FACTOR VII HEAVY CHAIN;                        
COMPND   7 CHAIN: H;                                                            
COMPND   8 EC: 3.4.21.21;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: TISSUE FACTOR;                                             
COMPND  12 CHAIN: T;                                                            
COMPND  13 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F7;                                                            
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 GENE: F7;                                                            
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: F3                                                             
KEYWDS    SERINE PROTEASE, TISSUE FACTOR, EGR, BLOOD COAGUALTION, CLOTTING,     
KEYWDS   2 CLOTTING FACTOR, COAGULATION FACTOR, HYDROLASE-HYDROLASE INHIBITOR   
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.P.BAJAJ,A.E.SCHMIDT,K.PADMANABHAN                                   
REVDAT   3   13-JUL-11 2B8O    1       VERSN                                    
REVDAT   2   24-FEB-09 2B8O    1       VERSN                                    
REVDAT   1   13-FEB-07 2B8O    0                                                
JRNL        AUTH   S.P.BAJAJ,A.E.SCHMIDT,K.PADMANABHAN                          
JRNL        TITL   CRYSTAL STRUCTURE OF FACTOR VIIA/SOLUBLE TISSUE FACTOR       
JRNL        TITL 2 COMPLEXED WITH GLU-GLY-ARG-CHLOROMETHYL KETONE               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 15973                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400                            
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            : 4660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 239                                     
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) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.10                            
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 2B8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB034813.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.725                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20351                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.17000                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, SODIUM CHLORIDE, CALCIUM           
REMARK 280  CHLORIDE, PEG 4000, ADA, MAGNESIUM CHLORIDE, PH 6.2, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       35.14000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.43000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.55500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.43000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.14000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.55500            
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 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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -210.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T                               
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     VAL T    83                                                      
REMARK 465     GLU T    84                                                      
REMARK 465     SER T    85                                                      
REMARK 465     THR T    86                                                      
REMARK 465     GLY T    87                                                      
REMARK 465     SER T    88                                                      
REMARK 465     ALA T    89                                                      
REMARK 465     LYS T   159                                                      
REMARK 465     SER T   160                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 465     SER T   163                                                      
REMARK 465     GLY T   164                                                      
REMARK 465     LYS T   165                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER L    52     O5   GLC L   501              2.12            
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    CYS L  17   CA  -  CB  -  SG  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO L 129   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO H  28   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG T 135   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ALA L   3       61.44   -154.81                                   
REMARK 500    PHE L   4      -95.87     26.36                                   
REMARK 500    ARG L  15      -73.97    -89.92                                   
REMARK 500    LYS L  18        2.36    -66.57                                   
REMARK 500    LYS L  32      -75.38     67.03                                   
REMARK 500    LYS L  38      -74.57    -51.75                                   
REMARK 500    LEU L  89       71.44    -69.98                                   
REMARK 500    GLN L 100      -92.39   -113.30                                   
REMARK 500    HIS L 105       30.36   -155.50                                   
REMARK 500    THR L 106       99.39    -25.10                                   
REMARK 500    LEU L 121     -166.07    -77.37                                   
REMARK 500    LYS H  24      106.07    -52.41                                   
REMARK 500    PRO H  28        8.02    -69.84                                   
REMARK 500    LEU H  41      -77.27   -106.40                                   
REMARK 500    CYS H  42     -155.90   -137.10                                   
REMARK 500    ASN H  48     -154.14    166.55                                   
REMARK 500    SER H  54     -164.35   -166.39                                   
REMARK 500    HIS H  71      -77.80   -127.17                                   
REMARK 500    SER H  74       22.52    -68.56                                   
REMARK 500    HIS H 101       37.22     80.00                                   
REMARK 500    ASP H 102       40.16    -69.94                                   
REMARK 500    HIS H 109      -60.43    -29.65                                   
REMARK 500    ARG H 134      -72.29    -51.71                                   
REMARK 500    PRO H 170I    -155.96    -64.51                                   
REMARK 500    ALA H 183      123.95   -171.14                                   
REMARK 500    SER H 188A     -32.53   -136.21                                   
REMARK 500    ASP H 189      157.82    173.24                                   
REMARK 500    SER H 195      149.98    -21.95                                   
REMARK 500    HIS H 199       78.00   -104.11                                   
REMARK 500    ARG H 204       47.13     32.51                                   
REMARK 500    VAL H 213       85.39    -58.69                                   
REMARK 500    SER H 214      -92.94    -71.29                                   
REMARK 500    TRP H 215     -141.15   -123.21                                   
REMARK 500    TRP H 237      -72.38    -61.11                                   
REMARK 500    PRO H 248     -130.26     11.22                                   
REMARK 500    LYS T  41       65.89    -21.86                                   
REMARK 500    SER T  42       31.48    142.33                                   
REMARK 500    THR T  55       41.52   -100.56                                   
REMARK 500    ASP T  66      107.52   -165.17                                   
REMARK 500    VAL T 119       53.55    -98.28                                   
REMARK 500    VAL T 134       79.41    -66.60                                   
REMARK 500    ARG T 135       37.64    -60.90                                   
REMARK 500    ASN T 137       -0.42     68.20                                   
REMARK 500    ASN T 138      -85.96    140.37                                   
REMARK 500    THR T 172     -163.60   -160.78                                   
REMARK 500    ASN T 184       94.80     53.55                                   
REMARK 500    SER T 188      110.86   -168.31                                   
REMARK 500    ASN T 199       31.86     70.07                                   
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 L  44         0.08    SIDE CHAIN                              
REMARK 500    TYR T 103         0.08    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    PHE L   4        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR H 165        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN T 137        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH T 596        DISTANCE =  5.60 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE UNBOUND FORM OF THE INHIBITOR IS GLU-GLY-ARG-CMK-                
REMARK 600 CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN IT NORMALLY FORMS     
REMARK 600 TWO COVALENT BONDS: 1) A COVALENT BOND TO SER 195 FORMING A          
REMARK 600 HEMIKETAL AR7 AND 2) A COVALENT BOND TO NE2 OF HIS 57. THE GEOMETRY  
REMARK 600 OF THE LIGAND, AS REFINED, HOWEVER DOES NOT SUPPORT SUCH COVALENT    
REMARK 600 BONDING OR HEMIKETAL FORMATION.                                      
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     0GJ H    1                                                       
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                              CA H 510  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  80   OE2                                                    
REMARK 620 2 ASP H  72   O   128.7                                              
REMARK 620 3 GLU H  75   O   106.4  91.3                                        
REMARK 620 4 GLU H  70   OE2  74.8  97.1 168.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H 511  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 224   O                                                      
REMARK 620 2 TYR H 184   O   108.2                                              
REMARK 620 3 THR H 221   O    68.7 115.7                                        
REMARK 620 4 HOH H 574   O   100.0  75.7 165.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 513  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H 525   O                                                      
REMARK 620 2 LYS H  24   NZ  169.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   6  OE21                                                    
REMARK 620 2 CGU L   6  OE12  71.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 508  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  14  OE22                                                    
REMARK 620 2 CGU L  19  OE22 132.5                                              
REMARK 620 3 CGU L  14  OE21  54.5 140.7                                        
REMARK 620 4 CGU L  19  OE21  81.7  61.8 134.7                                  
REMARK 620 5 CGU L  14  OE11  93.3 128.5  81.0 115.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  16  OE11                                                    
REMARK 620 2 CGU L  16  OE21  89.4                                              
REMARK 620 3 CGU L  26  OE22 139.5 124.0                                        
REMARK 620 4 CGU L  26  OE12  94.2 155.4  65.6                                  
REMARK 620 5 CGU L  26  OE11  86.6 108.4 101.4  47.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  29  OE11                                                    
REMARK 620 2 HOH L 514   O   115.3                                              
REMARK 620 3 CGU L  29  OE12  39.1 153.5                                        
REMARK 620 4 CGU L  25  OE11 100.6  60.9 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  29  OE12                                                    
REMARK 620 2 HOH L 522   O    57.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE11                                                    
REMARK 620 2 HOH L 535   O    80.3                                              
REMARK 620 3 CGU L  16  OE12 138.8 140.1                                        
REMARK 620 4 CGU L  16  OE11 105.4 125.9  50.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 509  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN L  49   OE1                                                    
REMARK 620 2 GLY L  47   O    75.5                                              
REMARK 620 3 HOH L 551   O   155.4 121.0                                        
REMARK 620 4 ASP L  46   OD2  73.8  90.5  87.1                                  
REMARK 620 5 GLN L  64   O    87.5 162.9  74.8  83.4                            
REMARK 620 6 ASP L  63   OD2 126.2 114.0  66.8 150.6  77.0                      
REMARK 620 7 ASP L  63   OD1  78.9  93.9 115.1 150.3  83.9  48.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: L-ALPHA-GLUTAMYL-N-{(1S)-4-{[AMINO(IMINIO)METHYL]     
REMARK 630 AMINO}-1-[(1S)-2-CHLORO-1-HYDROXYETHYL]BUTYL}GLYCINAMIDE             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     0GJ H     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    GLU GLY AR7 0QE                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0GJ H 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC L 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC L 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 511                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 513                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 514                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 515                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL T 516                  
DBREF  2B8O L    1   142  UNP    P08709   FA7_HUMAN       61    202             
DBREF  2B8O H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  2B8O T    6   210  UNP    P13726   TF_HUMAN        38    242             
SEQRES   1 L  142  ALA ASN ALA PHE LEU CGU CGU LEU ARG PRO GLY SER LEU          
SEQRES   2 L  142  CGU ARG CGU CYS LYS CGU CGU GLN CYS SER PHE CGU CGU          
SEQRES   3 L  142  ALA ARG CGU ILE PHE LYS ASP ALA CGU ARG THR LYS LEU          
SEQRES   4 L  142  PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER          
SEQRES   5 L  142  SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU          
SEQRES   6 L  142  GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY          
SEQRES   7 L  142  ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS          
SEQRES   8 L  142  VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP          
SEQRES   9 L  142  HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY          
SEQRES  10 L  142  TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR          
SEQRES  11 L  142  VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU              
SEQRES   1 H  254  ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO          
SEQRES   2 H  254  TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS          
SEQRES   3 H  254  GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA          
SEQRES   4 H  254  ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU          
SEQRES   5 H  254  ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP          
SEQRES   6 H  254  GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE          
SEQRES   7 H  254  PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE          
SEQRES   8 H  254  ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP          
SEQRES   9 H  254  HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER          
SEQRES  10 H  254  GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER          
SEQRES  11 H  254  GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU          
SEQRES  12 H  254  GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN          
SEQRES  13 H  254  ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO          
SEQRES  14 H  254  ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP          
SEQRES  15 H  254  GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO          
SEQRES  16 H  254  HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY          
SEQRES  17 H  254  ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS          
SEQRES  18 H  254  PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP          
SEQRES  19 H  254  LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL          
SEQRES  20 H  254  LEU LEU ARG ALA PRO PHE PRO                                  
SEQRES   1 T  205  THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR ASN          
SEQRES   2 T  205  PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL ASN          
SEQRES   3 T  205  GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY ASP          
SEQRES   4 T  205  TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU CYS          
SEQRES   5 T  205  ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN THR          
SEQRES   6 T  205  TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY ASN VAL          
SEQRES   7 T  205  GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR GLU ASN          
SEQRES   8 T  205  SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN LEU GLY          
SEQRES   9 T  205  GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY THR LYS          
SEQRES  10 T  205  VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU VAL ARG          
SEQRES  11 T  205  ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL PHE GLY          
SEQRES  12 T  205  LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS SER SER          
SEQRES  13 T  205  SER SER GLY LYS LYS THR ALA LYS THR ASN THR ASN GLU          
SEQRES  14 T  205  PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR CYS PHE          
SEQRES  15 T  205  SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL ASN ARG          
SEQRES  16 T  205  LYS SER THR ASP SER PRO VAL GLU CYS MET                      
MODRES 2B8O SER L   52  SER  GLYCOSYLATION SITE                                 
MODRES 2B8O SER L   60  SER  GLYCOSYLATION SITE                                 
MODRES 2B8O CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2B8O CGU L   35  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
HET    CGU  L   6      12                                                       
HET    CGU  L   7      12                                                       
HET    CGU  L  14      12                                                       
HET    CGU  L  16      12                                                       
HET    CGU  L  19      12                                                       
HET    CGU  L  20      12                                                       
HET    CGU  L  25      12                                                       
HET    CGU  L  26      12                                                       
HET    CGU  L  29      12                                                       
HET    CGU  L  35      12                                                       
HET    GLC  L 501      11                                                       
HET    FUC  L 502      10                                                       
HET     CA  L 503       1                                                       
HET     CA  L 504       1                                                       
HET     MG  L 505       1                                                       
HET     CA  L 506       1                                                       
HET     CA  L 507       1                                                       
HET     MG  L 508       1                                                       
HET     CA  L 509       1                                                       
HET    0GJ  H   1      25                                                       
HET     CA  H 510       1                                                       
HET     NA  H 511       1                                                       
HET     ZN  H 512       1                                                       
HET     ZN  H 513       1                                                       
HET     CL  H 514       1                                                       
HET     CL  H 515       1                                                       
HET     CL  T 516       1                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     0GJ L-ALPHA-GLUTAMYL-N-{(1S)-4-{[AMINO(IMINIO)                       
HETNAM   2 0GJ  METHYL]AMINO}-1-[(1S)-2-CHLORO-1-                               
HETNAM   3 0GJ  HYDROXYETHYL]BUTYL}GLYCINAMIDE                                  
HETNAM      NA SODIUM ION                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   4  GLC    C6 H12 O6                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6   CA    6(CA 2+)                                                     
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL  13  0GJ    C14 H28 CL N6 O5 1+                                          
FORMUL  15   NA    NA 1+                                                        
FORMUL  16   ZN    2(ZN 2+)                                                     
FORMUL  18   CL    3(CL 1-)                                                     
FORMUL  21  HOH   *239(H2 O)                                                    
HELIX    1   1 ALA L    3  CGU L    7  5                                   5    
HELIX    2   2 SER L   12  CYS L   17  1                                   6    
HELIX    3   3 SER L   23  LYS L   32  1                                  10    
HELIX    4   4 ASP L   33  SER L   45  1                                  13    
HELIX    5   5 ASP L   48  SER L   53  5                                   6    
HELIX    6   6 ASP L   86  GLN L   88  5                                   3    
HELIX    7   7 GLU L   94  CYS L   98  5                                   5    
HELIX    8   8 ALA H   55  PHE H   59  5                                   5    
HELIX    9   9 GLU H  125  THR H  129C 1                                   8    
HELIX   10  10 LEU H  129D VAL H  129G 5                                   4    
HELIX   11  11 MET H  164  SER H  170B 1                                   9    
HELIX   12  12 VAL H  231  GLN H  233  5                                   3    
HELIX   13  13 TYR H  234  LEU H  241  1                                   8    
HELIX   14  14 LEU T   59  VAL T   64  1                                   6    
HELIX   15  15 THR T  101  GLU T  105  5                                   5    
HELIX   16  16 SER T  142  GLY T  148  1                                   7    
HELIX   17  17 LYS T  149  LEU T  151  5                                   3    
SHEET    1   A 2 SER L  60  ASP L  63  0                                        
SHEET    2   A 2 TYR L  68  PHE L  71 -1  O  PHE L  71   N  SER L  60           
SHEET    1   B 2 PHE L  76  GLU L  77  0                                        
SHEET    2   B 2 THR L  83  HIS L  84 -1  O  THR L  83   N  GLU L  77           
SHEET    1   C 2 TYR L 101  SER L 103  0                                        
SHEET    2   C 2 SER L 111  ARG L 113 -1  O  SER L 111   N  SER L 103           
SHEET    1   D 2 TYR L 118  LEU L 120  0                                        
SHEET    2   D 2 CYS L 127  PRO L 129 -1  O  THR L 128   N  SER L 119           
SHEET    1   E 5 LYS H  20  VAL H  21  0                                        
SHEET    2   E 5 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3   E 5 PHE H 135  VAL H 138 -1  N  SER H 136   O  VAL H 160           
SHEET    4   E 5 PRO H 198  TYR H 203 -1  O  ALA H 200   N  LEU H 137           
SHEET    5   E 5 THR H 206  ILE H 212 -1  O  THR H 206   N  TYR H 203           
SHEET    1   F 4 LYS H  20  VAL H  21  0                                        
SHEET    2   F 4 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3   F 4 MET H 180  ALA H 183 -1  O  CYS H 182   N  LEU H 163           
SHEET    4   F 4 GLY H 226  THR H 229 -1  O  TYR H 228   N  PHE H 181           
SHEET    1   G 8 LEU H 251  ALA H 254  0                                        
SHEET    2   G 8 GLN H  81  PRO H  91  1  N  ILE H  90   O  ALA H 254           
SHEET    3   G 8 ALA H 104  LEU H 108 -1  O  LEU H 105   N  ILE H  89           
SHEET    4   G 8 TRP H  51  SER H  54 -1  N  VAL H  52   O  LEU H 106           
SHEET    5   G 8 ALA H  39  LEU H  46 -1  N  THR H  45   O  VAL H  53           
SHEET    6   G 8 GLN H  30  VAL H  35 -1  N  VAL H  31   O  GLY H  44           
SHEET    7   G 8 LEU H  64  LEU H  68 -1  O  VAL H  67   N  LEU H  32           
SHEET    8   G 8 GLN H  81  PRO H  91 -1  O  ARG H  83   N  ALA H  66           
SHEET    1   H 3 THR T  13  THR T  17  0                                        
SHEET    2   H 3 LYS T  20  GLU T  24 -1  O  ILE T  22   N  LYS T  15           
SHEET    3   H 3 GLU T  56  CYS T  57 -1  O  CYS T  57   N  LEU T  23           
SHEET    1   I 4 LYS T  46  THR T  52  0                                        
SHEET    2   I 4 GLN T  32  SER T  39 -1  N  VAL T  36   O  LYS T  48           
SHEET    3   I 4 LEU T  72  PRO T  79 -1  O  LEU T  72   N  SER T  39           
SHEET    4   I 4 LEU T  93  ASN T  96 -1  O  LEU T  93   N  SER T  77           
SHEET    1   J 3 ILE T 113  GLN T 118  0                                        
SHEET    2   J 3 LYS T 122  VAL T 127 -1  O  ASN T 124   N  GLU T 117           
SHEET    3   J 3 GLU T 174  ASP T 178 -1  O  ILE T 177   N  VAL T 123           
SHEET    1   K 4 THR T 167  THR T 170  0                                        
SHEET    2   K 4 ILE T 152  TYR T 157 -1  N  LEU T 155   O  ALA T 168           
SHEET    3   K 4 CYS T 186  VAL T 192 -1  O  SER T 188   N  TYR T 156           
SHEET    4   K 4 GLU T 208  CYS T 209 -1  O  GLU T 208   N  PHE T 187           
SSBOND   1 CYS L   17    CYS L   22                          1555   1555  2.04  
SSBOND   2 CYS L   50    CYS L   61                          1555   1555  2.04  
SSBOND   3 CYS L   55    CYS L   70                          1555   1555  2.01  
SSBOND   4 CYS L   72    CYS L   81                          1555   1555  2.06  
SSBOND   5 CYS L   91    CYS L  102                          1555   1555  2.04  
SSBOND   6 CYS L   98    CYS L  112                          1555   1555  2.02  
SSBOND   7 CYS L  114    CYS L  127                          1555   1555  2.04  
SSBOND   8 CYS L  135    CYS H  122                          1555   1555  2.03  
SSBOND   9 CYS H   22    CYS H   27                          1555   1555  2.05  
SSBOND  10 CYS H   42    CYS H   58                          1555   1555  2.04  
SSBOND  11 CYS H  168    CYS H  182                          1555   1555  2.02  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.03  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.05  
SSBOND  14 CYS T  186    CYS T  209                          1555   1555  2.03  
LINK         OG  SER L  52                 C1  GLC L 501     1555   1555  1.34  
LINK         OG  SER L  60                 C1  FUC L 502     1555   1555  1.35  
LINK        CA    CA H 510                 OE2 GLU H  80     1555   1555  2.53  
LINK        CA    CA H 510                 O   ASP H  72     1555   1555  2.25  
LINK        CA    CA H 510                 O   GLU H  75     1555   1555  1.97  
LINK        CA    CA H 510                 OE2 GLU H  70     1555   1555  2.21  
LINK        NA    NA H 511                 O   HIS H 224     1555   1555  2.54  
LINK        ZN    ZN H 513                 O   HOH H 525     1555   1555  2.67  
LINK        ZN    ZN H 513                 NZ  LYS H  24     1555   1555  2.28  
LINK         C   LEU L   5                 N   CGU L   6     1555   1555  1.34  
LINK         C   CGU L   6                 N   CGU L   7     1555   1555  1.33  
LINK        OE21 CGU L   6                CA    CA L 507     1555   1555  1.87  
LINK         C   CGU L   7                 N   LEU L   8     1555   1555  1.34  
LINK         C   LEU L  13                 N   CGU L  14     1555   1555  1.34  
LINK        OE22 CGU L  14                MG    MG L 508     1555   1555  1.82  
LINK         C   CGU L  14                 N   ARG L  15     1555   1555  1.33  
LINK         C   ARG L  15                 N   CGU L  16     1555   1555  1.33  
LINK        OE11 CGU L  16                MG    MG L 505     1555   1555  1.90  
LINK         C   CGU L  16                 N   CYS L  17     1555   1555  1.34  
LINK        OE21 CGU L  16                MG    MG L 505     1555   1555  1.86  
LINK         C   LYS L  18                 N   CGU L  19     1555   1555  1.33  
LINK        OE22 CGU L  19                MG    MG L 508     1555   1555  1.86  
LINK         C   CGU L  19                 N   CGU L  20     1555   1555  1.33  
LINK         C   CGU L  20                 N   GLN L  21     1555   1555  1.33  
LINK         C   PHE L  24                 N   CGU L  25     1555   1555  1.34  
LINK         C   CGU L  25                 N   CGU L  26     1555   1555  1.34  
LINK         C   CGU L  26                 N   ALA L  27     1555   1555  1.33  
LINK         C   ARG L  28                 N   CGU L  29     1555   1555  1.33  
LINK        OE11 CGU L  29                CA    CA L 503     1555   1555  2.02  
LINK        OE12 CGU L  29                CA    CA L 504     1555   1555  1.88  
LINK         C   CGU L  29                 N   ILE L  30     1555   1555  1.32  
LINK         C   ALA L  34                 N   CGU L  35     1555   1555  1.34  
LINK         C   CGU L  35                 N   ARG L  36     1555   1555  1.33  
LINK        CA    CA L 503                 O   HOH L 514     1555   1555  2.31  
LINK        CA    CA L 503                OE12 CGU L  29     1555   1555  3.30  
LINK        CA    CA L 503                OE11 CGU L  25     1555   1555  3.38  
LINK        CA    CA L 504                 O   HOH L 522     1555   1555  3.19  
LINK        MG    MG L 505                OE22 CGU L  26     1555   1555  2.94  
LINK        MG    MG L 505                OE12 CGU L  26     1555   1555  2.82  
LINK        MG    MG L 505                OE11 CGU L  26     1555   1555  2.50  
LINK        CA    CA L 506                OE11 CGU L   7     1555   1555  2.67  
LINK        CA    CA L 506                 O   HOH L 535     1555   1555  2.12  
LINK        CA    CA L 506                OE12 CGU L  16     1555   1555  2.18  
LINK        CA    CA L 506                OE11 CGU L  16     1555   1555  2.79  
LINK        CA    CA L 507                OE12 CGU L   6     1555   1555  3.17  
LINK        MG    MG L 508                OE21 CGU L  14     1555   1555  2.67  
LINK        MG    MG L 508                OE21 CGU L  19     1555   1555  2.31  
LINK        MG    MG L 508                OE11 CGU L  14     1555   1555  2.34  
LINK        CA    CA L 509                 OE1 GLN L  49     1555   1555  2.20  
LINK        CA    CA L 509                 O   GLY L  47     1555   1555  2.00  
LINK        CA    CA L 509                 O   HOH L 551     1555   1555  2.09  
LINK        CA    CA L 509                 OD2 ASP L  46     1555   1555  2.49  
LINK        CA    CA L 509                 O   GLN L  64     1555   1555  2.63  
LINK        CA    CA L 509                 OD2 ASP L  63     1555   1555  2.37  
LINK        CA    CA L 509                 OD1 ASP L  63     1555   1555  2.80  
LINK         O   TYR H 184                NA    NA H 511     1555   1555  2.77  
LINK         O   THR H 221                NA    NA H 511     1555   1555  2.96  
LINK        NA    NA H 511                 O   HOH H 574     1555   1555  2.84  
CISPEP   1 PHE H  256    PRO H  257          0        -4.60                     
CISPEP   2 GLU T   26    PRO T   27          0        -4.03                     
SITE     1 AC1 15 HIS H  57  ASP H 189  SER H 190  CYS H 191                    
SITE     2 AC1 15 LYS H 192  GLY H 193  ASP H 194  SER H 195                    
SITE     3 AC1 15 SER H 214  TRP H 215  GLY H 216  GLY H 219                    
SITE     4 AC1 15  CL H 514  HOH H 605  HOH H 606                               
SITE     1 AC2  4 GLN L  49  SER L  52  PRO L  54  TYR L  68                    
SITE     1 AC3  4 SER L  60  ARG T 131  ARG T 135  PHE T 140                    
SITE     1 AC4  3 CGU L  25  CGU L  29  HOH L 514                               
SITE     1 AC5  1 CGU L  29                                                     
SITE     1 AC6  2 CGU L  16  CGU L  26                                          
SITE     1 AC7  4 ALA L   1  CGU L   7  CGU L  16  HOH L 535                    
SITE     1 AC8  2 CGU L   6  CGU L  20                                          
SITE     1 AC9  2 CGU L  14  CGU L  19                                          
SITE     1 BC1  6 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 BC1  6 GLN L  64  HOH L 551                                          
SITE     1 BC2  4 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     1 BC3  5 TYR H 184  THR H 221  ALA H 221A HIS H 224                    
SITE     2 BC3  5 HOH H 574                                                     
SITE     1 BC4  1 HIS H  76                                                     
SITE     1 BC5  3 LYS H  24  GLY H  69  HOH H 525                               
SITE     1 BC6  3 0GJ H   1  GLY H 216  GLY H 219                               
SITE     1 BC7  4 ARG H  83  ARG H  84  HIS H 109  GLN H 110                    
SITE     1 BC8  3 GLU T 130  TYR T 153  ASN T 173                               
CRYST1   70.280   81.110  126.860  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014229  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012329  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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