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Database: PDB
Entry: 1DX5
LinkDB: 1DX5
Original site: 1DX5 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           20-DEC-99   1DX5              
TITLE     CRYSTAL STRUCTURE OF THE THROMBIN-THROMBOMODULIN COMPLEX              
CAVEAT     1DX5    NAG M 301 HAS WRONG CHIRALITY AT ATOM C1 0GJ M 305 HAS WRONG 
CAVEAT   2 1DX5    CHIRALITY AT ATOM C2 NAG N 301 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 1DX5    C1 0GJ N 305 HAS WRONG CHIRALITY AT ATOM C2 NAG O 301 HAS    
CAVEAT   4 1DX5    WRONG CHIRALITY AT ATOM C1 0GJ O 305 HAS WRONG CHIRALITY AT  
CAVEAT   5 1DX5    ATOM C2 NAG P 301 HAS WRONG CHIRALITY AT ATOM C1 0GJ P 306   
CAVEAT   6 1DX5    HAS WRONG CHIRALITY AT ATOM C2 NAG M 600 WRONG CHIRALITY AT  
CAVEAT   7 1DX5    ATOM C1 NAG N 600 WRONG CHIRALITY AT ATOM C1 NAG O 600       
CAVEAT   8 1DX5    WRONG CHIRALITY AT ATOM C1 NAG P 600 WRONG CHIRALITY AT      
CAVEAT   9 1DX5    ATOM C1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBIN LIGHT CHAIN;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: COAGULATION FACTOR II;                                      
COMPND   5 EC: 3.4.21.5;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: THROMBOMODULIN;                                            
COMPND   8 CHAIN: I, J, K, L;                                                   
COMPND   9 FRAGMENT: EGF-LIKE DOMAINS 4 - 6;                                    
COMPND  10 SYNONYM: TM,FETOMODULIN;                                             
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES;                                                       
COMPND  13 OTHER_DETAILS: ENZYMATICALLY DEGLYCOSYLATED (PNGASE F);              
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: THROMBIN HEAVY CHAIN;                                      
COMPND  16 CHAIN: M, N, O, P;                                                   
COMPND  17 SYNONYM: COAGULATION FACTOR II;                                      
COMPND  18 EC: 3.4.21.5                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 SECRETION: BLOOD PLASMA;                                             
SOURCE   6 OTHER_DETAILS: PURIFIED FROM FROZEN PLASMA;                          
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 TISSUE: ENDOTHELIUM;                                                 
SOURCE  12 GENE: THBD, THRM;                                                    
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 SECRETION: BLOOD PLASMA;                                             
SOURCE  21 OTHER_DETAILS: PURIFIED FROM FROZEN PLASMA                           
KEYWDS    SERINE PROTEINASE, EGF-LIKE DOMAINS, ANTICOAGULANT COMPLEX,           
KEYWDS   2 ANTIFIBRINOLYTIC COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FUENTES-PRIOR,Y.IWANAGA,R.HUBER,R.PAGILA,G.RUMENNIK,M.SETO,         
AUTHOR   2 J.MORSER,D.R.LIGHT,W.BODE                                            
REVDAT   6   29-JUL-20 1DX5    1       COMPND REMARK HETNAM LINK                
REVDAT   6 2                   1       SITE                                     
REVDAT   5   27-JUN-18 1DX5    1       CAVEAT COMPND SOURCE REMARK              
REVDAT   5 2                   1       DBREF  SEQADV SEQRES HET                 
REVDAT   5 3                   1       HETNAM HETSYN FORMUL HELIX               
REVDAT   5 4                   1       SHEET  SSBOND LINK   SITE                
REVDAT   5 5                   1       ATOM                                     
REVDAT   4   21-DEC-16 1DX5    1       CAVEAT SOURCE REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL SSBOND LINK                
REVDAT   4 3                   1       HETATM CONECT MASTER                     
REVDAT   3   13-JUL-11 1DX5    1       VERSN                                    
REVDAT   2   24-FEB-09 1DX5    1       VERSN                                    
REVDAT   1   10-APR-00 1DX5    0                                                
JRNL        AUTH   P.FUENTES-PRIOR,Y.IWANAGA,R.HUBER,R.PAGILA,G.RUMENNIK,       
JRNL        AUTH 2 M.SETO,J.MORSER,D.R.LIGHT,W.BODE                             
JRNL        TITL   STRUCTURAL BASIS FOR THE ANTICOAGULANT ACTIVITY OF THE       
JRNL        TITL 2 THROMBIN-THROMBOMODULIN COMPLEX                              
JRNL        REF    NATURE                        V. 404   518 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10761923                                                     
JRNL        DOI    10.1038/35006683                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 98582                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1964                            
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            : 13020                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 183                                     
REMARK   3   SOLVENT ATOMS            : 815                                     
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) : 0.080                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.540                           
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: RESIDUES 14L-15 NOT SEEN IN THE DENSITY   
REMARK   3  MAP                                                                 
REMARK   4                                                                      
REMARK   4 1DX5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-99.                  
REMARK 100 THE DEPOSITION ID IS D_1290004490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.105                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM V. 6.00                     
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 670680                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.870                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: THROMBIN-PPACK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA ACETATE (PH 4.6), 1.8 M NA      
REMARK 280  FORMATE, 0.002 M CA CHLORIDE, PH 6.50                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      107.20000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.89195            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.80333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000      107.20000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       61.89195            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.80333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000      107.20000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       61.89195            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.80333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      123.78390            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       87.60667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      123.78390            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       87.60667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      123.78390            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       87.60667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, M                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J, N                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11200 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K, O                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11930 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L, P                               
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE UNBOUND FORM OF THE INHIBITOR IS GLU-GLY-ARG-                    
REMARK 400 CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN IT FORMS TWO          
REMARK 400 COVALENT BONDS: 1) A COVALENT BOND TO SER 195 FORMING A HEMIKETAL    
REMARK 400 AR7 AND 2) A COVALENT BOND TO NE2 OF HIS 57                          
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     THR A     1H                                                     
REMARK 475     ASP A    14L                                                     
REMARK 475     GLY A    14M                                                     
REMARK 475     ARG A    15                                                      
REMARK 475     THR B     1H                                                     
REMARK 475     ASP B    14L                                                     
REMARK 475     GLY B    14M                                                     
REMARK 475     ARG B    15                                                      
REMARK 475     THR C     1H                                                     
REMARK 475     ASP C    14L                                                     
REMARK 475     GLY C    14M                                                     
REMARK 475     ARG C    15                                                      
REMARK 475     THR D     1H                                                     
REMARK 475     ASP D    14L                                                     
REMARK 475     GLY D    14M                                                     
REMARK 475     ARG D    15                                                      
REMARK 475     VAL I   345                                                      
REMARK 475     GLU I   346                                                      
REMARK 475     PRO I   450                                                      
REMARK 475     ASP I   451                                                      
REMARK 475     SER I   452                                                      
REMARK 475     ALA I   453                                                      
REMARK 475     LEU I   454                                                      
REMARK 475     VAL J   345                                                      
REMARK 475     GLU J   346                                                      
REMARK 475     PRO J   347                                                      
REMARK 475     PRO J   450                                                      
REMARK 475     ASP J   451                                                      
REMARK 475     SER J   452                                                      
REMARK 475     ALA J   453                                                      
REMARK 475     LEU J   454                                                      
REMARK 475     ALA J   455                                                      
REMARK 475     VAL K   345                                                      
REMARK 475     GLU K   346                                                      
REMARK 475     GLY K   449                                                      
REMARK 475     PRO K   450                                                      
REMARK 475     ASP K   451                                                      
REMARK 475     SER K   452                                                      
REMARK 475     ALA K   453                                                      
REMARK 475     LEU K   454                                                      
REMARK 475     VAL L   345                                                      
REMARK 475     GLU L   346                                                      
REMARK 475     PRO L   450                                                      
REMARK 475     ASP L   451                                                      
REMARK 475     SER L   452                                                      
REMARK 475     ALA L   453                                                      
REMARK 475     LEU L   454                                                      
REMARK 475     ALA L   455                                                      
REMARK 475     THR M   147                                                      
REMARK 475     TRP M   148                                                      
REMARK 475     THR M   149                                                      
REMARK 475     ALA M   149A                                                     
REMARK 475     ASN M   149B                                                     
REMARK 475     VAL M   149C                                                     
REMARK 475     GLY M   149D                                                     
REMARK 475     TRP N   148                                                      
REMARK 475     THR N   149                                                      
REMARK 475     ALA N   149A                                                     
REMARK 475     ASN N   149B                                                     
REMARK 475     VAL N   149C                                                     
REMARK 475     GLY N   149D                                                     
REMARK 475     THR O   147                                                      
REMARK 475     TRP O   148                                                      
REMARK 475     THR O   149                                                      
REMARK 475     ALA O   149A                                                     
REMARK 475     ASN O   149B                                                     
REMARK 475     VAL O   149C                                                     
REMARK 475     GLY O   149D                                                     
REMARK 475     TRP P   148                                                      
REMARK 475     THR P   149                                                      
REMARK 475     ALA P   149A                                                     
REMARK 475     ASN P   149B                                                     
REMARK 475     VAL P   149C                                                     
REMARK 475     GLY P   149D                                                     
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   14A  CD   CE   NZ                                        
REMARK 480     ARG A   14D  CD   NE   CZ   NH1  NH2                             
REMARK 480     LEU A   14G  CG   CD1  CD2                                       
REMARK 480     GLU A   14H  CG   CD   OE1  OE2                                  
REMARK 480     LYS B   14A  CE   NZ                                             
REMARK 480     ARG B   14D  CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C   14A  CG   CD   CE   NZ                                   
REMARK 480     ARG C   14D  CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU C   14H  CD   OE1  OE2                                       
REMARK 480     ILE C   14K  CB   CG1  CG2  CD1                                  
REMARK 480     LYS D   14A  CG   CD   CE   NZ                                   
REMARK 480     ARG D   14D  NE   CZ   NH1  NH2                                  
REMARK 480     GLN I  365   CB   CG   CD   OE1  NE2                             
REMARK 480     GLU I  374   CD   OE1  OE2                                       
REMARK 480     GLU I  411   CD   OE1  OE2                                       
REMARK 480     GLN J  365   CB   CG   CD   OE1  NE2                             
REMARK 480     GLU J  374   CD   OE1  OE2                                       
REMARK 480     ARG J  385   NE   CZ   NH1  NH2                                  
REMARK 480     GLU J  411   CD   OE1  OE2                                       
REMARK 480     GLN J  457   CG   CD   OE1  NE2                                  
REMARK 480     GLN K  365   CB   CG   CD   OE1  NE2                             
REMARK 480     GLU K  374   CD   OE1  OE2                                       
REMARK 480     ARG K  385   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU K  411   CG   CD   OE1  OE2                                  
REMARK 480     ALA K  455   N    CA   CB                                        
REMARK 480     GLN L  365   CG   CD   OE1  NE2                                  
REMARK 480     GLU L  374   CD   OE1  OE2                                       
REMARK 480     GLN L  404   CB   CG   OE1  NE2                                  
REMARK 480     GLU L  411   CD   OE1  OE2                                       
REMARK 480     LYS M  145   CE   NZ                                             
REMARK 480     LYS M  149E  CG   CD   CE   NZ                                   
REMARK 480     LYS M  169   CD   CE   NZ                                        
REMARK 480     ARG M  173   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU M  192   CD   OE1  OE2                                       
REMARK 480     LYS M  236   CD   CE   NZ                                        
REMARK 480     ARG N   93   CZ   NH1  NH2                                       
REMARK 480     GLU N   97A  CG   CD   OE1  OE2                                  
REMARK 480     LYS N  145   CE   NZ                                             
REMARK 480     LYS N  149E  CG   CD   CE   NZ                                   
REMARK 480     LYS N  169   CD   CE   NZ                                        
REMARK 480     ARG N  173   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS N  236   CD   CE   NZ                                        
REMARK 480     LYS N  240   NZ                                                  
REMARK 480     GLU O   97A  CD   OE1  OE2                                       
REMARK 480     LYS O  107   NZ                                                  
REMARK 480     LYS O  110   NZ                                                  
REMARK 480     LYS O  145   CD   CE   NZ                                        
REMARK 480     LYS O  149E  CB   CG   CD   CE   NZ                              
REMARK 480     LYS O  169   CD   CE   NZ                                        
REMARK 480     ARG O  173   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS O  186D  NZ                                                  
REMARK 480     LYS O  236   CE   NZ                                             
REMARK 480     LYS P  145   NZ                                                  
REMARK 480     THR P  147   CA   C    O    CB   OG1  CG2                        
REMARK 480     LYS P  149E  N    CB   CG   CD   CE   NZ                         
REMARK 480     LYS P  169   CD   CE   NZ                                        
REMARK 480     ARG P  173   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS P  236   CD   CE   NZ                                        
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 M   195     O2   0GJ M   305              2.16            
REMARK 500   OG   SER N   195     O2   0GJ N   305              2.16            
REMARK 500   OG   SER P   195     O2   0GJ P   306              2.17            
REMARK 500   OG   SER O   195     C3   0GJ O   306              2.17            
REMARK 500   OG   SER O   195     O2   0GJ O   305              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A   1C  CG    GLU A   1C  CD      0.093                       
REMARK 500    GLU A   8   CG    GLU A   8   CD      0.094                       
REMARK 500    GLU A  13   CG    GLU A  13   CD      0.094                       
REMARK 500    GLU A  14E  CG    GLU A  14E  CD      0.090                       
REMARK 500    GLU A  14H  CG    GLU A  14H  CD      0.093                       
REMARK 500    GLU B   1C  CG    GLU B   1C  CD      0.101                       
REMARK 500    GLU B   8   CG    GLU B   8   CD      0.093                       
REMARK 500    GLU B  13   CG    GLU B  13   CD      0.091                       
REMARK 500    GLU B  14E  CG    GLU B  14E  CD      0.092                       
REMARK 500    GLU B  14H  CG    GLU B  14H  CD      0.091                       
REMARK 500    GLU C   8   CG    GLU C   8   CD      0.095                       
REMARK 500    GLU C  13   CG    GLU C  13   CD      0.098                       
REMARK 500    GLU C  14E  CG    GLU C  14E  CD      0.094                       
REMARK 500    GLU C  14H  CG    GLU C  14H  CD      0.092                       
REMARK 500    GLU D   1C  CG    GLU D   1C  CD      0.093                       
REMARK 500    GLU D   8   CG    GLU D   8   CD      0.099                       
REMARK 500    GLU D  13   CG    GLU D  13   CD      0.094                       
REMARK 500    GLU D  14E  CG    GLU D  14E  CD      0.094                       
REMARK 500    GLU D  14H  CG    GLU D  14H  CD      0.094                       
REMARK 500    GLU I 346   CG    GLU I 346   CD      0.091                       
REMARK 500    GLU I 374   CG    GLU I 374   CD      0.096                       
REMARK 500    GLU I 382   CG    GLU I 382   CD      0.092                       
REMARK 500    GLU I 408   CG    GLU I 408   CD      0.092                       
REMARK 500    GLU I 411   CG    GLU I 411   CD      0.095                       
REMARK 500    GLU I 426   CG    GLU I 426   CD      0.095                       
REMARK 500    GLU I 428   CG    GLU I 428   CD      0.102                       
REMARK 500    GLU J 346   CG    GLU J 346   CD      0.094                       
REMARK 500    GLU J 374   CG    GLU J 374   CD      0.095                       
REMARK 500    GLU J 382   CG    GLU J 382   CD      0.100                       
REMARK 500    GLU J 408   CG    GLU J 408   CD      0.095                       
REMARK 500    GLU J 411   CG    GLU J 411   CD      0.092                       
REMARK 500    GLU J 428   CG    GLU J 428   CD      0.102                       
REMARK 500    GLU K 346   CG    GLU K 346   CD      0.095                       
REMARK 500    GLU K 374   CG    GLU K 374   CD      0.092                       
REMARK 500    GLU K 411   CG    GLU K 411   CD      0.094                       
REMARK 500    GLU K 428   CG    GLU K 428   CD      0.102                       
REMARK 500    GLU L 374   CG    GLU L 374   CD      0.098                       
REMARK 500    GLU L 408   CG    GLU L 408   CD      0.090                       
REMARK 500    GLU L 411   CG    GLU L 411   CD      0.097                       
REMARK 500    GLU L 428   CG    GLU L 428   CD      0.100                       
REMARK 500    GLU M  97A  CG    GLU M  97A  CD      0.093                       
REMARK 500    GLU M 127   CG    GLU M 127   CD      0.096                       
REMARK 500    GLU M 164   CG    GLU M 164   CD      0.105                       
REMARK 500    GLU M 192   CG    GLU M 192   CD      0.095                       
REMARK 500    GLU M 217   CG    GLU M 217   CD      0.092                       
REMARK 500    GLU M 247   CG    GLU M 247   CD      0.095                       
REMARK 500    GLU N  18   CG    GLU N  18   CD      0.093                       
REMARK 500    GLU N  23   CG    GLU N  23   CD      0.090                       
REMARK 500    GLU N  97A  CG    GLU N  97A  CD      0.095                       
REMARK 500    GLU N 127   CG    GLU N 127   CD      0.099                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   7      -84.74   -127.26                                   
REMARK 500    PHE B   7      -87.24   -126.29                                   
REMARK 500    PHE C   7      -85.10   -127.79                                   
REMARK 500    PHE D   7      -84.83   -125.28                                   
REMARK 500    GLU I 346      123.71     23.41                                   
REMARK 500    TYR I 358      -77.10   -108.71                                   
REMARK 500    LEU I 363      -61.40   -108.38                                   
REMARK 500    ASP I 364     -156.69   -111.90                                   
REMARK 500    THR I 443     -154.19   -158.27                                   
REMARK 500    ALA I 453      -43.10     71.57                                   
REMARK 500    LEU I 454      127.91     61.23                                   
REMARK 500    TYR J 358      -77.35   -107.95                                   
REMARK 500    ASP J 364     -154.61   -133.78                                   
REMARK 500    THR J 443     -154.98   -159.73                                   
REMARK 500    ASP J 451       93.40     52.68                                   
REMARK 500    SER J 452      -72.65     67.40                                   
REMARK 500    ALA J 453      -86.29   -155.73                                   
REMARK 500    LEU J 454      -94.20    -75.74                                   
REMARK 500    ALA J 455       98.64     89.40                                   
REMARK 500    GLU K 346      -83.22     87.27                                   
REMARK 500    TYR K 358      -83.23   -108.93                                   
REMARK 500    ASP K 364     -156.47   -134.01                                   
REMARK 500    THR K 443     -152.94   -163.31                                   
REMARK 500    PRO K 450      -80.57    -65.80                                   
REMARK 500    ASP K 451      -32.28   -166.05                                   
REMARK 500    GLU L 346      -88.09     69.23                                   
REMARK 500    TYR L 358      -84.00   -104.76                                   
REMARK 500    ASP L 364     -153.10   -132.27                                   
REMARK 500    THR L 443     -158.51   -156.58                                   
REMARK 500    ASP L 451     -155.92    152.75                                   
REMARK 500    SER L 452     -107.59     60.80                                   
REMARK 500    LEU L 454       86.66     59.60                                   
REMARK 500    TYR M  60A      85.94   -154.43                                   
REMARK 500    ASN M  60G      80.53   -168.20                                   
REMARK 500    HIS M  71      -67.90   -126.93                                   
REMARK 500    GLU M  97A     -73.96   -141.81                                   
REMARK 500    SER M 115     -167.12   -166.05                                   
REMARK 500    HIS M 119      127.80   -173.27                                   
REMARK 500    THR M 147     -133.92     39.95                                   
REMARK 500    TRP M 148       54.47     26.12                                   
REMARK 500    THR M 149     -156.19    165.38                                   
REMARK 500    ASN M 149B     136.58   -170.38                                   
REMARK 500    SER N  48     -177.26   -172.35                                   
REMARK 500    TYR N  60A      87.47   -163.49                                   
REMARK 500    HIS N  71      -63.54   -125.64                                   
REMARK 500    GLU N  97A     -73.80   -138.05                                   
REMARK 500    THR N 147     -118.04     27.36                                   
REMARK 500    THR N 149      -50.54   -162.88                                   
REMARK 500    ALA N 149A     118.78    170.11                                   
REMARK 500    ASN N 149B     136.45   -173.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     NAG M   301                                                      
REMARK 615     NAG N   301                                                      
REMARK 615     NAG O   301                                                      
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 I 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 423   OD1                                                    
REMARK 620 2 ASP I 423   OD2  48.1                                              
REMARK 620 3 ILE I 424   O    87.3  79.4                                        
REMARK 620 4 GLU I 426   OE1 141.6 139.7  65.4                                  
REMARK 620 5 ASN I 439   OD1 127.6  80.0  89.7  80.9                            
REMARK 620 6 LEU I 440   O    75.2  73.9 153.3 138.9  85.4                      
REMARK 620 7 THR I 443   O   126.2 139.3 139.1  73.8  86.5  66.8                
REMARK 620 8 HOH I 609   O    72.1 118.4  85.1  78.8 159.5 107.8  84.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT I 501   O1                                                     
REMARK 620 2 FMT I 501   O2   42.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA J 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J 423   OD1                                                    
REMARK 620 2 ASP J 423   OD2  50.2                                              
REMARK 620 3 ILE J 424   O    88.1  80.7                                        
REMARK 620 4 GLU J 426   OE1 143.1 140.1  66.1                                  
REMARK 620 5 ASN J 439   OD1 132.0  82.5  92.5  77.6                            
REMARK 620 6 LEU J 440   O    78.5  75.9 156.5 134.0  82.6                      
REMARK 620 7 THR J 443   O   124.1 137.9 139.4  73.6  83.3  63.1                
REMARK 620 8 HOH J 609   O    70.5 118.6  83.3  80.2 157.2 109.6  85.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA J 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT J 501   O1                                                     
REMARK 620 2 FMT J 501   O2   42.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K 423   OD1                                                    
REMARK 620 2 ASP K 423   OD2  48.8                                              
REMARK 620 3 ILE K 424   O    86.2  78.3                                        
REMARK 620 4 GLU K 426   OE1 143.9 138.0  66.9                                  
REMARK 620 5 ASN K 439   OD1 126.0  77.9  91.9  80.5                            
REMARK 620 6 LEU K 440   O    76.9  75.8 154.1 136.0  82.6                      
REMARK 620 7 THR K 443   O   127.3 140.0 139.1  72.5  85.8  66.0                
REMARK 620 8 HOH K 604   O    73.4 119.9  83.9  79.9 160.1 109.3  84.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA K 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT K 501   O1                                                     
REMARK 620 2 FMT K 501   O2   44.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 423   OD1                                                    
REMARK 620 2 ASP L 423   OD2  49.0                                              
REMARK 620 3 ILE L 424   O    86.6  77.8                                        
REMARK 620 4 GLU L 426   OE1 142.3 138.8  66.7                                  
REMARK 620 5 ASN L 439   OD1 128.6  80.2  89.6  79.4                            
REMARK 620 6 LEU L 440   O    76.8  75.3 153.0 137.0  84.6                      
REMARK 620 7 THR L 443   O   125.3 137.8 141.8  75.1  85.3  64.0                
REMARK 620 8 HOH L 606   O    71.7 118.5  85.0  79.5 158.6 109.1  86.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA L 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT L 501   O1                                                     
REMARK 620 2 FMT L 501   O2   43.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA M 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP M 221   OD1                                                    
REMARK 620 2 HOH M 444   O    79.5                                              
REMARK 620 3 HOH M 446   O   129.3 111.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA N 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG N 221A  O                                                      
REMARK 620 2 LYS N 224   O    91.4                                              
REMARK 620 3 HOH N 404   O   150.7  65.3                                        
REMARK 620 4 HOH N 493   O    86.4  87.9  75.7                                  
REMARK 620 5 HOH N 500   O   100.5  75.9  91.1 162.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA O 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG O 221A  O                                                      
REMARK 620 2 LYS O 224   O    94.2                                              
REMARK 620 3 HOH O 435   O   109.1 156.5                                        
REMARK 620 4 HOH O 436   O   157.1  64.1  93.2                                  
REMARK 620 5 HOH O 478   O    92.5  93.1  89.1  82.2                            
REMARK 620 6 HOH O 491   O    95.4  73.9 100.1  85.7 165.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA P 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG P 221A  O                                                      
REMARK 620 2 LYS P 224   O    89.3                                              
REMARK 620 3 HOH P 427   O   148.3  61.7                                        
REMARK 620 4 HOH P 455   O    91.6  87.5  75.7                                  
REMARK 620 5 HOH P 509   O    96.0  76.0  89.4 161.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
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 M   303                                                      
REMARK 630     0GJ M   304                                                      
REMARK 630     0GJ M   305                                                      
REMARK 630     0GJ M   306                                                      
REMARK 630     0GJ N   303                                                      
REMARK 630     0GJ N   304                                                      
REMARK 630     0GJ N   305                                                      
REMARK 630     0GJ N   306                                                      
REMARK 630     0GJ O   303                                                      
REMARK 630     0GJ O   304                                                      
REMARK 630     0GJ O   305                                                      
REMARK 630     0GJ O   306                                                      
REMARK 630     0GJ P   304                                                      
REMARK 630     0GJ P   305                                                      
REMARK 630     0GJ P   306                                                      
REMARK 630     0GJ P   307                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    GLU GLY AR7 0QE                                          
REMARK 630 DETAILS: NULL                                                        
DBREF  1DX5 A    1H   15  UNP    P00734   THRB_HUMAN     328    363             
DBREF  1DX5 B    1H   15  UNP    P00734   THRB_HUMAN     328    363             
DBREF  1DX5 C    1H   15  UNP    P00734   THRB_HUMAN     328    363             
DBREF  1DX5 D    1H   15  UNP    P00734   THRB_HUMAN     328    363             
DBREF  1DX5 I  345   462  UNP    P07204   TRBM_HUMAN     363    480             
DBREF  1DX5 J  345   462  UNP    P07204   TRBM_HUMAN     363    480             
DBREF  1DX5 K  345   462  UNP    P07204   TRBM_HUMAN     363    480             
DBREF  1DX5 L  345   462  UNP    P07204   TRBM_HUMAN     363    480             
DBREF  1DX5 M   16   247  UNP    P00734   THRB_HUMAN     364    622             
DBREF  1DX5 N   16   247  UNP    P00734   THRB_HUMAN     364    622             
DBREF  1DX5 O   16   247  UNP    P00734   THRB_HUMAN     364    622             
DBREF  1DX5 P   16   247  UNP    P00734   THRB_HUMAN     364    622             
SEQADV 1DX5 ASP I  364  UNP  P07204    ASN   382 CONFLICT                       
SEQADV 1DX5 GLY I  456  UNP  P07204    ARG   474 CONFLICT                       
SEQADV 1DX5 GLN I  457  UNP  P07204    HIS   475 CONFLICT                       
SEQADV 1DX5 ASP J  364  UNP  P07204    ASN   382 CONFLICT                       
SEQADV 1DX5 GLY J  456  UNP  P07204    ARG   474 CONFLICT                       
SEQADV 1DX5 GLN J  457  UNP  P07204    HIS   475 CONFLICT                       
SEQADV 1DX5 ASP K  364  UNP  P07204    ASN   382 CONFLICT                       
SEQADV 1DX5 GLY K  456  UNP  P07204    ARG   474 CONFLICT                       
SEQADV 1DX5 GLN K  457  UNP  P07204    HIS   475 CONFLICT                       
SEQADV 1DX5 ASP L  364  UNP  P07204    ASN   382 CONFLICT                       
SEQADV 1DX5 GLY L  456  UNP  P07204    ARG   474 CONFLICT                       
SEQADV 1DX5 GLN L  457  UNP  P07204    HIS   475 CONFLICT                       
SEQADV 1DX5 ILE M   60I UNP  P00734    THR   418 CONFLICT                       
SEQADV 1DX5 ILE N   60I UNP  P00734    THR   418 CONFLICT                       
SEQADV 1DX5 ILE O   60I UNP  P00734    THR   418 CONFLICT                       
SEQADV 1DX5 ILE P   60I UNP  P00734    THR   418 CONFLICT                       
SEQRES   1 A   36  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   2 A   36  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   3 A   36  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 B   36  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   2 B   36  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   3 B   36  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 C   36  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   2 C   36  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   3 C   36  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 D   36  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   2 D   36  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   3 D   36  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 I  118  VAL GLU PRO VAL ASP PRO CYS PHE ARG ALA ASN CYS GLU          
SEQRES   2 I  118  TYR GLN CYS GLN PRO LEU ASP GLN THR SER TYR LEU CYS          
SEQRES   3 I  118  VAL CYS ALA GLU GLY PHE ALA PRO ILE PRO HIS GLU PRO          
SEQRES   4 I  118  HIS ARG CYS GLN MET PHE CYS ASN GLN THR ALA CYS PRO          
SEQRES   5 I  118  ALA ASP CYS ASP PRO ASN THR GLN ALA SER CYS GLU CYS          
SEQRES   6 I  118  PRO GLU GLY TYR ILE LEU ASP ASP GLY PHE ILE CYS THR          
SEQRES   7 I  118  ASP ILE ASP GLU CYS GLU ASN GLY GLY PHE CYS SER GLY          
SEQRES   8 I  118  VAL CYS HIS ASN LEU PRO GLY THR PHE GLU CYS ILE CYS          
SEQRES   9 I  118  GLY PRO ASP SER ALA LEU ALA GLY GLN ILE GLY THR ASP          
SEQRES  10 I  118  CYS                                                          
SEQRES   1 J  118  VAL GLU PRO VAL ASP PRO CYS PHE ARG ALA ASN CYS GLU          
SEQRES   2 J  118  TYR GLN CYS GLN PRO LEU ASP GLN THR SER TYR LEU CYS          
SEQRES   3 J  118  VAL CYS ALA GLU GLY PHE ALA PRO ILE PRO HIS GLU PRO          
SEQRES   4 J  118  HIS ARG CYS GLN MET PHE CYS ASN GLN THR ALA CYS PRO          
SEQRES   5 J  118  ALA ASP CYS ASP PRO ASN THR GLN ALA SER CYS GLU CYS          
SEQRES   6 J  118  PRO GLU GLY TYR ILE LEU ASP ASP GLY PHE ILE CYS THR          
SEQRES   7 J  118  ASP ILE ASP GLU CYS GLU ASN GLY GLY PHE CYS SER GLY          
SEQRES   8 J  118  VAL CYS HIS ASN LEU PRO GLY THR PHE GLU CYS ILE CYS          
SEQRES   9 J  118  GLY PRO ASP SER ALA LEU ALA GLY GLN ILE GLY THR ASP          
SEQRES  10 J  118  CYS                                                          
SEQRES   1 K  118  VAL GLU PRO VAL ASP PRO CYS PHE ARG ALA ASN CYS GLU          
SEQRES   2 K  118  TYR GLN CYS GLN PRO LEU ASP GLN THR SER TYR LEU CYS          
SEQRES   3 K  118  VAL CYS ALA GLU GLY PHE ALA PRO ILE PRO HIS GLU PRO          
SEQRES   4 K  118  HIS ARG CYS GLN MET PHE CYS ASN GLN THR ALA CYS PRO          
SEQRES   5 K  118  ALA ASP CYS ASP PRO ASN THR GLN ALA SER CYS GLU CYS          
SEQRES   6 K  118  PRO GLU GLY TYR ILE LEU ASP ASP GLY PHE ILE CYS THR          
SEQRES   7 K  118  ASP ILE ASP GLU CYS GLU ASN GLY GLY PHE CYS SER GLY          
SEQRES   8 K  118  VAL CYS HIS ASN LEU PRO GLY THR PHE GLU CYS ILE CYS          
SEQRES   9 K  118  GLY PRO ASP SER ALA LEU ALA GLY GLN ILE GLY THR ASP          
SEQRES  10 K  118  CYS                                                          
SEQRES   1 L  118  VAL GLU PRO VAL ASP PRO CYS PHE ARG ALA ASN CYS GLU          
SEQRES   2 L  118  TYR GLN CYS GLN PRO LEU ASP GLN THR SER TYR LEU CYS          
SEQRES   3 L  118  VAL CYS ALA GLU GLY PHE ALA PRO ILE PRO HIS GLU PRO          
SEQRES   4 L  118  HIS ARG CYS GLN MET PHE CYS ASN GLN THR ALA CYS PRO          
SEQRES   5 L  118  ALA ASP CYS ASP PRO ASN THR GLN ALA SER CYS GLU CYS          
SEQRES   6 L  118  PRO GLU GLY TYR ILE LEU ASP ASP GLY PHE ILE CYS THR          
SEQRES   7 L  118  ASP ILE ASP GLU CYS GLU ASN GLY GLY PHE CYS SER GLY          
SEQRES   8 L  118  VAL CYS HIS ASN LEU PRO GLY THR PHE GLU CYS ILE CYS          
SEQRES   9 L  118  GLY PRO ASP SER ALA LEU ALA GLY GLN ILE GLY THR ASP          
SEQRES  10 L  118  CYS                                                          
SEQRES   1 M  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 M  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 M  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 M  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 M  259  ASN PHE ILE GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 M  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 M  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 M  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 M  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 M  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 M  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 M  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 M  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 M  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 M  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 M  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 M  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 M  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 M  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 M  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
SEQRES   1 N  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 N  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 N  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 N  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 N  259  ASN PHE ILE GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 N  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 N  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 N  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 N  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 N  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 N  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 N  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 N  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 N  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 N  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 N  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 N  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 N  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 N  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 N  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
SEQRES   1 O  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 O  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 O  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 O  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 O  259  ASN PHE ILE GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 O  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 O  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 O  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 O  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 O  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 O  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 O  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 O  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 O  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 O  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 O  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 O  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 O  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 O  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 O  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
SEQRES   1 P  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 P  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 P  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 P  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 P  259  ASN PHE ILE GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 P  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 P  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 P  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 P  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 P  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 P  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 P  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 P  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 P  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 P  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 P  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 P  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 P  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 P  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 P  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
MODRES 1DX5 ASN M   60G ASN  GLYCOSYLATION SITE                                 
MODRES 1DX5 ASN N   60G ASN  GLYCOSYLATION SITE                                 
MODRES 1DX5 ASN O   60G ASN  GLYCOSYLATION SITE                                 
MODRES 1DX5 ASN P   60G ASN  GLYCOSYLATION SITE                                 
HET    FMT  I 501       3                                                       
HET     CA  I 502       1                                                       
HET     NA  I 503       1                                                       
HET    FMT  J 501       3                                                       
HET     CA  J 502       1                                                       
HET     NA  J 503       1                                                       
HET    FMT  K 501       3                                                       
HET     CA  K 502       1                                                       
HET     NA  K 503       1                                                       
HET    FMT  L 501       3                                                       
HET     CA  L 502       1                                                       
HET     NA  L 503       1                                                       
HET    NAG  M 301      14                                                       
HET     NA  M 302       1                                                       
HET    0GJ  M 303       9                                                       
HET    0GJ  M 304       4                                                       
HET    0GJ  M 305      11                                                       
HET    0GJ  M 306       1                                                       
HET    NAG  N 301      14                                                       
HET     NA  N 302       1                                                       
HET    0GJ  N 303       9                                                       
HET    0GJ  N 304       4                                                       
HET    0GJ  N 305      11                                                       
HET    0GJ  N 306       1                                                       
HET    NAG  O 301      14                                                       
HET     NA  O 302       1                                                       
HET    0GJ  O 303       9                                                       
HET    0GJ  O 304       4                                                       
HET    0GJ  O 305      11                                                       
HET    0GJ  O 306       1                                                       
HET    NAG  P 301      14                                                       
HET     NA  P 302       1                                                       
HET    FMT  P 303       3                                                       
HET    0GJ  P 304       9                                                       
HET    0GJ  P 305       4                                                       
HET    0GJ  P 306      11                                                       
HET    0GJ  P 307       1                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
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                                  
FORMUL  13  FMT    5(C H2 O2)                                                   
FORMUL  14   CA    4(CA 2+)                                                     
FORMUL  15   NA    8(NA 1+)                                                     
FORMUL  25  NAG    4(C8 H15 N O6)                                               
FORMUL  27  0GJ    16(C14 H28 CL N6 O5 1+)                                      
FORMUL  50  HOH   *815(H2 O)                                                    
HELIX    1 AA1 PHE A    7  SER A   11  5                                   5    
HELIX    2 AA2 THR A   14B TYR A   14J 1                                   9    
HELIX    3 AA3 PHE B    7  SER B   11  5                                   5    
HELIX    4 AA4 THR B   14B SER B   14I 1                                   8    
HELIX    5 AA5 PHE C    7  SER C   11  5                                   5    
HELIX    6 AA6 THR C   14B SER C   14I 1                                   8    
HELIX    7 AA7 PHE D    7  SER D   11  5                                   5    
HELIX    8 AA8 THR D   14B TYR D   14J 1                                   9    
HELIX    9 AA9 ASP I  349  ALA I  354  5                                   6    
HELIX   10 AB1 ASP I  425  GLY I  430  1                                   6    
HELIX   11 AB2 ASP J  349  ALA J  354  5                                   6    
HELIX   12 AB3 ASP J  425  GLY J  430  1                                   6    
HELIX   13 AB4 ASP K  349  ALA K  354  5                                   6    
HELIX   14 AB5 ASP K  425  GLY K  430  1                                   6    
HELIX   15 AB6 ASP L  349  ALA L  354  5                                   6    
HELIX   16 AB7 ASP L  425  GLY L  430  1                                   6    
HELIX   17 AB8 ALA M   55  CYS M   58  5                                   4    
HELIX   18 AB9 PRO M   60B ASP M   60E 5                                   4    
HELIX   19 AC1 ILE M   60I ASN M   62  5                                   3    
HELIX   20 AC2 ASP M  125  LEU M  130  1                                   9    
HELIX   21 AC3 GLU M  164  SER M  171  1                                   8    
HELIX   22 AC4 LYS M  185  GLY M  186C 5                                   5    
HELIX   23 AC5 LEU M  234  PHE M  245  1                                  12    
HELIX   24 AC6 ALA N   55  CYS N   58  5                                   4    
HELIX   25 AC7 PRO N   60B ASP N   60E 5                                   4    
HELIX   26 AC8 ILE N   60I ASN N   62  5                                   3    
HELIX   27 AC9 ASP N  125  LEU N  130  1                                   9    
HELIX   28 AD1 GLU N  164  SER N  171  1                                   8    
HELIX   29 AD2 LYS N  185  GLY N  186C 5                                   5    
HELIX   30 AD3 LEU N  234  PHE N  245  1                                  12    
HELIX   31 AD4 ALA O   55  CYS O   58  5                                   4    
HELIX   32 AD5 PRO O   60B ASP O   60E 5                                   4    
HELIX   33 AD6 ILE O   60I ASN O   62  5                                   3    
HELIX   34 AD7 ASP O  125  LEU O  130  1                                   9    
HELIX   35 AD8 GLU O  164  SER O  171  1                                   8    
HELIX   36 AD9 LYS O  185  GLY O  186C 5                                   5    
HELIX   37 AE1 LEU O  234  PHE O  245  1                                  12    
HELIX   38 AE2 ALA P   55  CYS P   58  5                                   4    
HELIX   39 AE3 PRO P   60B ASP P   60E 5                                   4    
HELIX   40 AE4 ILE P   60I ASN P   62  5                                   3    
HELIX   41 AE5 ASP P  125  LEU P  130  1                                   9    
HELIX   42 AE6 GLU P  164  SER P  171  1                                   8    
HELIX   43 AE7 LYS P  185  GLY P  186C 5                                   5    
HELIX   44 AE8 VAL P  231  PHE P  245  1                                  15    
SHEET    1 AA1 2 GLN I 359  PRO I 362  0                                        
SHEET    2 AA1 2 TYR I 368  VAL I 371 -1  O  LEU I 369   N  GLN I 361           
SHEET    1 AA2 2 PHE I 376  ILE I 379  0                                        
SHEET    2 AA2 2 GLU I 382  MET I 388 -1  O  GLN I 387   N  ALA I 377           
SHEET    1 AA3 3 ALA I 394  PRO I 396  0                                        
SHEET    2 AA3 3 ILE I 420  ASP I 423 -1  O  CYS I 421   N  CYS I 395           
SHEET    3 AA3 3 TYR I 413  ASP I 416 -1  N  ILE I 414   O  THR I 422           
SHEET    1 AA4 2 ASP I 398  CYS I 399  0                                        
SHEET    2 AA4 2 CYS I 407  GLU I 408 -1  O  GLU I 408   N  ASP I 398           
SHEET    1 AA5 3 VAL I 436  ASN I 439  0                                        
SHEET    2 AA5 3 PHE I 444  CYS I 448 -1  O  GLU I 445   N  HIS I 438           
SHEET    3 AA5 3 ALA I 455  ILE I 458 -1  O  GLN I 457   N  CYS I 446           
SHEET    1 AA6 2 GLN J 359  PRO J 362  0                                        
SHEET    2 AA6 2 TYR J 368  VAL J 371 -1  O  LEU J 369   N  GLN J 361           
SHEET    1 AA7 2 PHE J 376  ILE J 379  0                                        
SHEET    2 AA7 2 GLU J 382  MET J 388 -1  O  GLN J 387   N  ALA J 377           
SHEET    1 AA8 3 ALA J 394  PRO J 396  0                                        
SHEET    2 AA8 3 ILE J 420  ASP J 423 -1  O  CYS J 421   N  CYS J 395           
SHEET    3 AA8 3 TYR J 413  ASP J 416 -1  N  ASP J 416   O  ILE J 420           
SHEET    1 AA9 2 ASP J 398  CYS J 399  0                                        
SHEET    2 AA9 2 CYS J 407  GLU J 408 -1  O  GLU J 408   N  ASP J 398           
SHEET    1 AB1 3 VAL J 436  ASN J 439  0                                        
SHEET    2 AB1 3 PHE J 444  ILE J 447 -1  O  ILE J 447   N  VAL J 436           
SHEET    3 AB1 3 GLY J 456  ILE J 458 -1  O  GLN J 457   N  CYS J 446           
SHEET    1 AB2 2 GLN K 359  PRO K 362  0                                        
SHEET    2 AB2 2 TYR K 368  VAL K 371 -1  O  VAL K 371   N  GLN K 359           
SHEET    1 AB3 2 PHE K 376  ILE K 379  0                                        
SHEET    2 AB3 2 GLU K 382  MET K 388 -1  O  GLN K 387   N  ALA K 377           
SHEET    1 AB4 3 ALA K 394  PRO K 396  0                                        
SHEET    2 AB4 3 ILE K 420  ASP K 423 -1  O  CYS K 421   N  CYS K 395           
SHEET    3 AB4 3 TYR K 413  ASP K 416 -1  N  ILE K 414   O  THR K 422           
SHEET    1 AB5 2 ASP K 398  ASP K 400  0                                        
SHEET    2 AB5 2 SER K 406  GLU K 408 -1  O  GLU K 408   N  ASP K 398           
SHEET    1 AB6 3 VAL K 436  ASN K 439  0                                        
SHEET    2 AB6 3 PHE K 444  ILE K 447 -1  O  GLU K 445   N  HIS K 438           
SHEET    3 AB6 3 GLY K 456  ILE K 458 -1  O  GLN K 457   N  CYS K 446           
SHEET    1 AB7 2 GLN L 359  PRO L 362  0                                        
SHEET    2 AB7 2 TYR L 368  VAL L 371 -1  O  LEU L 369   N  GLN L 361           
SHEET    1 AB8 2 PHE L 376  ILE L 379  0                                        
SHEET    2 AB8 2 GLU L 382  MET L 388 -1  O  GLN L 387   N  ALA L 377           
SHEET    1 AB9 3 ALA L 394  PRO L 396  0                                        
SHEET    2 AB9 3 ILE L 420  ASP L 423 -1  O  CYS L 421   N  CYS L 395           
SHEET    3 AB9 3 TYR L 413  ASP L 416 -1  N  ASP L 416   O  ILE L 420           
SHEET    1 AC1 2 ASP L 398  ASP L 400  0                                        
SHEET    2 AC1 2 SER L 406  GLU L 408 -1  O  SER L 406   N  ASP L 400           
SHEET    1 AC2 3 VAL L 436  ASN L 439  0                                        
SHEET    2 AC2 3 PHE L 444  ILE L 447 -1  O  GLU L 445   N  HIS L 438           
SHEET    3 AC2 3 GLN L 457  ILE L 458 -1  O  GLN L 457   N  CYS L 446           
SHEET    1 AC3 7 SER M  20  ASP M  21  0                                        
SHEET    2 AC3 7 GLN M 156  PRO M 161 -1  O  VAL M 157   N  SER M  20           
SHEET    3 AC3 7 LYS M 135  GLY M 140 -1  N  GLY M 136   O  LEU M 160           
SHEET    4 AC3 7 PRO M 198  LYS M 202 -1  O  VAL M 200   N  ARG M 137           
SHEET    5 AC3 7 TRP M 207  TRP M 215 -1  O  TYR M 208   N  MET M 201           
SHEET    6 AC3 7 GLY M 226  HIS M 230 -1  O  PHE M 227   N  TRP M 215           
SHEET    7 AC3 7 MET M 180  ALA M 183 -1  N  PHE M 181   O  TYR M 228           
SHEET    1 AC4 7 LYS M  81  SER M  83  0                                        
SHEET    2 AC4 7 LEU M  64  ILE M  68 -1  N  ILE M  68   O  LYS M  81           
SHEET    3 AC4 7 GLN M  30  ARG M  35 -1  N  PHE M  34   O  LEU M  65           
SHEET    4 AC4 7 GLU M  39  LEU M  46 -1  O  CYS M  42   N  LEU M  33           
SHEET    5 AC4 7 TRP M  51  THR M  54 -1  O  LEU M  53   N  SER M  45           
SHEET    6 AC4 7 ALA M 104  LEU M 108 -1  O  ALA M 104   N  THR M  54           
SHEET    7 AC4 7 LEU M  85  ILE M  90 -1  N  TYR M  89   O  LEU M 105           
SHEET    1 AC5 2 LEU M  60  TYR M  60A 0                                        
SHEET    2 AC5 2 LYS M  60F ASN M  60G-1  O  LYS M  60F  N  TYR M  60A          
SHEET    1 AC6 7 SER N  20  ASP N  21  0                                        
SHEET    2 AC6 7 GLN N 156  PRO N 161 -1  O  VAL N 157   N  SER N  20           
SHEET    3 AC6 7 LYS N 135  GLY N 140 -1  N  GLY N 136   O  LEU N 160           
SHEET    4 AC6 7 PRO N 198  LYS N 202 -1  O  VAL N 200   N  ARG N 137           
SHEET    5 AC6 7 TRP N 207  TRP N 215 -1  O  TYR N 208   N  MET N 201           
SHEET    6 AC6 7 GLY N 226  HIS N 230 -1  O  PHE N 227   N  TRP N 215           
SHEET    7 AC6 7 MET N 180  ALA N 183 -1  N  PHE N 181   O  TYR N 228           
SHEET    1 AC7 7 LYS N  81  SER N  83  0                                        
SHEET    2 AC7 7 LEU N  64  ILE N  68 -1  N  ILE N  68   O  LYS N  81           
SHEET    3 AC7 7 GLN N  30  ARG N  35 -1  N  PHE N  34   O  LEU N  65           
SHEET    4 AC7 7 GLU N  39  LEU N  46 -1  O  CYS N  42   N  LEU N  33           
SHEET    5 AC7 7 TRP N  51  THR N  54 -1  O  LEU N  53   N  SER N  45           
SHEET    6 AC7 7 ALA N 104  LEU N 108 -1  O  MET N 106   N  VAL N  52           
SHEET    7 AC7 7 LEU N  85  ILE N  90 -1  N  TYR N  89   O  LEU N 105           
SHEET    1 AC8 2 LEU N  60  TYR N  60A 0                                        
SHEET    2 AC8 2 LYS N  60F ASN N  60G-1  O  LYS N  60F  N  TYR N  60A          
SHEET    1 AC9 7 SER O  20  ASP O  21  0                                        
SHEET    2 AC9 7 GLN O 156  PRO O 161 -1  O  VAL O 157   N  SER O  20           
SHEET    3 AC9 7 LYS O 135  GLY O 140 -1  N  GLY O 136   O  LEU O 160           
SHEET    4 AC9 7 PRO O 198  LYS O 202 -1  O  VAL O 200   N  ARG O 137           
SHEET    5 AC9 7 TRP O 207  TRP O 215 -1  O  GLY O 211   N  PHE O 199           
SHEET    6 AC9 7 GLY O 226  HIS O 230 -1  O  PHE O 227   N  TRP O 215           
SHEET    7 AC9 7 MET O 180  ALA O 183 -1  N  PHE O 181   O  TYR O 228           
SHEET    1 AD1 7 LYS O  81  SER O  83  0                                        
SHEET    2 AD1 7 LEU O  64  ILE O  68 -1  N  ILE O  68   O  LYS O  81           
SHEET    3 AD1 7 GLN O  30  ARG O  35 -1  N  PHE O  34   O  LEU O  65           
SHEET    4 AD1 7 GLU O  39  LEU O  46 -1  O  CYS O  42   N  LEU O  33           
SHEET    5 AD1 7 TRP O  51  THR O  54 -1  O  LEU O  53   N  SER O  45           
SHEET    6 AD1 7 ALA O 104  LEU O 108 -1  O  ALA O 104   N  THR O  54           
SHEET    7 AD1 7 LEU O  85  ILE O  90 -1  N  TYR O  89   O  LEU O 105           
SHEET    1 AD2 2 LEU O  60  TYR O  60A 0                                        
SHEET    2 AD2 2 LYS O  60F ASN O  60G-1  O  LYS O  60F  N  TYR O  60A          
SHEET    1 AD3 7 SER P  20  ASP P  21  0                                        
SHEET    2 AD3 7 GLN P 156  PRO P 161 -1  O  VAL P 157   N  SER P  20           
SHEET    3 AD3 7 LYS P 135  GLY P 140 -1  N  GLY P 136   O  LEU P 160           
SHEET    4 AD3 7 PRO P 198  LYS P 202 -1  O  VAL P 200   N  ARG P 137           
SHEET    5 AD3 7 TRP P 207  TRP P 215 -1  O  TYR P 208   N  MET P 201           
SHEET    6 AD3 7 GLY P 226  HIS P 230 -1  O  PHE P 227   N  TRP P 215           
SHEET    7 AD3 7 MET P 180  ALA P 183 -1  N  PHE P 181   O  TYR P 228           
SHEET    1 AD4 7 LYS P  81  SER P  83  0                                        
SHEET    2 AD4 7 LEU P  64  ILE P  68 -1  N  ILE P  68   O  LYS P  81           
SHEET    3 AD4 7 GLN P  30  ARG P  35 -1  N  PHE P  34   O  LEU P  65           
SHEET    4 AD4 7 GLU P  39  LEU P  46 -1  O  ALA P  44   N  VAL P  31           
SHEET    5 AD4 7 TRP P  51  THR P  54 -1  O  LEU P  53   N  SER P  45           
SHEET    6 AD4 7 ALA P 104  LEU P 108 -1  O  ALA P 104   N  THR P  54           
SHEET    7 AD4 7 LEU P  85  ILE P  90 -1  N  TYR P  89   O  LEU P 105           
SHEET    1 AD5 2 LEU P  60  TYR P  60A 0                                        
SHEET    2 AD5 2 LYS P  60F ASN P  60G-1  O  LYS P  60F  N  TYR P  60A          
SSBOND   1 CYS A    1    CYS M  122                          1555   1555  2.04  
SSBOND   2 CYS B    1    CYS N  122                          1555   1555  2.03  
SSBOND   3 CYS C    1    CYS O  122                          1555   1555  2.04  
SSBOND   4 CYS D    1    CYS P  122                          1555   1555  2.04  
SSBOND   5 CYS I  351    CYS I  360                          1555   1555  2.04  
SSBOND   6 CYS I  356    CYS I  370                          1555   1555  2.03  
SSBOND   7 CYS I  372    CYS I  386                          1555   1555  2.04  
SSBOND   8 CYS I  390    CYS I  395                          1555   1555  2.03  
SSBOND   9 CYS I  399    CYS I  407                          1555   1555  2.03  
SSBOND  10 CYS I  409    CYS I  421                          1555   1555  2.04  
SSBOND  11 CYS I  427    CYS I  437                          1555   1555  2.03  
SSBOND  12 CYS I  433    CYS I  446                          1555   1555  2.03  
SSBOND  13 CYS I  448    CYS I  462                          1555   1555  2.03  
SSBOND  14 CYS J  351    CYS J  360                          1555   1555  2.04  
SSBOND  15 CYS J  356    CYS J  370                          1555   1555  2.03  
SSBOND  16 CYS J  372    CYS J  386                          1555   1555  2.05  
SSBOND  17 CYS J  390    CYS J  395                          1555   1555  2.03  
SSBOND  18 CYS J  399    CYS J  407                          1555   1555  2.04  
SSBOND  19 CYS J  409    CYS J  421                          1555   1555  2.04  
SSBOND  20 CYS J  427    CYS J  437                          1555   1555  2.03  
SSBOND  21 CYS J  433    CYS J  446                          1555   1555  2.03  
SSBOND  22 CYS J  448    CYS J  462                          1555   1555  2.03  
SSBOND  23 CYS K  351    CYS K  360                          1555   1555  2.04  
SSBOND  24 CYS K  356    CYS K  370                          1555   1555  2.03  
SSBOND  25 CYS K  372    CYS K  386                          1555   1555  2.04  
SSBOND  26 CYS K  390    CYS K  395                          1555   1555  2.03  
SSBOND  27 CYS K  399    CYS K  407                          1555   1555  2.03  
SSBOND  28 CYS K  409    CYS K  421                          1555   1555  2.03  
SSBOND  29 CYS K  427    CYS K  437                          1555   1555  2.03  
SSBOND  30 CYS K  433    CYS K  446                          1555   1555  2.03  
SSBOND  31 CYS K  448    CYS K  462                          1555   1555  2.03  
SSBOND  32 CYS L  351    CYS L  360                          1555   1555  2.04  
SSBOND  33 CYS L  356    CYS L  370                          1555   1555  2.02  
SSBOND  34 CYS L  372    CYS L  386                          1555   1555  2.04  
SSBOND  35 CYS L  390    CYS L  395                          1555   1555  2.02  
SSBOND  36 CYS L  399    CYS L  407                          1555   1555  2.04  
SSBOND  37 CYS L  409    CYS L  421                          1555   1555  2.03  
SSBOND  38 CYS L  427    CYS L  437                          1555   1555  2.03  
SSBOND  39 CYS L  433    CYS L  446                          1555   1555  2.03  
SSBOND  40 CYS L  448    CYS L  462                          1555   1555  2.03  
SSBOND  41 CYS M   42    CYS M   58                          1555   1555  2.04  
SSBOND  42 CYS M  168    CYS M  182                          1555   1555  2.03  
SSBOND  43 CYS M  191    CYS M  220                          1555   1555  2.03  
SSBOND  44 CYS N   42    CYS N   58                          1555   1555  2.04  
SSBOND  45 CYS N  168    CYS N  182                          1555   1555  2.03  
SSBOND  46 CYS N  191    CYS N  220                          1555   1555  2.04  
SSBOND  47 CYS O   42    CYS O   58                          1555   1555  2.04  
SSBOND  48 CYS O  168    CYS O  182                          1555   1555  2.03  
SSBOND  49 CYS O  191    CYS O  220                          1555   1555  2.04  
SSBOND  50 CYS P   42    CYS P   58                          1555   1555  2.04  
SSBOND  51 CYS P  168    CYS P  182                          1555   1555  2.03  
SSBOND  52 CYS P  191    CYS P  220                          1555   1555  2.04  
LINK         NE2 HIS M  57                 C3  0GJ M 306     1555   1555  1.46  
LINK         ND2 ASN M  60G                C1  NAG M 301     1555   1555  1.58  
LINK         OG  SER M 195                 C2  0GJ M 305     1555   1555  1.35  
LINK         C   0GJ M 303                 N1  0GJ M 304     1555   1555  1.33  
LINK         C1  0GJ M 304                 N2  0GJ M 305     1555   1555  1.33  
LINK         C2  0GJ M 305                 C3  0GJ M 306     1555   1555  1.62  
LINK         NE2 HIS N  57                 C3  0GJ N 306     1555   1555  1.47  
LINK         ND2 ASN N  60G                C1  NAG N 301     1555   1555  1.57  
LINK         OG  SER N 195                 C2  0GJ N 305     1555   1555  1.35  
LINK         C   0GJ N 303                 N1  0GJ N 304     1555   1555  1.33  
LINK         C1  0GJ N 304                 N2  0GJ N 305     1555   1555  1.33  
LINK         C2  0GJ N 305                 C3  0GJ N 306     1555   1555  1.62  
LINK         NE2 HIS O  57                 C3  0GJ O 306     1555   1555  1.46  
LINK         ND2 ASN O  60G                C1  NAG O 301     1555   1555  1.58  
LINK         OG  SER O 195                 C2  0GJ O 305     1555   1555  1.35  
LINK         C   0GJ O 303                 N1  0GJ O 304     1555   1555  1.33  
LINK         C1  0GJ O 304                 N2  0GJ O 305     1555   1555  1.34  
LINK         C2  0GJ O 305                 C3  0GJ O 306     1555   1555  1.63  
LINK         NE2 HIS P  57                 C3  0GJ P 307     1555   1555  1.47  
LINK         ND2 ASN P  60G                C1  NAG P 301     1555   1555  1.58  
LINK         OG  SER P 195                 C2  0GJ P 306     1555   1555  1.35  
LINK         C   0GJ P 304                 N1  0GJ P 305     1555   1555  1.33  
LINK         C1  0GJ P 305                 N2  0GJ P 306     1555   1555  1.33  
LINK         C2  0GJ P 306                 C3  0GJ P 307     1555   1555  1.62  
LINK         OD1 ASP I 423                CA    CA I 502     1555   1555  2.40  
LINK         OD2 ASP I 423                CA    CA I 502     1555   1555  2.87  
LINK         O   ILE I 424                CA    CA I 502     1555   1555  2.38  
LINK         OE1 GLU I 426                CA    CA I 502     1555   1555  2.50  
LINK         OD1 ASN I 439                CA    CA I 502     1555   1555  2.42  
LINK         O   LEU I 440                CA    CA I 502     1555   1555  2.40  
LINK         O   THR I 443                CA    CA I 502     1555   1555  2.76  
LINK         O1  FMT I 501                NA    NA I 503     1555   1555  2.87  
LINK         O2  FMT I 501                NA    NA I 503     1555   1555  2.96  
LINK        CA    CA I 502                 O   HOH I 609     1555   1555  2.42  
LINK         OD1 ASP J 423                CA    CA J 502     1555   1555  2.40  
LINK         OD2 ASP J 423                CA    CA J 502     1555   1555  2.71  
LINK         O   ILE J 424                CA    CA J 502     1555   1555  2.31  
LINK         OE1 GLU J 426                CA    CA J 502     1555   1555  2.49  
LINK         OD1 ASN J 439                CA    CA J 502     1555   1555  2.44  
LINK         O   LEU J 440                CA    CA J 502     1555   1555  2.37  
LINK         O   THR J 443                CA    CA J 502     1555   1555  2.80  
LINK         O1  FMT J 501                NA    NA J 503     1555   1555  3.04  
LINK         O2  FMT J 501                NA    NA J 503     1555   1555  2.85  
LINK        CA    CA J 502                 O   HOH J 609     1555   1555  2.47  
LINK         OD1 ASP K 423                CA    CA K 502     1555   1555  2.29  
LINK         OD2 ASP K 423                CA    CA K 502     1555   1555  2.84  
LINK         O   ILE K 424                CA    CA K 502     1555   1555  2.41  
LINK         OE1 GLU K 426                CA    CA K 502     1555   1555  2.43  
LINK         OD1 ASN K 439                CA    CA K 502     1555   1555  2.44  
LINK         O   LEU K 440                CA    CA K 502     1555   1555  2.46  
LINK         O   THR K 443                CA    CA K 502     1555   1555  2.77  
LINK         O1  FMT K 501                NA    NA K 503     1555   1555  2.80  
LINK         O2  FMT K 501                NA    NA K 503     1555   1555  2.79  
LINK        CA    CA K 502                 O   HOH K 604     1555   1555  2.58  
LINK         OD1 ASP L 423                CA    CA L 502     1555   1555  2.46  
LINK         OD2 ASP L 423                CA    CA L 502     1555   1555  2.78  
LINK         O   ILE L 424                CA    CA L 502     1555   1555  2.42  
LINK         OE1 GLU L 426                CA    CA L 502     1555   1555  2.48  
LINK         OD1 ASN L 439                CA    CA L 502     1555   1555  2.45  
LINK         O   LEU L 440                CA    CA L 502     1555   1555  2.43  
LINK         O   THR L 443                CA    CA L 502     1555   1555  2.72  
LINK         O1  FMT L 501                NA    NA L 503     1555   1555  2.78  
LINK         O2  FMT L 501                NA    NA L 503     1555   1555  2.90  
LINK        CA    CA L 502                 O   HOH L 606     1555   1555  2.47  
LINK         OD1 ASP M 221                NA    NA M 302     1555   1555  2.67  
LINK        NA    NA M 302                 O   HOH M 444     1555   1555  3.14  
LINK        NA    NA M 302                 O   HOH M 446     1555   1555  2.83  
LINK         O   ARG N 221A               NA    NA N 302     1555   1555  2.25  
LINK         O   LYS N 224                NA    NA N 302     1555   1555  2.62  
LINK        NA    NA N 302                 O   HOH N 404     1555   1555  2.54  
LINK        NA    NA N 302                 O   HOH N 493     1555   1555  2.71  
LINK        NA    NA N 302                 O   HOH N 500     1555   1555  2.38  
LINK         O   ARG O 221A               NA    NA O 302     1555   1555  2.25  
LINK         O   LYS O 224                NA    NA O 302     1555   1555  2.56  
LINK        NA    NA O 302                 O   HOH O 435     1555   1555  2.50  
LINK        NA    NA O 302                 O   HOH O 436     1555   1555  2.55  
LINK        NA    NA O 302                 O   HOH O 478     1555   1555  2.68  
LINK        NA    NA O 302                 O   HOH O 491     1555   1555  2.44  
LINK         O   ARG P 221A               NA    NA P 302     1555   1555  2.33  
LINK         O   LYS P 224                NA    NA P 302     1555   1555  2.70  
LINK        NA    NA P 302                 O   HOH P 427     1555   1555  2.56  
LINK        NA    NA P 302                 O   HOH P 455     1555   1555  2.71  
LINK        NA    NA P 302                 O   HOH P 509     1555   1555  2.37  
CISPEP   1 GLU I  346    PRO I  347          0        -0.77                     
CISPEP   2 GLY I  449    PRO I  450          0        -0.68                     
CISPEP   3 GLY J  449    PRO J  450          0        -0.34                     
CISPEP   4 GLY L  449    PRO L  450          0        -0.99                     
CISPEP   5 SER M   36A   PRO M   37          0        -0.57                     
CISPEP   6 SER N   36A   PRO N   37          0        -0.75                     
CISPEP   7 SER O   36A   PRO O   37          0        -0.65                     
CISPEP   8 SER P   36A   PRO P   37          0        -0.59                     
CRYST1  214.400  214.400  131.410  90.00  90.00 120.00 H 3          36          
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      0.004664  0.002693  0.000000        0.00000                         
SCALE2      0.000000  0.005386  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007610        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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