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Database: PDB
Entry: 1F13
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Original site: 1F13 
HEADER    COAGULATION FACTOR                      16-JAN-98   1F13              
TITLE     RECOMBINANT HUMAN CELLULAR COAGULATION FACTOR XIII                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR COAGULATION FACTOR XIII ZYMOGEN;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: A2-HOMODIMER;                                              
COMPND   5 SYNONYM: CFXIII;                                                     
COMPND   6 EC: 2.3.2.13;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: PLACENTA;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    COAGULATION, TRANSGLUTAMINASE, TRANSFERASE, ACYLTRANSFERASE, BLOOD    
KEYWDS   2 COAGULATION, COAGULATION FACTOR                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.WEISS,R.HILGENFELD                                                
REVDAT   3   13-JUL-11 1F13    1       SHEET                                    
REVDAT   2   24-FEB-09 1F13    1       VERSN                                    
REVDAT   1   12-AUG-98 1F13    0                                                
JRNL        AUTH   M.S.WEISS,H.J.METZNER,R.HILGENFELD                           
JRNL        TITL   TWO NON-PROLINE CIS PEPTIDE BONDS MAY BE IMPORTANT FOR       
JRNL        TITL 2 FACTOR XIII FUNCTION.                                        
JRNL        REF    FEBS LETT.                    V. 423   291 1998              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   9515726                                                      
JRNL        DOI    10.1016/S0014-5793(98)00098-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   V.C.YEE,L.C.PEDERSEN,P.D.BISHOP,R.E.STENKAMP,D.C.TELLER      
REMARK   1  TITL   STRUCTURAL EVIDENCE THAT THE ACTIVATION PEPTIDE IS NOT       
REMARK   1  TITL 2 RELEASED UPON THROMBIN CLEAVAGE OF FACTOR XIII               
REMARK   1  REF    THROMB.RES.                   V.  78   389 1995              
REMARK   1  REFN                   ISSN 0049-3848                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,R.E.STENKAMP,     
REMARK   1  AUTH 2 D.C.TELLER                                                   
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN     
REMARK   1  TITL 2 BLOOD COAGULATION FACTOR XIII                                
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  91  7296 1994              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.HILGENFELD,A.LIESUM,R.STORM,H.J.METZNER,H.E.KARGES         
REMARK   1  TITL   CRYSTALLIZATION OF BLOOD COAGULATION FACTOR XIII BY AN       
REMARK   1  TITL 2 AUTOMATED PROCEDURE                                          
REMARK   1  REF    FEBS LETT.                    V. 265   110 1990              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000000.000                
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 89649                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1796                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 40.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4303                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 86                           
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            : 11556                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 487                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 40.00                           
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.56                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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 : RESTRAINTS                                              
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL INCLUDED               
REMARK   4                                                                      
REMARK   4 1F13 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.2-6.4                            
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.912                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89672                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1GGT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS CRYSTALLIZED FROM 1-2%   
REMARK 280  PEG 6000, 100 MM MES, PH 6.2-6.4                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.39000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THERE ARE TWO CHAINS IN THE ASYMMETRIC UNIT WITH CHAIN       
REMARK 300 IDENTIFIERS A AND B.  DISORDERED REGIONS INCLUDE RESIDUES            
REMARK 300 1 - 4, 37 - 38, 729 - 731 OF CHAIN A AND RESIDUES 1 - 5,             
REMARK 300 37 - 40, 729 - 731 OF CHAIN B.  POORLY ORDERED REGIONS ARE           
REMARK 300 RESIDUES 5 - 6 OF CHAIN A AND 6 OF CHAIN B, RESIDUES                 
REMARK 300 35 - 36, 39, 510 - 516 OF CHAIN A AND 35 - 36, AND                   
REMARK 300 510 - 516 OF CHAIN B.                                                
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     PRO A   729                                                      
REMARK 465     SER A   730                                                      
REMARK 465     MET A   731                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     PRO B   729                                                      
REMARK 465     SER B   730                                                      
REMARK 465     MET B   731                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A  36    O                                                   
REMARK 470     PRO B  36    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 535   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    LEU B 535   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A   6     -110.39    -74.88                                   
REMARK 500    ALA A   7      -47.32    171.04                                   
REMARK 500    PHE A   8      136.04      7.57                                   
REMARK 500    VAL A  35      -93.92    -95.33                                   
REMARK 500    GLU A 138      108.48   -163.88                                   
REMARK 500    ASP A 139     -130.00     67.36                                   
REMARK 500    VAL A 205      -55.37   -126.06                                   
REMARK 500    TYR A 214     -148.51   -138.66                                   
REMARK 500    ASP A 219       72.08   -158.89                                   
REMARK 500    ASP A 270     -123.39     70.03                                   
REMARK 500    ASN A 281       -2.34     65.66                                   
REMARK 500    ILE A 282      -62.39   -108.16                                   
REMARK 500    PHE A 339       83.13     64.53                                   
REMARK 500    ASP A 345       27.68     49.12                                   
REMARK 500    ASN A 402     -165.39   -126.79                                   
REMARK 500    VAL A 511       22.67    -76.42                                   
REMARK 500    MET A 512        4.95    -69.17                                   
REMARK 500    LYS A 513       30.71    -71.71                                   
REMARK 500    SER A 514       33.68    -71.53                                   
REMARK 500    ASN A 545      154.42    175.22                                   
REMARK 500    LEU A 580       25.01     49.69                                   
REMARK 500    GLN A 601       -3.39     91.72                                   
REMARK 500    ALA A 602       56.25     39.27                                   
REMARK 500    GLU A 614      -72.05    -67.74                                   
REMARK 500    GLN A 640       61.46     69.15                                   
REMARK 500    VAL A 672      -45.67   -131.35                                   
REMARK 500    SER A 713      -72.90   -121.97                                   
REMARK 500    ALA B   7      129.81     93.59                                   
REMARK 500    GLU B  30       73.88   -109.02                                   
REMARK 500    VAL B  35       61.34     15.86                                   
REMARK 500    GLN B  42      -53.33     67.60                                   
REMARK 500    ARG B  96      -18.38     92.38                                   
REMARK 500    ASP B 139     -123.10     61.54                                   
REMARK 500    ASP B 196       22.82    -76.56                                   
REMARK 500    VAL B 205      -50.21   -128.33                                   
REMARK 500    TYR B 214     -147.29   -136.45                                   
REMARK 500    ASP B 219       73.83   -158.76                                   
REMARK 500    ASP B 270     -135.00     66.45                                   
REMARK 500    PHE B 339       75.59     69.62                                   
REMARK 500    THR B 365       89.61    -69.34                                   
REMARK 500    ASN B 402     -166.78   -115.78                                   
REMARK 500    MET B 512       -2.86     63.18                                   
REMARK 500    LYS B 513       67.24   -100.00                                   
REMARK 500    GLN B 601       -5.82     89.84                                   
REMARK 500    GLU B 614      -74.23    -61.70                                   
REMARK 500    GLN B 640       64.41     74.53                                   
REMARK 500    LYS B 657       31.22    -83.74                                   
REMARK 500    SER B 713      -85.62   -118.15                                   
REMARK 500    HIS B 716       43.06     77.96                                   
REMARK 500    ARG B 727     -155.17    -80.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  35        23.8      L          L   OUTSIDE RANGE           
REMARK 500    CYS A 314        23.9      L          L   OUTSIDE RANGE           
REMARK 500    CYS B 314        23.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2174        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH B2220        DISTANCE =  6.24 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CT1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD OF SUBUNIT 1 COMPRISING THE        
REMARK 800  ACTIVE SITE.                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CT2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD OF SUBUNIT 2 COMPRISING THE        
REMARK 800  ACTIVE SITE.                                                        
DBREF  1F13 A    1   731  UNP    P00488   F13A_HUMAN       1    731             
DBREF  1F13 B    1   731  UNP    P00488   F13A_HUMAN       1    731             
SEQADV 1F13 GLU A  651  UNP  P00488    GLN   651 CONFLICT                       
SEQADV 1F13 GLU B  651  UNP  P00488    GLN   651 CONFLICT                       
SEQRES   1 A  731  SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA          
SEQRES   2 A  731  VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU          
SEQRES   3 A  731  PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL          
SEQRES   4 A  731  ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU          
SEQRES   5 A  731  PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS          
SEQRES   6 A  731  THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG          
SEQRES   7 A  731  GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO          
SEQRES   8 A  731  TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL          
SEQRES   9 A  731  ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE          
SEQRES  10 A  731  PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP          
SEQRES  11 A  731  GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG          
SEQRES  12 A  731  LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS          
SEQRES  13 A  731  PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL          
SEQRES  14 A  731  LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE          
SEQRES  15 A  731  LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU          
SEQRES  16 A  731  ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP          
SEQRES  17 A  731  ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS          
SEQRES  18 A  731  THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE          
SEQRES  19 A  731  LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET          
SEQRES  20 A  731  ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG          
SEQRES  21 A  731  VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY          
SEQRES  22 A  731  VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY          
SEQRES  23 A  731  VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU          
SEQRES  24 A  731  LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY          
SEQRES  25 A  731  GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU          
SEQRES  26 A  731  ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR          
SEQRES  27 A  731  PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP          
SEQRES  28 A  731  ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU          
SEQRES  29 A  731  THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU          
SEQRES  30 A  731  ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY          
SEQRES  31 A  731  GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER          
SEQRES  32 A  731  ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA          
SEQRES  33 A  731  ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO          
SEQRES  34 A  731  PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE          
SEQRES  35 A  731  THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL          
SEQRES  36 A  731  ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN          
SEQRES  37 A  731  ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR          
SEQRES  38 A  731  LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU          
SEQRES  39 A  731  GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN          
SEQRES  40 A  731  THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET          
SEQRES  41 A  731  ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE          
SEQRES  42 A  731  LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG          
SEQRES  43 A  731  TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE          
SEQRES  44 A  731  TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR          
SEQRES  45 A  731  PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU          
SEQRES  46 A  731  ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU          
SEQRES  47 A  731  LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG          
SEQRES  48 A  731  ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER          
SEQRES  49 A  731  THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG          
SEQRES  50 A  731  GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL          
SEQRES  51 A  731  GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL          
SEQRES  52 A  731  TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET          
SEQRES  53 A  731  LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL          
SEQRES  54 A  731  GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS          
SEQRES  55 A  731  ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG          
SEQRES  56 A  731  HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG          
SEQRES  57 A  731  PRO SER MET                                                  
SEQRES   1 B  731  SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA          
SEQRES   2 B  731  VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU          
SEQRES   3 B  731  PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL          
SEQRES   4 B  731  ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU          
SEQRES   5 B  731  PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS          
SEQRES   6 B  731  THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG          
SEQRES   7 B  731  GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO          
SEQRES   8 B  731  TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL          
SEQRES   9 B  731  ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE          
SEQRES  10 B  731  PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP          
SEQRES  11 B  731  GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG          
SEQRES  12 B  731  LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS          
SEQRES  13 B  731  PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL          
SEQRES  14 B  731  LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE          
SEQRES  15 B  731  LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU          
SEQRES  16 B  731  ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP          
SEQRES  17 B  731  ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS          
SEQRES  18 B  731  THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE          
SEQRES  19 B  731  LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET          
SEQRES  20 B  731  ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG          
SEQRES  21 B  731  VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY          
SEQRES  22 B  731  VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY          
SEQRES  23 B  731  VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU          
SEQRES  24 B  731  LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY          
SEQRES  25 B  731  GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU          
SEQRES  26 B  731  ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR          
SEQRES  27 B  731  PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP          
SEQRES  28 B  731  ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU          
SEQRES  29 B  731  THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU          
SEQRES  30 B  731  ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY          
SEQRES  31 B  731  GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER          
SEQRES  32 B  731  ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA          
SEQRES  33 B  731  ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO          
SEQRES  34 B  731  PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE          
SEQRES  35 B  731  THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL          
SEQRES  36 B  731  ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN          
SEQRES  37 B  731  ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR          
SEQRES  38 B  731  LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU          
SEQRES  39 B  731  GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN          
SEQRES  40 B  731  THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET          
SEQRES  41 B  731  ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE          
SEQRES  42 B  731  LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG          
SEQRES  43 B  731  TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE          
SEQRES  44 B  731  TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR          
SEQRES  45 B  731  PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU          
SEQRES  46 B  731  ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU          
SEQRES  47 B  731  LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG          
SEQRES  48 B  731  ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER          
SEQRES  49 B  731  THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG          
SEQRES  50 B  731  GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL          
SEQRES  51 B  731  GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL          
SEQRES  52 B  731  TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET          
SEQRES  53 B  731  LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL          
SEQRES  54 B  731  GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS          
SEQRES  55 B  731  ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG          
SEQRES  56 B  731  HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG          
SEQRES  57 B  731  PRO SER MET                                                  
FORMUL   3  HOH   *487(H2 O)                                                    
HELIX    1  H1 ASP A   58  HIS A   65  1                                   8    
HELIX    2  H2 ASN A  197  LEU A  206  1                                  10    
HELIX    3  H3 ILE A  234  GLN A  246  1                                  13    
HELIX    4  H4 ASN A  254  VAL A  266  1                                  13    
HELIX    5  H5 SER A  295  GLU A  306  1                                  12    
HELIX    6  H9 GLN A  313  GLY A  329  1                                  17    
HELIX    7  H0 VAL A  414  GLY A  420  1                                   7    
HELIX    8 H11 ASP A  427  SER A  437  1                                  11    
HELIX    9 H12 THR A  478  TYR A  481  1                                   4    
HELIX   10 H13 GLU A  488  TYR A  500  1                                  13    
HELIX   11 H14 ALA A  591  MET A  595  1                                   5    
HELIX   12 H1B ASP B   58  HIS B   65  1                                   8    
HELIX   13 H2B ASN B  197  LEU B  206  1                                  10    
HELIX   14 H3B ILE B  234  GLN B  246  1                                  13    
HELIX   15 H4B ASN B  254  VAL B  266  1                                  13    
HELIX   16 H5B SER B  295  GLU B  306  1                                  12    
HELIX   17 H9B GLN B  313  GLY B  329  1                                  17    
HELIX   18 B10 VAL B  414  GLY B  420  1                                   7    
HELIX   19 B11 ASP B  427  SER B  437  1                                  11    
HELIX   20 B12 THR B  478  TYR B  481  1                                   4    
HELIX   21 B13 GLU B  488  TYR B  500  1                                  13    
HELIX   22 B14 ALA B  591  MET B  595  1                                   5    
SHEET    1  A111 ASN A  46  HIS A  51  0                                        
SHEET    2  A111 PHE A  82  SER A  89 -1                                        
SHEET    3  A111 SER A 141  GLN A 147 -1                                        
SHEET    4  A111 GLY A 131  GLU A 138 -1                                        
SHEET    5  A111 THR A 115  VAL A 122  1                                        
SHEET    6  A111 LEU A  98  ILE A 105 -1                                        
SHEET    7  A111 GLY A 155  THR A 165 -1                                        
SHEET    8  A111 GLY A 168  THR A 172 -1                                        
SHEET    9  A111 THR A 180  LEU A 183 -1                                        
SHEET   10  A111 THR A  28  GLN A  32 -1                                        
SHEET   11  A111 LEU A  74  ARG A  77  1                                        
SHEET    1  A2 2 ASP A 208  GLU A 216  0                                        
SHEET    2  A2 2 ASP A 219  TYR A 227 -1                                        
SHEET    1  A3 6 GLY A 405  SER A 413  0                                        
SHEET    2  A3 6 GLY A 391  ASN A 402 -1                                        
SHEET    3  A3 6 TRP A 370  MET A 380 -1                                        
SHEET    4  A3 6 PRO A 331  SER A 340 -1                                        
SHEET    5  A3 6 LEU A 463  GLN A 468 -1                                        
SHEET    6  A3 6 GLY A 473  ILE A 477 -1                                        
SHEET    1  A4 3 LEU A 348  VAL A 455  0                                        
SHEET    2  A4 3 ASP A 438  LYS A 445  1                                        
SHEET    3  A4 3 THR A 449  ASP A 456 -1                                        
SHEET    1  A5 7 ASN A 517  VAL A 528  0                                        
SHEET    2  A5 7 PHE A 533  ASN A 542 -1                                        
SHEET    3  A5 7 SER A 581  GLN A 590 -1                                        
SHEET    4  A5 7 VAL A 563  GLU A 578 -1                                        
SHEET    5  A5 7 TYR A 547  PHE A 559 -1                                        
SHEET    6  A5 7 ALA A 602  ASN A 613 -1                                        
SHEET    7  A5 7 ARG A 616  THR A 628 -1                                        
SHEET    1  A6 7 ILE A 632  GLY A 638  0                                        
SHEET    2  A6 7 MET A 646  ASN A 654 -1                                        
SHEET    3  A6 7 SER A 687  CYS A 695 -1                                        
SHEET    4  A6 7 MET A 676  ARG A 684 -1                                        
SHEET    5  A6 7 LEU A 660  GLY A 669 -1                                        
SHEET    6  A6 7 GLY A 701  SER A 711 -1                                        
SHEET    7  A6 7 LEU A 714  GLN A 726 -1                                        
SHEET    1  B111 ASN B  46  HIS B  51  0                                        
SHEET    2  B111 PHE B  82  SER B  89 -1                                        
SHEET    3  B111 SER B 141  GLN B 147 -1                                        
SHEET    4  B111 GLY B 131  GLU B 138 -1                                        
SHEET    5  B111 THR B 115  VAL B 122  1                                        
SHEET    6  B111 LEU B  98  ILE B 105 -1                                        
SHEET    7  B111 GLY B 155  THR B 165 -1                                        
SHEET    8  B111 GLY B 168  THR B 172 -1                                        
SHEET    9  B111 THR B 180  LEU B 183 -1                                        
SHEET   10  B111 THR B  28  GLN B  32 -1                                        
SHEET   11  B111 LEU B  74  ARG B  77  1                                        
SHEET    1  B2 2 ASP B 208  GLU B 216  0                                        
SHEET    2  B2 2 ASP B 219  TYR B 227 -1                                        
SHEET    1  B3 6 GLY B 405  SER B 413  0                                        
SHEET    2  B3 6 GLY B 391  ASN B 402 -1                                        
SHEET    3  B3 6 TRP B 370  MET B 380 -1                                        
SHEET    4  B3 6 PRO B 331  SER B 340 -1                                        
SHEET    5  B3 6 LEU B 463  GLN B 468 -1                                        
SHEET    6  B3 6 GLY B 473  ILE B 477 -1                                        
SHEET    1  B4 3 LEU B 348  VAL B 455  0                                        
SHEET    2  B4 3 ASP B 438  LYS B 445  1                                        
SHEET    3  B4 3 THR B 449  ASP B 456 -1                                        
SHEET    1  B5 7 ASN B 517  VAL B 528  0                                        
SHEET    2  B5 7 PHE B 533  ASN B 542 -1                                        
SHEET    3  B5 7 SER B 581  GLN B 590 -1                                        
SHEET    4  B5 7 VAL B 563  GLU B 578 -1                                        
SHEET    5  B5 7 TYR B 547  PHE B 559 -1                                        
SHEET    6  B5 7 ALA B 602  ASN B 613 -1                                        
SHEET    7  B5 7 ARG B 616  THR B 628 -1                                        
SHEET    1  B6 7 ILE B 632  GLY B 638  0                                        
SHEET    2  B6 7 MET B 646  ASN B 654 -1                                        
SHEET    3  B6 7 SER B 687  CYS B 695 -1                                        
SHEET    4  B6 7 MET B 676  ARG B 684 -1                                        
SHEET    5  B6 7 LEU B 660  GLY B 669 -1                                        
SHEET    6  B6 7 GLY B 701  SER B 711 -1                                        
SHEET    7  B6 7 LEU B 714  GLN B 726 -1                                        
CISPEP   1 VAL A   35    PRO A   36          0        -0.16                     
CISPEP   2 ARG A  310    TYR A  311          0         0.20                     
CISPEP   3 GLY A  410    PRO A  411          0         0.42                     
CISPEP   4 GLN A  425    PHE A  426          0         0.36                     
CISPEP   5 VAL B   35    PRO B   36          0        -0.26                     
CISPEP   6 ARG B  310    TYR B  311          0         0.22                     
CISPEP   7 GLY B  410    PRO B  411          0         0.13                     
CISPEP   8 GLN B  425    PHE B  426          0         0.17                     
SITE     1 CT1  3 CYS A 314  HIS A 373  ASP A 396                               
SITE     1 CT2  3 CYS B 314  HIS B 373  ASP B 396                               
CRYST1  134.590   72.780  101.050  90.00 106.08  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007430  0.000000  0.002142        0.00000                         
SCALE2      0.000000  0.013740  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010299        0.00000                         
MTRIX1   1 -0.395373 -0.917773  0.037045       74.22790    1                    
MTRIX2   1 -0.917811  0.393162 -0.055189       51.85510    1                    
MTRIX3   1  0.036086 -0.055821 -0.997788       68.77750    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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