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Database: PDB
Entry: 1QRK
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Original site: 1QRK 
HEADER    TRANSFERASE                             14-JUN-99   1QRK              
TITLE     HUMAN FACTOR XIII WITH STRONTIUM BOUND IN THE ION SITE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (COAGULATION FACTOR XIII);                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: FULL LENGTH DIMER;                                         
COMPND   5 EC: 2.3.2.13;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: STRONTIUM BOUND IN THE ION SITE                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    TRANSGLUTAMINASE, BLOOD COAGULATION, CALCIUM, STRONTIUM,              
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.A.FOX,V.C.YEE,L.C.PEDERSON,I.LE TRONG,P.D.BISHOP,                   
AUTHOR   2 R.E.STENKAMP,D.C.TELLER                                              
REVDAT   3   24-FEB-09 1QRK    1       VERSN                                    
REVDAT   2   01-APR-03 1QRK    1       JRNL                                     
REVDAT   1   02-JUL-99 1QRK    0                                                
SPRSDE     02-JUL-99 1QRK      1BL2                                             
JRNL        AUTH   B.A.FOX,V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,          
JRNL        AUTH 2 R.E.STENKAMP,D.C.TELLER                                      
JRNL        TITL   IDENTIFICATION OF THE CALCIUM BINDING SITE AND A             
JRNL        TITL 2 NOVEL YTTERBIUM SITE IN BLOOD COAGULATION FACTOR             
JRNL        TITL 3 XIII BY X-RAY CRYSTALLOGRAPHY.                               
JRNL        REF    J.BIOL.CHEM.                  V. 274  4917 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9988734                                                      
JRNL        DOI    10.1074/JBC.274.8.4917                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50777                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOMLY PICKED 5% OF DATA      
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2558                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5598                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 279                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11260                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.50                            
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) : 2.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.550 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.420 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.620 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; 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  : PARAM19.ION                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.ION                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QRK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009183.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50777                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1FIE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1,2-PROPANEDIOL (24%) AND NAKPO4         
REMARK 280  (100MM) PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 25K      
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       36.16000            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     VAL A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     GLN A    42                                                      
REMARK 465     GLU A    43                                                      
REMARK 465     PHE A    44                                                      
REMARK 465     MET A   512                                                      
REMARK 465     LYS A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     ARG A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     ARG A   728                                                      
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     THR B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     THR B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     GLY B   510                                                      
REMARK 465     VAL B   511                                                      
REMARK 465     MET B   512                                                      
REMARK 465     LYS B   513                                                      
REMARK 465     SER B   514                                                      
REMARK 465     ARG B   515                                                      
REMARK 465     ARG B   728                                                      
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     GLU A  30    O                                                   
REMARK 470     VAL A 511    O                                                   
REMARK 470     ARG A 727    O                                                   
REMARK 470     VAL B  34    CG1  CG2                                            
REMARK 470     VAL B  35    O    CG1  CG2                                       
REMARK 470     LEU B  41    CG   CD1  CD2                                       
REMARK 470     ASN B 507    O                                                   
REMARK 470     ARG B 727    O                                                   
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  53       68.64   -104.47                                   
REMARK 500    LYS A  54      -75.74    -59.67                                   
REMARK 500    GLU A  55      117.07     -1.22                                   
REMARK 500    MET A 136      136.75    173.84                                   
REMARK 500    ASP A 139       80.23     13.70                                   
REMARK 500    GLU A 177        2.53    -66.42                                   
REMARK 500    ASN A 197      109.91   -170.45                                   
REMARK 500    TYR A 214     -152.32   -162.15                                   
REMARK 500    ARG A 223      136.20   -173.53                                   
REMARK 500    ALA A 268      101.96    -51.31                                   
REMARK 500    ASP A 270       80.43     65.97                                   
REMARK 500    GLU A 272      -74.13   -122.64                                   
REMARK 500    VAL A 274      -71.06    -75.62                                   
REMARK 500    SER A 278      129.43   -175.20                                   
REMARK 500    ASN A 281       11.38    -51.13                                   
REMARK 500    VAL A 296      -73.06    -42.95                                   
REMARK 500    PHE A 339       74.01     74.26                                   
REMARK 500    MET A 406       72.99     71.49                                   
REMARK 500    SER A 437      162.32    -47.01                                   
REMARK 500    ASP A 472       17.80    -67.90                                   
REMARK 500    GLU A 509     -100.83    -76.24                                   
REMARK 500    HIS A 544       42.23    -86.37                                   
REMARK 500    GLU A 571      115.42   -167.92                                   
REMARK 500    TYR A 594      -37.29   -135.62                                   
REMARK 500    GLU A 600      -50.02    -28.42                                   
REMARK 500    ASN A 613      -37.01    -31.03                                   
REMARK 500    LYS A 621      137.34   -172.22                                   
REMARK 500    SER A 713      -83.01   -125.74                                   
REMARK 500    PRO B  15      171.44    -56.76                                   
REMARK 500    LEU B  45      132.79    123.26                                   
REMARK 500    SER B  49      159.85    179.66                                   
REMARK 500    LEU B  52       63.50   -119.30                                   
REMARK 500    PHE B  53       70.08    -21.59                                   
REMARK 500    LYS B  54      -77.52    -84.59                                   
REMARK 500    GLU B  55      122.90      6.98                                   
REMARK 500    ARG B  56      -32.89    -32.14                                   
REMARK 500    ASP B  58      152.99    -49.64                                   
REMARK 500    ASN B  60      -73.75    -48.52                                   
REMARK 500    PRO B  91      136.76    -31.77                                   
REMARK 500    PRO B  94        7.80    -64.44                                   
REMARK 500    ARG B 100      148.51   -176.19                                   
REMARK 500    TYR B 108       66.13   -117.27                                   
REMARK 500    VAL B 119       87.59     55.65                                   
REMARK 500    MET B 136      135.70   -172.12                                   
REMARK 500    THR B 172      172.93    -59.43                                   
REMARK 500    VAL B 205      -53.75   -126.85                                   
REMARK 500    TYR B 214     -154.73   -134.20                                   
REMARK 500    ASP B 219       71.67    177.85                                   
REMARK 500    ARG B 252       13.80    -65.94                                   
REMARK 500    ALA B 268       93.36    -61.02                                   
REMARK 500    ASP B 270     -111.33     70.39                                   
REMARK 500    ASP B 271       46.03   -141.76                                   
REMARK 500    GLU B 272      -66.35   -103.15                                   
REMARK 500    ASN B 281       -4.13     68.83                                   
REMARK 500    ILE B 282      -60.02   -103.06                                   
REMARK 500    TYR B 283       63.93     66.20                                   
REMARK 500    ALA B 284      -71.28    -36.05                                   
REMARK 500    CYS B 314      -34.43    -38.11                                   
REMARK 500    PHE B 339       78.23     69.59                                   
REMARK 500    ALA B 346       -7.82     68.00                                   
REMARK 500    SER B 362      -19.68    -44.61                                   
REMARK 500    MET B 406       59.84     78.58                                   
REMARK 500    GLN B 487      143.92    -32.43                                   
REMARK 500    LYS B 504       70.74   -155.70                                   
REMARK 500    PRO B 505      -83.58    -46.28                                   
REMARK 500    ASP B 521      151.56    178.19                                   
REMARK 500    ARG B 540      135.40   -177.51                                   
REMARK 500    HIS B 544       50.12    -98.94                                   
REMARK 500    SER B 581     -153.24   -125.90                                   
REMARK 500    PHE B 582      142.79   -174.16                                   
REMARK 500    GLN B 597       44.20   -146.71                                   
REMARK 500    GLN B 601       -6.14     73.00                                   
REMARK 500    ILE B 612       66.86   -103.73                                   
REMARK 500    ASN B 613      -34.46    -25.67                                   
REMARK 500    VAL B 672      -35.41   -132.89                                   
REMARK 500    ARG B 703     -166.70   -112.00                                   
REMARK 500    SER B 713      -93.71    -92.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR B 732  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 457   O                                                      
REMARK 620 2 GLU B 485   OE1  81.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN A                         
REMARK 800 SITE_IDENTIFIER: CBT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN B                         
REMARK 800 SITE_IDENTIFIER: INA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE A STRONTIUM LIGANDS               
REMARK 800 SITE_IDENTIFIER: INB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE B STRONTIUM LIGANDS               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR A 732                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 732                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GGT   RELATED DB: PDB                                   
REMARK 900 FACTOR XIII - ZYMOGEN                                                
REMARK 900 RELATED ID: 1FIE   RELATED DB: PDB                                   
REMARK 900 FACTOR XIII - THROMBIN CLEAVED                                       
REMARK 900 RELATED ID: 1GGU   RELATED DB: PDB                                   
REMARK 900 FACTOR XIII - CALCIUM BOUND                                          
REMARK 900 RELATED ID: 1GGY   RELATED DB: PDB                                   
REMARK 900 FACTOR XIII - YTTERBIUM BOUND                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES NOT VISIBLE IN ELECTRON DENSITY MAPS:                       
REMARK 999 CHAIN A 1-8, 31-44, 512-516, 728-731                                 
REMARK 999 CHAIN B 1-9, 36-40, 508-515, 728-731                                 
DBREF  1QRK A    1   731  UNP    P00488   F13A_HUMAN       1    731             
DBREF  1QRK B    1   731  UNP    P00488   F13A_HUMAN       1    731             
SEQADV 1QRK GLU A  651  UNP  P00488    GLN   651 CONFLICT                       
SEQADV 1QRK 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                                                  
HET     SR  A 732       1                                                       
HET     SR  B 732       1                                                       
HETNAM      SR STRONTIUM ION                                                    
FORMUL   3   SR    2(SR 2+)                                                     
FORMUL   5  HOH   *230(H2 O)                                                    
HELIX    1   1 THR A   59  HIS A   64  1                                   6    
HELIX    2   2 PRO A  176  THR A  178  5                                   3    
HELIX    3   3 GLU A  198  LEU A  206  1                                   9    
HELIX    4   4 ILE A  234  ARG A  244  1                                  11    
HELIX    5   5 LEU A  249  GLY A  251  5                                   3    
HELIX    6   6 PRO A  255  VAL A  266  1                                  12    
HELIX    7   7 VAL A  296  SER A  305  1                                  10    
HELIX    8   8 CYS A  314  LEU A  328  1                                  15    
HELIX    9   9 VAL A  414  HIS A  419  1                                   6    
HELIX   10  10 ALA A  428  ASN A  436  1                                   9    
HELIX   11  11 THR A  478  TYR A  481  1                                   4    
HELIX   12  12 GLU A  488  TYR A  500  1                                  13    
HELIX   13  13 ALA A  591  GLU A  593  5                                   3    
HELIX   14  14 MET A  595  GLN A  597  5                                   3    
HELIX   15  15 THR B   59  ASP B   63  1                                   5    
HELIX   16  16 GLU B  111  LYS B  113  5                                   3    
HELIX   17  17 PRO B  176  THR B  178  5                                   3    
HELIX   18  18 GLU B  198  TYR B  204  1                                   7    
HELIX   19  19 ILE B  234  ARG B  244  1                                  11    
HELIX   20  20 LEU B  249  GLY B  251  5                                   3    
HELIX   21  21 PRO B  255  VAL B  266  1                                  12    
HELIX   22  22 SER B  295  SER B  305  1                                  11    
HELIX   23  23 CYS B  314  LEU B  328  1                                  15    
HELIX   24  24 VAL B  414  LYS B  418  1                                   5    
HELIX   25  25 ALA B  428  VAL B  435  1                                   8    
HELIX   26  26 THR B  478  TYR B  481  1                                   4    
HELIX   27  27 GLU B  488  TYR B  500  1                                  13    
HELIX   28  28 ALA B  591  GLN B  597  5                                   7    
SHEET    1   A 3 LEU A  74  ARG A  77  0                                        
SHEET    2   A 3 THR A 180  LEU A 183  1  N  TYR A 181   O  LEU A  74           
SHEET    3   A 3 GLY A 155  PHE A 157 -1  N  PHE A 157   O  THR A 180           
SHEET    1   B 4 VAL A  47  LEU A  52  0                                        
SHEET    2   B 4 PHE A  82  PHE A  88 -1  N  ASP A  87   O  THR A  48           
SHEET    3   B 4 SER A 141  GLN A 147 -1  N  ILE A 146   O  PHE A  82           
SHEET    4   B 4 GLY A 131  GLU A 138 -1  N  GLU A 138   O  SER A 141           
SHEET    1   C 4 TYR A 116  VAL A 119  0                                        
SHEET    2   C 4 PHE A  99  VAL A 104 -1  N  TYR A 103   O  ILE A 117           
SHEET    3   C 4 ARG A 158  THR A 165 -1  N  ALA A 162   O  ARG A 100           
SHEET    4   C 4 GLY A 168  ARG A 171 -1  N  LEU A 170   O  VAL A 163           
SHEET    1   D 2 GLY A 210  GLU A 216  0                                        
SHEET    2   D 2 ASP A 219  TRP A 225 -1  N  TRP A 225   O  GLY A 210           
SHEET    1   E 5 MET A 474  ASP A 476  0                                        
SHEET    2   E 5 LEU A 463  LYS A 467 -1  N  THR A 466   O  MET A 475           
SHEET    3   E 5 ALA A 332  TYR A 338 -1  N  TYR A 338   O  LEU A 463           
SHEET    4   E 5 TYR A 372  MET A 380 -1  N  GLU A 377   O  ARG A 333           
SHEET    5   E 5 GLY A 391  VAL A 395 -1  N  VAL A 395   O  ASN A 376           
SHEET    1   F 3 GLN A 349  LEU A 354  0                                        
SHEET    2   F 3 ASP A 438  LYS A 445  1  N  ASP A 438   O  MET A 350           
SHEET    3   F 3 THR A 449  ASP A 456 -1  N  ASP A 456   O  LEU A 439           
SHEET    1   G 3 VAL A 518  VAL A 524  0                                        
SHEET    2   G 3 PHE A 533  ASN A 541 -1  N  ARG A 540   O  ASP A 519           
SHEET    3   G 3 SER A 581  ILE A 589 -1  N  ILE A 589   O  PHE A 533           
SHEET    1   H 4 ASP A 617  VAL A 626  0                                        
SHEET    2   H 4 SER A 603  ILE A 612 -1  N  ILE A 612   O  ASP A 617           
SHEET    3   H 4 TYR A 547  THR A 558 -1  N  THR A 558   O  SER A 603           
SHEET    4   H 4 ALA A 566  LEU A 577 -1  N  LEU A 577   O  TYR A 547           
SHEET    1   I 3 ILE A 633  GLY A 638  0                                        
SHEET    2   I 3 ASP A 645  GLU A 651 -1  N  GLU A 651   O  ILE A 633           
SHEET    3   I 3 TRP A 691  ARG A 696 -1  N  CYS A 695   O  MET A 646           
SHEET    1   J 4 MET A 676  PHE A 680  0                                        
SHEET    2   J 4 VAL A 663  ASP A 668 -1  N  LEU A 667   O  MET A 676           
SHEET    3   J 4 LEU A 705  SER A 710 -1  N  SER A 710   O  TRP A 664           
SHEET    4   J 4 ARG A 715  LEU A 721 -1  N  LEU A 721   O  LEU A 705           
SHEET    1   K 4 VAL B  29  LEU B  31  0                                        
SHEET    2   K 4 GLY B 168  ARG B 171 -1  N  VAL B 169   O  GLU B  30           
SHEET    3   K 4 ARG B 158  THR B 165 -1  N  THR B 165   O  GLY B 168           
SHEET    4   K 4 PHE B  99  VAL B 104 -1  N  VAL B 104   O  ARG B 158           
SHEET    1   L 3 LEU B  74  ARG B  77  0                                        
SHEET    2   L 3 THR B 180  LEU B 183  1  N  TYR B 181   O  LEU B  74           
SHEET    3   L 3 GLY B 155  PHE B 157 -1  N  PHE B 157   O  THR B 180           
SHEET    1   M 4 VAL B  47  HIS B  51  0                                        
SHEET    2   M 4 PHE B  82  PHE B  88 -1  N  ASP B  87   O  THR B  48           
SHEET    3   M 4 SER B 141  GLN B 147 -1  N  ILE B 146   O  PHE B  82           
SHEET    4   M 4 GLY B 131  GLU B 138 -1  N  GLU B 138   O  SER B 141           
SHEET    1   N 2 ILE B 209  GLU B 216  0                                        
SHEET    2   N 2 ASP B 219  SER B 226 -1  N  TRP B 225   O  GLY B 210           
SHEET    1   O 5 MET B 474  ASP B 476  0                                        
SHEET    2   O 5 LEU B 463  LYS B 467 -1  N  THR B 466   O  MET B 475           
SHEET    3   O 5 ALA B 332  TYR B 338 -1  N  TYR B 338   O  LEU B 463           
SHEET    4   O 5 TYR B 372  MET B 380 -1  N  GLU B 377   O  ARG B 333           
SHEET    5   O 5 GLY B 391  VAL B 395 -1  N  VAL B 395   O  ASN B 376           
SHEET    1   P 3 GLN B 349  LEU B 354  0                                        
SHEET    2   P 3 ASP B 438  ALA B 444  1  N  ASP B 438   O  MET B 350           
SHEET    3   P 3 HIS B 450  ASP B 456 -1  N  ASP B 456   O  LEU B 439           
SHEET    1   Q 3 MET B 520  VAL B 524  0                                        
SHEET    2   Q 3 PHE B 533  PHE B 539 -1  N  THR B 538   O  ASP B 521           
SHEET    3   Q 3 LYS B 583  ILE B 589 -1  N  ILE B 589   O  PHE B 533           
SHEET    1   R 4 ASP B 617  VAL B 626  0                                        
SHEET    2   R 4 SER B 603  ILE B 612 -1  N  ILE B 612   O  ASP B 617           
SHEET    3   R 4 TYR B 547  THR B 558 -1  N  THR B 558   O  SER B 603           
SHEET    4   R 4 ALA B 566  LEU B 577 -1  N  LEU B 577   O  TYR B 547           
SHEET    1   S 3 ILE B 633  GLY B 638  0                                        
SHEET    2   S 3 ASP B 645  THR B 653 -1  N  GLU B 651   O  ILE B 633           
SHEET    3   S 3 THR B 688  ARG B 696 -1  N  CYS B 695   O  MET B 646           
SHEET    1   T 4 MET B 676  PHE B 680  0                                        
SHEET    2   T 4 VAL B 663  ASP B 668 -1  N  LEU B 667   O  MET B 676           
SHEET    3   T 4 GLY B 701  SER B 710 -1  N  SER B 710   O  TRP B 664           
SHEET    4   T 4 ARG B 715  ILE B 725 -1  N  ILE B 725   O  GLY B 701           
LINK         O   ALA A 457                SR    SR A 732     1555   1555  2.55  
LINK         O   ALA B 457                SR    SR B 732     1555   1555  2.75  
LINK        SR    SR B 732                 OE1 GLU B 485     1555   1555  2.93  
CISPEP   1 ARG A  310    TYR A  311          0         0.27                     
CISPEP   2 GLY A  410    PRO A  411          0         0.82                     
CISPEP   3 GLN A  425    PHE A  426          0        -0.99                     
CISPEP   4 ARG B  310    TYR B  311          0         0.80                     
CISPEP   5 GLY B  410    PRO B  411          0         0.25                     
CISPEP   6 GLN B  425    PHE B  426          0         0.77                     
SITE     1 CAT  3 CYS A 314  HIS A 373  ASP A 396                               
SITE     1 CBT  3 CYS B 314  HIS B 373  ASP B 396                               
SITE     1 INA  4 ALA A 457  ASN A 436  GLU A 485  GLU A 490                    
SITE     1 INB  4 ALA B 457  ASN B 436  GLU B 485  GLU B 490                    
SITE     1 AC1  2 ALA A 457  GLU A 485                                          
SITE     1 AC2  3 ASN B 436  ALA B 457  GLU B 485                               
CRYST1  101.900   72.320  135.030  90.00 105.90  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      0.009814  0.000000  0.002795        0.00000                         
SCALE2      0.000000  0.013827  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007700        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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