GenomeNet

Database: PDB
Entry: 1GGT
LinkDB: 1GGT
Original site: 1GGT 
HEADER    BLOOD COAGULATION                       25-JAN-94   1GGT              
TITLE     THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN              
TITLE    2 BLOOD COAGULATION FACTOR XIII                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR XIII;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.3.2.13;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: BLOOD                                                         
KEYWDS    BLOOD COAGULATION                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.C.YEE,L.C.PEDERSEN,I.L.TRONG,P.D.BISHOP,R.E.STENKAMP,               
AUTHOR   2 D.C.TELLER                                                           
REVDAT   3   24-FEB-09 1GGT    1       VERSN                                    
REVDAT   2   01-APR-03 1GGT    1       JRNL                                     
REVDAT   1   31-JUL-95 1GGT    0                                                
JRNL        AUTH   V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,                  
JRNL        AUTH 2 R.E.STENKAMP,D.C.TELLER                                      
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE:           
JRNL        TITL 2 HUMAN BLOOD COAGULATION FACTOR XIII.                         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  91  7296 1994              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   7913750                                                      
JRNL        DOI    10.1073/PNAS.91.15.7296                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.C.PEDERSEN,V.C.YEE,I.L.TRONG,P.D.BISHOP,                   
REMARK   1  AUTH 2 D.C.TELLER,R.E.STENKAMP                                      
REMARK   1  TITL   THE CATALYTIC TRIAD AND PROPOSED MECHANISM OF                
REMARK   1  TITL 2 TRANSGLUTAMINASES BASED ON THE CRYSTAL STRUCTURE             
REMARK   1  TITL 3 OF FACTOR XIII                                               
REMARK   1  REF    PROTEIN SCI.                  V.   3  1131 1994              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.D.BISHOP,G.W.LASSER,I.L.TRONG,R.E.STENKAMP,                
REMARK   1  AUTH 2 D.C.TELLER                                                   
REMARK   1  TITL   HUMAN RECOMBINANT FACTOR XIII FROM SACCHAROMYCES             
REMARK   1  TITL 2 CEREVISIAE: CRYSTALLIZATION AND PRELIMINARY X-RAY            
REMARK   1  TITL 3 DATA                                                         
REMARK   1  REF    J.BIOL.CHEM.                  V.  23 13888 1990              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.D.BISHOP,D.C.TELLER,R.A.SMITH,G.W.LASSER,                  
REMARK   1  AUTH 2 T.GILBERT,R.L.SEALE                                          
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF            
REMARK   1  TITL 2 HUMAN FACTOR XIII IN SACCHAROMYCES CEREVISIAE                
REMARK   1  REF    BIOCHEMISTRY                  V.  29  1861 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 65937                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11382                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.18                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GGT 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       50.60000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.60000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK:                                                              
REMARK 300 MTRIX                                                                
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
REMARK 300  SECOND.                                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO           TRANSFORMED TO                       
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD             
REMARK 300    M1   A    8  ..     727     B    8  ..     727   0.815            
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     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     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     LEU B    31                                                      
REMARK 465     GLN B    32                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     VAL B    35                                                      
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     LEU B    41                                                      
REMARK 465     GLN B    42                                                      
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     PRO A 729    O                                                   
REMARK 470     GLU B  30    O                                                   
REMARK 470     ARG B 727    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 651   CD    GLU A 651   OE2     0.076                       
REMARK 500    CYS B 188   CB    CYS B 188   SG     -0.099                       
REMARK 500    GLU B 651   CD    GLU B 651   OE2     0.093                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A 365   N   -  CA  -  C   ANGL. DEV. = -26.8 DEGREES          
REMARK 500    THR B 365   N   -  CA  -  C   ANGL. DEV. = -19.9 DEGREES          
REMARK 500    GLN B 425   N   -  CA  -  C   ANGL. DEV. =  18.9 DEGREES          
REMARK 500    ILE B 460   N   -  CA  -  C   ANGL. DEV. =  22.1 DEGREES          
REMARK 500    LEU B 553   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    PHE A  44       41.41     25.23                                   
REMARK 500    ASN A  46      132.09    -30.86                                   
REMARK 500    TYR A  69      106.47    172.38                                   
REMARK 500    GLU A  70       78.04    -64.42                                   
REMARK 500    ARG A  78      148.59    -35.30                                   
REMARK 500    PRO A  91      134.79    -15.21                                   
REMARK 500    ARG A  96       14.83   -148.23                                   
REMARK 500    VAL A 135      -65.18    -97.84                                   
REMARK 500    GLU A 138      103.55    -21.06                                   
REMARK 500    ASP A 139      119.32     16.76                                   
REMARK 500    ARG A 140      -29.15     65.38                                   
REMARK 500    TYR A 167       30.63    -96.30                                   
REMARK 500    VAL A 205      -51.77   -128.98                                   
REMARK 500    TYR A 214     -154.67   -151.71                                   
REMARK 500    VAL A 217      -41.54    -26.00                                   
REMARK 500    ASP A 219       69.50   -150.06                                   
REMARK 500    ALA A 268       97.88    -57.88                                   
REMARK 500    ASP A 270       95.01     58.41                                   
REMARK 500    ASP A 271      -45.80     78.38                                   
REMARK 500    ASN A 281       -7.19     69.51                                   
REMARK 500    TYR A 285       55.84    -99.03                                   
REMARK 500    TYR A 311      121.80     75.34                                   
REMARK 500    TYR A 338      -83.03    -75.84                                   
REMARK 500    LEU A 364      102.57   -161.84                                   
REMARK 500    THR A 365       72.36   -159.57                                   
REMARK 500    ASN A 402     -160.41   -122.89                                   
REMARK 500    MET A 406       63.50     80.60                                   
REMARK 500    GLN A 425      146.66    -37.08                                   
REMARK 500    PHE A 426       68.06     90.49                                   
REMARK 500    GLU A 485      108.07    -52.84                                   
REMARK 500    GLU A 509       66.43    -54.25                                   
REMARK 500    MET A 512      -65.40    171.38                                   
REMARK 500    LYS A 513     -179.34     50.02                                   
REMARK 500    ARG A 515       84.39    -56.63                                   
REMARK 500    SER A 516        7.58     49.63                                   
REMARK 500    ASN A 517       42.00     75.94                                   
REMARK 500    GLU A 525     -155.30    -80.83                                   
REMARK 500    ASN A 526      122.61   -172.23                                   
REMARK 500    ALA A 527     -156.85   -106.33                                   
REMARK 500    HIS A 544       53.01    -91.94                                   
REMARK 500    ALA A 566      148.55   -178.38                                   
REMARK 500    LEU A 580       87.25     34.35                                   
REMARK 500    LYS A 583      137.00   -171.15                                   
REMARK 500    ALA A 591       -9.63    -55.32                                   
REMARK 500    ASN A 654      101.64    -50.16                                   
REMARK 500    ASN A 662       60.92     35.04                                   
REMARK 500    ASN A 686       -1.69     56.74                                   
REMARK 500    SER A 687     -178.54    -57.56                                   
REMARK 500    HIS A 716       34.76     83.86                                   
REMARK 500    LEU B  45      127.91    102.74                                   
REMARK 500    LYS B  54      -91.53    -58.88                                   
REMARK 500    GLU B  55      121.54     14.25                                   
REMARK 500    ARG B  56       -5.25    -58.46                                   
REMARK 500    PRO B  91      140.31    -38.53                                   
REMARK 500    GLN B 110      110.79   -163.74                                   
REMARK 500    SER B 127      125.58    -37.25                                   
REMARK 500    MET B 136      138.08    169.64                                   
REMARK 500    ASP B 139       98.95    -53.11                                   
REMARK 500    ARG B 140      -21.11     78.85                                   
REMARK 500    PRO B 150        4.20    -68.56                                   
REMARK 500    PRO B 166      -14.77    -48.17                                   
REMARK 500    GLU B 189      -16.11    -45.46                                   
REMARK 500    VAL B 205      -56.00   -128.86                                   
REMARK 500    TYR B 214     -159.00   -134.94                                   
REMARK 500    ASP B 232      104.34    -42.90                                   
REMARK 500    ARG B 252        9.29    -61.15                                   
REMARK 500    ASP B 270       99.28     32.66                                   
REMARK 500    ASP B 271      -22.95     75.79                                   
REMARK 500    GLU B 272     -105.88    -61.59                                   
REMARK 500    ASN B 281        8.13    -64.25                                   
REMARK 500    ILE B 282      -64.08    -93.41                                   
REMARK 500    TYR B 311      114.65     69.86                                   
REMARK 500    PHE B 339       78.36     79.04                                   
REMARK 500    ALA B 341       57.54    -90.90                                   
REMARK 500    LEU B 348       37.19    -91.92                                   
REMARK 500    SER B 362       12.50   -140.24                                   
REMARK 500    THR B 365       68.44    170.80                                   
REMARK 500    ASN B 402     -154.73   -129.53                                   
REMARK 500    MET B 406       68.45     78.57                                   
REMARK 500    GLN B 425      156.30    -42.52                                   
REMARK 500    PHE B 426       71.80     76.72                                   
REMARK 500    ASN B 436       19.53   -140.23                                   
REMARK 500    LYS B 445     -170.09    -64.89                                   
REMARK 500    ASP B 447       25.39    -71.14                                   
REMARK 500    ILE B 460      -20.97    -37.79                                   
REMARK 500    TYR B 500       42.02   -102.27                                   
REMARK 500    THR B 508       54.51    -94.63                                   
REMARK 500    GLU B 509      -66.35     10.91                                   
REMARK 500    MET B 512      -64.27   -126.12                                   
REMARK 500    LYS B 513     -161.22   -114.35                                   
REMARK 500    SER B 514      -25.34   -168.44                                   
REMARK 500    ASP B 521     -148.94   -127.15                                   
REMARK 500    PHE B 522      119.24    161.90                                   
REMARK 500    HIS B 544       35.31    -98.60                                   
REMARK 500    ALA B 566      150.90    173.49                                   
REMARK 500    MET B 595      -36.91    -26.56                                   
REMARK 500    ARG B 616       42.11     75.41                                   
REMARK 500    THR B 628      105.67    -60.00                                   
REMARK 500    GLU B 631      161.14    -42.83                                   
REMARK 500    ASN B 686       17.07     56.74                                   
REMARK 500    PRO B 697      165.63    -46.30                                   
REMARK 500    SER B 713      -90.85   -102.06                                   
REMARK 500    HIS B 716       44.56     87.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 214         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 SHEET *B1A* FORMS A BETA SANDWICH DOMAIN WITH SHEETS *B2A*           
REMARK 700 AND *B2B*.  SHEET *B1B* FORMS A BETA SANDWICH DOMAIN WITH            
REMARK 700 SHEETS *B2C* AND *B2D*.                                              
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED.  IN              
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 THE BIFURCATED SHEET IS REPRESENTED BY TWO SHEETS WHICH              
REMARK 700 HAVE ONE OR MORE IDENTICAL STRANDS.  STRANDS 3, 4, AND 5             
REMARK 700 OF SHEET *B2A* AND *B2B* ARE IDENTICAL.  STRANDS 3, 4, AND           
REMARK 700 5 OF SHEET *B2C* AND *B2D* ARE IDENTICAL.                            
REMARK 700 IN SHEET *B7A* AND *B7B* OF *SHEET* RECORDS BELOW, STRANDS           
REMARK 700 1 - 3 AND 4 - 7 FORM TWO BETA SHEETS THAT COME TOGETHER TO           
REMARK 700 MAKE A BARREL.  IN SHEET *B8A* AND *B8B* OF *SHEET* RECORDS          
REMARK 700 BELOW, STRANDS 1 - 3 AND 4 - 7 FORM TWO BETA SHEETS THAT             
REMARK 700 COME TOGETHER TO MAKE A BARREL.                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES IN CHAIN A                
REMARK 800 SITE_IDENTIFIER: CBT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES IN CHAIN B                
DBREF  1GGT A    1   731  UNP    P00488   F13A_HUMAN       1    731             
DBREF  1GGT B    1   731  UNP    P00488   F13A_HUMAN       1    731             
SEQADV 1GGT GLU A  651  UNP  P00488    GLN   651 CONFLICT                       
SEQADV 1GGT 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                                                  
HELIX    1  A1 THR A   59  ASP A   63  1                                   5    
HELIX    2  A2 PRO A  176  THR A  178  5                                   3    
HELIX    3  A3 GLU A  198  ASN A  207  1                                  10    
HELIX    4  A4 ILE A  234  ARG A  244  1                                  11    
HELIX    5  A5 PRO A  255  MET A  265  1                                  11    
HELIX    6  A6 SER A  295  SER A  304  1                                  10    
HELIX    7  A7 CYS A  314  CYS A  327  1                                  14    
HELIX    8  A8 VAL A  414  HIS A  419  1                                   6    
HELIX    9  A9 ALA A  428  ASN A  436  1                                   9    
HELIX   10 A10 THR A  478  TYR A  481  1                                   4    
HELIX   11 A11 GLU A  488  MET A  499  1                                  12    
HELIX   12 A12 GLY A  592  GLN A  597  1                                   6    
HELIX   13  B1 THR B   59  ASP B   63  1                                   5    
HELIX   14  B2 PRO B  176  THR B  178  5                                   3    
HELIX   15  B3 GLU B  198  ASN B  207  1                                  10    
HELIX   16  B4 ILE B  234  ARG B  244  1                                  11    
HELIX   17  B5 PRO B  255  MET B  265  1                                  11    
HELIX   18  B6 SER B  295  SER B  304  1                                  10    
HELIX   19  B7 CYS B  314  CYS B  327  1                                  14    
HELIX   20  B8 VAL B  414  HIS B  419  1                                   6    
HELIX   21  B9 ALA B  428  ASN B  436  1                                   9    
HELIX   22 B10 THR B  478  TYR B  481  1                                   4    
HELIX   23 B11 GLU B  488  MET B  499  1                                  12    
HELIX   24 B12 GLY B  592  GLN B  597  1                                   6    
SHEET    1 B1A 4 ASN A  46  PHE A  53  0                                        
SHEET    2 B1A 4 PHE A  82  PHE A  88 -1  O  GLN A  85   N  HIS A  51           
SHEET    3 B1A 4 SER A 141  SER A 148 -1  O  LEU A 144   N  VAL A  84           
SHEET    4 B1A 4 GLY A 131  GLU A 138 -1  O  LYS A 133   N  SER A 145           
SHEET    1 B1B 4 ASN B  46  PHE B  53  0                                        
SHEET    2 B1B 4 PHE B  82  PHE B  88 -1  O  GLN B  85   N  HIS B  51           
SHEET    3 B1B 4 SER B 141  SER B 148 -1  O  LEU B 144   N  VAL B  84           
SHEET    4 B1B 4 GLY B 131  GLU B 138 -1  O  LYS B 133   N  SER B 145           
SHEET    1 B2A 4 GLY A 168  ARG A 171  0                                        
SHEET    2 B2A 4 GLY A 155  THR A 165 -1  N  VAL A 163   O  LEU A 170           
SHEET    3 B2A 4 PHE A  99  VAL A 104 -1  N  GLU A 102   O  TYR A 160           
SHEET    4 B2A 4 TYR A 116  PRO A 120 -1  N  VAL A 119   O  VAL A 101           
SHEET    1 B2C 4 GLY B 168  ARG B 171  0                                        
SHEET    2 B2C 4 GLY B 155  THR B 165 -1  N  VAL B 163   O  LEU B 170           
SHEET    3 B2C 4 PHE B  99  VAL B 104 -1  N  GLU B 102   O  TYR B 160           
SHEET    4 B2C 4 TYR B 116  PRO B 120 -1  N  VAL B 119   O  VAL B 101           
SHEET    1 B2B 5 LEU A  74  ARG A  77  0                                        
SHEET    2 B2B 5 THR A 180  LEU A 183  1  N  TYR A 181   O  LEU A  74           
SHEET    3 B2B 5 GLY A 155  THR A 165 -1  N  PHE A 157   O  THR A 180           
SHEET    4 B2B 5 PHE A  99  VAL A 104 -1  N  GLU A 102   O  TYR A 160           
SHEET    5 B2B 5 TYR A 116  PRO A 120 -1  N  VAL A 119   O  VAL A 101           
SHEET    1 B2D 5 LEU B  74  ARG B  77  0                                        
SHEET    2 B2D 5 THR B 180  LEU B 183  1  N  TYR B 181   O  LEU B  74           
SHEET    3 B2D 5 GLY B 155  THR B 165 -1  N  PHE B 157   O  THR B 180           
SHEET    4 B2D 5 PHE B  99  VAL B 104 -1  N  GLU B 102   O  TYR B 160           
SHEET    5 B2D 5 TYR B 116  PRO B 120 -1  N  VAL B 119   O  VAL B 101           
SHEET    1 B3A 2 ILE A 209  GLU A 216  0                                        
SHEET    2 B3A 2 ASP A 219  SER A 226 -1  O  ARG A 223   N  ILE A 212           
SHEET    1 B3B 2 ILE B 209  GLU B 216  0                                        
SHEET    2 B3B 2 ASP B 219  SER B 226 -1  O  ARG B 223   N  ILE B 212           
SHEET    1 B4A 2 LEU A 275  GLY A 277  0                                        
SHEET    2 B4A 2 VAL A 309  GLY A 312  1  N  TYR A 311   O  VAL A 276           
SHEET    1 B4B 2 LEU B 275  GLY B 277  0                                        
SHEET    2 B4B 2 VAL B 309  GLY B 312  1  N  TYR B 311   O  VAL B 276           
SHEET    1 B5A 3 ASP A 351  GLU A 355  0                                        
SHEET    2 B5A 3 LEU A 439  THR A 443  1  O  ILE A 440   N  PHE A 353           
SHEET    3 B5A 3 VAL A 451  ASP A 456 -1  O  ASN A 454   N  TYR A 441           
SHEET    1 B5B 3 ASP B 351  GLU B 355  0                                        
SHEET    2 B5B 3 LEU B 439  THR B 443  1  O  ILE B 440   N  PHE B 353           
SHEET    3 B5B 3 VAL B 451  ASP B 456 -1  O  ASN B 454   N  TYR B 441           
SHEET    1 B6A 6 MET A 474  ASP A 476  0                                        
SHEET    2 B6A 6 ILE A 464  LYS A 467 -1  N  THR A 466   O  MET A 475           
SHEET    3 B6A 6 ALA A 332  ASN A 337 -1  N  THR A 336   O  VAL A 465           
SHEET    4 B6A 6 ASN A 376  MET A 380 -1  N  GLU A 377   O  ARG A 333           
SHEET    5 B6A 6 GLY A 391  GLN A 400 -1  N  VAL A 395   O  ASN A 376           
SHEET    6 B6A 6 TYR A 407  SER A 413 -1  N  CYS A 409   O  ASP A 396           
SHEET    1 B6B 6 MET B 474  ASP B 476  0                                        
SHEET    2 B6B 6 ILE B 464  LYS B 467 -1  N  THR B 466   O  MET B 475           
SHEET    3 B6B 6 ALA B 332  ASN B 337 -1  N  THR B 336   O  VAL B 465           
SHEET    4 B6B 6 ASN B 376  MET B 380 -1  N  GLU B 377   O  ARG B 333           
SHEET    5 B6B 6 GLY B 391  GLN B 400 -1  N  VAL B 395   O  ASN B 376           
SHEET    6 B6B 6 TYR B 407  SER B 413 -1  N  CYS B 409   O  ASP B 396           
SHEET    1 B7A 8 VAL A 518  VAL A 524  0                                        
SHEET    2 B7A 8 LYS A 534  ASN A 541 -1  N  THR A 538   O  ASP A 521           
SHEET    3 B7A 8 LYS A 583  LEU A 588 -1  N  GLU A 585   O  ILE A 537           
SHEET    4 B7A 8 PRO A 564  LEU A 577 -1  N  THR A 572   O  ALA A 586           
SHEET    5 B7A 8 TYR A 547  THR A 558 -1  N  LEU A 553   O  GLU A 571           
SHEET    6 B7A 8 SER A 603  ILE A 612 -1  N  THR A 609   O  TYR A 552           
SHEET    7 B7A 8 ASP A 617  VAL A 626 -1  N  LYS A 621   O  VAL A 608           
SHEET    8 B7A 8 VAL A 518  VAL A 524  1  O  PHE A 522   N  LYS A 623           
SHEET    1 B7B 8 VAL B 518  VAL B 524  0                                        
SHEET    2 B7B 8 LYS B 534  ASN B 541 -1  N  THR B 538   O  ASP B 521           
SHEET    3 B7B 8 LYS B 583  LEU B 588 -1  N  GLU B 585   O  ILE B 537           
SHEET    4 B7B 8 PRO B 564  LEU B 577 -1  N  THR B 572   O  ALA B 586           
SHEET    5 B7B 8 TYR B 547  THR B 558 -1  N  LEU B 553   O  GLU B 571           
SHEET    6 B7B 8 SER B 603  ILE B 612 -1  N  THR B 609   O  TYR B 552           
SHEET    7 B7B 8 ASP B 617  VAL B 626 -1  N  LYS B 621   O  VAL B 608           
SHEET    8 B7B 8 VAL B 518  VAL B 524  1  O  PHE B 522   N  LYS B 623           
SHEET    1 B8A 8 ILE A 633  ARG A 637  0                                        
SHEET    2 B8A 8 MET A 646  THR A 653 -1  N  THR A 649   O  LYS A 635           
SHEET    3 B8A 8 THR A 688  CYS A 695 -1  N  GLU A 693   O  VAL A 648           
SHEET    4 B8A 8 MET A 676  ILE A 683 -1  O  MET A 679   N  GLN A 690           
SHEET    5 B8A 8 LEU A 660  ASP A 668 -1  O  VAL A 665   N  LYS A 678           
SHEET    6 B8A 8 LYS A 704  SER A 710 -1  O  SER A 708   N  HIS A 666           
SHEET    7 B8A 8 ARG A 715  ASP A 722 -1  O  VAL A 717   N  MET A 709           
SHEET    8 B8A 8 ILE A 633  ARG A 637  1  N  ILE A 632   O  TYR A 718           
SHEET    1 B8B 8 ILE B 633  ARG B 637  0                                        
SHEET    2 B8B 8 MET B 646  THR B 653 -1  N  THR B 649   O  LYS B 635           
SHEET    3 B8B 8 THR B 688  CYS B 695 -1  N  GLU B 693   O  VAL B 648           
SHEET    4 B8B 8 MET B 676  ILE B 683 -1  O  MET B 679   N  GLN B 690           
SHEET    5 B8B 8 LEU B 660  ASP B 668 -1  O  VAL B 665   N  LYS B 678           
SHEET    6 B8B 8 LYS B 704  SER B 710 -1  O  SER B 708   N  HIS B 666           
SHEET    7 B8B 8 ARG B 715  ASP B 722 -1  O  VAL B 717   N  MET B 709           
SHEET    8 B8B 8 ILE B 633  ARG B 637  1  N  ILE B 632   O  TYR B 718           
CISPEP   1 GLY A  410    PRO A  411          0         0.58                     
CISPEP   2 GLY B  410    PRO B  411          0         0.58                     
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                               
CRYST1  101.200  182.700   93.400  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009881  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005473  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010707        0.00000                         
MTRIX1   1  0.590321  0.807168  0.000528      -53.00930    1                    
MTRIX2   1  0.807132 -0.590300  0.009151      104.47170    1                    
MTRIX3   1  0.007699  0.007699 -0.999960       75.66453    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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