GenomeNet

Database: PDB
Entry: 3ENS
LinkDB: 3ENS
Original site: 3ENS 
HEADER    HYDROLASE, BLOOD CLOTTING               25-SEP-08   3ENS              
TITLE     CRYSTAL STRUCTURE OF HUMAN FXA IN COMPLEX WITH METHYL (2Z)-3-[(3-     
TITLE    2 CHLORO-1H-INDOL-7-YL)AMINO]-2-CYANO-3-{[(3S)-2-OXO-1-(2-OXO-2-       
TITLE    3 PYRROLIDIN-1-YLETHYL)AZEPAN-3-YL]AMINO}ACRYLATE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FACTOR X LIGHT CHAIN;                                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 93-178;                         
COMPND   5 EC: 3.4.21.6;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ACTIVATED FACTOR XA HEAVY CHAIN;                           
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: SEQUENCE DATABASE RESIDUES 235-472;                        
COMPND  10 EC: 3.4.21.6                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 OTHER_DETAILS: BLOOD;                                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 OTHER_DETAILS: BLOOD                                                 
KEYWDS    SERINE PROTEASE, HYDROLASE, EPIDERMAL GROWTH FACTOR LIKE DOMAIN,      
KEYWDS   2 BLOOD COAGULATION FACTOR, CLEAVAGE ON PAIR OF BASIC RESIDUES, EGF-   
KEYWDS   3 LIKE DOMAIN, GAMMA-CARBOXYGLUTAMIC ACID, GLYCOPROTEIN,               
KEYWDS   4 HYDROXYLATION, ZYMOGEN, BLOOD CLOTTING                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.KLEI                                                              
REVDAT   3   25-OCT-17 3ENS    1       REMARK                                   
REVDAT   2   13-JUL-11 3ENS    1       VERSN                                    
REVDAT   1   30-DEC-08 3ENS    0                                                
JRNL        AUTH   Y.SHI,D.SITKOFF,J.ZHANG,H.E.KLEI,K.KISH,E.C.LIU,K.S.HARTL,   
JRNL        AUTH 2 S.M.SEILER,M.CHANG,C.HUANG,S.YOUSSEF,T.E.STEINBACHER,        
JRNL        AUTH 3 W.A.SCHUMACHER,N.GRAZIER,A.PUDZIANOWSKI,A.APEDO,L.DISCENZA,  
JRNL        AUTH 4 J.YANCHUNAS,P.D.STEIN,K.S.ATWAL                              
JRNL        TITL   DESIGN, STRUCTURE-ACTIVITY RELATIONSHIPS, X-RAY CRYSTAL      
JRNL        TITL 2 STRUCTURE, AND ENERGETIC CONTRIBUTIONS OF A CRITICAL P1      
JRNL        TITL 3 PHARMACOPHORE: 3-CHLOROINDOLE-7-YL-BASED FACTOR XA           
JRNL        TITL 4 INHIBITORS.                                                  
JRNL        REF    J.MED.CHEM.                   V.  51  7541 2008              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   18998662                                                     
JRNL        DOI    10.1021/JM800855X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.480                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 30221                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.310                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.0292 -  4.3843    0.99     4331   148  0.2072 0.2468        
REMARK   3     2  4.3843 -  3.4869    0.99     4237   146  0.1892 0.2488        
REMARK   3     3  3.4869 -  3.0482    0.98     4217   144  0.2159 0.2739        
REMARK   3     4  3.0482 -  2.7704    0.97     4170   142  0.2426 0.3393        
REMARK   3     5  2.7704 -  2.5724    0.97     4128   142  0.2420 0.3087        
REMARK   3     6  2.5724 -  2.4210    0.96     4101   140  0.2533 0.3254        
REMARK   3     7  2.4210 -  2.3000    0.95     4037   138  0.2550 0.3573        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 46.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.95910                                              
REMARK   3    B22 (A**2) : -5.07220                                             
REMARK   3    B33 (A**2) : -0.88690                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.72480                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           5237                                  
REMARK   3   ANGLE     :  0.946           7018                                  
REMARK   3   CHIRALITY :  0.064            740                                  
REMARK   3   PLANARITY :  0.004            907                                  
REMARK   3   DIHEDRAL  : 18.112           1938                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ENS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049551.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.50                               
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) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30240                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10000                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-22% W/V PEG MME 5000, 0.01 M          
REMARK 280  CALCIUM ACETATE, 0.35 M SODIUM ACETATE, 0.1 M LITHIUM SULFATE,      
REMARK 280  0.1 M MES, PH 6.500000, VAPOR DIFFUSION HANGING DROP,               
REMARK 280  TEMPERATURE 298K, VAPOR DIFFUSION, HANGING DROP                     
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       39.43050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     LYS A    85                                                      
REMARK 465     ASP A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     GLN A    89                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     THR A    92                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     LYS C    85                                                      
REMARK 465     ASP C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     THR C    92                                                      
REMARK 465     SER C    93                                                      
REMARK 465     GLY C   104                                                      
REMARK 465     LEU C   105                                                      
REMARK 465     GLY C   106                                                      
REMARK 465     GLU C   107                                                      
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     CYS A  90    O                                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     LYS A 102    CD   CE   NZ                                        
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     GLN C  89    N    CB   CG   CD   OE1  NE2                        
REMARK 470     GLU C  91    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU C  91    OE2                                                 
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
REMARK 470     GLN C 144    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  62    CE   NZ                                             
REMARK 470     GLU D  74    CD   OE1  OE2                                       
REMARK 470     GLN D  75    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 148    CG   CD   CE   NZ                                   
REMARK 470     ARG D 150    CG   CD   NE   CZ   NH1  NH2                        
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    ARG A 126      103.80    -58.58                                   
REMARK 500    GLN A 138     -109.90   -127.46                                   
REMARK 500    ASN A 145       18.74     51.57                                   
REMARK 500    LYS A 162      -51.04   -126.06                                   
REMARK 500    PHE B  41      -20.43   -140.51                                   
REMARK 500    SER B  48     -167.89   -165.32                                   
REMARK 500    GLU B  76       72.11    -65.41                                   
REMARK 500    ARG B 245     -157.06     55.65                                   
REMARK 500    CYS C  90       41.73    -84.92                                   
REMARK 500    GLN C 138     -110.45   -126.48                                   
REMARK 500    SER D 214      -57.92   -123.01                                   
REMARK 500    ARG D 245     -153.12     51.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENS B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENS D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 308                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE PROTEIN, AS ISOLATED FROM HUMAN BLOOD BY ENZYME RESEARCH         
REMARK 999 LABORATORIES (SOUTH BEND, IN), WAS FOUND TO BE HETEROGENEOUS BY      
REMARK 999 MASS SPECTROMETRY. THE REPROTED SEQRES RECORDS INCLUDE THE           
REMARK 999 RESIDUES CONSISTENT WITH THE CARBOXYPEPTIDASE B CLEAVAGE SITE TO     
REMARK 999 FORM DES-GLA PROTEIN AND THE RESIDUES MODELED IN ELECTRON            
REMARK 999 DENSITY. N-TERMINI OF LIGHT CHAINS (CHAINS A AND C) MODELED          
REMARK 999 BASED ON 1XKA. THERE MAY BE MORE RESIDUES BEYOND THESE TERMINI.      
DBREF  3ENS A   85   178  UNP    P00742   FA10_HUMAN      85    178             
DBREF  3ENS B   16   248  UNP    P00742   FA10_HUMAN     235    472             
DBREF  3ENS C   85   178  UNP    P00742   FA10_HUMAN      85    178             
DBREF  3ENS D   16   248  UNP    P00742   FA10_HUMAN     235    472             
SEQRES   1 A   94  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 A   94  GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 A   94  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 A   94  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 A   94  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 A   94  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 A   94  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 A   94  THR LEU GLU                                                  
SEQRES   1 B  238  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 B  238  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 B  238  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 B  238  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 B  238  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 B  238  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 B  238  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 B  238  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 B  238  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 B  238  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 B  238  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 B  238  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 B  238  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 B  238  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 B  238  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 B  238  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 B  238  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 B  238  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 B  238  ARG GLY LEU PRO                                              
SEQRES   1 C   94  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 C   94  GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 C   94  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 C   94  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 C   94  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 C   94  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 C   94  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 C   94  THR LEU GLU                                                  
SEQRES   1 D  238  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 D  238  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 D  238  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 D  238  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 D  238  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 D  238  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 D  238  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 D  238  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 D  238  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 D  238  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 D  238  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 D  238  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 D  238  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 D  238  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 D  238  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 D  238  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 D  238  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 D  238  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 D  238  ARG GLY LEU PRO                                              
HET    GOL  A 201       6                                                       
HET    GOL  A 202       6                                                       
HET    GOL  A 203       6                                                       
HET    ENS  B 301      36                                                       
HET     CA  B 302       1                                                       
HET     NA  B 303       1                                                       
HET    MES  B 304      12                                                       
HET    GOL  B 305       6                                                       
HET    ACT  B 306       4                                                       
HET    ENS  D 301      36                                                       
HET     CA  D 302       1                                                       
HET     NA  D 303       1                                                       
HET    MES  D 304      12                                                       
HET    GOL  D 305       6                                                       
HET    GOL  D 306       6                                                       
HET    GOL  D 307       6                                                       
HET    ACT  D 308       4                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     ENS METHYL (2Z)-3-[(3-CHLORO-1H-INDOL-7-YL)AMINO]-2-CYANO-           
HETNAM   2 ENS  3-{[(3S)-2-OXO-1-(2-OXO-2-PYRROLIDIN-1-YLETHYL)AZEPAN-          
HETNAM   3 ENS  3-YL]AMINO}ACRYLATE                                             
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     ENS METHYL (2Z)-3-[(3-CHLORO-1H-INDOL-7-YL)AMINO]-2-CYANO-           
HETSYN   2 ENS  3-{[(3S)-2-OXO-1-(2-OXO-2-PYRROLIDIN-1-YLETHYL)AZEPAN-          
HETSYN   3 ENS  3-YL]AMINO}PROP-2-ENOATE                                        
FORMUL   5  GOL    7(C3 H8 O3)                                                  
FORMUL   8  ENS    2(C25 H29 CL N6 O4)                                          
FORMUL   9   CA    2(CA 2+)                                                     
FORMUL  10   NA    2(NA 1+)                                                     
FORMUL  11  MES    2(C6 H13 N O4 S)                                             
FORMUL  13  ACT    2(C2 H3 O2 1-)                                               
FORMUL  22  HOH   *304(H2 O)                                                    
HELIX    1   1 LEU A  131  CYS A  136  5                                   6    
HELIX    2   2 ALA B   55  ALA B   61A 5                                   8    
HELIX    3   3 GLU B  124A LEU B  131A 1                                   9    
HELIX    4   4 ASP B  164  SER B  172  1                                   9    
HELIX    5   5 PHE B  234  THR B  244  1                                  11    
HELIX    6   6 CYS C   95  GLY C   99  5                                   5    
HELIX    7   7 LEU C  131  CYS C  136  5                                   6    
HELIX    8   8 ALA D   55  GLN D   61  5                                   7    
HELIX    9   9 GLU D  124A LEU D  131A 1                                   9    
HELIX   10  10 ASP D  164  SER D  172  1                                   9    
HELIX   11  11 PHE D  234  THR D  244  1                                  11    
SHEET    1   A 2 LYS A 100  CYS A 101  0                                        
SHEET    2   A 2 CYS A 110  THR A 111 -1  O  THR A 111   N  LYS A 100           
SHEET    1   B 2 PHE A 116  GLU A 117  0                                        
SHEET    2   B 2 LEU A 123  PHE A 124 -1  O  LEU A 123   N  GLU A 117           
SHEET    1   C 2 PHE A 139  GLU A 142  0                                        
SHEET    2   C 2 VAL A 147  SER A 150 -1  O  VAL A 148   N  HIS A 141           
SHEET    1   D 2 TYR A 155  LEU A 157  0                                        
SHEET    2   D 2 CYS A 164  PRO A 166 -1  O  ILE A 165   N  THR A 156           
SHEET    1   E 8 GLN B  20  GLU B  21  0                                        
SHEET    2   E 8 LYS B 156  VAL B 163 -1  O  MET B 157   N  GLN B  20           
SHEET    3   E 8 MET B 180  ALA B 183 -1  O  CYS B 182   N  VAL B 163           
SHEET    4   E 8 GLY B 226  LYS B 230 -1  O  TYR B 228   N  PHE B 181           
SHEET    5   E 8 THR B 206  GLY B 216 -1  N  TRP B 215   O  ILE B 227           
SHEET    6   E 8 PRO B 198  PHE B 203 -1  N  HIS B 199   O  THR B 210           
SHEET    7   E 8 THR B 135  GLY B 140 -1  N  ILE B 137   O  VAL B 200           
SHEET    8   E 8 LYS B 156  VAL B 163 -1  O  VAL B 160   N  GLY B 136           
SHEET    1   F 7 ALA B  81  HIS B  83  0                                        
SHEET    2   F 7 LYS B  65  VAL B  68 -1  N  VAL B  66   O  HIS B  83           
SHEET    3   F 7 GLN B  30  ILE B  34 -1  N  LEU B  32   O  ARG B  67           
SHEET    4   F 7 GLY B  40  ILE B  46 -1  O  CYS B  42   N  LEU B  33           
SHEET    5   F 7 TYR B  51  THR B  54 -1  O  LEU B  53   N  THR B  45           
SHEET    6   F 7 ALA B 104  LEU B 108 -1  O  LEU B 106   N  ILE B  52           
SHEET    7   F 7 VAL B  85  LYS B  90 -1  N  GLU B  86   O  ARG B 107           
SHEET    1   G 2 LYS C 100  CYS C 101  0                                        
SHEET    2   G 2 CYS C 110  THR C 111 -1  O  THR C 111   N  LYS C 100           
SHEET    1   H 2 PHE C 116  GLU C 117  0                                        
SHEET    2   H 2 LEU C 123  PHE C 124 -1  O  LEU C 123   N  GLU C 117           
SHEET    1   I 2 PHE C 139  GLU C 142  0                                        
SHEET    2   I 2 VAL C 147  SER C 150 -1  O  VAL C 148   N  HIS C 141           
SHEET    1   J 2 TYR C 155  LEU C 157  0                                        
SHEET    2   J 2 CYS C 164  PRO C 166 -1  O  ILE C 165   N  THR C 156           
SHEET    1   K 8 GLN D  20  GLU D  21  0                                        
SHEET    2   K 8 LYS D 156  VAL D 163 -1  O  MET D 157   N  GLN D  20           
SHEET    3   K 8 MET D 180  ALA D 183 -1  O  CYS D 182   N  VAL D 163           
SHEET    4   K 8 GLY D 226  LYS D 230 -1  O  TYR D 228   N  PHE D 181           
SHEET    5   K 8 THR D 206  TRP D 215 -1  N  TRP D 215   O  ILE D 227           
SHEET    6   K 8 PRO D 198  PHE D 203 -1  N  HIS D 199   O  THR D 210           
SHEET    7   K 8 THR D 135  GLY D 140 -1  N  ILE D 137   O  VAL D 200           
SHEET    8   K 8 LYS D 156  VAL D 163 -1  O  VAL D 160   N  GLY D 136           
SHEET    1   L 7 ALA D  81  HIS D  83  0                                        
SHEET    2   L 7 LYS D  65  VAL D  68 -1  N  VAL D  66   O  HIS D  83           
SHEET    3   L 7 GLN D  30  ILE D  34 -1  N  LEU D  32   O  ARG D  67           
SHEET    4   L 7 GLY D  40  ILE D  46 -1  O  CYS D  42   N  LEU D  33           
SHEET    5   L 7 TYR D  51  THR D  54 -1  O  LEU D  53   N  THR D  45           
SHEET    6   L 7 ALA D 104  LEU D 108 -1  O  LEU D 106   N  ILE D  52           
SHEET    7   L 7 VAL D  85  LYS D  90 -1  N  GLU D  86   O  ARG D 107           
SSBOND   1 CYS A   90    CYS A  101                          1555   1555  2.04  
SSBOND   2 CYS A   95    CYS A  110                          1555   1555  2.03  
SSBOND   3 CYS A  112    CYS A  121                          1555   1555  2.04  
SSBOND   4 CYS A  129    CYS A  140                          1555   1555  2.04  
SSBOND   5 CYS A  136    CYS A  149                          1555   1555  2.04  
SSBOND   6 CYS A  151    CYS A  164                          1555   1555  2.04  
SSBOND   7 CYS A  172    CYS B  122                          1555   1555  2.04  
SSBOND   8 CYS B   22    CYS B   27                          1555   1555  2.05  
SSBOND   9 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND  10 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND  11 CYS B  191    CYS B  220                          1555   1555  2.03  
SSBOND  12 CYS C   90    CYS C  101                          1555   1555  2.04  
SSBOND  13 CYS C   95    CYS C  110                          1555   1555  2.03  
SSBOND  14 CYS C  112    CYS C  121                          1555   1555  2.05  
SSBOND  15 CYS C  129    CYS C  140                          1555   1555  2.04  
SSBOND  16 CYS C  136    CYS C  149                          1555   1555  2.04  
SSBOND  17 CYS C  151    CYS C  164                          1555   1555  2.04  
SSBOND  18 CYS C  172    CYS D  122                          1555   1555  2.05  
SSBOND  19 CYS D   22    CYS D   27                          1555   1555  2.04  
SSBOND  20 CYS D   42    CYS D   58                          1555   1555  2.06  
SSBOND  21 CYS D  168    CYS D  182                          1555   1555  2.04  
SSBOND  22 CYS D  191    CYS D  220                          1555   1555  2.03  
SITE     1 AC1 15 GLU B  97  THR B  98  TYR B  99  GLU B 147                    
SITE     2 AC1 15 ASP B 189  ALA B 190  CYS B 191  GLN B 192                    
SITE     3 AC1 15 VAL B 213  TRP B 215  GLY B 216  GLY B 218                    
SITE     4 AC1 15 CYS B 220  GLY B 226  ILE B 227                               
SITE     1 AC2 17 ASN A 120  GLU D  97  TYR D  99  GLU D 147                    
SITE     2 AC2 17 ASP D 189  ALA D 190  CYS D 191  GLN D 192                    
SITE     3 AC2 17 VAL D 213  TRP D 215  GLY D 216  GLY D 218                    
SITE     4 AC2 17 CYS D 220  GLY D 226  ILE D 227  HOH D 333                    
SITE     5 AC2 17 HOH D 374                                                     
SITE     1 AC3  5 ASP B  70  ASN B  72  THR B  73  GLN B  75                    
SITE     2 AC3  5 GLU B  80                                                     
SITE     1 AC4  4 ASP D  70  ASN D  72  GLN D  75  GLU D  80                    
SITE     1 AC5  6 TYR B 185  ASP B 185A LYS B 186  ALA B 221                    
SITE     2 AC5  6 ARG B 222  LYS B 224                                          
SITE     1 AC6  5 TYR D 185  ASP D 185A LYS D 186  ALA D 221                    
SITE     2 AC6  5 ARG D 222                                                     
SITE     1 AC7  6 ARG B 125  ASN B 179  ALA B 233  LYS B 236                    
SITE     2 AC7  6 HOH B 366  HOH B 412                                          
SITE     1 AC8  8 PHE D 101  ARG D 125  ASN D 179  ALA D 233                    
SITE     2 AC8  8 LYS D 236  HOH D 349  HOH D 389  HOH D 418                    
SITE     1 AC9  5 PRO A 166  GLY A 168  GOL A 203  HOH A 215                    
SITE     2 AC9  5 HOH A 222                                                     
SITE     1 BC1  2 LEU A 157  HOH A 213                                          
SITE     1 BC2  4 PRO A 171  LYS A 174  LEU A 177  GOL A 201                    
SITE     1 BC3  5 PRO B 124  LEU B 235  ASP B 239  HOH B 337                    
SITE     2 BC3  5 HOH B 398                                                     
SITE     1 BC4  4 LEU D 123  PRO D 124  ASP D 239  HOH D 412                    
SITE     1 BC5  4 ARG D  93  THR D  95  ASP D 100  HOH D 367                    
SITE     1 BC6  6 SER A 130  THR B 132  VAL D  87  VAL D  88                    
SITE     2 BC6  6 ILE D  89  HOH D 378                                          
SITE     1 BC7  3 ASP B 185A THR B 185B LYS B 186                               
SITE     1 BC8  4 TYR D 185  ASP D 185A THR D 185B LYS D 186                    
CRYST1   62.311   78.861   73.850  90.00 102.82  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      0.016049  0.000000  0.003652        0.00000                         
SCALE2      0.000000  0.012681  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013887        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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