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Database: PDB
Entry: 3JZ1
LinkDB: 3JZ1
Original site: 3JZ1 
HEADER    HYDROLASE                               22-SEP-09   3JZ1              
TITLE     CRYSTAL STRUCTURE OF HUMAN THROMBIN MUTANT N143P IN E:NA+ FORM        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBIN LIGHT CHAIN;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.5;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: THROMBIN HEAVY CHAIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 3.4.21.5;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F2;                                                            
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: F2;                                                            
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    SERINE PROTEASE, ACUTE PHASE, BLOOD COAGULATION, CLEAVAGE ON PAIR OF  
KEYWDS   2 BASIC RESIDUES, DISEASE MUTATION, DISULFIDE BOND, GAMMA-             
KEYWDS   3 CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, HYDROLASE, KRINGLE, PROTEASE,    
KEYWDS   4 SECRETED, ZYMOGEN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.NIU,Z.CHEN,L.A.BUSH-PELC,A.BAH,P.S.GANDHI,E.DI CERA                 
REVDAT   6   06-SEP-23 3JZ1    1       REMARK                                   
REVDAT   5   13-OCT-21 3JZ1    1       SEQADV HETSYN                            
REVDAT   4   29-JUL-20 3JZ1    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 3JZ1    1       VERSN                                    
REVDAT   2   12-JAN-10 3JZ1    1       JRNL                                     
REVDAT   1   20-OCT-09 3JZ1    0                                                
JRNL        AUTH   W.NIU,Z.CHEN,L.A.BUSH-PELC,A.BAH,P.S.GANDHI,E.DI CERA        
JRNL        TITL   MUTANT N143P REVEALS HOW NA+ ACTIVATES THROMBIN              
JRNL        REF    J.BIOL.CHEM.                  V. 284 36175 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19846563                                                     
JRNL        DOI    10.1074/JBC.M109.069500                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.O.PINEDA,C.J.CARRELL,L.A.BUSH,S.PRASAD,S.CACCIA,Z.CHEN,    
REMARK   1  AUTH 2 F.S.MATHEWS,E.DI CERA                                        
REMARK   1  TITL   MOLECULAR DISSECTION OF NA+ BINDING TO THROMBIN              
REMARK   1  REF    J.BIOL.CHEM.                  V. 279 31842 2004              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   15152000                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.S.GANDHI,Z.CHEN,F.S.MATHEWS,E.DI CERA                      
REMARK   1  TITL   STRUCTURAL IDENTIFICATION OF THE PATHWAY OF LONG-RANGE       
REMARK   1  TITL 2 COMMUNICATION IN AN ALLOSTERIC ENZYME                        
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 105  1832 2009              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   18250335                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 343924.060                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 36289                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1818                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5370                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3580                       
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 274                          
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            : 2238                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.130                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 3JZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055338.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36932                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP FROM CCP4                                      
REMARK 200 STARTING MODEL: PDB ENTRY 1SHH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NANO3 AND 20% PEG 3350, PH 6.8,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       59.98950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.83500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.98950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.83500            
REMARK 290   SMTRY3   4  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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   BIOMT1   2 -1.000000  0.000000  0.000000       -2.02536            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       50.64752            
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: 3090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 N    NO3 A 404  LIES ON A SPECIAL POSITION.                          
REMARK 375 O2   NO3 A 404  LIES ON A SPECIAL POSITION.                          
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     THR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     TYR B    76                                                      
REMARK 465     GLU B    77                                                      
REMARK 465     ARG B    77A                                                     
REMARK 465     TRP B   148                                                      
REMARK 465     THR B   149                                                      
REMARK 465     ALA B   149A                                                     
REMARK 465     ASN B   149B                                                     
REMARK 465     VAL B   149C                                                     
REMARK 465     GLY B   149D                                                     
REMARK 465     LYS B   149E                                                     
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    TRP B  60D  CB    TRP B  60D  CG     -0.126                       
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    ARG B  93   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 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   7      -87.51   -129.90                                   
REMARK 500    SER B  48     -179.25   -170.31                                   
REMARK 500    TYR B  60A      82.67   -157.11                                   
REMARK 500    PRO B  60C      -3.12    -57.25                                   
REMARK 500    ASN B  60G      76.59   -157.14                                   
REMARK 500    ILE B  79      -11.22     65.50                                   
REMARK 500    GLU B  97A     -74.56   -104.81                                   
REMARK 500    LYS B 145     -158.89    167.28                                   
REMARK 500    GLU B 146       54.04   -118.61                                   
REMARK 500    ASP B 186A      -4.41     87.50                                   
REMARK 500    GLU B 192     -112.65     45.89                                   
REMARK 500    PHE B 245     -149.85   -109.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  14J  O                                                      
REMARK 620 2 NO3 A 404   O1   81.6                                              
REMARK 620 3 NO3 A 404   N   103.8  25.9                                        
REMARK 620 4 NO3 A 404   O3  103.0  47.4  28.3                                  
REMARK 620 5 HOH A1132   O    79.7  73.3  90.4 118.4                            
REMARK 620 6 TYR B 134   OH   93.3 174.9 158.2 134.6 106.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B 221A  O                                                      
REMARK 620 2 LYS B 224   O    95.1                                              
REMARK 620 3 HOH B1119   O    87.2  97.3                                        
REMARK 620 4 HOH B1124   O   160.7  73.3  79.2                                  
REMARK 620 5 HOH B1131   O   102.2 162.4  80.6  89.1                            
REMARK 620 6 HOH B1138   O   101.1  80.2 171.5  92.2  99.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SHH   RELATED DB: PDB                                   
REMARK 900 SLOW FORM OF THROMBIN BOUND WITH PPACK                               
REMARK 900 RELATED ID: 3BEI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SLOW FORM OF THROMBIN IN A SELF-INHIBITED   
REMARK 900 CONFORMATION                                                         
REMARK 900 RELATED ID: 3JZ2   RELATED DB: PDB                                   
DBREF  3JZ1 A   -4    15  UNP    P00734   THRB_HUMAN     328    363             
DBREF  3JZ1 B   16   247  UNP    P00734   THRB_HUMAN     364    622             
SEQADV 3JZ1 PRO B  143  UNP  P00734    ASN   506 ENGINEERED MUTATION            
SEQRES   1 A   36  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   2 A   36  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   3 A   36  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 B  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 B  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 B  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 B  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 B  259  ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 B  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 B  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 B  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 B  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 B  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 B  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY PRO          
SEQRES  12 B  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 B  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 B  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 B  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 B  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 B  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 B  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 B  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 B  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
MODRES 3JZ1 ASN B   60G ASN  GLYCOSYLATION SITE                                 
HET     NA  A 402       1                                                       
HET    NO3  A 404       4                                                       
HET    NAG  B 301      14                                                       
HET     NA  B 401       1                                                       
HET    NO3  B 403       4                                                       
HET    GOL  B 405       6                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     NO3 NITRATE ION                                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   4  NO3    2(N O3 1-)                                                   
FORMUL   5  NAG    C8 H15 N O6                                                  
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *214(H2 O)                                                    
HELIX    1   1 PHE A    7  SER A   11  5                                   5    
HELIX    2   2 THR A   14B ASP A   14L 1                                  11    
HELIX    3   3 ALA B   55  CYS B   58  5                                   4    
HELIX    4   4 PRO B   60B ASP B   60E 5                                   4    
HELIX    5   5 THR B   60I ASN B   62  5                                   3    
HELIX    6   6 ASP B  125  LEU B  130  1                                   9    
HELIX    7   7 GLU B  164  SER B  171  1                                   8    
HELIX    8   8 CYS B  191  SER B  195  5                                   5    
HELIX    9   9 LEU B  234  PHE B  245  1                                  12    
SHEET    1   A 7 SER B  20  ASP B  21  0                                        
SHEET    2   A 7 GLN B 156  PRO B 161 -1  O  VAL B 157   N  SER B  20           
SHEET    3   A 7 LYS B 135  GLY B 140 -1  N  VAL B 138   O  VAL B 158           
SHEET    4   A 7 PRO B 198  LYS B 202 -1  O  VAL B 200   N  ARG B 137           
SHEET    5   A 7 TRP B 207  TRP B 215 -1  O  TYR B 208   N  MET B 201           
SHEET    6   A 7 GLY B 226  HIS B 230 -1  O  PHE B 227   N  TRP B 215           
SHEET    7   A 7 MET B 180  ALA B 183 -1  N  PHE B 181   O  TYR B 228           
SHEET    1   B 7 LYS B  81  SER B  83  0                                        
SHEET    2   B 7 LEU B  64  ILE B  68 -1  N  ILE B  68   O  LYS B  81           
SHEET    3   B 7 GLN B  30  ARG B  35 -1  N  PHE B  34   O  LEU B  65           
SHEET    4   B 7 GLU B  39  LEU B  46 -1  O  LEU B  41   N  LEU B  33           
SHEET    5   B 7 TRP B  51  THR B  54 -1  O  LEU B  53   N  SER B  45           
SHEET    6   B 7 ALA B 104  LEU B 108 -1  O  MET B 106   N  VAL B  52           
SHEET    7   B 7 LEU B  85  ILE B  90 -1  N  GLU B  86   O  LYS B 107           
SHEET    1   C 2 LEU B  60  TYR B  60A 0                                        
SHEET    2   C 2 LYS B  60F ASN B  60G-1  O  LYS B  60F  N  TYR B  60A          
SSBOND   1 CYS A    1    CYS B  122                          1555   1555  2.04  
SSBOND   2 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   3 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND   4 CYS B  191    CYS B  220                          1555   1555  2.03  
LINK         ND2 ASN B  60G                C1  NAG B 301     1555   1555  1.47  
LINK         O   TYR A  14J               NA    NA A 402     1555   1555  2.30  
LINK        NA    NA A 402                 O1  NO3 A 404     1555   1555  2.80  
LINK        NA    NA A 402                 N   NO3 A 404     1555   1555  2.55  
LINK        NA    NA A 402                 O3  NO3 A 404     1555   1555  2.37  
LINK        NA    NA A 402                 O   HOH A1132     1555   1555  2.38  
LINK        NA    NA A 402                 OH  TYR B 134     1555   1555  2.35  
LINK         O   ARG B 221A               NA    NA B 401     1555   1555  2.42  
LINK         O   LYS B 224                NA    NA B 401     1555   1555  2.30  
LINK        NA    NA B 401                 O   HOH B1119     1555   1555  2.85  
LINK        NA    NA B 401                 O   HOH B1124     1555   1555  2.37  
LINK        NA    NA B 401                 O   HOH B1131     1555   1555  2.12  
LINK        NA    NA B 401                 O   HOH B1138     1555   1555  2.37  
CISPEP   1 SER B   36A   PRO B   37          0        -3.19                     
CRYST1  119.979   47.670   50.688  90.00  92.29  90.00 C 1 2 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      0.008335  0.000000  0.000333        0.00000                         
SCALE2      0.000000  0.020978  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019744        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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