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Database: PDB
Entry: 2VJ8
LinkDB: 2VJ8
Original site: 2VJ8 
HEADER    HYDROLASE                               07-DEC-07   2VJ8              
TITLE     COMPLEX OF HUMAN LEUKOTRIENE A4 HYDROLASE WITH A HYDROXAMIC ACID      
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LTA4H PROTEIN;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUKOTRIENE A4 HYDROLASE;                                   
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PT3-MB4                                   
KEYWDS    HYDROXAMIC ACID, LEUKOTRIENE HYDROLASE, ZINC, PROTEASE, HYDROLASE,    
KEYWDS   2 METALLOPROTEASE                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.G.M.THUNNISSEN,B.ANDERSSON,C.-H.WONG,B.SAMUELSSON,J.Z.HAEGGSTROM  
REVDAT   4   27-FEB-19 2VJ8    1       REMARK                                   
REVDAT   3   17-JAN-18 2VJ8    1       REMARK                                   
REVDAT   2   24-FEB-09 2VJ8    1       VERSN                                    
REVDAT   1   15-JAN-08 2VJ8    0                                                
JRNL        AUTH   M.M.G.M.THUNNISSEN,B.ANDERSSON,C.-H.WONG,B.SAMUELSSON,       
JRNL        AUTH 2 J.Z.HAEGGSTROM                                               
JRNL        TITL   CRYSTAL STRUCTURES OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX    
JRNL        TITL 2 WITH CAPTOPRIL AND TWO COMPETITIVE TIGHT-BINDING INHIBITORS  
JRNL        REF    FASEB J.                      V.  16  1648 2002              
JRNL        REFN                   ISSN 0892-6638                               
JRNL        PMID   12207002                                                     
JRNL        DOI    10.1096/FJ.01-1017FJE                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 2.0                                              
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 62521                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1950                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.235                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.10                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4877                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 599                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 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  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2VJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034707.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.991                              
REMARK 200  MONOCHROMATOR                  : S (111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62521                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1HS6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, IMIDAZOLE, SODIUM               
REMARK 280  ACETATE,YTTERBIUM CHLORIDE, BESTATIN, PH 6.8, LIQUID DIFFUSION,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       33.88500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.23500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.88500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.23500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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      HOH A2508  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     MET A     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  YB     YB A  1613     O    HOH A  2097              1.38            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2199     O    HOH A  2199     2665     1.16            
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    GLN A  79       72.27   -115.07                                   
REMARK 500    SER A  80     -127.20     48.12                                   
REMARK 500    LYS A 126       -1.01     66.00                                   
REMARK 500    PRO A 184      179.99    -50.36                                   
REMARK 500    SER A 185      -24.09     82.58                                   
REMARK 500    GLU A 271       42.98    -68.12                                   
REMARK 500    CYS A 274      -10.38     75.34                                   
REMARK 500    LEU A 275       81.34   -154.13                                   
REMARK 500    PHE A 432       42.55    -97.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2058        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A2064        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH A2168        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A2197        DISTANCE =  6.56 ANGSTROMS                       
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                              ZN A1611  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 299   NE2                                                    
REMARK 620 2 HIS A 295   NE2 102.7                                              
REMARK 620 3 GLU A 318   OE1 106.1 101.5                                        
REMARK 620 4 HA2 A1616   O2  132.6 103.9 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1612  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 422   OD1                                                    
REMARK 620 2 ASP A 481   OD1 135.0                                              
REMARK 620 3 HOH A2460   O    72.0  77.3                                        
REMARK 620 4 HOH A2461   O    75.8  67.0  80.0                                  
REMARK 620 5 ASP A 422   OD2  55.2 140.3  71.7 128.6                            
REMARK 620 6 ASP A 426   OD1  77.2 117.1 145.8  78.4 102.4                      
REMARK 620 7 ASP A 426   OD2  93.4 130.5 140.7 132.8  70.1  54.4                
REMARK 620 8 ASP A 481   OD2 148.0  54.0 130.8  86.0 144.4  73.5  79.9          
REMARK 620 9 HOH A2456   O   132.9  76.2  87.5 142.9  78.3 125.1  76.1  76.1    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1613  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 107   OE1                                                    
REMARK 620 2 GLU A 107   OE2  55.1                                              
REMARK 620 3 HOH A2096   O    83.0  92.6                                        
REMARK 620 4 HOH A2098   O   128.7  75.8  85.9                                  
REMARK 620 5 GLU A 127   OE1 145.6 159.3  90.2  83.9                            
REMARK 620 6 HOH A2133   O    81.2 135.1  91.7 149.1  65.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1617  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2132   O                                                      
REMARK 620 2 GLU A 127   OE2  83.3                                              
REMARK 620 3 HOH A2041   O    83.5 157.2                                        
REMARK 620 4 HOH A2097   O   101.1  70.0  94.4                                  
REMARK 620 5 HOH A2131   O   134.9  94.7 107.8 120.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A1612                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A1617                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A1613                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HA2 A1616                 
DBREF  2VJ8 A    0   610  UNP    Q6IAT6   Q6IAT6_HUMAN     1    611             
SEQRES   1 A  611  MET PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO          
SEQRES   2 A  611  ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS          
SEQRES   3 A  611  SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA          
SEQRES   4 A  611  ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER          
SEQRES   5 A  611  LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL          
SEQRES   6 A  611  VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU          
SEQRES   7 A  611  ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU          
SEQRES   8 A  611  PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU          
SEQRES   9 A  611  ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN          
SEQRES  10 A  611  TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO          
SEQRES  11 A  611  TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA          
SEQRES  12 A  611  ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR          
SEQRES  13 A  611  TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA          
SEQRES  14 A  611  LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO          
SEQRES  15 A  611  GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS          
SEQRES  16 A  611  VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY          
SEQRES  17 A  611  ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL          
SEQRES  18 A  611  TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU          
SEQRES  19 A  611  PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP          
SEQRES  20 A  611  LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU          
SEQRES  21 A  611  VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN          
SEQRES  22 A  611  PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY          
SEQRES  23 A  611  ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER          
SEQRES  24 A  611  HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP          
SEQRES  25 A  611  ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU          
SEQRES  26 A  611  GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE          
SEQRES  27 A  611  ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN          
SEQRES  28 A  611  ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR          
SEQRES  29 A  611  LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL          
SEQRES  30 A  611  ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU          
SEQRES  31 A  611  LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE          
SEQRES  32 A  611  PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER          
SEQRES  33 A  611  TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU          
SEQRES  34 A  611  TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN          
SEQRES  35 A  611  VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO          
SEQRES  36 A  611  PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA          
SEQRES  37 A  611  CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU          
SEQRES  38 A  611  ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP          
SEQRES  39 A  611  LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR          
SEQRES  40 A  611  LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG          
SEQRES  41 A  611  MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER          
SEQRES  42 A  611  GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER          
SEQRES  43 A  611  LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA          
SEQRES  44 A  611  THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE          
SEQRES  45 A  611  LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA          
SEQRES  46 A  611  VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO          
SEQRES  47 A  611  VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP          
HET     ZN  A1611       1                                                       
HET     YB  A1612       1                                                       
HET     YB  A1613       1                                                       
HET    IMD  A1614       5                                                       
HET    ACT  A1615       4                                                       
HET    HA2  A1616      29                                                       
HET     YB  A1617       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     ACT ACETATE ION                                                      
HETNAM     HA2 6-[{(2S)-2-AMINO-3-[4-(BENZYLOXY)                                
HETNAM   2 HA2  PHENYL]PROPYL}(HYDROXY)AMINO]-6-OXOHEXANOIC ACID)               
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    3(YB 3+)                                                     
FORMUL   5  IMD    C3 H5 N2 1+                                                  
FORMUL   6  ACT    C2 H3 O2 1-                                                  
FORMUL   7  HA2    C22 H28 N2 O5                                                
FORMUL   9  HOH   *599(H2 O)                                                    
HELIX    1   1 GLN A   79  GLY A   83  5                                   5    
HELIX    2   2 THR A  119  THR A  123  5                                   5    
HELIX    3   3 HIS A  139  ILE A  143  5                                   5    
HELIX    4   4 TYR A  200  ILE A  202  5                                   3    
HELIX    5   5 GLU A  223  PHE A  234  1                                  12    
HELIX    6   6 GLU A  236  GLY A  249  1                                  14    
HELIX    7   7 PRO A  280  LEU A  283  5                                   4    
HELIX    8   8 SER A  290  HIS A  299  1                                  10    
HELIX    9   9 THR A  310  ASP A  312  5                                   3    
HELIX   10  10 HIS A  313  GLY A  334  1                                  22    
HELIX   11  11 GLY A  334  GLY A  357  1                                  24    
HELIX   12  12 HIS A  360  LYS A  364  5                                   5    
HELIX   13  13 ASP A  373  TYR A  378  1                                   6    
HELIX   14  14 SER A  380  LEU A  397  1                                  18    
HELIX   15  15 GLY A  399  SER A  415  1                                  17    
HELIX   16  16 THR A  420  PHE A  432  1                                  13    
HELIX   17  17 LYS A  435  ASN A  440  1                                   6    
HELIX   18  18 ASP A  443  SER A  450  1                                   8    
HELIX   19  19 THR A  465  THR A  477  1                                  13    
HELIX   20  20 LYS A  479  PHE A  486  5                                   8    
HELIX   21  21 ASN A  487  LYS A  492  5                                   6    
HELIX   22  22 SER A  495  GLN A  508  1                                  14    
HELIX   23  23 PRO A  513  ASN A  525  1                                  13    
HELIX   24  24 PHE A  526  ILE A  529  5                                   4    
HELIX   25  25 ASN A  531  SER A  545  1                                  15    
HELIX   26  26 ASP A  549  GLN A  561  1                                  13    
HELIX   27  27 ARG A  563  PHE A  577  1                                  15    
HELIX   28  28 SER A  580  LYS A  592  1                                  13    
HELIX   29  29 ALA A  593  MET A  595  5                                   3    
HELIX   30  30 HIS A  596  LEU A  607  1                                  12    
SHEET    1  AA 8 GLN A  69  GLU A  70  0                                        
SHEET    2  AA 8 LEU A  59  ILE A  66 -1  O  ILE A  66   N  GLN A  69           
SHEET    3  AA 8 GLU A  99  THR A 108 -1  O  GLU A 103   N  VAL A  65           
SHEET    4  AA 8 THR A  33  SER A  44 -1  O  LEU A  34   N  THR A 108           
SHEET    5  AA 8 CYS A  16  ASP A  28 -1  O  ARG A  17   N  GLN A  43           
SHEET    6  AA 8 LYS A 153  PRO A 163  1  O  THR A 155   N  LEU A  21           
SHEET    7  AA 8 ARG A 186  PRO A 198 -1  O  LYS A 187   N  VAL A 162           
SHEET    8  AA 8 ILE A 173  PRO A 179 -1  O  ILE A 173   N  ILE A 192           
SHEET    1  AB 3 LEU A  49  THR A  56  0                                        
SHEET    2  AB 3 SER A  84  LEU A  94 -1  O  SER A  84   N  THR A  56           
SHEET    3  AB 3 TYR A  73  LEU A  75 -1  O  ALA A  74   N  GLU A  87           
SHEET    1  AC 4 LEU A 115  LEU A 118  0                                        
SHEET    2  AC 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3  AC 4 LEU A 204  GLY A 207 -1  O  LEU A 204   N  SER A 133           
SHEET    4  AC 4 VAL A 167  MET A 170 -1  O  VAL A 167   N  GLY A 207           
SHEET    1  AD 5 GLU A 210  GLY A 215  0                                        
SHEET    2  AD 5 THR A 218  SER A 222 -1  O  THR A 218   N  ILE A 214           
SHEET    3  AD 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4  AD 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5  AD 5 GLY A 269  MET A 270 -1  O  MET A 270   N  PHE A 277           
SHEET    1  AE 2 VAL A 306  ASN A 308  0                                        
SHEET    2  AE 2 LYS A 417  ILE A 419  1  O  LYS A 417   N  THR A 307           
LINK        ZN    ZN A1611                 NE2 HIS A 299     1555   1555  1.96  
LINK        ZN    ZN A1611                 NE2 HIS A 295     1555   1555  2.05  
LINK        ZN    ZN A1611                 OE1 GLU A 318     1555   1555  1.95  
LINK        ZN    ZN A1611                 O2  HA2 A1616     1555   1555  2.02  
LINK        YB    YB A1612                 OD1 ASP A 422     1555   4557  2.30  
LINK        YB    YB A1612                 OD1 ASP A 481     1555   1555  2.54  
LINK        YB    YB A1612                 O   HOH A2460     1555   1555  2.29  
LINK        YB    YB A1612                 O   HOH A2461     1555   1555  2.35  
LINK        YB    YB A1612                 OD2 ASP A 422     1555   4557  2.48  
LINK        YB    YB A1612                 OD1 ASP A 426     1555   4557  2.35  
LINK        YB    YB A1612                 OD2 ASP A 426     1555   4557  2.35  
LINK        YB    YB A1612                 OD2 ASP A 481     1555   1555  2.31  
LINK        YB    YB A1612                 O   HOH A2456     1555   1555  2.27  
LINK        YB    YB A1613                 OE1 GLU A 107     1555   1555  2.41  
LINK        YB    YB A1613                 OE2 GLU A 107     1555   1555  2.35  
LINK        YB    YB A1613                 O   HOH A2096     1555   1555  1.84  
LINK        YB    YB A1613                 O   HOH A2098     1555   1555  2.71  
LINK        YB    YB A1613                 OE1 GLU A 127     1555   2565  2.48  
LINK        YB    YB A1613                 O   HOH A2133     1555   2565  2.41  
LINK        YB    YB A1617                 O   HOH A2132     1555   2565  2.46  
LINK        YB    YB A1617                 OE2 GLU A 127     1555   2565  2.41  
LINK        YB    YB A1617                 O   HOH A2041     1555   2565  2.20  
LINK        YB    YB A1617                 O   HOH A2097     1555   1555  2.42  
LINK        YB    YB A1617                 O   HOH A2131     1555   2565  1.64  
CISPEP   1 GLN A  136    ALA A  137          0        -0.44                     
CISPEP   2 ALA A  510    PRO A  511          0         1.78                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  HA2 A1616                    
SITE     1 AC2  6 ASP A 422  ASP A 426  ASP A 481  HOH A2456                    
SITE     2 AC2  6 HOH A2460  HOH A2461                                          
SITE     1 AC3  6 GLU A 127   YB A1613  HOH A2041  HOH A2097                    
SITE     2 AC3  6 HOH A2131  HOH A2132                                          
SITE     1 AC4  7 GLU A 107  GLU A 127   YB A1617  HOH A2096                    
SITE     2 AC4  7 HOH A2097  HOH A2098  HOH A2133                               
SITE     1 AC5  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC5  6 ALA A 504  GLN A 508                                          
SITE     1 AC6  5 LYS A 425  ASP A 426  TYR A 429  ASP A 481                    
SITE     2 AC6  5 HOH A2461                                                     
SITE     1 AC7 22 GLN A 134  GLN A 136  ALA A 137  TYR A 267                    
SITE     2 AC7 22 GLY A 268  GLY A 269  GLU A 271  HIS A 295                    
SITE     3 AC7 22 GLU A 296  HIS A 299  TRP A 311  PHE A 314                    
SITE     4 AC7 22 GLU A 318  PRO A 374  TYR A 378  TYR A 383                    
SITE     5 AC7 22 ARG A 563  LYS A 565   ZN A1611  HOH A2283                    
SITE     6 AC7 22 HOH A2558  HOH A2599                                          
CRYST1   67.770  132.470   83.700  90.00  90.00  90.00 P 21 21 2     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      0.014756  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007549  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011947        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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