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Database: PDB
Entry: 1SQM
LinkDB: 1SQM
Original site: 1SQM 
HEADER    HYDROLASE                               19-MAR-04   1SQM              
TITLE     STRUCTURE OF [R563A] LEUKOTRIENE A4 HYDROLASE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE; LEUKOTRIENE A(4) HYDROLASE;                
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT3-MB4                                   
KEYWDS    EPOXIDE HYDROLASE; ALPHA-BETA PROTEIN; LEUKOTRIENE BIOSYNTHESIS;      
KEYWDS   2 METALLOPROTEASE, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.O.T.THOLANDER,P.C.RUDBERG,M.M.G.M.THUNNISSEN,J.Z.HAEGGSTROM         
REVDAT   4   20-NOV-19 1SQM    1       LINK                                     
REVDAT   3   11-OCT-17 1SQM    1       REMARK                                   
REVDAT   2   24-FEB-09 1SQM    1       VERSN                                    
REVDAT   1   03-AUG-04 1SQM    0                                                
JRNL        AUTH   P.C.RUDBERG,F.O.T.THOLANDER,M.ANDBERG,M.M.G.M.THUNNISSEN     
JRNL        TITL   LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON         
JRNL        TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND   
JRNL        TITL 3 AMINOPEPTIDASE SUBSTRATES                                    
JRNL        REF    J.BIOL.CHEM.                  V. 279 27376 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15078870                                                     
JRNL        DOI    10.1074/JBC.M401031200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 29962                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4871                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 598                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.445                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.849                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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 1SQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000021923.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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) : 0.96800                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30528                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09200                            
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) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, IMIDEAZOLE     
REMARK 280  PH 6.8, YBCL2, BESTATIN, PH 8.0, LIQUID DIFFUSION, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.47500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.42500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.47500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.42500            
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 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 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    SER A  80     -127.54     27.56                                   
REMARK 500    ASN A  97       -0.18     74.97                                   
REMARK 500    ASP A 183       88.10    171.41                                   
REMARK 500    SER A 222     -179.45   -177.45                                   
REMARK 500    GLU A 271       44.45    -74.47                                   
REMARK 500    CYS A 274      -16.83     78.83                                   
REMARK 500    SER A 379     -165.70   -165.69                                   
REMARK 500    PHE A 432       44.46   -101.59                                   
REMARK 500    LYS A 435       27.08   -144.48                                   
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                              YB A2001  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  47   OD1                                                    
REMARK 620 2 ASP A  47   OD2  50.9                                              
REMARK 620 3 HOH A3382   O    72.7 123.6                                        
REMARK 620 4 HOH A3300   O    83.0  69.9 108.4                                  
REMARK 620 5 ASP A 481   OD1  35.6  27.0 102.4  91.8                            
REMARK 620 6 ASP A 481   OD2  35.9  27.0 102.6  91.9   0.3                      
REMARK 620 7 HOH A3187   O   147.6 141.8  87.1  79.6 168.9 168.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 105.5                                              
REMARK 620 3 GLU A 318   OE1 105.5 106.5                                        
REMARK 620 4 ACY A3001   O   106.0 134.9  95.1                                  
REMARK 620 5 ACY A3001   OXT  88.5  93.3 151.2  56.4                            
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 A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 3001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GW6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT                   
REMARK 900 RELATED ID: 1H19   RELATED DB: PDB                                   
REMARK 900 [E271Q] LEUKOTRIENE A4 HYDROLASE                                     
REMARK 900 RELATED ID: 1HS6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN        
DBREF  1SQM A    1   610  UNP    P09960   LKHA4_HUMAN      1    610             
SEQADV 1SQM ALA A  563  UNP  P09960    ARG   563 ENGINEERED                     
SEQRES   1 A  610  PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO ALA          
SEQRES   2 A  610  SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS SER          
SEQRES   3 A  610  VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA ALA          
SEQRES   4 A  610  LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER LEU          
SEQRES   5 A  610  VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL VAL          
SEQRES   6 A  610  ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU ARG          
SEQRES   7 A  610  GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU PRO          
SEQRES   8 A  610  ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU ILE          
SEQRES   9 A  610  SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN TRP          
SEQRES  10 A  610  LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO TYR          
SEQRES  11 A  610  LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA ILE          
SEQRES  12 A  610  LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR TYR          
SEQRES  13 A  610  THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA LEU          
SEQRES  14 A  610  MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO GLU          
SEQRES  15 A  610  ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS VAL          
SEQRES  16 A  610  PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY ALA          
SEQRES  17 A  610  LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL TRP          
SEQRES  18 A  610  SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU PHE          
SEQRES  19 A  610  SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP LEU          
SEQRES  20 A  610  GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU VAL          
SEQRES  21 A  610  LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN PRO          
SEQRES  22 A  610  CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY ASP          
SEQRES  23 A  610  LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER HIS          
SEQRES  24 A  610  SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP ASP          
SEQRES  25 A  610  HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU GLU          
SEQRES  26 A  610  ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE ARG          
SEQRES  27 A  610  HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN ASN          
SEQRES  28 A  610  SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR LYS          
SEQRES  29 A  610  LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL ALA          
SEQRES  30 A  610  TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU LEU          
SEQRES  31 A  610  PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE PHE          
SEQRES  32 A  610  LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER TYR          
SEQRES  33 A  610  LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU TYR          
SEQRES  34 A  610  SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN VAL          
SEQRES  35 A  610  ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO PRO          
SEQRES  36 A  610  ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA CYS          
SEQRES  37 A  610  ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU ASP          
SEQRES  38 A  610  ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP LEU          
SEQRES  39 A  610  SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR LEU          
SEQRES  40 A  610  GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG MET          
SEQRES  41 A  610  GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER GLU          
SEQRES  42 A  610  ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER LYS          
SEQRES  43 A  610  TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA THR          
SEQRES  44 A  610  GLU GLN GLY ALA MET LYS PHE THR ARG PRO LEU PHE LYS          
SEQRES  45 A  610  ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA VAL          
SEQRES  46 A  610  ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO VAL          
SEQRES  47 A  610  THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP              
HET     ZN  A1001       1                                                       
HET     YB  A2001       1                                                       
HET    IMD  A2002       5                                                       
HET    ACY  A3001       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    YB 3+                                                        
FORMUL   4  IMD    C3 H5 N2 1+                                                  
FORMUL   5  ACY    C2 H4 O2                                                     
FORMUL   6  HOH   *598(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 PRO A  198  ILE A  202  5                                   5    
HELIX    5   5 GLU A  223  GLU A  225  5                                   3    
HELIX    6   6 GLN A  226  PHE A  234  1                                   9    
HELIX    7   7 GLU A  236  GLY A  249  1                                  14    
HELIX    8   8 PRO A  280  LEU A  283  5                                   4    
HELIX    9   9 SER A  290  HIS A  299  1                                  10    
HELIX   10  10 THR A  310  ASP A  312  5                                   3    
HELIX   11  11 HIS A  313  GLY A  334  1                                  22    
HELIX   12  12 GLY A  334  GLY A  357  1                                  24    
HELIX   13  13 HIS A  360  LYS A  364  5                                   5    
HELIX   14  14 ASP A  373  TYR A  378  1                                   6    
HELIX   15  15 SER A  380  LEU A  397  1                                  18    
HELIX   16  16 GLY A  399  SER A  415  1                                  17    
HELIX   17  17 THR A  420  PHE A  432  1                                  13    
HELIX   18  18 LYS A  435  ASN A  440  1                                   6    
HELIX   19  19 ASP A  443  SER A  450  1                                   8    
HELIX   20  20 THR A  465  ALA A  478  1                                  14    
HELIX   21  21 LYS A  479  PHE A  486  5                                   8    
HELIX   22  22 ASN A  487  LYS A  492  5                                   6    
HELIX   23  23 SER A  495  GLN A  508  1                                  14    
HELIX   24  24 PRO A  513  ASN A  525  1                                  13    
HELIX   25  25 PHE A  526  ILE A  529  5                                   4    
HELIX   26  26 ASN A  531  SER A  545  1                                  15    
HELIX   27  27 ASP A  549  GLN A  561  1                                  13    
HELIX   28  28 ALA A  563  PHE A  577  1                                  15    
HELIX   29  29 SER A  580  LYS A  592  1                                  13    
HELIX   30  30 ALA A  593  MET A  595  5                                   3    
HELIX   31  31 HIS A  596  LYS A  608  1                                  13    
SHEET    1   A 8 GLN A  69  GLU A  70  0                                        
SHEET    2   A 8 THR A  60  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3   A 8 GLU A  99  GLU A 107 -1  O  SER A 105   N  LYS A  63           
SHEET    4   A 8 THR A  33  SER A  44 -1  N  ALA A  38   O  ILE A 104           
SHEET    5   A 8 CYS A  16  ASP A  28 -1  N  ARG A  17   O  GLN A  43           
SHEET    6   A 8 LEU A 154  PRO A 163  1  O  SER A 161   N  VAL A  27           
SHEET    7   A 8 ARG A 186  ILE A 197 -1  O  GLN A 193   N  TYR A 156           
SHEET    8   A 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1   B 3 LEU A  49  LEU A  54  0                                        
SHEET    2   B 3 MET A  86  LEU A  94 -1  O  MET A  86   N  LEU A  54           
SHEET    3   B 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1   C 4 LEU A 115  LEU A 118  0                                        
SHEET    2   C 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3   C 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4   C 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1   D 5 GLU A 210  GLY A 215  0                                        
SHEET    2   D 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3   D 5 ASP A 257  VAL A 260  1  O  VAL A 260   N  TRP A 221           
SHEET    4   D 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5   D 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1   E 2 VAL A 306  ASN A 308  0                                        
SHEET    2   E 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OD1 ASP A  47                YB    YB A2001     1555   1555  2.57  
LINK         OD2 ASP A  47                YB    YB A2001     1555   1555  2.57  
LINK         NE2 HIS A 295                ZN    ZN A1001     1555   1555  2.14  
LINK         NE2 HIS A 299                ZN    ZN A1001     1555   1555  2.09  
LINK         OE1 GLU A 318                ZN    ZN A1001     1555   1555  2.06  
LINK        ZN    ZN A1001                 O   ACY A3001     1555   1555  2.16  
LINK        ZN    ZN A1001                 OXT ACY A3001     1555   1555  2.61  
LINK        YB    YB A2001                 O   HOH A3382     1555   1555  2.94  
LINK        YB    YB A2001                 O   HOH A3300     1555   1555  2.98  
LINK         OD1 ASP A 481                YB    YB A2001     1555   1565  2.53  
LINK         OD2 ASP A 481                YB    YB A2001     1555   1565  2.50  
LINK        YB    YB A2001                 O   HOH A3187     1555   1545  2.67  
CISPEP   1 GLN A  136    ALA A  137          0         1.42                     
CISPEP   2 ALA A  510    PRO A  511          0         0.37                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  ACY A3001                    
SITE     1 AC2  5 ASP A  47  ASP A 481  HOH A3187  HOH A3300                    
SITE     2 AC2  5 HOH A3382                                                     
SITE     1 AC3  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC3  6 ALA A 504  GLN A 508                                          
SITE     1 AC4  8 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC4  8 HIS A 299  GLU A 318  TYR A 383   ZN A1001                    
CRYST1   78.000   86.850   98.950  90.00  90.00  90.00 P 21 21 21    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      0.012821  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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