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Database: PDB
Entry: 5FWQ
LinkDB: 5FWQ
Original site: 5FWQ 
HEADER    HYDROLASE                               19-FEB-16   5FWQ              
TITLE     APO STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN LEUKOTRIENE A4 HYDROLASE;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A(4) HYDROLASE, HUMAN          
COMPND   5 LEUKOTRIENE A4 HYDROLASE;                                            
COMPND   6 EC: 3.3.2.6;                                                         
COMPND   7 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: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET 24                                     
KEYWDS    HYDROLASE, LEUKOTRIENE (LT) A4 HYDROLASE/AMINOPEPTIDASE, LTA4H        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.WITTMANN,L.KALINOWSKY,J.KRAMER,R.BLOECHER,D.STEINHILBER,          
AUTHOR   2 D.POGORYELOV,E.PROSCHAK,J.HEERING                                    
REVDAT   3   08-MAY-19 5FWQ    1       JRNL   REMARK                            
REVDAT   2   09-NOV-16 5FWQ    1       JRNL                                     
REVDAT   1   05-OCT-16 5FWQ    0                                                
JRNL        AUTH   S.K.WITTMANN,L.KALINOWSKY,J.S.KRAMER,R.BLOECHER,S.KNAPP,     
JRNL        AUTH 2 D.STEINHILBER,D.POGORYELOV,E.PROSCHAK,J.HEERING              
JRNL        TITL   THERMODYNAMIC PROPERTIES OF LEUKOTRIENE A4HYDROLASE          
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.              V.  24  5243 2016              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   27651294                                                     
JRNL        DOI    10.1016/J.BMC.2016.08.047                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.K.WITTMANN,L.KALINOWSKY,J.S.KRAMER,R.BLOECHER,S.KNAPP,     
REMARK   1  AUTH 2 D.STEINHILBER,D.POGORYELOV,E.PROSCHAK,J.HEERING              
REMARK   1  TITL   THERMODYNAMIC PROPERTIES OF LEUKOTRIENE A4 HYDROLASE         
REMARK   1  TITL 2 INHIBITORS.                                                  
REMARK   1  REF    BIOORG.MED.CHEM.              V.  24  5243 2016              
REMARK   1  REFN                   ISSN 0968-0896                               
REMARK   1  PMID   27651294                                                     
REMARK   1  DOI    10.1016/J.BMC.2016.08.047                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.140                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 40948                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1374                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.3051 -  4.4098    1.00     7650   138  0.1808 0.1538        
REMARK   3     2  4.4098 -  3.5005    1.00     7660   139  0.1597 0.2052        
REMARK   3     3  3.5005 -  3.0581    1.00     7656   132  0.1840 0.2430        
REMARK   3     4  3.0581 -  2.7785    1.00     7651   136  0.1974 0.2243        
REMARK   3     5  2.7785 -  2.5794    1.00     7642   137  0.1971 0.2582        
REMARK   3     6  2.5794 -  2.4273    1.00     7700   137  0.2091 0.2856        
REMARK   3     7  2.4273 -  2.3058    1.00     7629   141  0.2081 0.2383        
REMARK   3     8  2.3058 -  2.2054    1.00     7655   141  0.2234 0.2662        
REMARK   3     9  2.2054 -  2.1205    1.00     7605   138  0.2356 0.2514        
REMARK   3    10  2.1205 -  2.0473    0.98     7560   135  0.2479 0.2859        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4988                                  
REMARK   3   ANGLE     :  1.008           6774                                  
REMARK   3   CHIRALITY :  0.044            754                                  
REMARK   3   PLANARITY :  0.004            864                                  
REMARK   3   DIHEDRAL  : 14.167           1827                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290066258.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000040                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40948                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 13.30                              
REMARK 200  R MERGE                    (I) : 0.31000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.16000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.870                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MR                                             
REMARK 200 STARTING MODEL: PDB ENTRY 5AEN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS-HCL, 25     
REMARK 280  MM KCL, 4-8 MG/ML PROTEIN (PH8); PRECIPITATE SOLUTION: 0,15M        
REMARK 280  IMIDAZOL/HCL PH6.5; 0,1 M NAACETAT, 14% PEG8000, 5 MM YBCL3 AND     
REMARK 280  25 MM 5-CHLORO-3-HYDROXYPYRIDINE; HANGING DROP VAPOR-DIFFUSION      
REMARK 280  AT 290.55 K, VAPOR DIFFUSION, HANGING DROP                          
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       38.16850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.15500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.15500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.16850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.49000            
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: PISA                                                  
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 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   -14                                                      
REMARK 465     ALA A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     MET A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLN A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     MET A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     LEU A   611                                                      
REMARK 465     GLU A   612                                                      
REMARK 465     HIS A   613                                                      
REMARK 465     HIS A   614                                                      
REMARK 465     HIS A   615                                                      
REMARK 465     HIS A   616                                                      
REMARK 465     HIS A   617                                                      
REMARK 465     HIS A   618                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 401    CD   OE1  OE2                                       
REMARK 470     ARG A 586    CZ   NH1  NH2                                       
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   O    HOH A  2195     O    HOH A  2283              2.14            
REMARK 500   O    HOH A  2202     O    HOH A  2384              2.17            
REMARK 500   O    HOH A  2312     O    HOH A  2313              2.19            
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  2036     O    HOH A  2407     1565     2.10            
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       60.17   -102.98                                   
REMARK 500    SER A  80     -134.05     60.76                                   
REMARK 500    GLU A 271       36.12    -78.53                                   
REMARK 500    CYS A 274      -13.78     70.66                                   
REMARK 500    LEU A 275       80.11   -153.31                                   
REMARK 500    ASP A 286       13.56   -144.63                                   
REMARK 500    TRP A 301      -63.17   -109.67                                   
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                              ZN A1612  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A1611   O                                                      
REMARK 620 2 GLU A 318   OE1 104.4                                              
REMARK 620 3 HIS A 299   NE2 126.1 106.1                                        
REMARK 620 4 HIS A 295   NE2 113.2 105.3 100.0                                  
REMARK 620 N                    1     2     3                                   
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 ASP A 481   OD1                                                    
REMARK 620 2 ASP A 481   OD2  46.1                                              
REMARK 620 3 ASP A  47   OD1 113.8  73.6                                        
REMARK 620 4 ASP A  47   OD2 122.0  79.3  50.4                                  
REMARK 620 5 HOH A2036   O    78.4  83.5 125.4  77.2                            
REMARK 620 6 HOH A2330   O    71.4  82.7  77.2 127.5 148.3                      
REMARK 620 7 HOH A2406   O   152.6 146.1  72.9  83.5 120.7  85.1                
REMARK 620 8 HOH A2331   O    79.9 126.0 148.1 147.1  84.6  80.7  82.5          
REMARK 620 9 HOH A2407   O   116.3 124.8 119.9  75.4  43.5 149.6  77.6  72.5    
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 A1614  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE2                                                    
REMARK 620 2 GLU A 121   OE1  96.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1615  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 426   OD2                                                    
REMARK 620 2 ASP A 426   OD1  50.4                                              
REMARK 620 3 ASP A 422   OD1  92.2  79.9                                        
REMARK 620 4 ASP A 422   OD2  73.5 102.0  50.0                                  
REMARK 620 5 HOH A2294   O    89.7  81.3 153.8 153.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1616  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD2                                                    
REMARK 620 2 ASP A 481   OD1  55.9                                              
REMARK 620 3 ASP A  47   OD1  76.9 122.4                                        
REMARK 620 4 ASP A  47   OD2  86.3 140.4  47.2                                  
REMARK 620 5 HOH A2036   O    99.7  93.5 128.1  81.0                            
REMARK 620 6 HOH A2330   O    88.1  75.8  71.2 117.8 160.3                      
REMARK 620 7 HOH A2331   O   141.1  85.7 127.5 132.6  87.4  75.4                
REMARK 620 8 HOH A2406   O   138.0 144.1  61.7  71.7 111.0  72.6  70.2          
REMARK 620 9 HOH A2407   O   139.2 128.6 108.4  71.7  44.3 132.5  68.2  67.0    
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 A1617  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD1                                                    
REMARK 620 2 HOH A2031   O    85.6                                              
REMARK 620 3 GLU A  46   OE1 157.9  76.9                                        
REMARK 620 4 GLU A  46   OE2 148.5 125.1  52.1                                  
REMARK 620 5 ASP A 175   O    67.2 128.3 134.7  86.0                            
REMARK 620 6 HOH A2138   O    72.2 142.3 114.5  83.8  70.6                      
REMARK 620 7 HOH A2032   O    90.9  44.1  86.0 106.6  91.4 158.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A2612  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2138   O                                                      
REMARK 620 2 HOH A2031   O   151.3                                              
REMARK 620 3 HOH A2032   O   155.7  44.9                                        
REMARK 620 4 ASP A 175   OD1  74.5  90.1  91.9                                  
REMARK 620 5 ASP A 175   O    69.3 126.6  86.9  66.3                            
REMARK 620 6 GLU A  46   OE2  81.9 121.9  99.0 143.4  79.5                      
REMARK 620 7 GLU A  46   OE1 114.0  77.8  83.4 166.7 125.6  49.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 2612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1611                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1618                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1619                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1620                
DBREF  5FWQ A    0   610  UNP    P09960   LKHA4_HUMAN      1    611             
SEQADV 5FWQ MET A  -14  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ ALA A  -13  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ SER A  -12  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ MET A  -11  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ THR A  -10  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLY A   -9  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLY A   -8  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLN A   -7  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLN A   -6  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ MET A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLY A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ ARG A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLY A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ SER A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ LEU A  611  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ GLU A  612  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  613  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  614  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  615  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  616  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  617  UNP  P09960              EXPRESSION TAG                 
SEQADV 5FWQ HIS A  618  UNP  P09960              EXPRESSION TAG                 
SEQRES   1 A  633  MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY          
SEQRES   2 A  633  SER MET PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER          
SEQRES   3 A  633  PRO ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG          
SEQRES   4 A  633  CYS SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR          
SEQRES   5 A  633  ALA ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG          
SEQRES   6 A  633  SER LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS          
SEQRES   7 A  633  VAL VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY          
SEQRES   8 A  633  GLU ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER          
SEQRES   9 A  633  LEU PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE          
SEQRES  10 A  633  GLU ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU          
SEQRES  11 A  633  GLN TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS          
SEQRES  12 A  633  PRO TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG          
SEQRES  13 A  633  ALA ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU          
SEQRES  14 A  633  THR TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL          
SEQRES  15 A  633  ALA LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP          
SEQRES  16 A  633  PRO GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN          
SEQRES  17 A  633  LYS VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL          
SEQRES  18 A  633  GLY ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU          
SEQRES  19 A  633  VAL TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR          
SEQRES  20 A  633  GLU PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU          
SEQRES  21 A  633  ASP LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU          
SEQRES  22 A  633  LEU VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU          
SEQRES  23 A  633  ASN PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA          
SEQRES  24 A  633  GLY ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE          
SEQRES  25 A  633  SER HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR          
SEQRES  26 A  633  TRP ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR          
SEQRES  27 A  633  LEU GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS          
SEQRES  28 A  633  PHE ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU          
SEQRES  29 A  633  GLN ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE          
SEQRES  30 A  633  THR LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP          
SEQRES  31 A  633  VAL ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA          
SEQRES  32 A  633  LEU LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU          
SEQRES  33 A  633  ILE PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE          
SEQRES  34 A  633  SER TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE          
SEQRES  35 A  633  LEU TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN          
SEQRES  36 A  633  GLN VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU          
SEQRES  37 A  633  PRO PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN          
SEQRES  38 A  633  ALA CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS          
SEQRES  39 A  633  GLU ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS          
SEQRES  40 A  633  ASP LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN          
SEQRES  41 A  633  THR LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS          
SEQRES  42 A  633  ARG MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN          
SEQRES  43 A  633  SER GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN          
SEQRES  44 A  633  SER LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET          
SEQRES  45 A  633  ALA THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU          
SEQRES  46 A  633  PHE LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN          
SEQRES  47 A  633  ALA VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS          
SEQRES  48 A  633  PRO VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL          
SEQRES  49 A  633  ASP LEU GLU HIS HIS HIS HIS HIS HIS                          
HET    ACT  A1611       4                                                       
HET     ZN  A1612       1                                                       
HET     YB  A1613       1                                                       
HET     YB  A1614       1                                                       
HET     YB  A1615       1                                                       
HET     YB  A1616       1                                                       
HET     YB  A1617       1                                                       
HET    IMD  A1618       5                                                       
HET    IMD  A1619       5                                                       
HET    IMD  A1620       5                                                       
HET     YB  A2612       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   2  ACT    C2 H3 O2 1-                                                  
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   YB    6(YB 3+)                                                     
FORMUL   9  IMD    3(C3 H5 N2 1+)                                               
FORMUL  13  HOH   *407(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  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  GLY A  398  1                                  19    
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  ALA A  478  1                                  14    
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 TRP A  547  ASP A  549  5                                   3    
HELIX   27  27 ALA A  550  GLN A  561  1                                  12    
HELIX   28  28 ARG 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  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 LEU A 154  PRO A 163  1  O  THR A 155   N  LEU A  21           
SHEET    7  AA 8 ASP A 183  ILE A 197 -1  O  LYS A 187   N  VAL A 162           
SHEET    8  AA 8 ILE A 173  ASP A 180 -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 THR A 307  ASN A 308  0                                        
SHEET    2  AE 2 SER A 418  ILE A 419  1  N  ILE A 419   O  THR A 307           
LINK        ZN    ZN A1612                 O   ACT A1611     1555   1555  2.02  
LINK        ZN    ZN A1612                 OE1 GLU A 318     1555   1555  2.09  
LINK        ZN    ZN A1612                 NE2 HIS A 299     1555   1555  2.08  
LINK        ZN    ZN A1612                 NE2 HIS A 295     1555   1555  2.07  
LINK        YB    YB A1613                 OD1 ASP A 481     1555   1555  2.80  
LINK        YB    YB A1613                 OD2 ASP A 481     1555   1555  2.82  
LINK        YB    YB A1613                 OD1 ASP A  47     1555   1545  2.62  
LINK        YB    YB A1613                 OD2 ASP A  47     1555   1545  2.57  
LINK        YB    YB A1613                 O   HOH A2036     1555   1545  2.89  
LINK        YB    YB A1613                 O   HOH A2330     1555   1555  2.69  
LINK        YB    YB A1613                 O   HOH A2406     1555   1555  2.46  
LINK        YB    YB A1613                 O   HOH A2331     1555   1555  2.60  
LINK        YB    YB A1613                 O   HOH A2407     1555   1555  2.78  
LINK        YB    YB A1614                 OE2 GLU A  70     1555   3544  2.58  
LINK        YB    YB A1614                 OE1 GLU A 121     1555   1555  2.25  
LINK        YB    YB A1615                 OD2 ASP A 426     1555   1555  2.65  
LINK        YB    YB A1615                 OD1 ASP A 426     1555   1555  2.49  
LINK        YB    YB A1615                 OD1 ASP A 422     1555   1555  2.60  
LINK        YB    YB A1615                 OD2 ASP A 422     1555   1555  2.63  
LINK        YB    YB A1615                 O   HOH A2294     1555   1555  2.40  
LINK        YB    YB A1616                 OD2 ASP A 481     1555   1565  2.37  
LINK        YB    YB A1616                 OD1 ASP A 481     1555   1565  2.34  
LINK        YB    YB A1616                 OD1 ASP A  47     1555   1555  2.85  
LINK        YB    YB A1616                 OD2 ASP A  47     1555   1555  2.66  
LINK        YB    YB A1616                 O   HOH A2036     1555   1555  2.61  
LINK        YB    YB A1616                 O   HOH A2330     1555   1565  2.85  
LINK        YB    YB A1616                 O   HOH A2331     1555   1565  2.75  
LINK        YB    YB A1616                 O   HOH A2406     1555   1565  3.03  
LINK        YB    YB A1616                 O   HOH A2407     1555   1565  2.92  
LINK        YB    YB A1617                 OD1 ASP A 175     1555   4555  2.67  
LINK        YB    YB A1617                 O   HOH A2031     1555   1555  3.12  
LINK        YB    YB A1617                 OE1 GLU A  46     1555   1555  2.68  
LINK        YB    YB A1617                 OE2 GLU A  46     1555   1555  2.22  
LINK        YB    YB A1617                 O   ASP A 175     1555   4555  2.93  
LINK        YB    YB A1617                 O   HOH A2138     1555   4555  3.20  
LINK        YB    YB A1617                 O   HOH A2032     1555   1555  2.65  
LINK        YB    YB A2612                 O   HOH A2138     1555   1555  3.16  
LINK        YB    YB A2612                 O   HOH A2031     1555   4455  3.01  
LINK        YB    YB A2612                 O   HOH A2032     1555   4455  2.73  
LINK        YB    YB A2612                 OD1 ASP A 175     1555   1555  2.54  
LINK        YB    YB A2612                 O   ASP A 175     1555   1555  3.08  
LINK        YB    YB A2612                 OE2 GLU A  46     1555   4455  2.42  
LINK        YB    YB A2612                 OE1 GLU A  46     1555   4455  2.74  
CISPEP   1 GLN A  136    ALA A  137          0        -0.79                     
CISPEP   2 ALA A  510    PRO A  511          0         0.37                     
SITE     1 AC1  4 GLU A  46  ASP A 175  HOH A2031  HOH A2032                    
SITE     1 AC2  9 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC2  9 HIS A 299  GLU A 318  TYR A 383   ZN A1612                    
SITE     3 AC2  9 HOH A2114                                                     
SITE     1 AC3  5 HIS A 295  HIS A 299  GLU A 318  TYR A 383                    
SITE     2 AC3  5 ACT A1611                                                     
SITE     1 AC4  7 ASP A  47  ASP A 481  HOH A2036  HOH A2330                    
SITE     2 AC4  7 HOH A2331  HOH A2406  HOH A2407                               
SITE     1 AC5  2 GLU A  70  GLU A 121                                          
SITE     1 AC6  3 ASP A 422  ASP A 426  HOH A2294                               
SITE     1 AC7  7 ASP A  47  ASP A 481  HOH A2036  HOH A2330                    
SITE     2 AC7  7 HOH A2331  HOH A2406  HOH A2407                               
SITE     1 AC8  3 GLU A  46  ASP A 175  HOH A2032                               
SITE     1 AC9  6 GLN A 136  TYR A 267  PHE A 314  PRO A 374                    
SITE     2 AC9  6 ASP A 375  HOH A2265                                          
SITE     1 BC1  4 TRP A 311  PHE A 314  ALA A 377  HOH A2265                    
SITE     1 BC2  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 BC2  6 ALA A 504  GLN A 508                                          
CRYST1   76.337   86.980   96.310  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      0.013100  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010383        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system