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Database: PDB
Entry: 5NI6
LinkDB: 5NI6
Original site: 5NI6 
HEADER    HYDROLASE                               23-MAR-17   5NI6              
TITLE     CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT D375N IN COMPLEX WITH LTA4    
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_PLASMID: PT3MB4                                    
KEYWDS    METALLOPEPTIDASE, EPOXIDE HYDROLASE, LEUKOTRIENE A4, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA                                                         
REVDAT   3   13-SEP-17 5NI6    1       JRNL                                     
REVDAT   2   06-SEP-17 5NI6    1       JRNL                                     
REVDAT   1   23-AUG-17 5NI6    0                                                
JRNL        AUTH   A.STSIAPANAVA,B.SAMUELSSON,J.Z.HAEGGSTROM                    
JRNL        TITL   CAPTURING LTA4 HYDROLASE IN ACTION: INSIGHTS TO THE          
JRNL        TITL 2 CHEMISTRY AND DYNAMICS OF CHEMOTACTIC LTB4 SYNTHESIS.        
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114  9689 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28827365                                                     
JRNL        DOI    10.1073/PNAS.1710850114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 100690                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5063                            
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 43.2461 -  4.7831    1.00     3453   174  0.1756 0.2168        
REMARK   3     2  4.7831 -  3.7972    1.00     3297   160  0.1249 0.1364        
REMARK   3     3  3.7972 -  3.3174    1.00     3278   162  0.1371 0.1650        
REMARK   3     4  3.3174 -  3.0142    1.00     3220   168  0.1381 0.1655        
REMARK   3     5  3.0142 -  2.7982    1.00     3239   185  0.1346 0.1742        
REMARK   3     6  2.7982 -  2.6332    1.00     3211   181  0.1310 0.1701        
REMARK   3     7  2.6332 -  2.5014    1.00     3237   153  0.1320 0.1595        
REMARK   3     8  2.5014 -  2.3925    1.00     3235   159  0.1294 0.1863        
REMARK   3     9  2.3925 -  2.3004    1.00     3155   185  0.1323 0.1730        
REMARK   3    10  2.3004 -  2.2210    1.00     3225   171  0.1376 0.1670        
REMARK   3    11  2.2210 -  2.1516    1.00     3241   140  0.1422 0.1734        
REMARK   3    12  2.1516 -  2.0901    1.00     3159   166  0.1497 0.1873        
REMARK   3    13  2.0901 -  2.0351    1.00     3209   155  0.1576 0.2104        
REMARK   3    14  2.0351 -  1.9854    1.00     3211   157  0.1709 0.1936        
REMARK   3    15  1.9854 -  1.9403    1.00     3199   163  0.1747 0.2074        
REMARK   3    16  1.9403 -  1.8990    1.00     3156   169  0.1675 0.1702        
REMARK   3    17  1.8990 -  1.8610    1.00     3153   173  0.1680 0.2094        
REMARK   3    18  1.8610 -  1.8259    1.00     3230   156  0.1766 0.2097        
REMARK   3    19  1.8259 -  1.7933    1.00     3176   163  0.1957 0.2292        
REMARK   3    20  1.7933 -  1.7629    1.00     3165   183  0.2063 0.2343        
REMARK   3    21  1.7629 -  1.7344    1.00     3170   159  0.2172 0.2716        
REMARK   3    22  1.7344 -  1.7077    1.00     3157   175  0.2327 0.2627        
REMARK   3    23  1.7077 -  1.6826    1.00     3161   204  0.2453 0.2887        
REMARK   3    24  1.6826 -  1.6589    1.00     3155   164  0.2603 0.3315        
REMARK   3    25  1.6589 -  1.6365    1.00     3145   183  0.2708 0.2912        
REMARK   3    26  1.6365 -  1.6153    1.00     3186   169  0.2864 0.2853        
REMARK   3    27  1.6153 -  1.5951    1.00     3145   179  0.2912 0.2874        
REMARK   3    28  1.5951 -  1.5758    1.00     3165   168  0.2972 0.3129        
REMARK   3    29  1.5758 -  1.5575    1.00     3121   186  0.2989 0.3510        
REMARK   3    30  1.5575 -  1.5400    0.88     2773   153  0.3190 0.3189        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.190           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.07                          
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  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      :  0.008           5225                                  
REMARK   3   ANGLE     :  0.947           7100                                  
REMARK   3   CHIRALITY :  0.054            786                                  
REMARK   3   PLANARITY :  0.007            917                                  
REMARK   3   DIHEDRAL  : 15.871           1963                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 3:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.6391 -14.6837   9.5892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2275 T22:   0.1495                                     
REMARK   3      T33:   0.1218 T12:  -0.0029                                     
REMARK   3      T13:  -0.0127 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0385 L22:   1.8461                                     
REMARK   3      L33:   0.7161 L12:  -0.6234                                     
REMARK   3      L13:  -0.0885 L23:   0.4461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0765 S12:  -0.1447 S13:  -0.0575                       
REMARK   3      S21:   0.3883 S22:   0.0764 S23:  -0.0475                       
REMARK   3      S31:   0.1391 S32:   0.0129 S33:  -0.0011                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 209:465                               
REMARK   3    ORIGIN FOR THE GROUP (A): -35.4298   4.8686 -10.0577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1723 T22:   0.2022                                     
REMARK   3      T33:   0.1818 T12:  -0.0276                                     
REMARK   3      T13:  -0.0102 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6662 L22:   0.9776                                     
REMARK   3      L33:   0.7846 L12:   0.0240                                     
REMARK   3      L13:  -0.1732 L23:   0.0390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0730 S12:   0.0923 S13:   0.0427                       
REMARK   3      S21:  -0.0849 S22:   0.0161 S23:  -0.1107                       
REMARK   3      S31:  -0.0032 S32:   0.0795 S33:   0.0576                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 466:610                               
REMARK   3    ORIGIN FOR THE GROUP (A): -29.8690  25.5313   5.4021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1167 T22:   0.1590                                     
REMARK   3      T33:   0.1525 T12:  -0.0047                                     
REMARK   3      T13:  -0.0160 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4688 L22:   3.8281                                     
REMARK   3      L33:   1.3086 L12:   0.6711                                     
REMARK   3      L13:  -0.1502 L23:  -1.1807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0448 S12:  -0.0287 S13:   0.0348                       
REMARK   3      S21:   0.2220 S22:  -0.0336 S23:  -0.0465                       
REMARK   3      S31:  -0.0270 S32:   0.0274 S33:  -0.0055                       
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 5NI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004024.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
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   : 100716                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.229                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.10450                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.72900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.060                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5NI2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (W/V) PEG 8000, 100 MM IMIDAZOLE     
REMARK 280  PH 7.0, 100 MM SODIUM ACETATE, 5 MM YBCL3, LIQUID DIFFUSION,        
REMARK 280  TEMPERATURE 277K                                                    
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       39.06500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.72500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.72500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 290 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 23810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
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    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
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  HH22  ARG A   331     O    HOH A   813              1.55            
REMARK 500   O    HOH A  1330     O    HOH A  1579              2.08            
REMARK 500   O    HOH A   912     O    HOH A  1504              2.08            
REMARK 500   OD1  ASN A   530     O    HOH A   803              2.12            
REMARK 500   OD2  ASP A   610     O    HOH A   804              2.13            
REMARK 500   OE2  GLU A   245     O    HOH A   805              2.17            
REMARK 500   OE1  GLN A   441     O    HOH A   806              2.17            
REMARK 500   O    HOH A  1273     O    HOH A  1401              2.18            
REMARK 500   O    HOH A  1252     O    HOH A  1354              2.19            
REMARK 500   O    HOH A  1389     O    HOH A  1403              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   885     O    HOH A  1336     4555     2.13            
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       70.49   -116.05                                   
REMARK 500    SER A  80     -134.28     49.26                                   
REMARK 500    SER A  80     -134.06     48.91                                   
REMARK 500    SER A 112      124.03    -36.61                                   
REMARK 500    ASP A 183       98.61   -161.95                                   
REMARK 500    GLU A 271       46.97    -79.93                                   
REMARK 500    CYS A 274      -14.10     76.34                                   
REMARK 500    LEU A 275       83.87   -155.21                                   
REMARK 500    PHE A 432       43.08    -96.24                                   
REMARK 500    LYS A 546       37.43     71.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1621        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A1622        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A1623        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A1624        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A1625        DISTANCE =  7.99 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  47   OD1                                                    
REMARK 620 2 ASP A  47   OD2  55.1                                              
REMARK 620 3 HOH A 893   O    71.9 126.8                                        
REMARK 620 4 HOH A1255   O    79.4  80.5  86.2                                  
REMARK 620 5 ACY A 704   O   121.7  70.1 151.4  73.3                            
REMARK 620 6 ACY A 704   OXT 125.5  80.2 143.4 126.0  52.7                      
REMARK 620 7 ASP A 481   OD1  24.4  37.9  92.7  93.2 107.9 101.1                
REMARK 620 8 ASP A 481   OD2  24.5  37.6  93.0  93.0 107.6 101.1   0.3          
REMARK 620 9 HOH A 866   O   143.7 145.0  78.7  77.8  77.6  90.8 167.9 167.9    
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 A 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD1                                                    
REMARK 620 2 HOH A1372   O    68.7                                              
REMARK 620 3 HOH A1221   O    85.1  93.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 100.1                                              
REMARK 620 3 GLU A 318   OE1  99.5 101.8                                        
REMARK 620 4 DJ3 A 705   OAT 101.1 131.2 117.1                                  
REMARK 620 5 DJ3 A 705   OAT 100.1 136.3 112.4   5.3                            
REMARK 620 6 ACY A 706   O   100.8 149.8  95.9  21.9  16.7                      
REMARK 620 7 ACY A 706   OXT  91.6  95.9 157.0  40.3  45.3  62.0                
REMARK 620 8 HOH A 801   O    91.5  79.6 168.4  56.5  61.5  78.3  16.6          
REMARK 620 N                    1     2     3     4     5     6     7           
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 706                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MS6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DPR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NI2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NI4   RELATED DB: PDB                                   
DBREF  5NI6 A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 5NI6 MET A   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NI6 HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI6 ASN A  375  UNP  P09960    ASP   376 ENGINEERED MUTATION            
SEQRES   1 A  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 A  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 A  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 A  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 A  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 A  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 A  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 A  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 A  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 A  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 A  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 A  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 A  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 A  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 A  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 A  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 A  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 A  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 A  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 A  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 A  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 A  617  TYR GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 A  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 A  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 A  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 A  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 A  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 A  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 A  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 A  617  ASP ILE ASP PRO ASN VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 A  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 A  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 A  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 A  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 A  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 A  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 A  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 A  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 A  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 A  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 A  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 A  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 A  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 A  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS          
SEQRES  45 A  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 A  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 A  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 A  617  LYS ASP LEU LYS VAL ASP                                      
HET     ZN  A 701       1                                                       
HET     YB  A 702       1                                                       
HET     YB  A 703       1                                                       
HET    ACY  A 704       7                                                       
HET    DJ3  A 705     104                                                       
HET    ACY  A 706       7                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     ACY ACETIC ACID                                                      
HETNAM     DJ3 5S-5,6-OXIDO-7,9-TRANS-11,14-CIS-EICOSATETRAENOIC ACID           
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    2(YB 3+)                                                     
FORMUL   5  ACY    2(C2 H4 O2)                                                  
FORMUL   6  DJ3    C20 H30 O3                                                   
FORMUL   8  HOH   *825(H2 O)                                                    
HELIX    1 AA1 GLN A   79  GLY A   83  5                                   5    
HELIX    2 AA2 THR A  119  THR A  123  5                                   5    
HELIX    3 AA3 HIS A  139  ILE A  143  5                                   5    
HELIX    4 AA4 TYR A  200  ILE A  202  5                                   3    
HELIX    5 AA5 GLU A  223  GLU A  225  5                                   3    
HELIX    6 AA6 GLN A  226  PHE A  234  1                                   9    
HELIX    7 AA7 GLU A  236  GLY A  249  1                                  14    
HELIX    8 AA8 PRO A  280  LEU A  283  5                                   4    
HELIX    9 AA9 SER A  290  HIS A  299  1                                  10    
HELIX   10 AB1 THR A  310  ASP A  312  5                                   3    
HELIX   11 AB2 HIS A  313  GLY A  334  1                                  22    
HELIX   12 AB3 GLY A  334  GLY A  357  1                                  24    
HELIX   13 AB4 HIS A  360  LYS A  364  5                                   5    
HELIX   14 AB5 ASP A  373  TYR A  378  1                                   6    
HELIX   15 AB6 SER A  380  LEU A  397  1                                  18    
HELIX   16 AB7 GLY A  399  SER A  415  1                                  17    
HELIX   17 AB8 THR A  420  PHE A  432  1                                  13    
HELIX   18 AB9 LYS A  435  ASN A  440  1                                   6    
HELIX   19 AC1 ASP A  443  SER A  450  1                                   8    
HELIX   20 AC2 THR A  465  ALA A  478  1                                  14    
HELIX   21 AC3 LYS A  479  PHE A  486  5                                   8    
HELIX   22 AC4 ASN A  487  LYS A  492  5                                   6    
HELIX   23 AC5 SER A  495  GLN A  508  1                                  14    
HELIX   24 AC6 PRO A  513  ASN A  525  1                                  13    
HELIX   25 AC7 PHE A  526  ILE A  529  5                                   4    
HELIX   26 AC8 ASN A  531  SER A  545  1                                  15    
HELIX   27 AC9 TRP A  547  ASP A  549  5                                   3    
HELIX   28 AD1 ALA A  550  GLN A  561  1                                  12    
HELIX   29 AD2 ARG A  563  PHE A  577  1                                  15    
HELIX   30 AD3 PHE A  577  LYS A  592  1                                  16    
HELIX   31 AD4 ALA A  593  MET A  595  5                                   3    
HELIX   32 AD5 HIS A  596  LYS A  608  1                                  13    
SHEET    1 AA1 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA1 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA1 8 GLU A  99  THR A 108 -1  O  SER A 105   N  GLU A  62           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6 AA1 8 LYS A 153  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7 AA1 8 ARG A 186  PRO A 198 -1  O  GLN A 193   N  TYR A 156           
SHEET    8 AA1 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1 AA2 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA2 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA2 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA3 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA3 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3 AA3 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA3 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1 AA4 5 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3 AA4 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  VAL A 278   N  LEU A 259           
SHEET    5 AA4 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1 AA5 2 VAL A 306  ASN A 308  0                                        
SHEET    2 AA5 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OD1 ASP A  47                YB    YB A 702     1555   1555  2.34  
LINK         OD2 ASP A  47                YB    YB A 702     1555   1555  2.44  
LINK         OD1 ASP A 175                YB    YB A 703     1555   1555  2.23  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.09  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.06  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.04  
LINK        ZN    ZN A 701                 OATADJ3 A 705     1555   1555  2.41  
LINK        ZN    ZN A 701                 OATBDJ3 A 705     1555   1555  2.19  
LINK        ZN    ZN A 701                 O  CACY A 706     1555   1555  1.86  
LINK        ZN    ZN A 701                 OXTCACY A 706     1555   1555  2.31  
LINK        ZN    ZN A 701                 O   HOH A 801     1555   1555  2.55  
LINK        YB    YB A 702                 O   HOH A 893     1555   1555  2.14  
LINK        YB    YB A 702                 O   HOH A1255     1555   1555  2.34  
LINK        YB    YB A 702                 O   ACY A 704     1555   1555  2.61  
LINK        YB    YB A 702                 OXT ACY A 704     1555   1555  2.32  
LINK        YB    YB A 703                 O   HOH A1372     1555   1555  3.33  
LINK         OD1 ASP A 481                YB    YB A 702     1555   1565  2.49  
LINK         OD2 ASP A 481                YB    YB A 702     1555   1565  2.34  
LINK        YB    YB A 702                 O   HOH A 866     1555   1545  2.27  
LINK        YB    YB A 703                 O   HOH A1221     1555   4445  2.49  
CISPEP   1 GLN A  136    ALA A  137          0         3.52                     
CISPEP   2 ALA A  510    PRO A  511          0         5.73                     
SITE     1 AC1  6 HIS A 295  HIS A 299  GLU A 318  DJ3 A 705                    
SITE     2 AC1  6 ACY A 706  HOH A 801                                          
SITE     1 AC2  6 ASP A  47  ASP A 481  ACY A 704  HOH A 866                    
SITE     2 AC2  6 HOH A 893  HOH A1255                                          
SITE     1 AC3  2 ASP A 175  HOH A1221                                          
SITE     1 AC4  9 ASP A  47  ASN A  48  ARG A 174  LYS A 479                    
SITE     2 AC4  9 ASP A 481   YB A 702  HOH A 866  HOH A 962                    
SITE     3 AC4  9 HOH A1255                                                     
SITE     1 AC5 23 GLN A 136  ALA A 137  TYR A 267  GLY A 268                    
SITE     2 AC5 23 GLY A 269  HIS A 295  GLU A 296  TRP A 311                    
SITE     3 AC5 23 PHE A 314  GLU A 318  VAL A 367  PRO A 374                    
SITE     4 AC5 23 PRO A 382  TYR A 383  ARG A 563   ZN A 701                    
SITE     5 AC5 23 ACY A 706  HOH A 801  HOH A 861  HOH A 878                    
SITE     6 AC5 23 HOH A1113  HOH A1224  HOH A1306                               
SITE     1 AC6 10 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC6 10 HIS A 299  GLU A 318  TYR A 383   ZN A 701                    
SITE     3 AC6 10 DJ3 A 705  HOH A 801                                          
CRYST1   78.130   87.450   99.460  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      0.012799  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011435  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010054        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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