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Database: PDB
Entry: 5NIE
LinkDB: 5NIE
Original site: 5NIE 
HEADER    HYDROLASE                               23-MAR-17   5NIE              
TITLE     CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT R563A IN OPEN CONFORMATION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT3MB4                                    
KEYWDS    METALLOPEPTIDASE, EPOXIDE HYDROLASE, OPEN CONFORMATION, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA                                                         
REVDAT   3   13-SEP-17 5NIE    1       JRNL                                     
REVDAT   2   06-SEP-17 5NIE    1       JRNL                                     
REVDAT   1   23-AUG-17 5NIE    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.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155)                                 
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.47                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 64057                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3105                            
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 49.4823 -  7.2863    1.00     3248   166  0.1748 0.2111        
REMARK   3     2  7.2863 -  5.7862    1.00     3071   156  0.2032 0.2502        
REMARK   3     3  5.7862 -  5.0556    0.99     3060   156  0.1781 0.2524        
REMARK   3     4  5.0556 -  4.5938    0.99     3015   150  0.1602 0.2040        
REMARK   3     5  4.5938 -  4.2647    0.98     2933   149  0.1688 0.2284        
REMARK   3     6  4.2647 -  4.0134    0.98     2915   149  0.1912 0.2528        
REMARK   3     7  4.0134 -  3.8125    0.98     2964   148  0.2099 0.2673        
REMARK   3     8  3.8125 -  3.6466    0.98     2899   151  0.2204 0.2599        
REMARK   3     9  3.6466 -  3.5062    0.98     2906   143  0.2357 0.3148        
REMARK   3    10  3.5062 -  3.3853    0.97     2888   154  0.2654 0.3452        
REMARK   3    11  3.3853 -  3.2794    0.96     2845   135  0.2759 0.3732        
REMARK   3    12  3.2794 -  3.1857    0.95     2849   146  0.2898 0.3456        
REMARK   3    13  3.1857 -  3.1018    0.94     2746   142  0.3023 0.3355        
REMARK   3    14  3.1018 -  3.0262    0.92     2720   139  0.3033 0.3268        
REMARK   3    15  3.0262 -  2.9574    0.92     2697   140  0.3160 0.3906        
REMARK   3    16  2.9574 -  2.8945    0.90     2606   129  0.3310 0.3948        
REMARK   3    17  2.8945 -  2.8366    0.88     2631   133  0.3731 0.4244        
REMARK   3    18  2.8366 -  2.7830    0.84     2477   127  0.3543 0.4275        
REMARK   3    19  2.7830 -  2.7334    0.82     2352   126  0.3459 0.3797        
REMARK   3    20  2.7334 -  2.6870    0.83     2482   126  0.3527 0.4356        
REMARK   3    21  2.6870 -  2.6437    0.81     2364   123  0.3713 0.3952        
REMARK   3    22  2.6437 -  2.6030    0.79     2284   117  0.3758 0.3866        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.380           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.83                          
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      :  0.003          14921                                  
REMARK   3   ANGLE     :  0.614          20273                                  
REMARK   3   CHIRALITY :  0.045           2264                                  
REMARK   3   PLANARITY :  0.004           2581                                  
REMARK   3   DIHEDRAL  : 12.010           8944                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 4:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8194 -44.7378  84.9945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2548 T22:   0.2747                                     
REMARK   3      T33:   0.2525 T12:  -0.0261                                     
REMARK   3      T13:  -0.0128 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0975 L22:   0.4509                                     
REMARK   3      L33:   0.3882 L12:   0.2473                                     
REMARK   3      L13:  -0.1378 L23:  -0.0317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0456 S12:  -0.0379 S13:  -0.0175                       
REMARK   3      S21:  -0.0696 S22:   0.0575 S23:   0.0319                       
REMARK   3      S31:   0.2366 S32:   0.0262 S33:   0.0015                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 209:465 OR (CHAIN A AND RESI 900      
REMARK   3               AND RESNAME ZN)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0239 -26.0774  80.5741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2469 T22:   0.3073                                     
REMARK   3      T33:   0.2897 T12:   0.0165                                     
REMARK   3      T13:  -0.0333 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3741 L22:   0.0109                                     
REMARK   3      L33:   0.6851 L12:   0.0457                                     
REMARK   3      L13:  -0.6665 L23:  -0.3657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0284 S12:   0.0004 S13:   0.0128                       
REMARK   3      S21:   0.0055 S22:  -0.0457 S23:  -0.0416                       
REMARK   3      S31:  -0.0148 S32:  -0.0401 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7663 -19.4623  53.0702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3080 T22:   0.4280                                     
REMARK   3      T33:   0.3470 T12:  -0.0356                                     
REMARK   3      T13:  -0.0052 T23:   0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2285 L22:   0.3869                                     
REMARK   3      L33:   0.4116 L12:   0.2993                                     
REMARK   3      L13:  -0.1021 L23:  -0.0243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0978 S12:   0.0531 S13:   0.0148                       
REMARK   3      S21:  -0.0178 S22:   0.1183 S23:  -0.0868                       
REMARK   3      S31:   0.0695 S32:   0.0426 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 3:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7173 -59.2028  44.4144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3225 T22:   0.3728                                     
REMARK   3      T33:   0.3654 T12:  -0.0509                                     
REMARK   3      T13:   0.0165 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3874 L22:   0.6468                                     
REMARK   3      L33:   0.8359 L12:  -0.1567                                     
REMARK   3      L13:   0.2898 L23:   0.2468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0477 S12:  -0.0515 S13:  -0.0005                       
REMARK   3      S21:   0.0506 S22:  -0.0916 S23:  -0.0879                       
REMARK   3      S31:  -0.0682 S32:   0.1549 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 209:465 OR (CHAIN B AND RESI 900      
REMARK   3               AND RESNAME ZN)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6551 -64.4551  24.5432              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4546 T22:   0.3027                                     
REMARK   3      T33:   0.3561 T12:  -0.0083                                     
REMARK   3      T13:   0.0485 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0628 L22:   0.3769                                     
REMARK   3      L33:   0.3503 L12:  -0.3052                                     
REMARK   3      L13:   0.1678 L23:  -0.4769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0970 S12:   0.0525 S13:   0.0008                       
REMARK   3      S21:  -0.0789 S22:   0.0196 S23:  -0.0132                       
REMARK   3      S31:  -0.0089 S32:  -0.0408 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3963 -44.5794   5.1455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6430 T22:   0.3337                                     
REMARK   3      T33:   0.3978 T12:  -0.0148                                     
REMARK   3      T13:   0.0460 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2816 L22:   0.6195                                     
REMARK   3      L33:   0.2778 L12:  -0.0528                                     
REMARK   3      L13:   0.2220 L23:  -0.1662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2584 S12:  -0.0132 S13:   0.1450                       
REMARK   3      S21:  -0.3172 S22:  -0.0907 S23:  -0.0674                       
REMARK   3      S31:   0.0657 S32:   0.0186 S33:   0.0021                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 4:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1525  20.4738  16.4534              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4798 T22:   0.3331                                     
REMARK   3      T33:   0.3111 T12:  -0.0078                                     
REMARK   3      T13:   0.0630 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1586 L22:   0.9059                                     
REMARK   3      L33:   0.7867 L12:   0.2782                                     
REMARK   3      L13:   0.3092 L23:  -0.1430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0672 S12:   0.0511 S13:  -0.0322                       
REMARK   3      S21:  -0.1582 S22:   0.0642 S23:  -0.1140                       
REMARK   3      S31:  -0.0458 S32:   0.1033 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 209:465 OR (CHAIN C AND RESI 900      
REMARK   3               AND RESNAME ZN)                                        
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6252   6.0107  29.5717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3239 T22:   0.3677                                     
REMARK   3      T33:   0.3151 T12:   0.0452                                     
REMARK   3      T13:  -0.0284 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1591 L22:   0.7698                                     
REMARK   3      L33:  -0.1343 L12:   0.2709                                     
REMARK   3      L13:  -0.4648 L23:  -0.0323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:  -0.0231 S13:  -0.0420                       
REMARK   3      S21:  -0.1129 S22:  -0.0210 S23:   0.0436                       
REMARK   3      S31:   0.0183 S32:  -0.0380 S33:   0.0001                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3573 -21.2955  23.5982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4325 T22:   0.2275                                     
REMARK   3      T33:   0.3397 T12:  -0.0301                                     
REMARK   3      T13:   0.0697 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4718 L22:   0.7383                                     
REMARK   3      L33:  -0.0976 L12:  -0.4251                                     
REMARK   3      L13:  -0.2906 L23:   0.0757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0118 S12:  -0.0487 S13:  -0.0475                       
REMARK   3      S21:   0.0572 S22:  -0.0759 S23:  -0.1372                       
REMARK   3      S31:   0.1482 S32:  -0.0210 S33:  -0.0006                       
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 5NIE 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_1200004165.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8729                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64086                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.603                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.473                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.19300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.10900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.940                              
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   (%): 54.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG MME 5000, 100 MM MES       
REMARK 280  MONOHYDRATE PH 6.0, 150 MM AMMONIUM SULFATE, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 294K                                      
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       25.98500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      160.06000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.07500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      160.06000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.98500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.07500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 465     ILE A     3                                                      
REMARK 465     ASP A   610                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ASP B   610                                                      
REMARK 465     MET C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ILE C     3                                                      
REMARK 465     ASP C   610                                                      
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     THR A 157    O                                                   
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   HH   TYR C   156     O    SER C   171              1.45            
REMARK 500   HH   TYR B   416     O    HOH B  1008              1.51            
REMARK 500   OD1  ASN C   527     HE1  TRP C   538              1.58            
REMARK 500   O    THR C   321     H    GLU C   325              1.59            
REMARK 500   OH   TYR C   156     O    SER C   171              1.96            
REMARK 500   OD1  ASN B   445     O    HOH B  1001              2.19            
REMARK 500   OG1  THR C   279     O    HOH C  1001              2.19            
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    VAL A  15      -62.95    -97.07                                   
REMARK 500    SER A  80     -128.21     41.78                                   
REMARK 500    ASN A  97       -3.16     77.14                                   
REMARK 500    GLU A 127      -58.97   -122.32                                   
REMARK 500    ILE A 143      -64.41   -100.99                                   
REMARK 500    THR A 149      136.02    176.83                                   
REMARK 500    ALA A 172      174.87    170.63                                   
REMARK 500    ASP A 175      -63.70   -106.00                                   
REMARK 500    SER A 222     -177.50   -170.38                                   
REMARK 500    CYS A 274      -16.00     70.13                                   
REMARK 500    PRO A 451     -178.54    -65.46                                   
REMARK 500    ALA A 510      169.98     78.51                                   
REMARK 500    PHE A 566      -61.32   -102.00                                   
REMARK 500    VAL B  15      -63.00   -103.44                                   
REMARK 500    ARG B  32       71.12     58.59                                   
REMARK 500    SER B  80     -127.00     40.33                                   
REMARK 500    ASN B  97       -2.61     76.51                                   
REMARK 500    LYS B 126      -14.42     69.51                                   
REMARK 500    ILE B 143      -67.53    -99.13                                   
REMARK 500    ALA B 172      174.59    169.68                                   
REMARK 500    CYS B 274      -20.30     75.17                                   
REMARK 500    TRP B 301      -61.79   -106.89                                   
REMARK 500    ASN B 317      -77.87    -82.26                                   
REMARK 500    VAL C  15      -61.21    -96.52                                   
REMARK 500    GLU C  62      -64.98    -95.25                                   
REMARK 500    SER C  80     -127.29     40.14                                   
REMARK 500    ILE C 143      -62.41    -99.07                                   
REMARK 500    CYS C 146     -178.73   -170.08                                   
REMARK 500    THR C 149      139.06    174.08                                   
REMARK 500    ALA C 172      176.12    178.96                                   
REMARK 500    ASP C 183      130.57   -175.87                                   
REMARK 500    PRO C 266       46.44    -93.46                                   
REMARK 500    CYS C 274      -17.63     70.30                                   
REMARK 500    LEU C 305      -60.86   -109.63                                   
REMARK 500    ASN C 317      -77.09    -82.43                                   
REMARK 500    ALA C 510      173.64     70.55                                   
REMARK 500    VAL C 523      -61.64    -94.76                                   
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 A 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2  96.5                                              
REMARK 620 3 GLU A 318   OE1  96.0  92.7                                        
REMARK 620 4 GLU A 318   OE2 152.1 104.9  65.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 295   NE2                                                    
REMARK 620 2 HIS B 299   NE2  90.1                                              
REMARK 620 3 GLU B 318   OE1  87.8  86.5                                        
REMARK 620 4 GLU B 318   OE2 148.7 102.7  65.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 295   NE2                                                    
REMARK 620 2 HIS C 299   NE2 102.7                                              
REMARK 620 3 GLU C 318   OE1  97.3  83.3                                        
REMARK 620 4 GLU C 318   OE2 133.3 117.2  66.4                                  
REMARK 620 N                    1     2     3                                   
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 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 900                  
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                                   
REMARK 900 RELATED ID: 5NI6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NIA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NID   RELATED DB: PDB                                   
DBREF  5NIE A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
DBREF  5NIE B    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
DBREF  5NIE C    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 5NIE MET A   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NIE HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE ALA A  563  UNP  P09960    ARG   564 ENGINEERED MUTATION            
SEQADV 5NIE MET B   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NIE HIS B   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS B   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS B   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS B   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS B   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS B    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE ALA B  563  UNP  P09960    ARG   564 ENGINEERED MUTATION            
SEQADV 5NIE MET C   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NIE HIS C   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS C   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS C   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS C   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS C   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE HIS C    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIE ALA C  563  UNP  P09960    ARG   564 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 ASP 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 ALA 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                                      
SEQRES   1 B  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 B  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 B  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 B  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 B  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 B  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 B  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 B  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 B  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 B  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 B  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 B  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 B  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 B  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 B  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 B  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 B  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 B  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 B  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 B  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 B  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 B  617  TYR GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 B  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 B  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 B  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 B  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 B  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 B  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 B  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 B  617  ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 B  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 B  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 B  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 B  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 B  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 B  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 B  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 B  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 B  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 B  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 B  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 B  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 B  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 B  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ALA MET LYS          
SEQRES  45 B  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 B  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 B  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 B  617  LYS ASP LEU LYS VAL ASP                                      
SEQRES   1 C  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 C  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 C  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 C  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 C  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 C  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 C  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 C  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 C  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 C  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 C  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 C  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 C  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 C  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 C  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 C  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 C  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 C  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 C  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 C  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 C  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 C  617  TYR GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 C  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 C  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 C  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 C  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 C  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 C  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 C  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 C  617  ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 C  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 C  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 C  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 C  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 C  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 C  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 C  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 C  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 C  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 C  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 C  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 C  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 C  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 C  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ALA MET LYS          
SEQRES  45 C  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 C  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 C  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 C  617  LYS ASP LEU LYS VAL ASP                                      
HET     ZN  A 900       1                                                       
HET     ZN  B 900       1                                                       
HET     ZN  C 900       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *154(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 ILE A  138  ILE A  143  5                                   6    
HELIX    4 AA4 TYR A  200  ILE A  202  5                                   3    
HELIX    5 AA5 GLN A  226  PHE A  234  1                                   9    
HELIX    6 AA6 GLU A  236  GLY A  249  1                                  14    
HELIX    7 AA7 THR A  279  LEU A  283  5                                   5    
HELIX    8 AA8 LEU A  289  VAL A  292  5                                   4    
HELIX    9 AA9 ILE A  293  THR A  302  1                                  10    
HELIX   10 AB1 THR A  310  HIS A  313  5                                   4    
HELIX   11 AB2 PHE A  314  GLY A  334  1                                  21    
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 SER A  380  LEU A  397  1                                  18    
HELIX   15 AB6 GLY A  399  SER A  415  1                                  17    
HELIX   16 AB7 THR A  420  PHE A  432  1                                  13    
HELIX   17 AB8 LYS A  435  ASN A  440  1                                   6    
HELIX   18 AB9 ASP A  443  SER A  450  1                                   8    
HELIX   19 AC1 MET A  462  THR A  477  1                                  16    
HELIX   20 AC2 ASN A  487  LYS A  492  5                                   6    
HELIX   21 AC3 SER A  495  ARG A  509  1                                  15    
HELIX   22 AC4 PRO A  513  ASN A  525  1                                  13    
HELIX   23 AC5 PHE A  526  ILE A  529  5                                   4    
HELIX   24 AC6 ASN A  531  SER A  545  1                                  15    
HELIX   25 AC7 ASP A  549  GLN A  561  1                                  13    
HELIX   26 AC8 ALA A  563  PHE A  577  1                                  15    
HELIX   27 AC9 SER A  580  LYS A  592  1                                  13    
HELIX   28 AD1 ALA A  593  MET A  595  5                                   3    
HELIX   29 AD2 HIS A  596  LEU A  607  1                                  12    
HELIX   30 AD3 GLN B   79  GLY B   83  5                                   5    
HELIX   31 AD4 THR B  119  THR B  123  5                                   5    
HELIX   32 AD5 HIS B  139  ILE B  143  5                                   5    
HELIX   33 AD6 PRO B  198  ILE B  202  5                                   5    
HELIX   34 AD7 GLN B  226  PHE B  234  1                                   9    
HELIX   35 AD8 GLU B  236  GLY B  249  1                                  14    
HELIX   36 AD9 THR B  279  LEU B  283  5                                   5    
HELIX   37 AE1 LEU B  289  VAL B  292  5                                   4    
HELIX   38 AE2 ILE B  293  SER B  300  1                                   8    
HELIX   39 AE3 THR B  310  HIS B  313  5                                   4    
HELIX   40 AE4 PHE B  314  GLY B  334  1                                  21    
HELIX   41 AE5 GLY B  334  GLY B  357  1                                  24    
HELIX   42 AE6 HIS B  360  LYS B  364  5                                   5    
HELIX   43 AE7 SER B  380  LEU B  397  1                                  18    
HELIX   44 AE8 GLY B  399  SER B  415  1                                  17    
HELIX   45 AE9 THR B  420  PHE B  432  1                                  13    
HELIX   46 AF1 LYS B  435  ASN B  440  1                                   6    
HELIX   47 AF2 ASP B  443  SER B  450  1                                   8    
HELIX   48 AF3 MET B  462  THR B  477  1                                  16    
HELIX   49 AF4 LYS B  479  PHE B  486  5                                   8    
HELIX   50 AF5 ASN B  487  LYS B  492  5                                   6    
HELIX   51 AF6 SER B  495  ARG B  509  1                                  15    
HELIX   52 AF7 PRO B  513  ASN B  525  1                                  13    
HELIX   53 AF8 ASN B  531  SER B  545  1                                  15    
HELIX   54 AF9 TRP B  547  ASP B  549  5                                   3    
HELIX   55 AG1 ALA B  550  GLN B  561  1                                  12    
HELIX   56 AG2 ALA B  563  PHE B  577  1                                  15    
HELIX   57 AG3 SER B  580  LYS B  592  1                                  13    
HELIX   58 AG4 ALA B  593  MET B  595  5                                   3    
HELIX   59 AG5 HIS B  596  LEU B  607  1                                  12    
HELIX   60 AG6 GLN C   79  GLY C   83  5                                   5    
HELIX   61 AG7 THR C  119  THR C  123  5                                   5    
HELIX   62 AG8 ILE C  138  ILE C  143  5                                   6    
HELIX   63 AG9 TYR C  200  ILE C  202  5                                   3    
HELIX   64 AH1 GLN C  226  PHE C  234  1                                   9    
HELIX   65 AH2 GLU C  236  GLY C  249  1                                  14    
HELIX   66 AH3 THR C  279  LEU C  283  5                                   5    
HELIX   67 AH4 LEU C  289  VAL C  292  5                                   4    
HELIX   68 AH5 ILE C  293  SER C  300  1                                   8    
HELIX   69 AH6 THR C  310  HIS C  313  5                                   4    
HELIX   70 AH7 PHE C  314  GLY C  334  1                                  21    
HELIX   71 AH8 GLY C  334  GLY C  357  1                                  24    
HELIX   72 AH9 HIS C  360  LYS C  364  5                                   5    
HELIX   73 AI1 ASP C  373  TYR C  378  1                                   6    
HELIX   74 AI2 SER C  380  GLY C  398  1                                  19    
HELIX   75 AI3 GLY C  399  SER C  415  1                                  17    
HELIX   76 AI4 THR C  420  PHE C  432  1                                  13    
HELIX   77 AI5 LYS C  435  ASN C  440  1                                   6    
HELIX   78 AI6 ASP C  443  SER C  450  1                                   8    
HELIX   79 AI7 MET C  462  THR C  477  1                                  16    
HELIX   80 AI8 ASP C  481  PHE C  486  5                                   6    
HELIX   81 AI9 ASN C  487  LYS C  492  5                                   6    
HELIX   82 AJ1 SER C  495  ARG C  509  1                                  15    
HELIX   83 AJ2 PRO C  513  ASN C  525  1                                  13    
HELIX   84 AJ3 PHE C  526  ILE C  529  5                                   4    
HELIX   85 AJ4 ASN C  531  SER C  545  1                                  15    
HELIX   86 AJ5 TRP C  547  ASP C  549  5                                   3    
HELIX   87 AJ6 ALA C  550  GLN C  561  1                                  12    
HELIX   88 AJ7 ALA C  563  PHE C  577  1                                  15    
HELIX   89 AJ8 SER C  580  LYS C  592  1                                  13    
HELIX   90 AJ9 ALA C  593  MET C  595  5                                   3    
HELIX   91 AK1 HIS C  596  LYS C  608  1                                  13    
SHEET    1 AA1 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA1 8 THR A  60  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA1 8 GLU A  99  GLU A 107 -1  O  GLU A 103   N  VAL A  65           
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  ARG A  24   O  THR A  37           
SHEET    6 AA1 8 LYS A 153  TYR A 156  1  O  THR A 155   N  LYS A  19           
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  ILE A 173   O  ILE A 192           
SHEET    1 AA2 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA2 8 THR A  60  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA2 8 GLU A  99  GLU A 107 -1  O  GLU A 103   N  VAL A  65           
SHEET    4 AA2 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5 AA2 8 CYS A  16  ASP A  28 -1  N  ARG A  24   O  THR A  37           
SHEET    6 AA2 8 GLU A 159  PRO A 163  1  O  SER A 161   N  VAL A  27           
SHEET    7 AA2 8 ARG A 186  PRO A 198 -1  O  LYS A 187   N  VAL A 162           
SHEET    8 AA2 8 ILE A 173  PRO A 179 -1  N  ILE A 173   O  ILE A 192           
SHEET    1 AA3 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA3 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA3 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA4 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA4 4 TYR A 130  SER A 133 -1  O  PHE A 132   N  GLN A 116           
SHEET    3 AA4 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA4 4 VAL A 167  MET A 170 -1  N  LEU A 169   O  VAL A 205           
SHEET    1 AA5 4 GLU A 210  GLN A 213  0                                        
SHEET    2 AA5 4 LEU A 219  SER A 222 -1  O  SER A 222   N  GLU A 210           
SHEET    3 AA5 4 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4 AA5 4 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    1 AA6 2 VAL A 306  ASN A 308  0                                        
SHEET    2 AA6 2 LYS A 417  ILE A 419  1  O  LYS A 417   N  THR A 307           
SHEET    1 AA7 8 GLN B  69  GLU B  70  0                                        
SHEET    2 AA7 8 THR B  60  ILE B  66 -1  N  ILE B  66   O  GLN B  69           
SHEET    3 AA7 8 GLU B  99  GLU B 107 -1  O  GLU B 103   N  VAL B  65           
SHEET    4 AA7 8 THR B  33  SER B  44 -1  N  VAL B  42   O  ILE B 100           
SHEET    5 AA7 8 CYS B  16  ASP B  28 -1  N  HIS B  20   O  THR B  41           
SHEET    6 AA7 8 LEU B 154  PRO B 163  1  O  SER B 161   N  VAL B  27           
SHEET    7 AA7 8 ARG B 186  ILE B 197 -1  O  ILE B 197   N  LEU B 154           
SHEET    8 AA7 8 ILE B 173  PRO B 179 -1  N  GLY B 176   O  LYS B 190           
SHEET    1 AA8 3 LEU B  49  THR B  56  0                                        
SHEET    2 AA8 3 SER B  84  LEU B  94 -1  O  ILE B  88   N  LEU B  52           
SHEET    3 AA8 3 TYR B  73  LEU B  75 -1  N  ALA B  74   O  GLU B  87           
SHEET    1 AA9 4 LEU B 115  LEU B 118  0                                        
SHEET    2 AA9 4 TYR B 130  SER B 133 -1  O  PHE B 132   N  GLN B 116           
SHEET    3 AA9 4 LEU B 204  GLY B 207 -1  O  VAL B 206   N  LEU B 131           
SHEET    4 AA9 4 VAL B 167  MET B 170 -1  N  VAL B 167   O  GLY B 207           
SHEET    1 AB1 4 GLU B 210  GLN B 213  0                                        
SHEET    2 AB1 4 LEU B 219  SER B 222 -1  O  SER B 222   N  GLU B 210           
SHEET    3 AB1 4 ASP B 257  VAL B 260  1  O  LEU B 258   N  TRP B 221           
SHEET    4 AB1 4 LEU B 275  VAL B 278  1  O  VAL B 278   N  LEU B 259           
SHEET    1 AB2 2 VAL B 306  ASN B 308  0                                        
SHEET    2 AB2 2 LYS B 417  ILE B 419  1  O  ILE B 419   N  THR B 307           
SHEET    1 AB3 7 THR C  60  VAL C  65  0                                        
SHEET    2 AB3 7 GLU C  99  GLU C 107 -1  O  GLU C 103   N  VAL C  65           
SHEET    3 AB3 7 THR C  33  SER C  44 -1  N  VAL C  42   O  ILE C 100           
SHEET    4 AB3 7 CYS C  16  ASP C  28 -1  N  ARG C  17   O  GLN C  43           
SHEET    5 AB3 7 LYS C 153  PRO C 163  1  O  GLU C 159   N  LEU C  23           
SHEET    6 AB3 7 ARG C 186  PRO C 198 -1  O  ILE C 197   N  LEU C 154           
SHEET    7 AB3 7 ILE C 173  PRO C 179 -1  N  ASP C 175   O  LYS C 190           
SHEET    1 AB4 3 LEU C  49  THR C  56  0                                        
SHEET    2 AB4 3 SER C  84  LEU C  94 -1  O  ILE C  88   N  LEU C  52           
SHEET    3 AB4 3 TYR C  73  LEU C  75 -1  N  ALA C  74   O  GLU C  87           
SHEET    1 AB5 4 LEU C 115  LEU C 118  0                                        
SHEET    2 AB5 4 TYR C 130  SER C 133 -1  O  TYR C 130   N  LEU C 118           
SHEET    3 AB5 4 LEU C 204  GLY C 207 -1  O  VAL C 206   N  LEU C 131           
SHEET    4 AB5 4 VAL C 167  MET C 170 -1  N  VAL C 167   O  GLY C 207           
SHEET    1 AB6 4 GLU C 210  GLN C 213  0                                        
SHEET    2 AB6 4 LEU C 219  SER C 222 -1  O  SER C 222   N  GLU C 210           
SHEET    3 AB6 4 ASP C 257  VAL C 260  1  O  LEU C 258   N  TRP C 221           
SHEET    4 AB6 4 LEU C 275  VAL C 278  1  O  THR C 276   N  ASP C 257           
SHEET    1 AB7 2 VAL C 306  ASN C 308  0                                        
SHEET    2 AB7 2 LYS C 417  ILE C 419  1  O  ILE C 419   N  THR C 307           
LINK         NE2 HIS A 295                ZN    ZN A 900     1555   1555  2.11  
LINK         NE2 HIS A 299                ZN    ZN A 900     1555   1555  2.02  
LINK         OE1 GLU A 318                ZN    ZN A 900     1555   1555  2.03  
LINK         OE2 GLU A 318                ZN    ZN A 900     1555   1555  2.01  
LINK         NE2 HIS B 295                ZN    ZN B 900     1555   1555  2.05  
LINK         NE2 HIS B 299                ZN    ZN B 900     1555   1555  2.11  
LINK         OE1 GLU B 318                ZN    ZN B 900     1555   1555  2.05  
LINK         OE2 GLU B 318                ZN    ZN B 900     1555   1555  2.03  
LINK         NE2 HIS C 295                ZN    ZN C 900     1555   1555  2.11  
LINK         NE2 HIS C 299                ZN    ZN C 900     1555   1555  2.03  
LINK         OE1 GLU C 318                ZN    ZN C 900     1555   1555  2.01  
LINK         OE2 GLU C 318                ZN    ZN C 900     1555   1555  2.00  
CISPEP   1 GLN A  136    ALA A  137          0         0.86                     
CISPEP   2 GLN B  136    ALA B  137          0        -1.41                     
CISPEP   3 ALA B  510    PRO B  511          0         0.16                     
CISPEP   4 GLN C  136    ALA C  137          0         2.51                     
SITE     1 AC1  4 GLU A 271  HIS A 295  HIS A 299  GLU A 318                    
SITE     1 AC2  4 GLU B 271  HIS B 295  HIS B 299  GLU B 318                    
SITE     1 AC3  4 HIS C 295  HIS C 299  GLU C 318  HOH C1002                    
CRYST1   51.970  132.150  320.120  90.00  90.00  90.00 P 21 21 21   12          
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      0.019242  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007567  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003124        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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