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Database: PDB
Entry: 5NIA
LinkDB: 5NIA
Original site: 5NIA 
HEADER    HYDROLASE                               23-MAR-17   5NIA              
TITLE     CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT D375N IN OPEN CONFORMATION    
TITLE    2 (CRYSTAL FORM I)                                                     
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, OPEN CONFORMATION, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA                                                         
REVDAT   3   13-SEP-17 5NIA    1       JRNL                                     
REVDAT   2   06-SEP-17 5NIA    1       JRNL                                     
REVDAT   1   23-AUG-17 5NIA    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.    1.76 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 64239                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3271                            
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 44.1811 -  5.0148    1.00     2653   149  0.1665 0.1893        
REMARK   3     2  5.0148 -  3.9812    1.00     2685   121  0.1352 0.1457        
REMARK   3     3  3.9812 -  3.4782    1.00     2603   190  0.1567 0.1801        
REMARK   3     4  3.4782 -  3.1603    1.00     2634   141  0.1755 0.2065        
REMARK   3     5  3.1603 -  2.9338    1.00     2628   185  0.1840 0.2202        
REMARK   3     6  2.9338 -  2.7609    1.00     2661   146  0.1856 0.2062        
REMARK   3     7  2.7609 -  2.6226    1.00     2648   128  0.1813 0.2272        
REMARK   3     8  2.6226 -  2.5085    1.00     2653   153  0.1783 0.2211        
REMARK   3     9  2.5085 -  2.4119    1.00     2660   125  0.1757 0.2038        
REMARK   3    10  2.4119 -  2.3287    1.00     2676   150  0.1861 0.2274        
REMARK   3    11  2.3287 -  2.2559    1.00     2646   134  0.1853 0.2209        
REMARK   3    12  2.2559 -  2.1914    1.00     2624   169  0.1848 0.2157        
REMARK   3    13  2.1914 -  2.1337    1.00     2631   153  0.1897 0.2596        
REMARK   3    14  2.1337 -  2.0816    1.00     2644   151  0.2027 0.2464        
REMARK   3    15  2.0816 -  2.0343    1.00     2697   124  0.2197 0.2376        
REMARK   3    16  2.0343 -  1.9910    1.00     2619   137  0.2160 0.2351        
REMARK   3    17  1.9910 -  1.9512    1.00     2664   147  0.2248 0.2329        
REMARK   3    18  1.9512 -  1.9144    1.00     2629   143  0.2335 0.2824        
REMARK   3    19  1.9144 -  1.8802    1.00     2689   128  0.2458 0.2588        
REMARK   3    20  1.8802 -  1.8483    1.00     2688   138  0.2781 0.2980        
REMARK   3    21  1.8483 -  1.8185    1.00     2670   136  0.3016 0.3572        
REMARK   3    22  1.8185 -  1.7905    1.00     2648   113  0.3234 0.3476        
REMARK   3    23  1.7905 -  1.7642    0.96     2618   110  0.3572 0.3973        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.54                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.94                          
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      :  0.015           5089                                  
REMARK   3   ANGLE     :  1.229           6925                                  
REMARK   3   CHIRALITY :  0.068            773                                  
REMARK   3   PLANARITY :  0.010            884                                  
REMARK   3   DIHEDRAL  : 16.714           1887                                  
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 1:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0465   8.2630 -25.7120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2580 T22:   0.2860                                     
REMARK   3      T33:   0.2220 T12:  -0.0261                                     
REMARK   3      T13:  -0.0077 T23:  -0.0600                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9023 L22:   1.4730                                     
REMARK   3      L33:   0.1907 L12:   0.6080                                     
REMARK   3      L13:  -0.4888 L23:  -0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1445 S12:   0.2282 S13:  -0.2317                       
REMARK   3      S21:  -0.1432 S22:   0.1258 S23:  -0.0296                       
REMARK   3      S31:   0.0564 S32:  -0.1830 S33:   0.0185                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 209:465 OR (RESI 900 AND RESNAME      
REMARK   3               ZN)                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8608  26.6673 -10.2289              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2539 T22:   0.2295                                     
REMARK   3      T33:   0.2836 T12:  -0.0337                                     
REMARK   3      T13:  -0.0260 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0914 L22:   0.5656                                     
REMARK   3      L33:   0.3291 L12:   0.5194                                     
REMARK   3      L13:  -0.4090 L23:  -0.3086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1833 S12:  -0.0440 S13:  -0.0059                       
REMARK   3      S21:   0.1284 S22:  -0.1474 S23:  -0.1013                       
REMARK   3      S31:  -0.1268 S32:   0.0228 S33:   0.0003                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A): -22.2256  18.7377  15.3466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7085 T22:   0.4854                                     
REMARK   3      T33:   0.4721 T12:  -0.1873                                     
REMARK   3      T13:  -0.1998 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5891 L22:   0.1421                                     
REMARK   3      L33:   0.6671 L12:  -0.1866                                     
REMARK   3      L13:   0.1745 L23:  -0.2035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5362 S12:  -0.3746 S13:  -0.6486                       
REMARK   3      S21:   0.6078 S22:  -0.2214 S23:  -0.1626                       
REMARK   3      S31:   0.1971 S32:   0.1814 S33:   0.2528                       
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 5NIA 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_1200004025.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.7-8.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
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   : 64241                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.764                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.167                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.10430                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.78500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.020                              
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: 8% (W/V) PEG 20 000, 15% (W/V) PEG MME   
REMARK 280  550, 100 MM HEPES/MOPS PH 7.7-8.0, 15 MM CACL2, 15 MM MGCL2,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.50000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.16730            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.96000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       76.50000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       44.16730            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       24.96000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       76.50000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       44.16730            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       24.96000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       88.33459            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       49.92000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       88.33459            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       49.92000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       88.33459            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       49.92000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 24080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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     ASP A   610                                                      
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       78.18   -115.65                                   
REMARK 500    SER A  80     -120.75     34.64                                   
REMARK 500    ASP A 183      107.18   -167.07                                   
REMARK 500    GLU A 271       46.66    -78.06                                   
REMARK 500    CYS A 274       -3.03     75.31                                   
REMARK 500    LEU A 275       79.31   -155.17                                   
REMARK 500    GLU A 358        1.06    -66.08                                   
REMARK 500    TYR A 378        2.46    -62.40                                   
REMARK 500    SER A 380      161.57    176.11                                   
REMARK 500    PRO A 382        5.31    -50.38                                   
REMARK 500    PHE A 486      150.06    -49.85                                   
REMARK 500    ASN A 531      118.89    -38.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH A  1164                                                      
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  93.5                                              
REMARK 620 3 GLU A 318   OE1  84.8  98.3                                        
REMARK 620 4 GLU A 318   OE1 100.6  91.5  16.8                                  
REMARK 620 5 GLU A 318   OE2 146.7  97.6  62.6  48.0                            
REMARK 620 6 HOH A1011   O   164.6  99.5 101.2  87.3  39.3                      
REMARK 620 7 HOH A1122   O    94.7  91.5 170.2 164.1 116.2  76.9                
REMARK 620 8 HOH A1162   O    94.0 168.9  90.5  95.1  80.5  72.0  79.7          
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 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                                   
DBREF  5NIA A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 5NIA MET A   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NIA HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NIA 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 900       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *351(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  PHE A  234  1                                  12    
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  SER A  300  1                                   8    
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 PRO A  382  LEU A  397  1                                  16    
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 MET A  462  THR A  477  1                                  16    
HELIX   21 AC3 LYS A  479  SER A  485  5                                   7    
HELIX   22 AC4 ASN A  487  LYS A  492  5                                   6    
HELIX   23 AC5 SER A  495  ARG A  509  1                                  15    
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 ASP A  549  GLN A  561  1                                  13    
HELIX   28 AD1 ARG A  563  PHE A  577  1                                  15    
HELIX   29 AD2 PHE A  577  LYS A  592  1                                  16    
HELIX   30 AD3 ALA A  593  MET A  595  5                                   3    
HELIX   31 AD4 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  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  17   O  GLN A  43           
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  LEU A  94   N  LEU A  49           
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  PHE A 132   N  GLN A 116           
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 4 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 4 THR A 218  SER A 222 -1  O  SER A 222   N  GLU A 210           
SHEET    3 AA4 4 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4 AA4 4 LEU A 275  VAL A 278  1  O  VAL A 278   N  LEU A 259           
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         NE2 HIS A 295                ZN    ZN A 900     1555   1555  2.10  
LINK         NE2 HIS A 299                ZN    ZN A 900     1555   1555  2.07  
LINK         OE1AGLU A 318                ZN    ZN A 900     1555   1555  2.13  
LINK         OE1BGLU A 318                ZN    ZN A 900     1555   1555  2.15  
LINK         OE2AGLU A 318                ZN    ZN A 900     1555   1555  2.11  
LINK        ZN    ZN A 900                 O  BHOH A1011     1555   1555  2.35  
LINK        ZN    ZN A 900                 O   HOH A1122     1555   1555  2.19  
LINK        ZN    ZN A 900                 O   HOH A1162     1555   1555  2.16  
CISPEP   1 GLN A  136    ALA A  137          0        -5.53                     
CISPEP   2 ALA A  510    PRO A  511          0         3.06                     
SITE     1 AC1  6 HIS A 295  HIS A 299  GLU A 318  HOH A1011                    
SITE     2 AC1  6 HOH A1122  HOH A1162                                          
CRYST1  153.000  153.000   74.880  90.00  90.00 120.00 H 3           9          
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      0.006536  0.003774  0.000000        0.00000                         
SCALE2      0.000000  0.007547  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013355        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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