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Database: PDB
Entry: 5NI2
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Original site: 5NI2 
HEADER    HYDROLASE                               23-MAR-17   5NI2              
TITLE     CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT E271A IN COMPLEX WITH LTA4    
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_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT3MB4                                    
KEYWDS    METALLOPEPTIDASE, EPOXIDE HYDROLASE, LEUKOTRIENE A4, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA                                                         
REVDAT   3   13-SEP-17 5NI2    1       JRNL                                     
REVDAT   2   06-SEP-17 5NI2    1       JRNL                                     
REVDAT   1   23-AUG-17 5NI2    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.    1.50 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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.37                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 122196                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6121                            
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 39.3823 -  4.6621    1.00     4178   212  0.1782 0.1861        
REMARK   3     2  4.6621 -  3.7013    1.00     4031   187  0.1351 0.1547        
REMARK   3     3  3.7013 -  3.2337    1.00     3927   212  0.1578 0.1797        
REMARK   3     4  3.2337 -  2.9381    1.00     3921   213  0.1686 0.1999        
REMARK   3     5  2.9381 -  2.7276    1.00     3921   186  0.1554 0.1979        
REMARK   3     6  2.7276 -  2.5668    1.00     3917   216  0.1554 0.1918        
REMARK   3     7  2.5668 -  2.4383    1.00     3899   227  0.1568 0.1938        
REMARK   3     8  2.4383 -  2.3322    1.00     3902   193  0.1537 0.1638        
REMARK   3     9  2.3322 -  2.2424    1.00     3920   173  0.1524 0.1572        
REMARK   3    10  2.2424 -  2.1650    1.00     3868   207  0.1544 0.1794        
REMARK   3    11  2.1650 -  2.0973    1.00     3883   211  0.1645 0.2042        
REMARK   3    12  2.0973 -  2.0374    1.00     3876   212  0.1653 0.1952        
REMARK   3    13  2.0374 -  1.9837    1.00     3847   216  0.1722 0.1883        
REMARK   3    14  1.9837 -  1.9353    0.99     3833   202  0.1831 0.2443        
REMARK   3    15  1.9353 -  1.8914    1.00     3870   206  0.1968 0.2123        
REMARK   3    16  1.8914 -  1.8511    1.00     3858   215  0.1932 0.2226        
REMARK   3    17  1.8511 -  1.8141    1.00     3874   200  0.2032 0.2410        
REMARK   3    18  1.8141 -  1.7798    1.00     3840   189  0.2316 0.2570        
REMARK   3    19  1.7798 -  1.7481    1.00     3876   195  0.2453 0.2774        
REMARK   3    20  1.7481 -  1.7184    1.00     3818   208  0.2482 0.2488        
REMARK   3    21  1.7184 -  1.6907    1.00     3868   208  0.2484 0.2506        
REMARK   3    22  1.6907 -  1.6647    1.00     3835   200  0.2571 0.2890        
REMARK   3    23  1.6647 -  1.6402    1.00     3865   217  0.2693 0.2934        
REMARK   3    24  1.6402 -  1.6171    1.00     3846   195  0.2808 0.3102        
REMARK   3    25  1.6171 -  1.5953    1.00     3822   219  0.2992 0.3056        
REMARK   3    26  1.5953 -  1.5745    1.00     3840   190  0.3065 0.3240        
REMARK   3    27  1.5745 -  1.5549    0.99     3848   209  0.3158 0.3088        
REMARK   3    28  1.5549 -  1.5361    1.00     3803   205  0.3394 0.3528        
REMARK   3    29  1.5361 -  1.5183    0.98     3763   212  0.3568 0.3505        
REMARK   3    30  1.5183 -  1.5012    0.91     3526   186  0.3672 0.3700        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           5116                                  
REMARK   3   ANGLE     :  0.995           6951                                  
REMARK   3   CHIRALITY :  0.053            773                                  
REMARK   3   PLANARITY :  0.006            887                                  
REMARK   3   DIHEDRAL  : 14.332           1934                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 3:208                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9118  52.7132  21.9584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4932 T22:   0.3266                                     
REMARK   3      T33:   0.4224 T12:  -0.1878                                     
REMARK   3      T13:  -0.1925 T23:   0.1734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3265 L22:   0.1253                                     
REMARK   3      L33:   0.3030 L12:   0.0999                                     
REMARK   3      L13:   0.0065 L23:   0.0797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1216 S12:  -0.0390 S13:  -0.0836                       
REMARK   3      S21:  -0.1695 S22:   0.2594 S23:   0.2373                       
REMARK   3      S31:   0.4156 S32:  -0.3347 S33:   0.2381                       
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):  20.6729  65.7243  31.1478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2490 T22:   0.2697                                     
REMARK   3      T33:   0.2843 T12:   0.0231                                     
REMARK   3      T13:  -0.0313 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1159 L22:   0.4302                                     
REMARK   3      L33:   0.6965 L12:   0.0598                                     
REMARK   3      L13:  -0.1195 L23:  -0.2948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:  -0.0971 S13:  -0.0757                       
REMARK   3      S21:  -0.0179 S22:   0.0570 S23:   0.0449                       
REMARK   3      S31:   0.1943 S32:   0.0160 S33:   0.0005                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7891  82.0586  10.8433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2492 T22:   0.2937                                     
REMARK   3      T33:   0.2397 T12:   0.0002                                     
REMARK   3      T13:  -0.0106 T23:   0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1869 L22:   0.3990                                     
REMARK   3      L33:   0.3692 L12:   0.1100                                     
REMARK   3      L13:  -0.0309 L23:  -0.1340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0009 S12:   0.0335 S13:  -0.0028                       
REMARK   3      S21:  -0.1108 S22:   0.0643 S23:   0.0231                       
REMARK   3      S31:   0.0472 S32:   0.0430 S33:  -0.0000                       
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 5NI2 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_1200003967.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122621                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.09879                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.07700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.670                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (W/V) PEG 8000, 100 MM IMIDAZOLE     
REMARK 280  PH 6.7, 5 MM YBCL3, LIQUID DIFFUSION, TEMPERATURE 277K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       33.85500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.71500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       33.85500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       66.71500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 300 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1139  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1437  LIES ON A SPECIAL POSITION.                          
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     ASP A   610                                                      
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   HG   SER A   352     OG   SER A   380              1.60            
REMARK 500   OE2  GLU A   121     O    HOH A   801              1.95            
REMARK 500   O    HOH A  1208     O    HOH A  1407              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  79       73.41   -116.63                                   
REMARK 500    SER A  80     -120.30     31.95                                   
REMARK 500    CYS A 274      -10.78     75.66                                   
REMARK 500    LEU A 275       85.63   -157.49                                   
REMARK 500    ASP A 286       10.37   -141.62                                   
REMARK 500    PHE A 432       46.06    -96.00                                   
REMARK 500    LYS A 546       34.06     74.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1439        DISTANCE =  6.49 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 107   OE1                                                    
REMARK 620 2 GLU A 107   OE2  51.3                                              
REMARK 620 3 HOH A1189   O    73.2  86.0                                        
REMARK 620 4 GLU A 127   OE1 109.9  67.4 136.1                                  
REMARK 620 5 GLU A 127   OE2 108.9  67.0 137.2   1.6                            
REMARK 620 6 HOH A1164   O   116.6  77.4 144.4  10.8  10.6                      
REMARK 620 7 HOH A1285   O    87.7 117.6 129.7  94.0  92.8  85.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 102.9                                              
REMARK 620 3 GLU A 318   OE1 100.1 114.0                                        
REMARK 620 4 DJ3 A 704   OAT  99.0 122.8 113.0                                  
REMARK 620 5 DJ3 A 704   OAT  98.3 123.1 113.2   0.7                            
REMARK 620 6 DJ3 A 704   OAT 104.1 123.1 109.1   5.7   6.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 422   OD1                                                    
REMARK 620 2 ASP A 422   OD2  53.2                                              
REMARK 620 3 ASP A 426   OD1  76.9 105.3                                        
REMARK 620 4 ASP A 426   OD2  94.5  77.1  53.2                                  
REMARK 620 5 HOH A 951   O    72.7 123.7  73.1 126.2                            
REMARK 620 6 ASP A 481   OD1  31.1  84.0  58.9  99.3  45.8                      
REMARK 620 7 ASP A 481   OD2  32.5  85.4  58.4  99.7  44.5   1.4                
REMARK 620 8 HOH A 828   O    76.4  72.9 147.0 148.0  80.8  88.5  88.9          
REMARK 620 9 HOH A1128   O   131.0  78.2 128.5  79.2 147.3 162.1 163.4  84.0    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 A 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MS6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DPR   RELATED DB: PDB                                   
DBREF  5NI2 A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 5NI2 MET A   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NI2 HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI2 ALA A  271  UNP  P09960    GLU   272 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 ALA 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 ARG MET LYS          
SEQRES  45 A  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 A  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 A  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 A  617  LYS ASP LEU LYS VAL ASP                                      
HET     ZN  A 701       1                                                       
HET     YB  A 702       1                                                       
HET     YB  A 703       1                                                       
HET    DJ3  A 704     156                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     DJ3 5S-5,6-OXIDO-7,9-TRANS-11,14-CIS-EICOSATETRAENOIC ACID           
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    2(YB 3+)                                                     
FORMUL   5  DJ3    C20 H30 O3                                                   
FORMUL   6  HOH   *639(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 PRO A  198  ILE A  202  5                                   5    
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 PRO A  280  LEU A  283  5                                   4    
HELIX    8 AA8 SER A  290  HIS A  299  1                                  10    
HELIX    9 AA9 THR A  310  ASP A  312  5                                   3    
HELIX   10 AB1 HIS A  313  GLY A  334  1                                  22    
HELIX   11 AB2 GLY A  334  GLY A  357  1                                  24    
HELIX   12 AB3 HIS A  360  LYS A  364  5                                   5    
HELIX   13 AB4 ASP A  373  TYR A  378  1                                   6    
HELIX   14 AB5 SER A  380  GLY A  398  1                                  19    
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 THR A  465  THR A  477  1                                  13    
HELIX   20 AC2 LYS A  479  PHE A  486  5                                   8    
HELIX   21 AC3 ASN A  487  LYS A  492  5                                   6    
HELIX   22 AC4 SER A  495  GLN A  508  1                                  14    
HELIX   23 AC5 PRO A  513  ASN A  525  1                                  13    
HELIX   24 AC6 PHE A  526  ILE A  529  5                                   4    
HELIX   25 AC7 ASN A  531  SER A  545  1                                  15    
HELIX   26 AC8 TRP A  547  ASP A  549  5                                   3    
HELIX   27 AC9 ALA A  550  GLN A  561  1                                  12    
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  SER A 105   N  LYS A  63           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6 AA1 8 LEU A 154  PRO A 163  1  O  SER A 161   N  VAL A  27           
SHEET    7 AA1 8 ARG A 186  ILE A 197 -1  O  GLN A 193   N  TYR A 156           
SHEET    8 AA1 8 ILE A 173  PRO A 179 -1  N  ASP A 175   O  LYS A 190           
SHEET    1 AA2 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA2 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA2 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA3 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA3 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3 AA3 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA3 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1 AA4 5 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 5 THR A 218  SER A 222 -1  O  SER A 222   N  GLU A 210           
SHEET    3 AA4 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5 AA4 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1 AA5 2 VAL A 306  ASN A 308  0                                        
SHEET    2 AA5 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OE1 GLU A 107                YB    YB A 703     1555   1555  2.52  
LINK         OE2 GLU A 107                YB    YB A 703     1555   1555  2.55  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.11  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.00  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  1.99  
LINK         OD1 ASP A 422                YB    YB A 702     1555   1555  2.33  
LINK         OD2 ASP A 422                YB    YB A 702     1555   1555  2.57  
LINK         OD1 ASP A 426                YB    YB A 702     1555   1555  2.60  
LINK         OD2 ASP A 426                YB    YB A 702     1555   1555  2.30  
LINK        ZN    ZN A 701                 OATADJ3 A 704     1555   1555  2.24  
LINK        ZN    ZN A 701                 OATBDJ3 A 704     1555   1555  2.21  
LINK        ZN    ZN A 701                 OATCDJ3 A 704     1555   1555  2.14  
LINK        YB    YB A 702                 O   HOH A 951     1555   1555  2.23  
LINK        YB    YB A 703                 O   HOH A1189     1555   1555  2.53  
LINK         OE1 GLU A 127                YB    YB A 703     1555   2555  2.42  
LINK         OE2 GLU A 127                YB    YB A 703     1555   2555  3.16  
LINK         OD1 ASP A 481                YB    YB A 702     1555   3575  2.58  
LINK         OD2 ASP A 481                YB    YB A 702     1555   3575  2.37  
LINK        YB    YB A 702                 O   HOH A 828     1555   3475  2.38  
LINK        YB    YB A 702                 O   HOH A1128     1555   3475  2.45  
LINK        YB    YB A 703                 O   HOH A1164     1555   2555  2.46  
LINK        YB    YB A 703                 O   HOH A1285     1555   2555  2.62  
CISPEP   1 GLN A  136    ALA A  137          0         1.14                     
CISPEP   2 ALA A  510    PRO A  511          0        -0.07                     
SITE     1 AC1  5 HIS A 295  HIS A 299  GLU A 318  DJ3 A 704                    
SITE     2 AC1  5 HOH A 802                                                     
SITE     1 AC2  6 ASP A 422  ASP A 426  ASP A 481  HOH A 828                    
SITE     2 AC2  6 HOH A 951  HOH A1128                                          
SITE     1 AC3  5 GLU A 107  GLU A 127  HOH A1164  HOH A1189                    
SITE     2 AC3  5 HOH A1285                                                     
SITE     1 AC4 26 GLN A 136  ALA A 137  TYR A 267  GLY A 268                    
SITE     2 AC4 26 GLY A 269  HIS A 295  GLU A 296  HIS A 299                    
SITE     3 AC4 26 TRP A 311  PHE A 314  GLU A 318  VAL A 367                    
SITE     4 AC4 26 PRO A 374  ALA A 377  TYR A 378  TYR A 383                    
SITE     5 AC4 26 ARG A 563  LYS A 565   ZN A 701  HOH A 802                    
SITE     6 AC4 26 HOH A 807  HOH A 825  HOH A 843  HOH A 867                    
SITE     7 AC4 26 HOH A 891  HOH A1192                                          
CRYST1   67.710   84.610  133.430  90.00  90.00  90.00 P 21 2 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014769  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011819  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007495        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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