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Database: PDB
Entry: 5W8H
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HEADER    OXIDOREDUCTASE                          21-JUN-17   5W8H              
TITLE     CRYSTAL STRUCTURE OF LACTATE DEHYDROGENASE A IN COMPLEX WITH INHIBITOR
TITLE    2 COMPOUND 11                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-LACTATE DEHYDROGENASE A CHAIN;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: LDH-A,CELL PROLIFERATION-INDUCING GENE 19 PROTEIN,LDH MUSCLE
COMPND   5 SUBUNIT,LDH-M,RENAL CARCINOMA ANTIGEN NY-REN-59;                     
COMPND   6 EC: 1.1.1.27;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LDHA, PIG19;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    OXIDOREDUCTASE, OXIDOREDUCTASE INHIBITOR                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.LUKACS,D.M.DRANOW                                                 
REVDAT   1   17-JAN-18 5W8H    0                                                
JRNL        AUTH   G.RAI,K.R.BRIMACOMBE,B.T.MOTT,D.J.URBAN,X.HU,S.M.YANG,       
JRNL        AUTH 2 T.D.LEE,D.M.CHEFF,J.KOUZNETSOVA,G.A.BENAVIDES,K.POHIDA,      
JRNL        AUTH 3 E.J.KUENSTNER,D.K.LUCI,C.M.LUKACS,D.R.DAVIES,D.M.DRANOW,     
JRNL        AUTH 4 H.ZHU,G.SULIKOWSKI,W.J.MOORE,G.M.STOTT,A.J.FLINT,M.D.HALL,   
JRNL        AUTH 5 V.M.DARLEY-USMAR,L.M.NECKERS,C.V.DANG,A.G.WATERSON,          
JRNL        AUTH 6 A.SIMEONOV,A.JADHAV,D.J.MALONEY                              
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF POTENT, CELL-ACTIVE            
JRNL        TITL 2 PYRAZOLE-BASED INHIBITORS OF LACTATE DEHYDROGENASE (LDH).    
JRNL        REF    J. MED. CHEM.                 V.  60  9184 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29120638                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00941                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 131863                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6602                            
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  1.8200 -  1.8000    1.00     4136   200  0.2150 0.2660        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.57                          
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      :  0.012          10752                                  
REMARK   3   ANGLE     :  1.259          14676                                  
REMARK   3   CHIRALITY :  0.066           1705                                  
REMARK   3   PLANARITY :  0.006           1864                                  
REMARK   3   DIHEDRAL  : 15.325           3995                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 20 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  49.1855  -3.2688   7.3210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2293 T22:   0.3066                                     
REMARK   3      T33:   0.2229 T12:  -0.0050                                     
REMARK   3      T13:   0.0367 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7925 L22:   0.8435                                     
REMARK   3      L33:   0.5534 L12:  -0.7670                                     
REMARK   3      L13:  -0.4009 L23:   0.5823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1312 S12:  -0.1432 S13:   0.4728                       
REMARK   3      S21:  -0.3207 S22:   0.1281 S23:  -0.6559                       
REMARK   3      S31:  -0.3578 S32:   0.1936 S33:   0.0331                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 150 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  47.2229  14.0091  32.2516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1604 T22:   0.1256                                     
REMARK   3      T33:   0.0985 T12:  -0.0646                                     
REMARK   3      T13:  -0.0187 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7948 L22:   2.2284                                     
REMARK   3      L33:   0.6113 L12:  -0.2040                                     
REMARK   3      L13:  -0.4023 L23:  -0.2616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0134 S12:  -0.0459 S13:   0.0996                       
REMARK   3      S21:   0.1233 S22:   0.0175 S23:  -0.1873                       
REMARK   3      S31:  -0.1741 S32:   0.2260 S33:  -0.0043                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 151 THROUGH 275 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6404  17.1792  43.7225              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2368 T22:   0.1156                                     
REMARK   3      T33:   0.1320 T12:   0.0332                                     
REMARK   3      T13:   0.0251 T23:  -0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0322 L22:   0.5024                                     
REMARK   3      L33:   0.4313 L12:  -0.0344                                     
REMARK   3      L13:  -0.0104 L23:  -0.0592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:  -0.1884 S13:   0.0697                       
REMARK   3      S21:   0.1859 S22:   0.0415 S23:   0.0300                       
REMARK   3      S31:  -0.2224 S32:  -0.0330 S33:  -0.0020                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 276 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3672  32.1221  38.5429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4124 T22:   0.0984                                     
REMARK   3      T33:   0.2394 T12:  -0.0258                                     
REMARK   3      T13:   0.0220 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4187 L22:   0.5333                                     
REMARK   3      L33:   0.3850 L12:   0.0663                                     
REMARK   3      L13:   0.2775 L23:  -0.1134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0358 S12:   0.0512 S13:   0.3726                       
REMARK   3      S21:   0.1374 S22:   0.0174 S23:   0.1324                       
REMARK   3      S31:  -0.4756 S32:  -0.0054 S33:   0.0023                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 41 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5125  -1.4969  45.4550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1863 T22:   0.1799                                     
REMARK   3      T33:   0.1492 T12:   0.0207                                     
REMARK   3      T13:   0.0347 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2757 L22:   0.5519                                     
REMARK   3      L33:   0.2518 L12:  -0.3524                                     
REMARK   3      L13:   0.1749 L23:   0.0497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0114 S12:  -0.1267 S13:  -0.1004                       
REMARK   3      S21:   0.0789 S22:   0.0041 S23:   0.1979                       
REMARK   3      S31:  -0.0926 S32:  -0.1807 S33:   0.0002                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9756  -3.7039  47.7843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1550 T22:   0.1375                                     
REMARK   3      T33:   0.1292 T12:   0.0072                                     
REMARK   3      T13:   0.0203 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3359 L22:   0.9879                                     
REMARK   3      L33:   0.3138 L12:  -0.2399                                     
REMARK   3      L13:  -0.3193 L23:   0.0544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0285 S12:  -0.1411 S13:   0.0152                       
REMARK   3      S21:   0.2474 S22:   0.0377 S23:   0.1130                       
REMARK   3      S31:  -0.0983 S32:  -0.0408 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 94 THROUGH 177 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6501 -18.0117  42.2616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0865 T22:   0.0636                                     
REMARK   3      T33:   0.1015 T12:  -0.0043                                     
REMARK   3      T13:  -0.0082 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5463 L22:   0.4148                                     
REMARK   3      L33:   1.4794 L12:  -0.1431                                     
REMARK   3      L13:   0.3300 L23:  -0.1023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0184 S12:  -0.0382 S13:  -0.0643                       
REMARK   3      S21:   0.0970 S22:   0.0057 S23:  -0.0506                       
REMARK   3      S31:   0.0088 S32:   0.0262 S33:  -0.0003                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 178 THROUGH 308 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.5398 -18.9908  27.4787              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0822 T22:   0.0948                                     
REMARK   3      T33:   0.1025 T12:   0.0146                                     
REMARK   3      T13:  -0.0156 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5539 L22:   0.4076                                     
REMARK   3      L33:   1.4087 L12:  -0.1841                                     
REMARK   3      L13:  -0.0679 L23:   0.1124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:   0.0634 S13:  -0.0663                       
REMARK   3      S21:   0.0133 S22:   0.0045 S23:  -0.0584                       
REMARK   3      S31:   0.0779 S32:   0.1371 S33:   0.0019                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 40 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0622 -18.9184  24.8311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1881 T22:   0.1447                                     
REMARK   3      T33:   0.2114 T12:  -0.0137                                     
REMARK   3      T13:  -0.0160 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3488 L22:   0.1897                                     
REMARK   3      L33:   0.3674 L12:  -0.0912                                     
REMARK   3      L13:  -0.1501 L23:   0.2264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:  -0.0918 S13:  -0.2144                       
REMARK   3      S21:   0.1045 S22:   0.1062 S23:  -0.0123                       
REMARK   3      S31:   0.2466 S32:  -0.0604 S33:   0.0076                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6477 -15.2883  21.5799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1197 T22:   0.1500                                     
REMARK   3      T33:   0.1973 T12:  -0.0196                                     
REMARK   3      T13:  -0.0186 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5123 L22:   0.4368                                     
REMARK   3      L33:   0.6857 L12:  -0.2815                                     
REMARK   3      L13:  -0.5112 L23:   0.0647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0380 S12:   0.0321 S13:  -0.2020                       
REMARK   3      S21:  -0.0439 S22:   0.0433 S23:   0.0715                       
REMARK   3      S31:   0.1587 S32:  -0.1267 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 94 THROUGH 275)                   
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2884   6.1796  28.0448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1373 T22:   0.2034                                     
REMARK   3      T33:   0.1858 T12:   0.0599                                     
REMARK   3      T13:   0.0083 T23:   0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8063 L22:   0.8740                                     
REMARK   3      L33:   0.5529 L12:   0.5067                                     
REMARK   3      L13:   0.0775 L23:   0.0458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0393 S12:   0.0401 S13:   0.1133                       
REMARK   3      S21:  -0.0881 S22:   0.0719 S23:   0.2071                       
REMARK   3      S31:  -0.1485 S32:  -0.2165 S33:   0.0002                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 276 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2932   6.3594  38.2344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1534 T22:   0.3310                                     
REMARK   3      T33:   0.2845 T12:   0.1041                                     
REMARK   3      T13:   0.0550 T23:   0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5153 L22:   0.3714                                     
REMARK   3      L33:   0.6225 L12:   0.4306                                     
REMARK   3      L13:   0.1145 L23:   0.1468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0547 S12:  -0.2580 S13:   0.0919                       
REMARK   3      S21:   0.1965 S22:  -0.0059 S23:   0.2687                       
REMARK   3      S31:  -0.1946 S32:  -0.4264 S33:   0.0059                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 40 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0475  15.0966  16.7760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2598 T22:   0.1113                                     
REMARK   3      T33:   0.1976 T12:   0.0192                                     
REMARK   3      T13:   0.0076 T23:   0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2710 L22:   0.0948                                     
REMARK   3      L33:   0.5565 L12:  -0.1172                                     
REMARK   3      L13:  -0.0517 L23:  -0.0073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0657 S12:   0.1032 S13:   0.1963                       
REMARK   3      S21:   0.0979 S22:   0.1157 S23:   0.0416                       
REMARK   3      S31:  -0.3716 S32:   0.0114 S33:   0.0045                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 41 THROUGH 150 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4635   4.9501   1.3275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1065 T22:   0.1310                                     
REMARK   3      T33:   0.1272 T12:  -0.0037                                     
REMARK   3      T13:  -0.0174 T23:   0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8433 L22:   0.7837                                     
REMARK   3      L33:   1.1592 L12:  -0.3659                                     
REMARK   3      L13:  -0.4205 L23:   0.0863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0599 S12:   0.0995 S13:   0.0169                       
REMARK   3      S21:  -0.0441 S22:  -0.0371 S23:   0.1031                       
REMARK   3      S31:  -0.1442 S32:  -0.0719 S33:  -0.0001                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 213 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4203 -18.2072   9.1136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1034 T22:   0.1239                                     
REMARK   3      T33:   0.1290 T12:   0.0089                                     
REMARK   3      T13:  -0.0169 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5279 L22:   0.6885                                     
REMARK   3      L33:   0.6523 L12:   0.0431                                     
REMARK   3      L13:   0.1395 L23:  -0.0451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0490 S12:   0.0979 S13:  -0.0902                       
REMARK   3      S21:  -0.0841 S22:   0.0329 S23:   0.1436                       
REMARK   3      S31:   0.1716 S32:  -0.0110 S33:  -0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 214 THROUGH 331)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2168 -13.7822   1.9727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1283 T22:   0.1803                                     
REMARK   3      T33:   0.1199 T12:   0.0168                                     
REMARK   3      T13:  -0.0152 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9826 L22:   0.8758                                     
REMARK   3      L33:   1.4102 L12:  -0.5122                                     
REMARK   3      L13:   0.0486 L23:   0.1242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0735 S12:   0.2210 S13:  -0.1938                       
REMARK   3      S21:  -0.0850 S22:  -0.0780 S23:   0.0850                       
REMARK   3      S31:   0.1542 S32:  -0.0265 S33:   0.0030                       
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 5W8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228610.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131874                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.630                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.68                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: PROPRIETARY STRUCTURE OF THE SAME TARGET             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350, 200 MM SODIUM MALONATE,    
REMARK 280  PH 6.8, 10% GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Z                                           
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        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       83.86500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.60500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.86500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.60500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 A 809  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     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     MET C     0                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     GLN C    16                                                      
REMARK 465     MET D     0                                                      
REMARK 465     GLU D    15                                                      
REMARK 465     GLN D    16                                                      
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     LYS A  13    CG   CD   CE   NZ                                   
REMARK 470     GLU A  14    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  16    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  80    CG   CD   CE   NZ                                   
REMARK 470     ARG A  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 101    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     LYS A 231    CG   CD   CE   NZ                                   
REMARK 470     LYS A 283    CG   CD   CE   NZ                                   
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     GLN A 330    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  15    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  16    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 221    CG   CD   CE   NZ                                   
REMARK 470     LYS B 223    CG   CD   CE   NZ                                   
REMARK 470     LYS B 283    CG   CD   CE   NZ                                   
REMARK 470     LYS B 317    CG   CD   CE   NZ                                   
REMARK 470     LYS C  13    CG   CD   CE   NZ                                   
REMARK 470     GLU C  14    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  80    CG   CD   CE   NZ                                   
REMARK 470     ARG C  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     ASP C 220    CG   OD1  OD2                                       
REMARK 470     LYS C 221    CG   CD   CE   NZ                                   
REMARK 470     LYS C 223    CG   CD   CE   NZ                                   
REMARK 470     GLN C 225    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 227    CG   CD   CE   NZ                                   
REMARK 470     GLU C 228    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 231    CG   CD   CE   NZ                                   
REMARK 470     LYS C 242    CG   CD   CE   NZ                                   
REMARK 470     LYS C 283    CG   CD   CE   NZ                                   
REMARK 470     GLU C 310    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  13    CG   CD   CE   NZ                                   
REMARK 470     GLU D  14    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  80    CG   CD   CE   NZ                                   
REMARK 470     ARG D  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 101    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 105    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 220    CG   OD1  OD2                                       
REMARK 470     LYS D 221    CG   CD   CE   NZ                                   
REMARK 470     LYS D 223    CG   CD   CE   NZ                                   
REMARK 470     LYS D 227    CG   CD   CE   NZ                                   
REMARK 470     LYS D 231    CG   CD   CE   NZ                                   
REMARK 470     LYS D 242    CG   CD   CE   NZ                                   
REMARK 470     LYS D 283    CG   CD   CE   NZ                                   
REMARK 470     GLU D 310    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 316    CG   CD   CE   NZ                                   
REMARK 470     LYS D 317    CG   CD   CE   NZ                                   
REMARK 470     GLN D 330    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   669     O    HOH C   811              1.95            
REMARK 500   OD1  ASP D   165     O    HOH D   501              2.00            
REMARK 500   O    HOH A   614     O    HOH A   655              2.07            
REMARK 500   O    HOH B   613     O    HOH B   695              2.11            
REMARK 500   O    HOH D   532     O    HOH D   694              2.12            
REMARK 500   O    HOH B   507     O    HOH B   748              2.12            
REMARK 500   O    HOH B   597     O    HOH B   717              2.12            
REMARK 500   OD2  ASP A   257     O    HOH A   601              2.14            
REMARK 500   OG   SER D   254     O    HOH D   502              2.16            
REMARK 500   O    HOH C   766     O    HOH C   795              2.16            
REMARK 500   OD1  ASP C   165     O    HOH C   601              2.17            
REMARK 500   NH1  ARG D    72     O    HOH D   503              2.18            
REMARK 500   O    HOH C   607     O    HOH C   767              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C   803     O    HOH D   683     2555     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    SER A 248      -50.95   -146.96                                   
REMARK 500    ASN B  20       56.82   -143.22                                   
REMARK 500    SER B 248      -48.42   -153.14                                   
REMARK 500    ASP B 285       40.39    -78.93                                   
REMARK 500    ASN C  20       58.95   -140.60                                   
REMARK 500    SER C 248      -51.13   -152.43                                   
REMARK 500    LYS D  13       60.65   -109.86                                   
REMARK 500    ASN D  20       55.61   -146.73                                   
REMARK 500    SER D 248      -47.93   -157.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLA B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y1 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403                 
DBREF  5W8H A    0   331  UNP    P00338   LDHA_HUMAN       1    332             
DBREF  5W8H B    0   331  UNP    P00338   LDHA_HUMAN       1    332             
DBREF  5W8H C    0   331  UNP    P00338   LDHA_HUMAN       1    332             
DBREF  5W8H D    0   331  UNP    P00338   LDHA_HUMAN       1    332             
SEQRES   1 A  332  MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU          
SEQRES   2 A  332  LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL          
SEQRES   3 A  332  GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE          
SEQRES   4 A  332  LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP          
SEQRES   5 A  332  VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU          
SEQRES   6 A  332  GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL          
SEQRES   7 A  332  SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU          
SEQRES   8 A  332  VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU          
SEQRES   9 A  332  SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE          
SEQRES  10 A  332  LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN          
SEQRES  11 A  332  CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU          
SEQRES  12 A  332  THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN          
SEQRES  13 A  332  ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG          
SEQRES  14 A  332  PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO          
SEQRES  15 A  332  LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP          
SEQRES  16 A  332  SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY          
SEQRES  17 A  332  VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP          
SEQRES  18 A  332  LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL          
SEQRES  19 A  332  VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR          
SEQRES  20 A  332  THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA          
SEQRES  21 A  332  GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL          
SEQRES  22 A  332  SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP          
SEQRES  23 A  332  VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY          
SEQRES  24 A  332  ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU          
SEQRES  25 A  332  GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY          
SEQRES  26 A  332  ILE GLN LYS GLU LEU GLN PHE                                  
SEQRES   1 B  332  MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU          
SEQRES   2 B  332  LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL          
SEQRES   3 B  332  GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE          
SEQRES   4 B  332  LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP          
SEQRES   5 B  332  VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU          
SEQRES   6 B  332  GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL          
SEQRES   7 B  332  SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU          
SEQRES   8 B  332  VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU          
SEQRES   9 B  332  SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE          
SEQRES  10 B  332  LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN          
SEQRES  11 B  332  CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU          
SEQRES  12 B  332  THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN          
SEQRES  13 B  332  ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG          
SEQRES  14 B  332  PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO          
SEQRES  15 B  332  LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP          
SEQRES  16 B  332  SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY          
SEQRES  17 B  332  VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP          
SEQRES  18 B  332  LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL          
SEQRES  19 B  332  VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR          
SEQRES  20 B  332  THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA          
SEQRES  21 B  332  GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL          
SEQRES  22 B  332  SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP          
SEQRES  23 B  332  VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY          
SEQRES  24 B  332  ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU          
SEQRES  25 B  332  GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY          
SEQRES  26 B  332  ILE GLN LYS GLU LEU GLN PHE                                  
SEQRES   1 C  332  MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU          
SEQRES   2 C  332  LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL          
SEQRES   3 C  332  GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE          
SEQRES   4 C  332  LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP          
SEQRES   5 C  332  VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU          
SEQRES   6 C  332  GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL          
SEQRES   7 C  332  SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU          
SEQRES   8 C  332  VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU          
SEQRES   9 C  332  SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE          
SEQRES  10 C  332  LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN          
SEQRES  11 C  332  CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU          
SEQRES  12 C  332  THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN          
SEQRES  13 C  332  ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG          
SEQRES  14 C  332  PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO          
SEQRES  15 C  332  LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP          
SEQRES  16 C  332  SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY          
SEQRES  17 C  332  VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP          
SEQRES  18 C  332  LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL          
SEQRES  19 C  332  VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR          
SEQRES  20 C  332  THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA          
SEQRES  21 C  332  GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL          
SEQRES  22 C  332  SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP          
SEQRES  23 C  332  VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY          
SEQRES  24 C  332  ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU          
SEQRES  25 C  332  GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY          
SEQRES  26 C  332  ILE GLN LYS GLU LEU GLN PHE                                  
SEQRES   1 D  332  MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU          
SEQRES   2 D  332  LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL          
SEQRES   3 D  332  GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE          
SEQRES   4 D  332  LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP          
SEQRES   5 D  332  VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU          
SEQRES   6 D  332  GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL          
SEQRES   7 D  332  SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU          
SEQRES   8 D  332  VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU          
SEQRES   9 D  332  SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE          
SEQRES  10 D  332  LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN          
SEQRES  11 D  332  CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU          
SEQRES  12 D  332  THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN          
SEQRES  13 D  332  ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG          
SEQRES  14 D  332  PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO          
SEQRES  15 D  332  LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP          
SEQRES  16 D  332  SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY          
SEQRES  17 D  332  VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP          
SEQRES  18 D  332  LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL          
SEQRES  19 D  332  VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR          
SEQRES  20 D  332  THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA          
SEQRES  21 D  332  GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL          
SEQRES  22 D  332  SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP          
SEQRES  23 D  332  VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY          
SEQRES  24 D  332  ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU          
SEQRES  25 D  332  GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY          
SEQRES  26 D  332  ILE GLN LYS GLU LEU GLN PHE                                  
HET    9Y1  A 501      24                                                       
HET    9Y1  A 502      24                                                       
HET    ACT  A 503       4                                                       
HET    ACT  A 504       4                                                       
HET    DMS  A 505       4                                                       
HET    MLA  B 401       7                                                       
HET    9Y1  B 402      24                                                       
HET    ACT  B 403       4                                                       
HET    DMS  B 404       4                                                       
HET    9Y1  C 501      24                                                       
HET    9Y1  C 502      24                                                       
HET    9Y1  C 503      24                                                       
HET    9Y1  C 504      24                                                       
HET    GOL  C 505       6                                                       
HET    ACT  D 401       4                                                       
HET    DMS  D 402       4                                                       
HET    GOL  D 403       6                                                       
HETNAM     9Y1 2-[3-(4-FLUOROPHENYL)-5-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-          
HETNAM   2 9Y1  YL]-1,3-THIAZOLE-4-CARBOXYLIC ACID                              
HETNAM     ACT ACETATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     MLA MALONIC ACID                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;                        
HETSYN   2 MLA  METHANEDICARBOXYLIC ACID                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  9Y1    7(C14 H7 F4 N3 O2 S)                                         
FORMUL   7  ACT    4(C2 H3 O2 1-)                                               
FORMUL   9  DMS    3(C2 H6 O S)                                                 
FORMUL  10  MLA    C3 H4 O4                                                     
FORMUL  18  GOL    2(C3 H8 O3)                                                  
FORMUL  22  HOH   *987(H2 O)                                                    
HELIX    1 AA1 THR A    2  LEU A    7  1                                   6    
HELIX    2 AA2 GLY A   28  LYS A   41  1                                  14    
HELIX    3 AA3 ILE A   53  GLY A   67  1                                  15    
HELIX    4 AA4 SER A   68  LEU A   71  5                                   4    
HELIX    5 AA5 ASP A   81  ALA A   86  5                                   6    
HELIX    6 AA6 SER A  104  SER A  127  1                                  24    
HELIX    7 AA7 PRO A  138  GLY A  151  1                                  14    
HELIX    8 AA8 PRO A  153  ASN A  155  5                                   3    
HELIX    9 AA9 CYS A  162  GLY A  178  1                                  17    
HELIX   10 AB1 HIS A  180  CYS A  184  5                                   5    
HELIX   11 AB2 TRP A  200  GLY A  202  5                                   3    
HELIX   12 AB3 LEU A  210  HIS A  214  1                                   5    
HELIX   13 AB4 TRP A  226  GLY A  245  1                                  20    
HELIX   14 AB5 SER A  248  LYS A  264  1                                  17    
HELIX   15 AB6 THR A  308  LYS A  327  1                                  20    
HELIX   16 AB7 THR B    2  LEU B    7  1                                   6    
HELIX   17 AB8 GLY B   28  LYS B   41  1                                  14    
HELIX   18 AB9 ILE B   53  GLY B   67  1                                  15    
HELIX   19 AC1 SER B   68  LEU B   71  5                                   4    
HELIX   20 AC2 ASP B   81  ALA B   86  5                                   6    
HELIX   21 AC3 SER B  104  ASN B  107  5                                   4    
HELIX   22 AC4 LEU B  108  SER B  127  1                                  20    
HELIX   23 AC5 PRO B  138  GLY B  151  1                                  14    
HELIX   24 AC6 PRO B  153  ASN B  155  5                                   3    
HELIX   25 AC7 CYS B  162  GLY B  178  1                                  17    
HELIX   26 AC8 HIS B  180  LEU B  182  5                                   3    
HELIX   27 AC9 TRP B  200  GLY B  202  5                                   3    
HELIX   28 AD1 LEU B  210  HIS B  214  1                                   5    
HELIX   29 AD2 TRP B  226  GLY B  245  1                                  20    
HELIX   30 AD3 SER B  248  LYS B  264  1                                  17    
HELIX   31 AD4 THR B  308  LYS B  327  1                                  20    
HELIX   32 AD5 THR C    2  LEU C    7  1                                   6    
HELIX   33 AD6 GLY C   28  LYS C   41  1                                  14    
HELIX   34 AD7 ILE C   53  GLY C   67  1                                  15    
HELIX   35 AD8 SER C   68  LEU C   71  5                                   4    
HELIX   36 AD9 ASP C   81  ALA C   86  5                                   6    
HELIX   37 AE1 SER C  104  SER C  127  1                                  24    
HELIX   38 AE2 PRO C  138  GLY C  151  1                                  14    
HELIX   39 AE3 PRO C  153  ASN C  155  5                                   3    
HELIX   40 AE4 CYS C  162  GLY C  178  1                                  17    
HELIX   41 AE5 HIS C  180  LEU C  182  5                                   3    
HELIX   42 AE6 TRP C  200  GLY C  202  5                                   3    
HELIX   43 AE7 LEU C  210  HIS C  214  1                                   5    
HELIX   44 AE8 TRP C  226  GLY C  245  1                                  20    
HELIX   45 AE9 SER C  248  LYS C  264  1                                  17    
HELIX   46 AF1 THR C  308  LYS C  327  1                                  20    
HELIX   47 AF2 THR D    2  LEU D    7  1                                   6    
HELIX   48 AF3 GLY D   28  LYS D   41  1                                  14    
HELIX   49 AF4 ILE D   53  GLY D   67  1                                  15    
HELIX   50 AF5 SER D   68  LEU D   71  5                                   4    
HELIX   51 AF6 ASP D   81  ALA D   86  5                                   6    
HELIX   52 AF7 SER D  104  SER D  127  1                                  24    
HELIX   53 AF8 PRO D  138  GLY D  151  1                                  14    
HELIX   54 AF9 PRO D  153  ASN D  155  5                                   3    
HELIX   55 AG1 CYS D  162  GLY D  178  1                                  17    
HELIX   56 AG2 HIS D  180  LEU D  182  5                                   3    
HELIX   57 AG3 TRP D  200  GLY D  202  5                                   3    
HELIX   58 AG4 LEU D  210  HIS D  214  1                                   5    
HELIX   59 AG5 TRP D  226  GLY D  245  1                                  20    
HELIX   60 AG6 SER D  248  LYS D  264  1                                  17    
HELIX   61 AG7 THR D  308  LYS D  327  1                                  20    
SHEET    1 AA1 4 ILE A   8  ASN A  10  0                                        
SHEET    2 AA1 4 GLY D 298  VAL D 303 -1  O  LEU D 302   N  TYR A   9           
SHEET    3 AA1 4 PHE D 287  GLY D 295 -1  N  PRO D 291   O  VAL D 303           
SHEET    4 AA1 4 ARG D 268  MET D 275 -1  N  HIS D 270   O  CYS D 292           
SHEET    1 AA2 6 LYS A  75  SER A  78  0                                        
SHEET    2 AA2 6 GLU A  46  VAL A  50  1  N  LEU A  47   O  VAL A  77           
SHEET    3 AA2 6 LYS A  21  VAL A  25  1  N  VAL A  24   O  ALA A  48           
SHEET    4 AA2 6 LEU A  90  ILE A  93  1  O  ILE A  92   N  VAL A  25           
SHEET    5 AA2 6 LYS A 131  ILE A 134  1  O  LEU A 133   N  VAL A  91           
SHEET    6 AA2 6 VAL A 157  GLY A 159  1  O  ILE A 158   N  ILE A 134           
SHEET    1 AA3 2 VAL A 188  LEU A 189  0                                        
SHEET    2 AA3 2 VAL A 197  PRO A 198 -1  O  VAL A 197   N  LEU A 189           
SHEET    1 AA4 2 ASN A 204  VAL A 205  0                                        
SHEET    2 AA4 2 VAL A 208  SER A 209 -1  O  VAL A 208   N  VAL A 205           
SHEET    1 AA5 4 ARG A 268  MET A 275  0                                        
SHEET    2 AA5 4 PHE A 287  GLY A 295 -1  O  CYS A 292   N  HIS A 270           
SHEET    3 AA5 4 GLY A 298  VAL A 303 -1  O  VAL A 303   N  PRO A 291           
SHEET    4 AA5 4 ILE D   8  ASN D  10 -1  O  TYR D   9   N  LEU A 302           
SHEET    1 AA6 4 ILE B   8  ASN B  10  0                                        
SHEET    2 AA6 4 GLY C 298  VAL C 303 -1  O  LEU C 302   N  TYR B   9           
SHEET    3 AA6 4 PHE C 287  GLY C 295 -1  N  PRO C 291   O  VAL C 303           
SHEET    4 AA6 4 ARG C 268  MET C 275 -1  N  HIS C 270   O  CYS C 292           
SHEET    1 AA7 6 LYS B  75  SER B  78  0                                        
SHEET    2 AA7 6 GLU B  46  VAL B  50  1  N  LEU B  47   O  VAL B  77           
SHEET    3 AA7 6 LYS B  21  VAL B  25  1  N  VAL B  24   O  ALA B  48           
SHEET    4 AA7 6 LEU B  90  ILE B  93  1  O  ILE B  92   N  VAL B  25           
SHEET    5 AA7 6 LYS B 131  ILE B 134  1  O  LEU B 133   N  VAL B  91           
SHEET    6 AA7 6 VAL B 157  GLY B 159  1  O  ILE B 158   N  LEU B 132           
SHEET    1 AA8 3 CYS B 184  HIS B 185  0                                        
SHEET    2 AA8 3 ASN B 204  VAL B 205 -1  O  ASN B 204   N  HIS B 185           
SHEET    3 AA8 3 VAL B 208  SER B 209 -1  O  VAL B 208   N  VAL B 205           
SHEET    1 AA9 2 VAL B 188  LEU B 189  0                                        
SHEET    2 AA9 2 VAL B 197  PRO B 198 -1  O  VAL B 197   N  LEU B 189           
SHEET    1 AB1 4 ARG B 268  MET B 275  0                                        
SHEET    2 AB1 4 PHE B 287  GLY B 295 -1  O  CYS B 292   N  HIS B 270           
SHEET    3 AB1 4 GLY B 298  VAL B 303 -1  O  VAL B 303   N  PRO B 291           
SHEET    4 AB1 4 ILE C   8  ASN C  10 -1  O  TYR C   9   N  LEU B 302           
SHEET    1 AB2 6 LYS C  75  SER C  78  0                                        
SHEET    2 AB2 6 GLU C  46  VAL C  50  1  N  LEU C  47   O  VAL C  77           
SHEET    3 AB2 6 LYS C  21  VAL C  25  1  N  VAL C  24   O  ALA C  48           
SHEET    4 AB2 6 LEU C  90  ILE C  93  1  O  ILE C  92   N  VAL C  25           
SHEET    5 AB2 6 LYS C 131  ILE C 134  1  O  LEU C 133   N  ILE C  93           
SHEET    6 AB2 6 VAL C 157  GLY C 159  1  O  ILE C 158   N  ILE C 134           
SHEET    1 AB3 3 CYS C 184  HIS C 185  0                                        
SHEET    2 AB3 3 ASN C 204  VAL C 205 -1  O  ASN C 204   N  HIS C 185           
SHEET    3 AB3 3 VAL C 208  SER C 209 -1  O  VAL C 208   N  VAL C 205           
SHEET    1 AB4 2 VAL C 188  LEU C 189  0                                        
SHEET    2 AB4 2 VAL C 197  PRO C 198 -1  O  VAL C 197   N  LEU C 189           
SHEET    1 AB5 6 LYS D  75  GLY D  79  0                                        
SHEET    2 AB5 6 GLU D  46  VAL D  50  1  N  LEU D  47   O  VAL D  77           
SHEET    3 AB5 6 LYS D  21  VAL D  25  1  N  VAL D  24   O  ALA D  48           
SHEET    4 AB5 6 LEU D  90  ILE D  93  1  O  ILE D  92   N  VAL D  25           
SHEET    5 AB5 6 LYS D 131  ILE D 134  1  O  LEU D 133   N  VAL D  91           
SHEET    6 AB5 6 VAL D 157  GLY D 159  1  O  ILE D 158   N  ILE D 134           
SHEET    1 AB6 3 CYS D 184  HIS D 185  0                                        
SHEET    2 AB6 3 ASN D 204  VAL D 205 -1  O  ASN D 204   N  HIS D 185           
SHEET    3 AB6 3 VAL D 208  SER D 209 -1  O  VAL D 208   N  VAL D 205           
SHEET    1 AB7 2 VAL D 188  LEU D 189  0                                        
SHEET    2 AB7 2 VAL D 197  PRO D 198 -1  O  VAL D 197   N  LEU D 189           
CISPEP   1 ASN A  137    PRO A  138          0         0.96                     
CISPEP   2 ASN B  137    PRO B  138          0        -3.58                     
CISPEP   3 ASN C  137    PRO C  138          0         0.68                     
CISPEP   4 ASN D  137    PRO D  138          0         1.66                     
SITE     1 AC1 11 GLN A  99  LEU A 108  ASN A 137  LEU A 164                    
SITE     2 AC1 11 ARG A 168  HIS A 192  GLY A 193  ASP A 194                    
SITE     3 AC1 11 TYR A 238  THR A 247  HOH A 776                               
SITE     1 AC2 10 VAL A  25  GLY A  26  VAL A  50  ASP A  51                    
SITE     2 AC2 10 VAL A  52  ALA A  95  ILE A 115  PHE A 118                    
SITE     3 AC2 10 ILE A 119  HOH A 616                                          
SITE     1 AC3  6 ARG A 170  HIS A 185  HOH A 603  HOH A 636                    
SITE     2 AC3  6 HOH A 653  HIS C 185                                          
SITE     1 AC4  5 LEU A 182  HIS A 185  HOH A 609  ARG C 170                    
SITE     2 AC4  5 HOH C 607                                                     
SITE     1 AC5  6 THR A 212  LEU A 213  HOH A 670  LYS B 125                    
SITE     2 AC5  6 TYR B 126  THR C 306                                          
SITE     1 AC6  8 ARG B 105  ASN B 137  LEU B 164  ARG B 168                    
SITE     2 AC6  8 HIS B 192  ALA B 237  THR B 247  HOH B 546                    
SITE     1 AC7  9 SER B 309  GLU B 310  ARG B 314  LYS B 317                    
SITE     2 AC7  9 HOH B 582  9Y1 C 504  LYS D 117  PHE D 331                    
SITE     3 AC7  9 HOH D 582                                                     
SITE     1 AC8  4 ASP B 220  LYS B 221  ASP B 222  GLN B 225                    
SITE     1 AC9  5 LEU A  69  ASN B 163  SER B 166  ARG B 170                    
SITE     2 AC9  5 VAL B 269                                                     
SITE     1 AD1 10 GLN C  99  LEU C 108  ASN C 137  ARG C 168                    
SITE     2 AD1 10 HIS C 192  GLY C 193  ASP C 194  ALA C 237                    
SITE     3 AD1 10 TYR C 238  THR C 247                                          
SITE     1 AD2 15 VAL C  25  GLY C  26  VAL C  50  ASP C  51                    
SITE     2 AD2 15 VAL C  52  ALA C  95  ASN C 114  ILE C 115                    
SITE     3 AD2 15 PHE C 118  ILE C 119  HOH C 605  HOH C 613                    
SITE     4 AD2 15 HOH C 716  GLU D 101  GLY D 102                               
SITE     1 AD3 10 SER C 104  ARG C 105  LEU C 106  ASP C 320                    
SITE     2 AD3 10 THR C 321  GLY C 324  ILE C 325  GLU C 328                    
SITE     3 AD3 10 9Y1 C 504  HOH C 647                                          
SITE     1 AD4  4 9Y1 B 402  HOH B 567  9Y1 C 503  HOH C 647                    
SITE     1 AD5  9 SER A 201  GLY A 202  GLY A 207  SER C 201                    
SITE     2 AD5  9 GLY C 202  MET C 203  ASN C 204  GLY C 207                    
SITE     3 AD5  9 SER C 209                                                     
SITE     1 AD6  3 PRO D 128  LEU D 307  GLU D 312                               
SITE     1 AD7  4 GLY D  96  ALA D  97  SER D 136  ASN D 137                    
SITE     1 AD8 11 SER B 201  GLY B 202  ASN B 204  GLY B 207                    
SITE     2 AD8 11 SER B 209  SER D 201  GLY D 202  MET D 203                    
SITE     3 AD8 11 ASN D 204  GLY D 207  SER D 209                               
CRYST1  167.730   81.210  120.650  90.00 118.22  90.00 C 1 2 1      16          
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      0.005962  0.000000  0.003199        0.00000                         
SCALE2      0.000000  0.012314  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009406        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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