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Database: PDB
Entry: 4L4S
LinkDB: 4L4S
Original site: 4L4S 
HEADER    OXIDOREDUCTASE                          09-JUN-13   4L4S              
TITLE     STRUCTURAL CHARACTERISATION OF THE NADH BINARY COMPLEX OF HUMAN       
TITLE    2 LACTATE DEHYDROGENASE M ISOZYME                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-LACTATE DEHYDROGENASE A CHAIN;                           
COMPND   3 CHAIN: H, A;                                                         
COMPND   4 SYNONYM: LDH-A, CELL PROLIFERATION-INDUCING GENE 19 PROTEIN, LDH     
COMPND   5 MUSCLE 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                                         
KEYWDS    GLYCOLYSIS, ANAEROBIC RESPIRATION, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEMPSTER,S.HARPER,J.E.MOSES,I.DREVENY                               
REVDAT   3   04-JUN-14 4L4S    1       JRNL                                     
REVDAT   2   07-MAY-14 4L4S    1       TITLE                                    
REVDAT   1   30-APR-14 4L4S    0                                                
JRNL        AUTH   S.DEMPSTER,S.HARPER,J.E.MOSES,I.DREVENY                      
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE APO FORM AND NADH BINARY  
JRNL        TITL 2 COMPLEX OF HUMAN LACTATE DEHYDROGENASE.                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70  1484 2014              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   24816116                                                     
JRNL        DOI    10.1107/S1399004714005422                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 23011                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1183                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.11                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 17.59                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.37                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.55680                                              
REMARK   3    B22 (A**2) : 4.55680                                              
REMARK   3    B33 (A**2) : -9.11370                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'H' and (resseq 1:20)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2414 -53.0985  21.1450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7370 T22:   0.3290                                     
REMARK   3      T33:   0.3497 T12:  -0.0937                                     
REMARK   3      T13:   0.0434 T23:  -0.0681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6788 L22:   5.3061                                     
REMARK   3      L33:   1.0011 L12:  -2.1505                                     
REMARK   3      L13:   1.2912 L23:   0.1265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7000 S12:   0.5343 S13:  -0.6935                       
REMARK   3      S21:  -1.2210 S22:  -0.0594 S23:   0.2022                       
REMARK   3      S31:   0.3709 S32:   0.2905 S33:  -0.5877                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'H' and (resseq 21:93)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2822 -30.9323  14.6045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1199 T22:   0.1567                                     
REMARK   3      T33:  -0.0255 T12:   0.0315                                     
REMARK   3      T13:   0.0079 T23:  -0.0738                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2507 L22:   1.1624                                     
REMARK   3      L33:   0.7026 L12:  -0.1967                                     
REMARK   3      L13:   0.5399 L23:   0.3102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0069 S12:   0.1439 S13:  -0.1641                       
REMARK   3      S21:  -0.1891 S22:   0.0130 S23:  -0.0949                       
REMARK   3      S31:   0.1118 S32:   0.0303 S33:   0.0031                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'H' and (resseq 94:126)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7178 -19.3603  -0.1036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1551 T22:   0.2030                                     
REMARK   3      T33:   0.0435 T12:  -0.0003                                     
REMARK   3      T13:   0.0790 T23:  -0.0507                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2429 L22:   6.4033                                     
REMARK   3      L33:   6.3198 L12:  -0.8245                                     
REMARK   3      L13:  -0.3268 L23:  -2.8500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1243 S12:   0.2825 S13:   0.3243                       
REMARK   3      S21:  -0.1548 S22:  -0.0547 S23:  -0.3269                       
REMARK   3      S31:  -0.7603 S32:   0.1262 S33:  -0.0644                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'H' and (resseq 127:308)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9049 -11.2687  20.2937              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0206 T22:   0.0516                                     
REMARK   3      T33:   0.0194 T12:  -0.0791                                     
REMARK   3      T13:  -0.0575 T23:  -0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5557 L22:   0.1047                                     
REMARK   3      L33:   0.8918 L12:   0.0595                                     
REMARK   3      L13:   0.0321 L23:   0.1334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0346 S12:   0.0575 S13:   0.1266                       
REMARK   3      S21:  -0.0772 S22:   0.0002 S23:   0.0704                       
REMARK   3      S31:  -0.1224 S32:  -0.0113 S33:   0.0277                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'H' and (resseq 309:331)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7884  -7.3159   5.7565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1748 T22:   0.1185                                     
REMARK   3      T33:   0.0779 T12:  -0.0196                                     
REMARK   3      T13:  -0.1048 T23:   0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1187 L22:   3.9608                                     
REMARK   3      L33:   0.7975 L12:  -1.0691                                     
REMARK   3      L13:  -0.4013 L23:   1.7746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0338 S12:   0.4473 S13:   0.0195                       
REMARK   3      S21:  -0.2784 S22:  -0.0942 S23:   0.0621                       
REMARK   3      S31:  -0.0135 S32:  -0.0777 S33:  -0.0044                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:20)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8498  -0.0545  43.7907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3639 T22:   0.2216                                     
REMARK   3      T33:   0.2358 T12:  -0.1022                                     
REMARK   3      T13:   0.0433 T23:  -0.0825                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4842 L22:   3.0326                                     
REMARK   3      L33:   1.3811 L12:  -1.1878                                     
REMARK   3      L13:  -0.7710 L23:   1.7568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2081 S12:  -0.3112 S13:   0.6056                       
REMARK   3      S21:   0.1317 S22:   0.3421 S23:  -0.6866                       
REMARK   3      S31:  -0.2282 S32:   0.3017 S33:  -0.1376                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 21:93)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3658 -11.5571  28.1725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0516 T22:   0.1488                                     
REMARK   3      T33:   0.0821 T12:  -0.0497                                     
REMARK   3      T13:   0.0209 T23:  -0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5738 L22:   1.1730                                     
REMARK   3      L33:   1.1429 L12:  -0.4215                                     
REMARK   3      L13:   0.7059 L23:   0.1322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0234 S12:  -0.0895 S13:   0.0745                       
REMARK   3      S21:   0.0068 S22:  -0.0461 S23:  -0.1925                       
REMARK   3      S31:  -0.1534 S32:   0.1194 S33:   0.0507                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 94:126)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.3511 -13.1492  20.8027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1852 T22:   0.3696                                     
REMARK   3      T33:   0.1919 T12:  -0.0347                                     
REMARK   3      T13:   0.0010 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3597 L22:   4.0134                                     
REMARK   3      L33:   4.5337 L12:  -1.1643                                     
REMARK   3      L13:  -1.9228 L23:   1.8152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1390 S12:   0.4533 S13:  -0.2291                       
REMARK   3      S21:  -0.7146 S22:  -0.2515 S23:   0.1493                       
REMARK   3      S31:  -0.0586 S32:  -0.0794 S33:   0.1028                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 127:308)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3788 -33.6737  27.5237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1873 T22:   0.3233                                     
REMARK   3      T33:   0.1699 T12:   0.0917                                     
REMARK   3      T13:  -0.0293 T23:  -0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2250 L22:   1.4581                                     
REMARK   3      L33:   1.1345 L12:   1.1351                                     
REMARK   3      L13:  -0.0303 L23:  -0.1900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:   0.0386 S13:  -0.3449                       
REMARK   3      S21:  -0.0870 S22:   0.0274 S23:  -0.4704                       
REMARK   3      S31:   0.3343 S32:   0.3860 S33:  -0.0387                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'A' and (resseq 309:331)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6619 -29.2571  24.7875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1669 T22:   0.4829                                     
REMARK   3      T33:   0.4017 T12:   0.1454                                     
REMARK   3      T13:   0.0853 T23:  -0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2520 L22:   7.1122                                     
REMARK   3      L33:   3.4462 L12:   3.5126                                     
REMARK   3      L13:  -2.0463 L23:  -1.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2414 S12:   0.1239 S13:   0.0429                       
REMARK   3      S21:  -0.1969 S22:  -0.1216 S23:  -0.7065                       
REMARK   3      S31:  -0.0401 S32:   0.2445 S33:  -0.1142                       
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 4L4S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080180.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : DIFFRACTOMETER                     
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23067                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.317                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.20300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.77100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 8000, 100 MM HEPES, 20 %        
REMARK 280  ETHYLENE GLYCOL, 10 % ACETONITRILE, PH 7.5, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
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      138.34550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.17275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      207.51825            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      138.34550            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      207.51825            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       69.17275            
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: 17560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 53910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       84.31700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU H   332                                                      
REMARK 465     GLU H   333                                                      
REMARK 465     HIS H   334                                                      
REMARK 465     HIS H   335                                                      
REMARK 465     HIS H   336                                                      
REMARK 465     HIS H   337                                                      
REMARK 465     HIS H   338                                                      
REMARK 465     HIS H   339                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     GLU A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     HIS A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN H   16   C                                                   
REMARK 480     GLN A   16   C                                                   
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    GLY A   281     NZ   LYS A   316              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL H  27       41.23   -105.37                                   
REMARK 500    ASN H  87       39.37     70.10                                   
REMARK 500    GLU H 101      109.38    -59.87                                   
REMARK 500    SER H 248      -58.25   -134.12                                   
REMARK 500    TYR H 280       14.76     49.90                                   
REMARK 500    ASP H 285       75.21    -67.79                                   
REMARK 500    GLU H 328       47.77   -100.57                                   
REMARK 500    VAL A  27       41.26   -104.95                                   
REMARK 500    ASN A  87       39.47     70.08                                   
REMARK 500    SER A 248      -58.36   -133.91                                   
REMARK 500    TYR A 280       15.74     49.75                                   
REMARK 500    ASP A 285       76.13    -66.68                                   
REMARK 500    GLU A 328       48.09    -98.79                                   
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 NAI H 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L4R   RELATED DB: PDB                                   
REMARK 900 HUMAN LACTATE DEHYDROGENASE M, APO STRUCTURE                         
DBREF  4L4S H    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4L4S A    1   331  UNP    P00338   LDHA_HUMAN       2    332             
SEQADV 4L4S LEU H  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S GLU H  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS H  339  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S LEU A  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S GLU A  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4L4S HIS A  339  UNP  P00338              EXPRESSION TAG                 
SEQRES   1 H  339  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 H  339  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 H  339  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 H  339  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 H  339  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 H  339  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 H  339  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 H  339  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 H  339  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 H  339  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 H  339  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 H  339  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 H  339  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 H  339  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 H  339  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 H  339  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 H  339  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 H  339  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 H  339  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 H  339  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 H  339  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 H  339  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 H  339  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 H  339  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 H  339  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 H  339  GLN LYS GLU LEU GLN PHE LEU GLU HIS HIS HIS HIS HIS          
SEQRES  27 H  339  HIS                                                          
SEQRES   1 A  339  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 A  339  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 A  339  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 A  339  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 A  339  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 A  339  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 A  339  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 A  339  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 A  339  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 A  339  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 A  339  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 A  339  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 A  339  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 A  339  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 A  339  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 A  339  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 A  339  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 A  339  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 A  339  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 A  339  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 A  339  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 A  339  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 A  339  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 A  339  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 A  339  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 A  339  GLN LYS GLU LEU GLN PHE LEU GLU HIS HIS HIS HIS HIS          
SEQRES  27 A  339  HIS                                                          
HET    NAI  H 401      44                                                       
HET    NAI  A 401      44                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     NAI NADH                                                             
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL   5  HOH   *37(H2 O)                                                     
HELIX    1   1 THR H    2  ILE H    8  1                                   7    
HELIX    2   2 GLY H   28  LYS H   41  1                                  14    
HELIX    3   3 ILE H   53  HIS H   66  1                                  14    
HELIX    4   4 GLY H   67  LEU H   71  5                                   5    
HELIX    5   5 ASP H   81  ALA H   86  5                                   6    
HELIX    6   6 SER H  104  SER H  127  1                                  24    
HELIX    7   7 PRO H  138  GLY H  151  1                                  14    
HELIX    8   8 PRO H  153  ASN H  155  5                                   3    
HELIX    9   9 CYS H  162  GLY H  178  1                                  17    
HELIX   10  10 LEU H  210  HIS H  214  1                                   5    
HELIX   11  11 TRP H  226  GLY H  245  1                                  20    
HELIX   12  12 SER H  248  LYS H  264  1                                  17    
HELIX   13  13 THR H  308  LYS H  327  1                                  20    
HELIX   14  14 THR A    2  ILE A    8  1                                   7    
HELIX   15  15 GLY A   28  LYS A   41  1                                  14    
HELIX   16  16 ILE A   53  HIS A   66  1                                  14    
HELIX   17  17 GLY A   67  LEU A   71  5                                   5    
HELIX   18  18 ASP A   81  ALA A   86  5                                   6    
HELIX   19  19 SER A  104  SER A  127  1                                  24    
HELIX   20  20 PRO A  138  GLY A  151  1                                  14    
HELIX   21  21 PRO A  153  ASN A  155  5                                   3    
HELIX   22  22 CYS A  162  GLY A  178  1                                  17    
HELIX   23  23 TRP A  200  GLY A  202  5                                   3    
HELIX   24  24 LEU A  210  HIS A  214  1                                   5    
HELIX   25  25 TRP A  226  GLY A  245  1                                  20    
HELIX   26  26 SER A  248  LYS A  264  1                                  17    
HELIX   27  27 THR A  308  LYS A  327  1                                  20    
SHEET    1   A 6 LYS H  75  GLY H  79  0                                        
SHEET    2   A 6 GLU H  46  VAL H  50  1  N  LEU H  47   O  LYS H  75           
SHEET    3   A 6 LYS H  21  VAL H  25  1  N  VAL H  24   O  ALA H  48           
SHEET    4   A 6 LEU H  90  ILE H  93  1  O  ILE H  92   N  THR H  23           
SHEET    5   A 6 LYS H 131  ILE H 134  1  O  LEU H 133   N  VAL H  91           
SHEET    6   A 6 VAL H 157  GLY H 159  1  O  ILE H 158   N  LEU H 132           
SHEET    1   B 3 CYS H 184  LEU H 189  0                                        
SHEET    2   B 3 VAL H 197  VAL H 205 -1  O  VAL H 197   N  LEU H 189           
SHEET    3   B 3 VAL H 208  SER H 209 -1  O  VAL H 208   N  VAL H 205           
SHEET    1   C 3 ARG H 268  MET H 275  0                                        
SHEET    2   C 3 PHE H 287  GLY H 295 -1  O  CYS H 292   N  HIS H 270           
SHEET    3   C 3 GLY H 298  LEU H 302 -1  O  GLY H 298   N  GLY H 295           
SHEET    1   D 6 LYS A  75  GLY A  79  0                                        
SHEET    2   D 6 GLU A  46  VAL A  50  1  N  LEU A  47   O  VAL A  77           
SHEET    3   D 6 LYS A  21  VAL A  25  1  N  VAL A  24   O  ALA A  48           
SHEET    4   D 6 LEU A  90  ILE A  93  1  O  ILE A  92   N  THR A  23           
SHEET    5   D 6 LYS A 131  ILE A 134  1  O  LYS A 131   N  VAL A  91           
SHEET    6   D 6 VAL A 157  GLY A 159  1  O  ILE A 158   N  ILE A 134           
SHEET    1   E 3 CYS A 184  HIS A 185  0                                        
SHEET    2   E 3 ASN A 204  VAL A 205 -1  O  ASN A 204   N  HIS A 185           
SHEET    3   E 3 VAL A 208  SER A 209 -1  O  VAL A 208   N  VAL A 205           
SHEET    1   F 2 VAL A 188  LEU A 189  0                                        
SHEET    2   F 2 VAL A 197  PRO A 198 -1  O  VAL A 197   N  LEU A 189           
SHEET    1   G 3 ARG A 268  MET A 275  0                                        
SHEET    2   G 3 PHE A 287  GLY A 295 -1  O  CYS A 292   N  HIS A 270           
SHEET    3   G 3 GLY A 298  LEU A 302 -1  O  GLY A 298   N  GLY A 295           
CISPEP   1 ASN H  137    PRO H  138          0        -4.73                     
CISPEP   2 ASN A  137    PRO A  138          0        -5.74                     
SITE     1 AC1 19 GLY H  28  ALA H  29  VAL H  30  ASP H  51                    
SITE     2 AC1 19 VAL H  52  ILE H  53  THR H  94  ALA H  95                    
SITE     3 AC1 19 GLY H  96  ARG H  98  ILE H 115  VAL H 135                    
SITE     4 AC1 19 SER H 136  ASN H 137  SER H 160  LEU H 164                    
SITE     5 AC1 19 HIS H 192  ILE H 251  HOH H 502                               
SITE     1 AC2 19 GLY A  28  ALA A  29  VAL A  30  ASP A  51                    
SITE     2 AC2 19 VAL A  52  ILE A  53  THR A  94  ALA A  95                    
SITE     3 AC2 19 GLY A  96  ILE A 115  VAL A 135  SER A 136                    
SITE     4 AC2 19 ASN A 137  SER A 160  LEU A 164  HIS A 192                    
SITE     5 AC2 19 ILE A 251  HOH A 506  HOH A 512                               
CRYST1   84.317   84.317  276.691  90.00  90.00  90.00 P 41 2 2     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      0.011860  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003614        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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