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Database: PDB
Entry: 4UUL
LinkDB: 4UUL
Original site: 4UUL 
HEADER    OXIDOREDUCTASE                          29-JUL-14   4UUL              
TITLE     APO TRICHOMONAS VAGINALIS LACTATE DEHYDROGENASE L91R                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-LACTATE DEHYDROGENASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LACTATE DEHYDROGENASE;                                      
COMPND   5 EC: 1.1.1.27;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRICHOMONAS VAGINALIS;                          
SOURCE   3 ORGANISM_TAXID: 5722;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-21B                                   
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.STEINDEL,E.H.CHEN,D.L THEOBALD                                    
REVDAT   5   10-JAN-24 4UUL    1       REMARK                                   
REVDAT   4   23-OCT-19 4UUL    1       ATOM                                     
REVDAT   3   06-JUL-16 4UUL    1       JRNL                                     
REVDAT   2   02-MAR-16 4UUL    1       JRNL                                     
REVDAT   1   12-AUG-15 4UUL    0                                                
JRNL        AUTH   P.A.STEINDEL,E.H.CHEN,J.D.WIRTH,D.L.THEOBALD                 
JRNL        TITL   GRADUAL NEOFUNCTIONALIZATION IN THE CONVERGENT EVOLUTION OF  
JRNL        TITL 2 TRICHOMONAD LACTATE AND MALATE DEHYDROGENASES.               
JRNL        REF    PROTEIN SCI.                  V.  25  1319 2016              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   26889885                                                     
JRNL        DOI    10.1002/PRO.2904                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 175050                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.131                           
REMARK   3   R VALUE            (WORKING SET) : 0.129                           
REMARK   3   FREE R VALUE                     : 0.155                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8784                            
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 30.7206 -  3.9738    0.88     5597   293  0.1570 0.1597        
REMARK   3     2  3.9738 -  3.1551    0.99     6197   324  0.1339 0.1567        
REMARK   3     3  3.1551 -  2.7566    1.00     6164   331  0.1335 0.1557        
REMARK   3     4  2.7566 -  2.5047    1.00     6163   318  0.1209 0.1312        
REMARK   3     5  2.5047 -  2.3252    1.00     6182   322  0.1134 0.1355        
REMARK   3     6  2.3252 -  2.1882    1.00     6112   321  0.1172 0.1539        
REMARK   3     7  2.1882 -  2.0786    1.00     6131   337  0.1198 0.1338        
REMARK   3     8  2.0786 -  1.9882    1.00     6106   325  0.1263 0.1699        
REMARK   3     9  1.9882 -  1.9116    1.00     6138   312  0.1340 0.1667        
REMARK   3    10  1.9116 -  1.8457    0.99     6118   331  0.1265 0.1480        
REMARK   3    11  1.8457 -  1.7880    0.99     6108   306  0.1209 0.1521        
REMARK   3    12  1.7880 -  1.7369    0.99     6117   311  0.1160 0.1553        
REMARK   3    13  1.7369 -  1.6911    0.99     6013   344  0.1154 0.1547        
REMARK   3    14  1.6911 -  1.6499    0.99     6090   330  0.1115 0.1537        
REMARK   3    15  1.6499 -  1.6124    0.99     6064   293  0.1083 0.1409        
REMARK   3    16  1.6124 -  1.5781    0.99     6093   334  0.1041 0.1405        
REMARK   3    17  1.5781 -  1.5465    0.99     6037   330  0.1076 0.1457        
REMARK   3    18  1.5465 -  1.5173    0.99     6018   310  0.1158 0.1630        
REMARK   3    19  1.5173 -  1.4902    0.99     5991   321  0.1123 0.1541        
REMARK   3    20  1.4902 -  1.4650    0.99     6076   323  0.1210 0.1629        
REMARK   3    21  1.4650 -  1.4413    0.98     6010   325  0.1256 0.1597        
REMARK   3    22  1.4413 -  1.4192    0.97     5886   307  0.1284 0.1755        
REMARK   3    23  1.4192 -  1.3983    0.92     5642   290  0.1328 0.1763        
REMARK   3    24  1.3983 -  1.3786    0.84     5102   278  0.1412 0.2008        
REMARK   3    25  1.3786 -  1.3600    0.77     4728   246  0.1676 0.2135        
REMARK   3    26  1.3600 -  1.3423    0.71     4308   222  0.1566 0.2248        
REMARK   3    27  1.3423 -  1.3255    0.65     3942   220  0.1643 0.2007        
REMARK   3    28  1.3255 -  1.3096    0.59     3607   190  0.1684 0.2008        
REMARK   3    29  1.3096 -  1.2943    0.52     3153   168  0.2018 0.2654        
REMARK   3    30  1.2943 -  1.2798    0.39     2373   122  0.2081 0.2625        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.100            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.40                          
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      :  0.013           5614                                  
REMARK   3   ANGLE     :  1.474           7667                                  
REMARK   3   CHIRALITY :  0.099            844                                  
REMARK   3   PLANARITY :  0.010            993                                  
REMARK   3   DIHEDRAL  : 12.675           2039                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4UUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290061313.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 175089                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.610                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : 13.10                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 47.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.610                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON PDB ENTRY 5MDH               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21 MG/ML PROTEIN, 100 MM HEPES PH 7.0,   
REMARK 280  10% PEG-6000, 5% MPD                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       29.80500            
REMARK 290   SMTRY3   2  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     HIS A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     HIS A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
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     ARG A  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 317   CD    GLU B 317   OE2    -0.068                       
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    ASP A 219      -66.22   -143.33                                   
REMARK 500    ALA A 241      -52.22   -140.82                                   
REMARK 500    ASP B 219      -66.90   -144.27                                   
REMARK 500    ALA B 241      -56.36   -139.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2049        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A2070        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A2091        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A2119        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A2166        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B2031        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH B2095        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B2112        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B2506        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B2507        DISTANCE =  7.22 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UUM   RELATED DB: PDB                                   
REMARK 900 APO TRICHOMONAS VAGINALIS LACTATE DEHYDROGENASE                      
REMARK 900 RELATED ID: 4UUN   RELATED DB: PDB                                   
REMARK 900 TRICHOMONAS VAGINALIS LACATATE DEHYDROGENASE IN COMPLEX WITH NADH    
REMARK 900 RELATED ID: 4UUO   RELATED DB: PDB                                   
REMARK 900 APO TRICHOMONAS VAGINALIS MALATE DEHYDROGENASE                       
REMARK 900 RELATED ID: 4UUP   RELATED DB: PDB                                   
REMARK 900 RECONSTRUCTED ANCESTRAL TRICHOMONAD MALATE DEHYDROGENASE IN COMPLEX  
REMARK 900 WITH NADH, SO4, AND PO4                                              
DBREF  4UUL A    1   333  UNP    O96445   O96445_TRIVA     1    333             
DBREF  4UUL B    1   333  UNP    O96445   O96445_TRIVA     1    333             
SEQADV 4UUL LEU A  334  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL GLU A  335  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  336  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  337  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  338  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  339  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  340  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS A  341  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL ARG A   91  UNP  O96445    LEU    91 ENGINEERED MUTATION            
SEQADV 4UUL LEU B  334  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL GLU B  335  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  336  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  337  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  338  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  339  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  340  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL HIS B  341  UNP  O96445              EXPRESSION TAG                 
SEQADV 4UUL ARG B   91  UNP  O96445    LEU    91 ENGINEERED MUTATION            
SEQRES   1 A  341  MET SER GLU ALA ALA HIS VAL LEU ILE THR GLY ALA ALA          
SEQRES   2 A  341  GLY GLN ILE GLY TYR ILE LEU SER HIS TRP ILE ALA SER          
SEQRES   3 A  341  GLY GLU LEU TYR GLY ASP ARG GLN VAL TYR LEU HIS LEU          
SEQRES   4 A  341  LEU ASP ILE PRO PRO ALA MET ASN ARG LEU THR ALA LEU          
SEQRES   5 A  341  THR MET GLU LEU GLU ASP CYS ALA PHE PRO HIS LEU ALA          
SEQRES   6 A  341  GLY PHE VAL ALA THR THR ASP PRO LYS ALA ALA PHE LYS          
SEQRES   7 A  341  ASP ILE ASP CYS ALA PHE LEU VAL ALA SER MET PRO ARG          
SEQRES   8 A  341  LYS PRO GLY GLN VAL ARG ALA ASP LEU ILE SER SER ASN          
SEQRES   9 A  341  SER VAL ILE PHE LYS ASN THR GLY GLU TYR LEU SER LYS          
SEQRES  10 A  341  TRP ALA LYS PRO SER VAL LYS VAL LEU VAL ILE GLY ASN          
SEQRES  11 A  341  PRO ASP ASN THR ASN CYS GLU ILE ALA MET LEU HIS ALA          
SEQRES  12 A  341  LYS ASN LEU LYS PRO GLU ASN PHE SER SER LEU SER MET          
SEQRES  13 A  341  LEU ASP GLN ASN ARG ALA TYR TYR GLU VAL ALA SER LYS          
SEQRES  14 A  341  LEU GLY VAL ASP VAL LYS ASP VAL HIS ASP ILE ILE VAL          
SEQRES  15 A  341  TRP GLY ASN HIS GLY GLU SER MET VAL ALA ASP LEU THR          
SEQRES  16 A  341  GLN ALA THR PHE THR LYS GLU GLY LYS THR GLN LYS VAL          
SEQRES  17 A  341  VAL ASP VAL LEU ASP HIS ASP TYR VAL PHE ASP THR PHE          
SEQRES  18 A  341  PHE LYS LYS ILE GLY HIS ARG ALA TRP ASP ILE LEU GLU          
SEQRES  19 A  341  HIS ARG GLY PHE THR SER ALA ALA SER PRO THR LYS ALA          
SEQRES  20 A  341  ALA ILE GLN HIS MET LYS ALA TRP LEU PHE GLY THR ALA          
SEQRES  21 A  341  PRO GLY GLU VAL LEU SER MET GLY ILE PRO VAL PRO GLU          
SEQRES  22 A  341  GLY ASN PRO TYR GLY ILE LYS PRO GLY VAL VAL PHE SER          
SEQRES  23 A  341  PHE PRO CYS ASN VAL ASP LYS GLU GLY LYS ILE HIS VAL          
SEQRES  24 A  341  VAL GLU GLY PHE LYS VAL ASN ASP TRP LEU ARG GLU LYS          
SEQRES  25 A  341  LEU ASP PHE THR GLU LYS ASP LEU PHE HIS GLU LYS GLU          
SEQRES  26 A  341  ILE ALA LEU ASN HIS LEU ALA GLN LEU GLU HIS HIS HIS          
SEQRES  27 A  341  HIS HIS HIS                                                  
SEQRES   1 B  341  MET SER GLU ALA ALA HIS VAL LEU ILE THR GLY ALA ALA          
SEQRES   2 B  341  GLY GLN ILE GLY TYR ILE LEU SER HIS TRP ILE ALA SER          
SEQRES   3 B  341  GLY GLU LEU TYR GLY ASP ARG GLN VAL TYR LEU HIS LEU          
SEQRES   4 B  341  LEU ASP ILE PRO PRO ALA MET ASN ARG LEU THR ALA LEU          
SEQRES   5 B  341  THR MET GLU LEU GLU ASP CYS ALA PHE PRO HIS LEU ALA          
SEQRES   6 B  341  GLY PHE VAL ALA THR THR ASP PRO LYS ALA ALA PHE LYS          
SEQRES   7 B  341  ASP ILE ASP CYS ALA PHE LEU VAL ALA SER MET PRO ARG          
SEQRES   8 B  341  LYS PRO GLY GLN VAL ARG ALA ASP LEU ILE SER SER ASN          
SEQRES   9 B  341  SER VAL ILE PHE LYS ASN THR GLY GLU TYR LEU SER LYS          
SEQRES  10 B  341  TRP ALA LYS PRO SER VAL LYS VAL LEU VAL ILE GLY ASN          
SEQRES  11 B  341  PRO ASP ASN THR ASN CYS GLU ILE ALA MET LEU HIS ALA          
SEQRES  12 B  341  LYS ASN LEU LYS PRO GLU ASN PHE SER SER LEU SER MET          
SEQRES  13 B  341  LEU ASP GLN ASN ARG ALA TYR TYR GLU VAL ALA SER LYS          
SEQRES  14 B  341  LEU GLY VAL ASP VAL LYS ASP VAL HIS ASP ILE ILE VAL          
SEQRES  15 B  341  TRP GLY ASN HIS GLY GLU SER MET VAL ALA ASP LEU THR          
SEQRES  16 B  341  GLN ALA THR PHE THR LYS GLU GLY LYS THR GLN LYS VAL          
SEQRES  17 B  341  VAL ASP VAL LEU ASP HIS ASP TYR VAL PHE ASP THR PHE          
SEQRES  18 B  341  PHE LYS LYS ILE GLY HIS ARG ALA TRP ASP ILE LEU GLU          
SEQRES  19 B  341  HIS ARG GLY PHE THR SER ALA ALA SER PRO THR LYS ALA          
SEQRES  20 B  341  ALA ILE GLN HIS MET LYS ALA TRP LEU PHE GLY THR ALA          
SEQRES  21 B  341  PRO GLY GLU VAL LEU SER MET GLY ILE PRO VAL PRO GLU          
SEQRES  22 B  341  GLY ASN PRO TYR GLY ILE LYS PRO GLY VAL VAL PHE SER          
SEQRES  23 B  341  PHE PRO CYS ASN VAL ASP LYS GLU GLY LYS ILE HIS VAL          
SEQRES  24 B  341  VAL GLU GLY PHE LYS VAL ASN ASP TRP LEU ARG GLU LYS          
SEQRES  25 B  341  LEU ASP PHE THR GLU LYS ASP LEU PHE HIS GLU LYS GLU          
SEQRES  26 B  341  ILE ALA LEU ASN HIS LEU ALA GLN LEU GLU HIS HIS HIS          
SEQRES  27 B  341  HIS HIS HIS                                                  
FORMUL   3  HOH   *1005(H2 O)                                                   
HELIX    1   1 GLY A   14  SER A   26  1                                  13    
HELIX    2   2 ILE A   42  PRO A   44  5                                   3    
HELIX    3   3 ALA A   45  ASP A   58  1                                  14    
HELIX    4   4 ASP A   72  LYS A   78  1                                   7    
HELIX    5   5 VAL A   96  ALA A  119  1                                  24    
HELIX    6   6 PRO A  131  HIS A  142  1                                  12    
HELIX    7   7 LYS A  147  GLU A  149  5                                   3    
HELIX    8   8 SER A  155  GLY A  171  1                                  17    
HELIX    9   9 ASP A  173  LYS A  175  5                                   3    
HELIX   10  10 HIS A  186  MET A  190  5                                   5    
HELIX   11  11 VAL A  208  LEU A  212  1                                   5    
HELIX   12  12 ASP A  213  ASP A  219  1                                   7    
HELIX   13  13 ASP A  219  GLY A  237  1                                  19    
HELIX   14  14 ALA A  241  GLY A  258  1                                  18    
HELIX   15  15 ASN A  306  GLU A  335  1                                  30    
HELIX   16  16 GLY B   14  SER B   26  1                                  13    
HELIX   17  17 ILE B   42  PRO B   44  5                                   3    
HELIX   18  18 ALA B   45  ASP B   58  1                                  14    
HELIX   19  19 ASP B   72  LYS B   78  1                                   7    
HELIX   20  20 VAL B   96  ALA B  119  1                                  24    
HELIX   21  21 PRO B  131  HIS B  142  1                                  12    
HELIX   22  22 LYS B  147  GLU B  149  5                                   3    
HELIX   23  23 SER B  155  GLY B  171  1                                  17    
HELIX   24  24 ASP B  173  LYS B  175  5                                   3    
HELIX   25  25 HIS B  186  MET B  190  5                                   5    
HELIX   26  26 VAL B  208  LEU B  212  1                                   5    
HELIX   27  27 ASP B  213  PHE B  218  1                                   6    
HELIX   28  28 ASP B  219  GLY B  237  1                                  19    
HELIX   29  29 ALA B  241  GLY B  258  1                                  18    
HELIX   30  30 ASN B  306  HIS B  338  1                                  33    
SHEET    1  AA 6 LEU A  64  THR A  70  0                                        
SHEET    2  AA 6 VAL A  35  LEU A  40  1  O  VAL A  35   N  ALA A  65           
SHEET    3  AA 6 ALA A   5  THR A  10  1  O  ALA A   5   N  TYR A  36           
SHEET    4  AA 6 CYS A  82  LEU A  85  1  O  CYS A  82   N  LEU A   8           
SHEET    5  AA 6 LYS A 124  VAL A 127  1  O  LYS A 124   N  ALA A  83           
SHEET    6  AA 6 PHE A 151  SER A 153  1  O  SER A 152   N  VAL A 127           
SHEET    1  AB 3 VAL A 177  HIS A 178  0                                        
SHEET    2  AB 3 THR A 198  LYS A 201 -1  O  THR A 198   N  HIS A 178           
SHEET    3  AB 3 LYS A 204  LYS A 207 -1  O  LYS A 204   N  LYS A 201           
SHEET    1  AC 2 ILE A 181  TRP A 183  0                                        
SHEET    2  AC 2 VAL A 191  ASP A 193 -1  O  VAL A 191   N  TRP A 183           
SHEET    1  AD 3 LEU A 265  PRO A 270  0                                        
SHEET    2  AD 3 VAL A 284  VAL A 291 -1  O  PHE A 285   N  ILE A 269           
SHEET    3  AD 3 ILE A 297  VAL A 299 -1  O  HIS A 298   N  ASN A 290           
SHEET    1  BA 6 LEU B  64  THR B  70  0                                        
SHEET    2  BA 6 VAL B  35  LEU B  40  1  O  VAL B  35   N  ALA B  65           
SHEET    3  BA 6 ALA B   5  THR B  10  1  O  ALA B   5   N  TYR B  36           
SHEET    4  BA 6 CYS B  82  LEU B  85  1  O  CYS B  82   N  LEU B   8           
SHEET    5  BA 6 LYS B 124  VAL B 127  1  O  LYS B 124   N  ALA B  83           
SHEET    6  BA 6 PHE B 151  SER B 153  1  O  SER B 152   N  VAL B 127           
SHEET    1  BB 3 VAL B 177  HIS B 178  0                                        
SHEET    2  BB 3 THR B 198  LYS B 201 -1  O  THR B 198   N  HIS B 178           
SHEET    3  BB 3 LYS B 204  LYS B 207 -1  O  LYS B 204   N  LYS B 201           
SHEET    1  BC 2 ILE B 181  TRP B 183  0                                        
SHEET    2  BC 2 VAL B 191  ASP B 193 -1  O  VAL B 191   N  TRP B 183           
SHEET    1  BD 3 LEU B 265  PRO B 270  0                                        
SHEET    2  BD 3 VAL B 284  VAL B 291 -1  O  PHE B 285   N  ILE B 269           
SHEET    3  BD 3 ILE B 297  VAL B 299 -1  O  HIS B 298   N  ASN B 290           
CISPEP   1 ASN A  130    PRO A  131          0        -6.18                     
CISPEP   2 ASN B  130    PRO B  131          0        -1.70                     
CISPEP   3 ASN B  130    PRO B  131          0        -9.28                     
CRYST1   82.570   59.610   86.490  90.00 116.18  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012111  0.000000  0.005954        0.00000                         
SCALE2      0.000000  0.016776  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012884        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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