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Database: PDB
Entry: 4AJP
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Original site: 4AJP 
HEADER    OXIDOREDUCTASE/INHIBITOR                16-FEB-12   4AJP              
TITLE     HUMAN LDHA IN COMPLEX WITH 2-((4-(4-((3-((2-METHYL-1,3-               
TITLE    2 BENZOTHIAZOL-6YL)AMINO)-3-OXO-PROPYL)AMINO)-4-OXO-BUTYL)             
TITLE    3 PHENYL)METHYL)PROPANEDIOIC ACID                                      
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     
COMPND   5  MUSCLE SUBUNIT, LDH-M, RENAL CARCINOMA ANTIGEN NY-REN-59, LACTATE   
COMPND   6  DEHYDROGENASE A;                                                    
COMPND   7 EC: 1.1.1.27;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: MUSCLE;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET29B                                     
KEYWDS    OXIDOREDUCTASE-INHIBITOR COMPLEX, FRAGMENT BASED LEAD GENERATED       
KEYWDS   2 INHIBITORS                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.TUCKER,C.BRASSINGTON,A.CAPUTO,R.WARD,S.PEARSON,M.WATSON,J.TART,   
AUTHOR   2 G.DAVIES                                                             
REVDAT   3   17-SEP-14 4AJP    1       REMARK HET    HETNAM FORMUL              
REVDAT   3 2                           HETATM                                   
REVDAT   2   25-APR-12 4AJP    1       JRNL                                     
REVDAT   1   21-MAR-12 4AJP    0                                                
JRNL        AUTH   R.WARD,C.BRASSINGTON,A.L.BREEZE,A.CAPUTO,S.CRITCHLOW,        
JRNL        AUTH 2 G.DAVIES,L.GOODWIN,G.HASSALL,R.GREENWOOD,G.HOLDGATE,         
JRNL        AUTH 3 M.MROSEK,R.A.NORMAN,S.PEARSON,J.TART,J.A.TUCKER,M.VOGTHERR,  
JRNL        AUTH 4 D.WHITTAKER,J.WINGFIELD,J.WINTER,K.HUDSON                    
JRNL        TITL   THE DESIGN AND SYNTHESIS OF NOVEL LACTATE DEHYDROGENASE A    
JRNL        TITL 2 INHIBITORS BY FRAGMENT-BASED LEAD GENERATION                 
JRNL        REF    J.MED.CHEM.                   V.  55  3285 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22417091                                                     
JRNL        DOI    10.1021/JM201734R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.83                          
REMARK   3   NUMBER OF REFLECTIONS             : 52964                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.16808                         
REMARK   3   R VALUE            (WORKING SET) : 0.16563                         
REMARK   3   FREE R VALUE                     : 0.21467                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2806                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.380                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.442                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3829                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.196                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.266                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10108                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 213                                     
REMARK   3   SOLVENT ATOMS            : 394                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.731                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.29                                                 
REMARK   3    B22 (A**2) : -2.19                                                
REMARK   3    B33 (A**2) : -1.58                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 1.22                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.415         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.235         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.167        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10500 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6925 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14249 ; 1.366 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17059 ; 0.913 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1324 ; 6.358 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;40.791 ;24.949       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1836 ;13.892 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;18.477 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1670 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11614 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1970 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6453  -0.2783  11.1742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0144 T22:   0.0977                                     
REMARK   3      T33:   0.1117 T12:   0.0063                                     
REMARK   3      T13:  -0.0056 T23:   0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0921 L22:   0.6558                                     
REMARK   3      L33:   0.5329 L12:   0.1921                                     
REMARK   3      L13:  -0.0762 L23:  -0.0733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0247 S12:  -0.0179 S13:  -0.0044                       
REMARK   3      S21:  -0.0786 S22:  -0.0065 S23:  -0.0977                       
REMARK   3      S31:  -0.0199 S32:   0.0281 S33:   0.0312                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2658  -3.3831  32.3727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0248 T22:   0.0901                                     
REMARK   3      T33:   0.0870 T12:   0.0130                                     
REMARK   3      T13:  -0.0003 T23:  -0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1279 L22:   0.5588                                     
REMARK   3      L33:   0.4803 L12:  -0.0423                                     
REMARK   3      L13:  -0.1624 L23:  -0.0470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:   0.0099 S13:   0.0181                       
REMARK   3      S21:   0.0948 S22:   0.0067 S23:   0.0896                       
REMARK   3      S31:  -0.0554 S32:  -0.0725 S33:  -0.0156                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9213 -29.9474   3.2860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0464 T22:   0.0717                                     
REMARK   3      T33:   0.0686 T12:  -0.0038                                     
REMARK   3      T13:  -0.0073 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0488 L22:   0.7585                                     
REMARK   3      L33:   0.4284 L12:   0.1134                                     
REMARK   3      L13:   0.0428 L23:   0.0819                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0321 S12:   0.0016 S13:  -0.0223                       
REMARK   3      S21:  -0.1446 S22:   0.0067 S23:   0.0353                       
REMARK   3      S31:   0.0345 S32:  -0.0490 S33:   0.0254                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6515 -33.3238  32.6116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0291 T22:   0.0816                                     
REMARK   3      T33:   0.0883 T12:  -0.0005                                     
REMARK   3      T13:  -0.0149 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0280 L22:   0.6251                                     
REMARK   3      L33:   0.3771 L12:  -0.0769                                     
REMARK   3      L13:  -0.0288 L23:  -0.1724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.0002 S13:  -0.0227                       
REMARK   3      S21:   0.0857 S22:  -0.0327 S23:  -0.0834                       
REMARK   3      S31:   0.0490 S32:   0.0335 S33:   0.0515                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. DISORDERED SIDE-CHAINS HAVE BEEN TRUNCATED.      
REMARK   3   U VALUES WITH TLS ADDED.                                           
REMARK   4                                                                      
REMARK   4 4AJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51330.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97627                            
REMARK 200  MONOCHROMATOR                  : SI(311) OR SI(111)                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59591                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.31                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.90                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.3                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1I10                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULPHATE, 0.1M             
REMARK 280  MES PH 6.5, 10% 1, 4-DIOXANE                                        
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       68.39000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -297.4 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 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     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     HIS A   332                                                      
REMARK 465     HIS A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     GLN B    16                                                      
REMARK 465     HIS B   332                                                      
REMARK 465     HIS B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     HIS B   335                                                      
REMARK 465     HIS B   336                                                      
REMARK 465     HIS B   337                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C   332                                                      
REMARK 465     HIS C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     HIS C   335                                                      
REMARK 465     HIS C   336                                                      
REMARK 465     HIS C   337                                                      
REMARK 465     HIS D   332                                                      
REMARK 465     HIS D   333                                                      
REMARK 465     HIS D   334                                                      
REMARK 465     HIS D   335                                                      
REMARK 465     HIS D   336                                                      
REMARK 465     HIS D   337                                                      
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     GLN A  16    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  80    CD   CE   NZ                                        
REMARK 470     LYS A 117    CE   NZ                                             
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     LYS A 223    CD   CE   NZ                                        
REMARK 470     GLN A 225    CD   OE1  NE2                                       
REMARK 470     LYS A 231    CD   CE   NZ                                        
REMARK 470     LYS A 242    CD   CE   NZ                                        
REMARK 470     LYS A 317    CD   CE   NZ                                        
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 117    NZ                                                  
REMARK 470     LYS B 221    CG   CD   CE   NZ                                   
REMARK 470     LYS B 223    CD   CE   NZ                                        
REMARK 470     LYS B 227    CE   NZ                                             
REMARK 470     LYS B 231    CD   CE   NZ                                        
REMARK 470     LYS B 242    CD   CE   NZ                                        
REMARK 470     LYS B 283    CD   CE   NZ                                        
REMARK 470     GLU B 328    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 330    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 331    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C  13    CG   CD   CE   NZ                                   
REMARK 470     GLN C  16    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  80    CG   CD   CE   NZ                                   
REMARK 470     LYS C 221    CG   CD   CE   NZ                                   
REMARK 470     LYS C 223    CG   CD   CE   NZ                                   
REMARK 470     LYS C 231    CG   CD   CE   NZ                                   
REMARK 470     LYS C 242    NZ                                                  
REMARK 470     LEU C 279    CG   CD1  CD2                                       
REMARK 470     LYS C 317    CG   CD   CE   NZ                                   
REMARK 470     GLU C 328    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 330    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  13    CG   CD   CE   NZ                                   
REMARK 470     GLU D  15    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  16    OE1  NE2                                            
REMARK 470     THR D  17    OG1  CG2                                            
REMARK 470     LYS D  80    CG   CD   CE   NZ                                   
REMARK 470     LYS D 117    CE   NZ                                             
REMARK 470     LYS D 221    CD   CE   NZ                                        
REMARK 470     LYS D 242    CD   CE   NZ                                        
REMARK 470     LYS D 283    CE   NZ                                             
REMARK 470     LYS D 327    CE   NZ                                             
REMARK 470     GLU D 328    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 330    CG   CD   OE1  NE2                                  
REMARK 470     PHE D 331    CG   CD1  CD2  CE1  CE2  CZ                         
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   O3   GOL B  1332     O    HOH B  2108              2.16            
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    ASN A  20       55.49   -140.82                                   
REMARK 500    ASP A 222      108.42    -23.57                                   
REMARK 500    SER A 248      -57.19   -153.86                                   
REMARK 500    ASN B  20       56.16   -142.76                                   
REMARK 500    SER B 248      -53.70   -153.08                                   
REMARK 500    ASN C  20       57.08   -142.55                                   
REMARK 500    ASP C 222      114.30    -18.42                                   
REMARK 500    SER C 248      -54.16   -148.26                                   
REMARK 500    ASP C 285       46.80    -70.56                                   
REMARK 500    LYS D  13       53.84   -110.77                                   
REMARK 500    ASN D  20       54.57   -143.13                                   
REMARK 500    ASP D 222      107.92    -39.78                                   
REMARK 500    SER D 248      -48.12   -148.63                                   
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 GOL C1332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 88N A1332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 88N B1333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 88N C1334                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 88N D1332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1334                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1335                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1334                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1335                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1335                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1334                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1I10   RELATED DB: PDB                                   
REMARK 900  HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN,                       
REMARK 900  TERNARYCOMPLEX WITH NADH AND OXAMATE                                
REMARK 900 RELATED ID: 4AJ1   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH N-(2-(METHYLAMINO)-1,3-                    
REMARK 900  BENZOTHIAZOL-6-YL)ACETAMIDE                                         
REMARK 900 RELATED ID: 4AJ2   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 5-(2-CHLOROPHENYL)-1H-                     
REMARK 900  TETRAZOLE                                                           
REMARK 900 RELATED ID: 4AJ4   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 4-((2-ALLYLSULFANYL-1,3-                   
REMARK 900  BENZOTHIZOL-6-YL)AMINO)-4-OXO-BUTANOIC ACID                         
REMARK 900 RELATED ID: 4AJE   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 2-(4-BROMOPHENOXY)                         
REMARK 900  PROPANEDIOIC ACID                                                   
REMARK 900 RELATED ID: 4AJH   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH N-(2-METHYL-1,3-                           
REMARK 900  BENZOTHIAZOL-6-YL)-3-UREIDO-PROPANAMIDE AND 2-(4-                   
REMARK 900  BROMOPHENOXY)PROPANEDIOIC ACID                                      
REMARK 900 RELATED ID: 4AJI   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 2-((3,4-DIMETHOXYPHENYL)                   
REMARK 900  METHYL))PROPANEDIOIC ACID                                           
REMARK 900 RELATED ID: 4AJJ   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 2-((3,4-DIMETHOXYPHENYL)                   
REMARK 900  METHYL))PROPANEDIOIC ACID AND N-(2-METHYL-1,3-                      
REMARK 900  BENZOTHIAZOL-6-YL)-3-UREIDO-PROPANAMIDE                             
REMARK 900 RELATED ID: 4AJK   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH N-(2-(METHYLAMINO)-1,3-                    
REMARK 900  BENZOTHIAZOL-6-YL)ACETAMIDE                                         
REMARK 900 RELATED ID: 4AJL   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 3-(ETHYLCARBAMOYLAMINO)-N-(2               
REMARK 900  -METHYL-1,3-BENZOTHIAZOL-6-YL)PROPANAMIDE                           
REMARK 900 RELATED ID: 4AJN   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 2-((4-(2-((3-((2-METHYL-                   
REMARK 900  1,3-BENZOTHIAZOL-6-YL)AMINO)-3-OXO-PROPYL)                          
REMARK 900  CARBAMOYLAMINO)ETHYL)PHENYL)METHYL)PROPANEDIOIC ACID                
REMARK 900 RELATED ID: 4AJO   RELATED DB: PDB                                   
REMARK 900  RAT LDHA IN COMPLEX WITH 2-((4-(4-((3-((2-METHYL-                   
REMARK 900  1,3-BENZOTHIAZOL-6YL)AMINO)-3-OXO-PROPYL)AMINO)-4-                  
REMARK 900  OXO-BUTYL)PHENYL)METHYL)PROPANEDIOIC ACID                           
DBREF  4AJP A    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4AJP B    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4AJP C    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4AJP D    1   331  UNP    P00338   LDHA_HUMAN       2    332             
SEQADV 4AJP HIS A  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS A  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS A  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS A  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS A  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS A  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS B  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS C  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  332  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4AJP HIS D  337  UNP  P00338              EXPRESSION TAG                 
SEQRES   1 A  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 A  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 A  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 A  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 A  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 A  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 A  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 A  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 A  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 A  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 A  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 A  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 A  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 A  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 A  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 A  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 A  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 A  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 A  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 A  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 A  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 A  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 A  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 A  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 A  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 A  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 B  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 B  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 B  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 B  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 B  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 B  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 B  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 B  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 B  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 B  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 B  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 B  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 B  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 B  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 B  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 B  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 B  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 B  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 B  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 B  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 B  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 B  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 B  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 B  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 B  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 C  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 C  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 C  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 C  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 C  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 C  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 C  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 C  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 C  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 C  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 C  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 C  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 C  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 C  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 C  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 C  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 C  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 C  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 C  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 C  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 C  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 C  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 C  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 C  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 C  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 C  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 D  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 D  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 D  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 D  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 D  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 D  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 D  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 D  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 D  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 D  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 D  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 D  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 D  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 D  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 D  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 D  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 D  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 D  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 D  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 D  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 D  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 D  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 D  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 D  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 D  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 D  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
HET    88N  A1332      35                                                       
HET    SO4  A1333       5                                                       
HET    SO4  A1334       5                                                       
HET    SO4  A1335       5                                                       
HET    SO4  A1336       5                                                       
HET    GOL  B1332       6                                                       
HET    88N  B1333      35                                                       
HET    SO4  B1334       5                                                       
HET    SO4  B1335       5                                                       
HET    SO4  B1336       5                                                       
HET    GOL  C1332       6                                                       
HET    GOL  C1333       6                                                       
HET    88N  C1334      35                                                       
HET    SO4  C1335       5                                                       
HET    SO4  C1336       5                                                       
HET    88N  D1332      35                                                       
HET    SO4  D1333       5                                                       
HET    SO4  D1334       5                                                       
HETNAM     88N {4-[4-({3-[(2-METHYL-1,3-BENZOTHIAZOL-6-YL)                      
HETNAM   2 88N  AMINO]-3-OXOPROPYL}AMINO)-4-OXOBUTYL]BENZYL}                    
HETNAM   3 88N  PROPANEDIOIC ACID                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  88N    4(C25 H27 N3 O6 S)                                           
FORMUL   6  SO4    11(O4 S 2-)                                                  
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *394(H2 O)                                                    
HELIX    1   1 THR A    2  LEU A    7  1                                   6    
HELIX    2   2 GLY A   28  LYS A   41  1                                  14    
HELIX    3   3 ILE A   53  GLY A   67  1                                  15    
HELIX    4   4 SER A   68  LEU A   71  5                                   4    
HELIX    5   5 ASP A   81  ALA A   86  5                                   6    
HELIX    6   6 SER A  104  ASN A  107  5                                   4    
HELIX    7   7 LEU A  108  SER A  127  1                                  20    
HELIX    8   8 PRO A  138  GLY A  151  1                                  14    
HELIX    9   9 PRO A  153  ASN A  155  5                                   3    
HELIX   10  10 CYS A  162  GLY A  178  1                                  17    
HELIX   11  11 HIS A  180  LEU A  182  5                                   3    
HELIX   12  12 TRP A  200  GLY A  202  5                                   3    
HELIX   13  13 LEU A  210  HIS A  214  1                                   5    
HELIX   14  14 TRP A  226  GLY A  245  1                                  20    
HELIX   15  15 SER A  248  LYS A  264  1                                  17    
HELIX   16  16 THR A  308  LYS A  327  1                                  20    
HELIX   17  17 THR B    2  LEU B    7  1                                   6    
HELIX   18  18 GLY B   28  LYS B   41  1                                  14    
HELIX   19  19 ILE B   53  HIS B   66  1                                  14    
HELIX   20  20 GLY B   67  LEU B   71  5                                   5    
HELIX   21  21 ASP B   81  ALA B   86  5                                   6    
HELIX   22  22 SER B  104  ASN B  107  5                                   4    
HELIX   23  23 LEU B  108  SER B  127  1                                  20    
HELIX   24  24 PRO B  138  GLY B  151  1                                  14    
HELIX   25  25 PRO B  153  ASN B  155  5                                   3    
HELIX   26  26 CYS B  162  GLY B  178  1                                  17    
HELIX   27  27 HIS B  180  LEU B  182  5                                   3    
HELIX   28  28 TRP B  200  GLY B  202  5                                   3    
HELIX   29  29 LEU B  210  HIS B  214  1                                   5    
HELIX   30  30 TRP B  226  GLY B  245  1                                  20    
HELIX   31  31 SER B  248  LYS B  264  1                                  17    
HELIX   32  32 THR B  308  GLU B  328  1                                  21    
HELIX   33  33 THR C    2  LEU C    7  1                                   6    
HELIX   34  34 GLY C   28  LYS C   41  1                                  14    
HELIX   35  35 ILE C   53  GLY C   67  1                                  15    
HELIX   36  36 SER C   68  LEU C   71  5                                   4    
HELIX   37  37 ASP C   81  ALA C   86  5                                   6    
HELIX   38  38 SER C  104  ASN C  107  5                                   4    
HELIX   39  39 LEU C  108  SER C  127  1                                  20    
HELIX   40  40 PRO C  138  GLY C  151  1                                  14    
HELIX   41  41 PRO C  153  ASN C  155  5                                   3    
HELIX   42  42 CYS C  162  GLY C  178  1                                  17    
HELIX   43  43 HIS C  180  LEU C  182  5                                   3    
HELIX   44  44 TRP C  200  GLY C  202  5                                   3    
HELIX   45  45 LEU C  210  HIS C  214  1                                   5    
HELIX   46  46 TRP C  226  GLY C  245  1                                  20    
HELIX   47  47 SER C  248  LYS C  264  1                                  17    
HELIX   48  48 THR C  308  LYS C  327  1                                  20    
HELIX   49  49 THR D    2  LEU D    7  1                                   6    
HELIX   50  50 GLY D   28  MET D   40  1                                  13    
HELIX   51  51 ILE D   53  HIS D   66  1                                  14    
HELIX   52  52 GLY D   67  LEU D   71  5                                   5    
HELIX   53  53 ASP D   81  ALA D   86  5                                   6    
HELIX   54  54 SER D  104  ASN D  107  5                                   4    
HELIX   55  55 LEU D  108  SER D  127  1                                  20    
HELIX   56  56 PRO D  138  GLY D  151  1                                  14    
HELIX   57  57 PRO D  153  ASN D  155  5                                   3    
HELIX   58  58 CYS D  162  GLY D  178  1                                  17    
HELIX   59  59 HIS D  180  LEU D  182  5                                   3    
HELIX   60  60 TRP D  200  GLY D  202  5                                   3    
HELIX   61  61 LEU D  210  HIS D  214  1                                   5    
HELIX   62  62 TRP D  226  GLY D  245  1                                  20    
HELIX   63  63 SER D  248  LYS D  264  1                                  17    
HELIX   64  64 THR D  308  LYS D  327  1                                  20    
SHEET    1  AA 4 ILE A   8  ASN A  10  0                                        
SHEET    2  AA 4 GLY D 298  VAL D 303 -1  O  LEU D 302   N  TYR A   9           
SHEET    3  AA 4 PHE D 287  GLY D 295 -1  O  PRO D 291   N  VAL D 303           
SHEET    4  AA 4 ARG D 268  MET D 275 -1  O  ARG D 268   N  LEU D 294           
SHEET    1  AB 6 LYS A  75  SER A  78  0                                        
SHEET    2  AB 6 GLU A  46  VAL A  50  1  O  LEU A  47   N  VAL A  77           
SHEET    3  AB 6 LYS A  21  VAL A  25  1  O  ILE A  22   N  ALA A  48           
SHEET    4  AB 6 LEU A  90  ILE A  93  1  O  LEU A  90   N  THR A  23           
SHEET    5  AB 6 LYS A 131  ILE A 134  1  O  LYS A 131   N  VAL A  91           
SHEET    6  AB 6 VAL A 157  GLY A 159  1  O  ILE A 158   N  ILE A 134           
SHEET    1  AC 3 CYS A 184  HIS A 185  0                                        
SHEET    2  AC 3 ASN A 204  VAL A 205 -1  O  ASN A 204   N  HIS A 185           
SHEET    3  AC 3 VAL A 208  SER A 209 -1  O  VAL A 208   N  VAL A 205           
SHEET    1  AD 2 VAL A 188  LEU A 189  0                                        
SHEET    2  AD 2 VAL A 197  PRO A 198 -1  O  VAL A 197   N  LEU A 189           
SHEET    1  AE 4 ARG A 268  MET A 275  0                                        
SHEET    2  AE 4 PHE A 287  GLY A 295 -1  O  LEU A 288   N  THR A 274           
SHEET    3  AE 4 GLY A 298  VAL A 303 -1  O  GLY A 298   N  GLY A 295           
SHEET    4  AE 4 ILE D   8  ASN D  10 -1  O  TYR D   9   N  LEU A 302           
SHEET    1  BA 4 ILE B   8  ASN B  10  0                                        
SHEET    2  BA 4 GLY C 298  VAL C 303 -1  O  LEU C 302   N  TYR B   9           
SHEET    3  BA 4 PHE C 287  GLY C 295 -1  O  PRO C 291   N  VAL C 303           
SHEET    4  BA 4 ARG C 268  MET C 275 -1  O  ARG C 268   N  LEU C 294           
SHEET    1  BB 6 LYS B  75  GLY B  79  0                                        
SHEET    2  BB 6 GLU B  46  VAL B  50  1  O  LEU B  47   N  VAL B  77           
SHEET    3  BB 6 LYS B  21  VAL B  25  1  O  ILE B  22   N  ALA B  48           
SHEET    4  BB 6 LEU B  90  ILE B  93  1  O  LEU B  90   N  THR B  23           
SHEET    5  BB 6 LYS B 131  ILE B 134  1  O  LYS B 131   N  VAL B  91           
SHEET    6  BB 6 VAL B 157  GLY B 159  1  O  ILE B 158   N  ILE B 134           
SHEET    1  BC 3 CYS B 184  HIS B 185  0                                        
SHEET    2  BC 3 ASN B 204  VAL B 205 -1  O  ASN B 204   N  HIS B 185           
SHEET    3  BC 3 VAL B 208  SER B 209 -1  O  VAL B 208   N  VAL B 205           
SHEET    1  BD 2 VAL B 188  LEU B 189  0                                        
SHEET    2  BD 2 VAL B 197  PRO B 198 -1  O  VAL B 197   N  LEU B 189           
SHEET    1  BE 4 ARG B 268  MET B 275  0                                        
SHEET    2  BE 4 PHE B 287  GLY B 295 -1  O  LEU B 288   N  THR B 274           
SHEET    3  BE 4 GLY B 298  VAL B 303 -1  O  GLY B 298   N  GLY B 295           
SHEET    4  BE 4 ILE C   8  ASN C  10 -1  O  TYR C   9   N  LEU B 302           
SHEET    1  CA 6 LYS C  75  GLY C  79  0                                        
SHEET    2  CA 6 GLU C  46  VAL C  50  1  O  LEU C  47   N  VAL C  77           
SHEET    3  CA 6 LYS C  21  VAL C  25  1  O  ILE C  22   N  ALA C  48           
SHEET    4  CA 6 LEU C  90  ILE C  93  1  O  LEU C  90   N  THR C  23           
SHEET    5  CA 6 LYS C 131  ILE C 134  1  O  LYS C 131   N  VAL C  91           
SHEET    6  CA 6 VAL C 157  GLY C 159  1  O  ILE C 158   N  ILE C 134           
SHEET    1  CB 3 CYS C 184  HIS C 185  0                                        
SHEET    2  CB 3 ASN C 204  VAL C 205 -1  O  ASN C 204   N  HIS C 185           
SHEET    3  CB 3 VAL C 208  SER C 209 -1  O  VAL C 208   N  VAL C 205           
SHEET    1  CC 2 VAL C 188  LEU C 189  0                                        
SHEET    2  CC 2 VAL C 197  PRO C 198 -1  O  VAL C 197   N  LEU C 189           
SHEET    1  DA 6 LYS D  75  SER D  78  0                                        
SHEET    2  DA 6 GLU D  46  VAL D  50  1  O  LEU D  47   N  VAL D  77           
SHEET    3  DA 6 LYS D  21  VAL D  25  1  O  ILE D  22   N  ALA D  48           
SHEET    4  DA 6 LEU D  90  ILE D  93  1  O  LEU D  90   N  THR D  23           
SHEET    5  DA 6 LYS D 131  ILE D 134  1  O  LYS D 131   N  VAL D  91           
SHEET    6  DA 6 VAL D 157  GLY D 159  1  O  ILE D 158   N  ILE D 134           
SHEET    1  DB 3 CYS D 184  HIS D 185  0                                        
SHEET    2  DB 3 ASN D 204  VAL D 205 -1  O  ASN D 204   N  HIS D 185           
SHEET    3  DB 3 VAL D 208  SER D 209 -1  O  VAL D 208   N  VAL D 205           
SHEET    1  DC 2 VAL D 188  LEU D 189  0                                        
SHEET    2  DC 2 VAL D 197  PRO D 198 -1  O  VAL D 197   N  LEU D 189           
CISPEP   1 LEU A   12    LYS A   13          0         3.46                     
CISPEP   2 ASN A  137    PRO A  138          0        -2.48                     
CISPEP   3 ASN B  137    PRO B  138          0        -1.61                     
CISPEP   4 ASN C  137    PRO C  138          0        -2.04                     
CISPEP   5 ASN D  137    PRO D  138          0        -3.34                     
SITE     1 AC1  9 SER A 201  GLY A 202  ASN A 204  GLY A 207                    
SITE     2 AC1  9 SER C 201  GLY C 202  ASN C 204  GLY C 207                    
SITE     3 AC1  9 SER C 209                                                     
SITE     1 AC2  4 ALA B  29  ARG B  98  HOH B2007  HOH B2108                    
SITE     1 AC3  3 PRO C 153  ASN C 155  ARG C 156                               
SITE     1 AC4 18 GLY A  28  VAL A  30  ASP A  51  VAL A  52                    
SITE     2 AC4 18 THR A  94  ALA A  95  GLY A  96  GLN A  99                    
SITE     3 AC4 18 ARG A 105  VAL A 135  ASN A 137  ARG A 168                    
SITE     4 AC4 18 HIS A 192  ALA A 237  THR A 247  HOH A2011                    
SITE     5 AC4 18 HOH A2014  HOH A2042                                          
SITE     1 AC5 20 GLY B  28  VAL B  30  ASP B  51  VAL B  52                    
SITE     2 AC5 20 THR B  94  ALA B  95  GLY B  96  GLN B  99                    
SITE     3 AC5 20 ARG B 105  VAL B 135  ASN B 137  LEU B 164                    
SITE     4 AC5 20 ARG B 168  HIS B 192  ALA B 237  THR B 247                    
SITE     5 AC5 20 HOH B2005  HOH B2007  HOH B2029  HOH B2039                    
SITE     1 AC6 18 VAL C  30  ASP C  51  VAL C  52  THR C  94                    
SITE     2 AC6 18 ALA C  95  GLY C  96  GLN C  99  ARG C 105                    
SITE     3 AC6 18 PHE C 118  VAL C 135  ASN C 137  ARG C 168                    
SITE     4 AC6 18 HIS C 192  ALA C 237  THR C 247  HOH C2004                    
SITE     5 AC6 18 HOH C2005  HOH C2033                                          
SITE     1 AC7 20 GLY D  26  VAL D  30  ASP D  51  VAL D  52                    
SITE     2 AC7 20 THR D  94  ALA D  95  GLY D  96  GLN D  99                    
SITE     3 AC7 20 ARG D 105  VAL D 135  ASN D 137  LEU D 164                    
SITE     4 AC7 20 ARG D 168  HIS D 192  ALA D 237  THR D 247                    
SITE     5 AC7 20 HOH D2005  HOH D2008  HOH D2023  HOH D2026                    
SITE     1 AC8  7 ARG B 170  HIS B 185  HOH B2063  HOH B2070                    
SITE     2 AC8  7 HOH B2099  HOH B2109  HIS D 185                               
SITE     1 AC9  7 HIS B 185  HOH B2069  HOH B2083  ARG D 170                    
SITE     2 AC9  7 HIS D 185  TRP D 187  HOH D2051                               
SITE     1 BC1  7 SER A 183  HIS A 185  HOH A2083  HOH A2094                    
SITE     2 BC1  7 ARG C 170  HIS C 185  HOH C2061                               
SITE     1 BC2  6 ARG A 170  HIS A 185  HOH A2078  HOH A2085                    
SITE     2 BC2  6 HOH A2121  HIS C 185                                          
SITE     1 BC3  3 TRP A 147  PRO A 153  LYS A 154                               
SITE     1 BC4  5 TRP B 147  PHE B 152  PRO B 153  LYS B 154                    
SITE     2 BC4  5 HOH B2057                                                     
SITE     1 BC5  4 LYS A 148  HOH A2065  ASN B  83  TYR B 126                    
SITE     1 BC6  3 ASN A  83  TYR A 126  LYS B 148                               
SITE     1 BC7  4 TRP C 147  PHE C 152  PRO C 153  LYS C 154                    
SITE     1 BC8  4 THR A 308  SER A 309  THR B 219  ASP B 220                    
SITE     1 BC9  4 TRP D 147  PHE D 152  PRO D 153  LYS D 154                    
CRYST1   63.980  136.780   83.790  90.00 102.31  90.00 P 1 21 1      8          
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      0.015630  0.000000  0.003411        0.00000                         
SCALE2      0.000000  0.007311  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012215        0.00000                         
MTRIX1   1 -0.999820 -0.019060  0.000030      -13.77443    1                    
MTRIX2   1 -0.018410  0.966160  0.257270       -5.81798    1                    
MTRIX3   1 -0.004940  0.257220 -0.966340       43.32919    1                    
MTRIX1   2 -0.917980  0.057600 -0.392410       -4.38953    1                    
MTRIX2   2  0.044280 -0.968330 -0.245730      -27.74323    1                    
MTRIX3   2 -0.394140 -0.242950  0.886360       -4.56010    1                    
MTRIX1   3  0.919480 -0.032110  0.391820       -8.75757    1                    
MTRIX2   3 -0.031610 -0.999470 -0.007720      -33.51753    1                    
MTRIX3   3  0.391860 -0.005290 -0.920010       40.79667    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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