GenomeNet

Database: PDB
Entry: 4QO7
LinkDB: 4QO7
Original site: 4QO7 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 19-JUN-14   4QO7              
TITLE     LACTATE DEHYDROGENASE A IN COMPLEX WITH SUBSTITUTED 3-HYDROXY-2-      
TITLE    2 MERCAPTOCYCLOHEX-2-ENONE COMPOUND 7                                  
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;            
COMPND   6 EC: 1.1.1.27;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LDHA, PIG19;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, NICOTINAMIDE ADENINE DINUCLEOTIDE, OXIDOREDUCTASE-    
KEYWDS   2 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,M.ULTSCH                                                  
REVDAT   3   03-SEP-14 4QO7    1       JRNL                                     
REVDAT   2   13-AUG-14 4QO7    1       JRNL                                     
REVDAT   1   16-JUL-14 4QO7    0                                                
JRNL        AUTH   P.S.DRAGOVICH,B.P.FAUBER,J.BOGGS,J.CHEN,L.B.CORSON,C.Z.DING, 
JRNL        AUTH 2 C.EIGENBROT,H.GE,A.M.GIANNETTI,T.HUNSAKER,S.LABADIE,C.LI,    
JRNL        AUTH 3 Y.LIU,Y.LIU,S.MA,S.MALEK,D.PETERSON,K.E.PITTS,H.E.PURKEY,    
JRNL        AUTH 4 K.ROBARGE,L.SALPHATI,S.SIDERIS,M.ULTSCH,E.VANDERPORTEN,      
JRNL        AUTH 5 J.WANG,B.WEI,Q.XU,I.YEN,Q.YUE,H.ZHANG,X.ZHANG,A.ZHOU         
JRNL        TITL   IDENTIFICATION OF SUBSTITUTED                                
JRNL        TITL 2 3-HYDROXY-2-MERCAPTOCYCLOHEX-2-ENONES AS POTENT INHIBITORS   
JRNL        TITL 3 OF HUMAN LACTATE DEHYDROGENASE.                              
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  24  3764 2014              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   25037916                                                     
JRNL        DOI    10.1016/J.BMCL.2014.06.076                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 74870                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3964                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.14                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10469                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 561                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10262                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 304                                     
REMARK   3   SOLVENT ATOMS            : 697                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.24000                                              
REMARK   3    B22 (A**2) : 0.46000                                              
REMARK   3    B33 (A**2) : -0.81000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.88000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.212         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.822         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10762 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10583 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14596 ; 1.362 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24408 ; 0.721 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1320 ; 5.753 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   406 ;38.680 ;25.123       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1951 ;12.993 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;19.557 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1699 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11816 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2212 ; 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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4QO7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086302.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78834                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4M49                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM MALONATE, PH 7.0,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.24050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.55050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.24050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.55050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 26700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU D 101    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 105    CG   CD   NE   CZ   NH1  NH2                        
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   OD1  ASN C   297     O    HOH C  1047              2.12            
REMARK 500   OD2  ASP C    55     O    HOH C   977              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    GLU A  14     -160.93     52.97                                   
REMARK 500    SER A 104     -145.13    -74.19                                   
REMARK 500    SER A 248      -51.45   -144.89                                   
REMARK 500    LYS B  13     -133.35   -102.80                                   
REMARK 500    GLU B  14      115.95     62.01                                   
REMARK 500    SER B 248      -50.87   -145.19                                   
REMARK 500    ASP B 285       39.34    -82.33                                   
REMARK 500    LYS C  13      -60.76   -106.72                                   
REMARK 500    GLU C  14      104.21    -44.06                                   
REMARK 500    SER C 248      -55.87   -142.97                                   
REMARK 500    MET C 275      107.92    -52.75                                   
REMARK 500    GLU D  15     -106.23     24.57                                   
REMARK 500    GLN D  16       81.76     71.37                                   
REMARK 500    ASN D  20       53.36   -146.52                                   
REMARK 500    SER D 248      -57.86   -141.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   13     GLU A   14                  146.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 36V A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2OP B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 36V C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI D 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 36V D 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 803                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QO8   RELATED DB: PDB                                   
DBREF  4QO7 A    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4QO7 B    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4QO7 C    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4QO7 D    1   331  UNP    P00338   LDHA_HUMAN       2    332             
SEQRES   1 A  331  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 A  331  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 A  331  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 A  331  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 A  331  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 A  331  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 A  331  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 A  331  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 A  331  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 A  331  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 A  331  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 A  331  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 A  331  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 A  331  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 A  331  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 A  331  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 A  331  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 A  331  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 A  331  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 A  331  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 A  331  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 A  331  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 A  331  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 A  331  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 A  331  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 A  331  GLN LYS GLU LEU GLN PHE                                      
SEQRES   1 B  331  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 B  331  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 B  331  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 B  331  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 B  331  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 B  331  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 B  331  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 B  331  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 B  331  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 B  331  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 B  331  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 B  331  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 B  331  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 B  331  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 B  331  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 B  331  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 B  331  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 B  331  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 B  331  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 B  331  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 B  331  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 B  331  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 B  331  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 B  331  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 B  331  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 B  331  GLN LYS GLU LEU GLN PHE                                      
SEQRES   1 C  331  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 C  331  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 C  331  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 C  331  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 C  331  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 C  331  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 C  331  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 C  331  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 C  331  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 C  331  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 C  331  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 C  331  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 C  331  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 C  331  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 C  331  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 C  331  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 C  331  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 C  331  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 C  331  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 C  331  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 C  331  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 C  331  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 C  331  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 C  331  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 C  331  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 C  331  GLN LYS GLU LEU GLN PHE                                      
SEQRES   1 D  331  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 D  331  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 D  331  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 D  331  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 D  331  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 D  331  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 D  331  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 D  331  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 D  331  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 D  331  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 D  331  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 D  331  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 D  331  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 D  331  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 D  331  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 D  331  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 D  331  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 D  331  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 D  331  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 D  331  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 D  331  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 D  331  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 D  331  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 D  331  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 D  331  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 D  331  GLN LYS GLU LEU GLN PHE                                      
HET    NAI  A 801      44                                                       
HET    EPE  A 802      15                                                       
HET    36V  A 803      24                                                       
HET    NAI  B 801      44                                                       
HET    2OP  B 802       6                                                       
HET    EPE  B 803      15                                                       
HET    NAI  C 801      44                                                       
HET    EPE  C 802      15                                                       
HET    36V  C 803      24                                                       
HET    NAI  D 801      44                                                       
HET    36V  D 802      24                                                       
HET    SO4  D 803       5                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     36V TRANS-2-[(2-NITROPHENYL)SULFANYL]-5-PHENYLCYCLOHEXANE-           
HETNAM   2 36V  1,3-DIONE                                                       
HETNAM     2OP (2S)-2-HYDROXYPROPANOIC ACID                                     
HETNAM     SO4 SULFATE ION                                                      
HETSYN     NAI NADH                                                             
HETSYN     EPE HEPES                                                            
FORMUL   5  NAI    4(C21 H29 N7 O14 P2)                                         
FORMUL   6  EPE    3(C8 H18 N2 O4 S)                                            
FORMUL   7  36V    3(C18 H15 N O4 S)                                            
FORMUL   9  2OP    C3 H6 O3                                                     
FORMUL  16  SO4    O4 S 2-                                                      
FORMUL  17  HOH   *697(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 ARG A  105  SER A  127  1                                  23    
HELIX    7   7 PRO A  138  GLY A  151  1                                  14    
HELIX    8   8 PRO A  153  ASN A  155  5                                   3    
HELIX    9   9 CYS A  162  GLY A  178  1                                  17    
HELIX   10  10 HIS A  180  LEU A  182  5                                   3    
HELIX   11  11 LEU A  210  HIS A  214  1                                   5    
HELIX   12  12 TRP A  226  GLY A  245  1                                  20    
HELIX   13  13 SER A  248  LYS A  264  1                                  17    
HELIX   14  14 THR A  308  LYS A  327  1                                  20    
HELIX   15  15 THR B    2  LEU B    7  1                                   6    
HELIX   16  16 GLY B   28  LYS B   41  1                                  14    
HELIX   17  17 ILE B   53  HIS B   66  1                                  14    
HELIX   18  18 GLY B   67  LEU B   71  5                                   5    
HELIX   19  19 ASP B   81  ALA B   86  5                                   6    
HELIX   20  20 SER B  104  ASN B  107  5                                   4    
HELIX   21  21 LEU B  108  SER B  127  1                                  20    
HELIX   22  22 PRO B  138  GLY B  151  1                                  14    
HELIX   23  23 PRO B  153  ASN B  155  5                                   3    
HELIX   24  24 CYS B  162  GLY B  178  1                                  17    
HELIX   25  25 HIS B  180  LEU B  182  5                                   3    
HELIX   26  26 TRP B  200  GLY B  202  5                                   3    
HELIX   27  27 LEU B  210  HIS B  214  1                                   5    
HELIX   28  28 TRP B  226  GLY B  245  1                                  20    
HELIX   29  29 SER B  248  LYS B  264  1                                  17    
HELIX   30  30 THR B  308  LYS B  327  1                                  20    
HELIX   31  31 THR C    2  LEU C    7  1                                   6    
HELIX   32  32 GLY C   28  LYS C   41  1                                  14    
HELIX   33  33 ILE C   53  HIS C   66  1                                  14    
HELIX   34  34 GLY C   67  LEU C   71  5                                   5    
HELIX   35  35 ASP C   81  ALA C   86  5                                   6    
HELIX   36  36 SER C  104  SER C  127  1                                  24    
HELIX   37  37 PRO C  138  GLY C  151  1                                  14    
HELIX   38  38 PRO C  153  ASN C  155  5                                   3    
HELIX   39  39 CYS C  162  GLY C  178  1                                  17    
HELIX   40  40 HIS C  180  CYS C  184  5                                   5    
HELIX   41  41 TRP C  200  GLY C  202  5                                   3    
HELIX   42  42 LEU C  210  HIS C  214  1                                   5    
HELIX   43  43 TRP C  226  GLY C  245  1                                  20    
HELIX   44  44 SER C  248  LYS C  264  1                                  17    
HELIX   45  45 THR C  308  GLU C  328  1                                  21    
HELIX   46  46 THR D    2  LEU D    7  1                                   6    
HELIX   47  47 GLY D   28  LYS D   41  1                                  14    
HELIX   48  48 ILE D   53  HIS D   66  1                                  14    
HELIX   49  49 GLY D   67  LEU D   71  5                                   5    
HELIX   50  50 ASP D   81  ALA D   86  5                                   6    
HELIX   51  51 SER D  104  SER D  127  1                                  24    
HELIX   52  52 PRO D  138  GLY D  151  1                                  14    
HELIX   53  53 PRO D  153  ASN D  155  5                                   3    
HELIX   54  54 CYS D  162  GLY D  178  1                                  17    
HELIX   55  55 HIS D  180  LEU D  182  5                                   3    
HELIX   56  56 TRP D  200  GLY D  202  5                                   3    
HELIX   57  57 LEU D  210  HIS D  214  1                                   5    
HELIX   58  58 TRP D  226  GLY D  245  1                                  20    
HELIX   59  59 SER D  248  LYS D  264  1                                  17    
HELIX   60  60 THR D  308  LYS D  327  1                                  20    
SHEET    1   A 4 ILE A   8  ASN A  10  0                                        
SHEET    2   A 4 GLY D 298  VAL D 303 -1  O  LEU D 302   N  TYR A   9           
SHEET    3   A 4 PHE D 287  GLY D 295 -1  N  PRO D 291   O  VAL D 303           
SHEET    4   A 4 ARG D 268  MET D 275 -1  N  HIS D 270   O  CYS D 292           
SHEET    1   B 6 LYS A  75  SER A  78  0                                        
SHEET    2   B 6 GLU A  46  VAL A  50  1  N  LEU A  47   O  VAL A  77           
SHEET    3   B 6 LYS A  21  VAL A  25  1  N  VAL A  24   O  ALA A  48           
SHEET    4   B 6 LEU A  90  ILE A  93  1  O  ILE A  92   N  THR A  23           
SHEET    5   B 6 LYS A 131  ILE A 134  1  O  LEU A 133   N  VAL A  91           
SHEET    6   B 6 VAL A 157  GLY A 159  1  O  ILE A 158   N  ILE A 134           
SHEET    1   C 3 CYS A 184  LEU A 189  0                                        
SHEET    2   C 3 VAL A 197  VAL A 205 -1  O  VAL A 197   N  LEU A 189           
SHEET    3   C 3 VAL A 208  SER A 209 -1  O  VAL A 208   N  VAL A 205           
SHEET    1   D 4 ARG A 268  MET A 275  0                                        
SHEET    2   D 4 PHE A 287  GLY A 295 -1  O  CYS A 292   N  HIS A 270           
SHEET    3   D 4 GLY A 298  VAL A 303 -1  O  VAL A 303   N  PRO A 291           
SHEET    4   D 4 ILE D   8  ASN D  10 -1  O  TYR D   9   N  LEU A 302           
SHEET    1   E 4 ILE B   8  ASN B  10  0                                        
SHEET    2   E 4 GLY C 298  VAL C 303 -1  O  LEU C 302   N  TYR B   9           
SHEET    3   E 4 PHE C 287  GLY C 295 -1  N  PRO C 291   O  VAL C 303           
SHEET    4   E 4 ARG C 268  MET C 275 -1  N  HIS C 270   O  CYS C 292           
SHEET    1   F 6 LYS B  75  SER B  78  0                                        
SHEET    2   F 6 GLU B  46  VAL B  50  1  N  LEU B  47   O  VAL B  77           
SHEET    3   F 6 LYS B  21  VAL B  25  1  N  VAL B  24   O  ALA B  48           
SHEET    4   F 6 LEU B  90  ILE B  93  1  O  ILE B  92   N  THR B  23           
SHEET    5   F 6 LYS B 131  ILE B 134  1  O  LYS B 131   N  VAL B  91           
SHEET    6   F 6 VAL B 157  GLY B 159  1  O  ILE B 158   N  LEU B 132           
SHEET    1   G 3 CYS B 184  HIS B 185  0                                        
SHEET    2   G 3 ASN B 204  VAL B 205 -1  O  ASN B 204   N  HIS B 185           
SHEET    3   G 3 VAL B 208  SER B 209 -1  O  VAL B 208   N  VAL B 205           
SHEET    1   H 2 VAL B 188  LEU B 189  0                                        
SHEET    2   H 2 VAL B 197  PRO B 198 -1  O  VAL B 197   N  LEU B 189           
SHEET    1   I 4 ARG B 268  MET B 275  0                                        
SHEET    2   I 4 PHE B 287  GLY B 295 -1  O  CYS B 292   N  HIS B 270           
SHEET    3   I 4 GLY B 298  VAL B 303 -1  O  VAL B 303   N  PRO B 291           
SHEET    4   I 4 ILE C   8  ASN C  10 -1  O  TYR C   9   N  LEU B 302           
SHEET    1   J 6 LYS C  75  SER C  78  0                                        
SHEET    2   J 6 GLU C  46  VAL C  50  1  N  LEU C  47   O  VAL C  77           
SHEET    3   J 6 LYS C  21  VAL C  25  1  N  VAL C  24   O  ALA C  48           
SHEET    4   J 6 LEU C  90  ILE C  93  1  O  ILE C  92   N  VAL C  25           
SHEET    5   J 6 LYS C 131  ILE C 134  1  O  LEU C 133   N  VAL C  91           
SHEET    6   J 6 VAL C 157  GLY C 159  1  O  ILE C 158   N  LEU C 132           
SHEET    1   K 2 VAL C 188  LEU C 189  0                                        
SHEET    2   K 2 VAL C 197  PRO C 198 -1  O  VAL C 197   N  LEU C 189           
SHEET    1   L 2 ASN C 204  VAL C 205  0                                        
SHEET    2   L 2 VAL C 208  SER C 209 -1  O  VAL C 208   N  VAL C 205           
SHEET    1   M 6 ILE D  76  SER D  78  0                                        
SHEET    2   M 6 GLU D  46  VAL D  50  1  N  LEU D  47   O  VAL D  77           
SHEET    3   M 6 LYS D  21  VAL D  25  1  N  VAL D  24   O  ALA D  48           
SHEET    4   M 6 LEU D  90  ILE D  93  1  O  ILE D  92   N  THR D  23           
SHEET    5   M 6 LYS D 131  ILE D 134  1  O  LEU D 133   N  VAL D  91           
SHEET    6   M 6 VAL D 157  GLY D 159  1  O  ILE D 158   N  ILE D 134           
SHEET    1   N 3 CYS D 184  HIS D 185  0                                        
SHEET    2   N 3 ASN D 204  VAL D 205 -1  O  ASN D 204   N  HIS D 185           
SHEET    3   N 3 VAL D 208  SER D 209 -1  O  VAL D 208   N  VAL D 205           
SHEET    1   O 2 VAL D 188  GLY D 190  0                                        
SHEET    2   O 2 SER D 196  PRO D 198 -1  O  VAL D 197   N  LEU D 189           
CISPEP   1 GLU A   14    GLU A   15          0       -23.42                     
CISPEP   2 ASN A  137    PRO A  138          0        -6.69                     
CISPEP   3 ASN B  137    PRO B  138          0        -4.35                     
CISPEP   4 ASN C  137    PRO C  138          0        -1.48                     
CISPEP   5 ASN D  137    PRO D  138          0        -4.57                     
SITE     1 AC1 26 GLY A  28  ALA A  29  VAL A  30  ASP A  51                    
SITE     2 AC1 26 VAL A  52  ILE A  53  THR A  94  ALA A  95                    
SITE     3 AC1 26 GLY A  96  ARG A  98  ILE A 115  ILE A 119                    
SITE     4 AC1 26 VAL A 135  ASN A 137  HIS A 192  THR A 247                    
SITE     5 AC1 26 ILE A 251  HOH A 903  HOH A 908  HOH A 909                    
SITE     6 AC1 26 HOH A 911  HOH A 930  HOH A1002  HOH A1031                    
SITE     7 AC1 26 HOH A1039  HOH A1046                                          
SITE     1 AC2  4 TRP A 147  GLY A 151  PRO A 153  LYS A 154                    
SITE     1 AC3 12 ASN A 137  LEU A 164  ASP A 165  ARG A 168                    
SITE     2 AC3 12 HIS A 192  GLY A 193  VAL A 233  ALA A 237                    
SITE     3 AC3 12 TYR A 238  ILE A 241  THR A 247  HOH A 994                    
SITE     1 AC4 32 GLY B  28  ALA B  29  VAL B  30  ASP B  51                    
SITE     2 AC4 32 VAL B  52  ILE B  53  LYS B  56  THR B  94                    
SITE     3 AC4 32 ALA B  95  GLY B  96  ALA B  97  ARG B  98                    
SITE     4 AC4 32 ILE B 115  ILE B 119  VAL B 135  SER B 136                    
SITE     5 AC4 32 ASN B 137  SER B 160  LEU B 164  HIS B 192                    
SITE     6 AC4 32 THR B 247  ILE B 251  2OP B 802  HOH B 901                    
SITE     7 AC4 32 HOH B 904  HOH B 905  HOH B 909  HOH B 919                    
SITE     8 AC4 32 HOH B 933  HOH B 964  HOH B1039  HOH B1091                    
SITE     1 AC5  8 GLN B  99  ARG B 105  ASN B 137  ARG B 168                    
SITE     2 AC5  8 HIS B 192  ALA B 237  THR B 247  NAI B 801                    
SITE     1 AC6  5 TRP B 147  GLY B 151  PHE B 152  PRO B 153                    
SITE     2 AC6  5 LYS B 154                                                     
SITE     1 AC7 28 GLY C  28  ALA C  29  VAL C  30  ASP C  51                    
SITE     2 AC7 28 VAL C  52  ILE C  53  THR C  94  ALA C  95                    
SITE     3 AC7 28 GLY C  96  ARG C  98  ILE C 115  VAL C 135                    
SITE     4 AC7 28 SER C 136  ASN C 137  HIS C 192  THR C 247                    
SITE     5 AC7 28 36V C 803  HOH C 903  HOH C 912  HOH C 913                    
SITE     6 AC7 28 HOH C 949  HOH C 974  HOH C 984  HOH C 992                    
SITE     7 AC7 28 HOH C1004  HOH C1010  HOH C1044  HOH C1046                    
SITE     1 AC8  3 TRP C 147  GLY C 151  LYS C 154                               
SITE     1 AC9 13 ASN C 137  LEU C 164  ASP C 165  ARG C 168                    
SITE     2 AC9 13 HIS C 192  GLY C 193  VAL C 233  ALA C 237                    
SITE     3 AC9 13 TYR C 238  ILE C 241  THR C 247  NAI C 801                    
SITE     4 AC9 13 HOH C1023                                                     
SITE     1 BC1 27 GLY D  28  ALA D  29  VAL D  30  ASP D  51                    
SITE     2 BC1 27 VAL D  52  ILE D  53  THR D  94  ALA D  95                    
SITE     3 BC1 27 GLY D  96  ILE D 115  VAL D 135  ASN D 137                    
SITE     4 BC1 27 HIS D 192  THR D 247  ILE D 251  HOH D 905                    
SITE     5 BC1 27 HOH D 916  HOH D 974  HOH D 976  HOH D 983                    
SITE     6 BC1 27 HOH D1000  HOH D1006  HOH D1032  HOH D1038                    
SITE     7 BC1 27 HOH D1040  HOH D1059  HOH D1061                               
SITE     1 BC2 12 ASN D 137  LEU D 164  ASP D 165  ARG D 168                    
SITE     2 BC2 12 HIS D 192  GLY D 193  VAL D 233  ALA D 237                    
SITE     3 BC2 12 TYR D 238  ILE D 241  THR D 247  HOH D1019                    
SITE     1 BC3  6 HIS B 185  ARG D 170  HIS D 185  HOH D 903                    
SITE     2 BC3  6 HOH D 929  HOH D 939                                          
CRYST1  168.481   81.101  120.307  90.00 117.38  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005935  0.000000  0.003074        0.00000                         
SCALE2      0.000000  0.012330  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009361        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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