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Database: PDB
Entry: 5IXY
LinkDB: 5IXY
Original site: 5IXY 
HEADER    OXIREDUCTASE/OXIREDUCTASE INHIBITOR     23-MAR-16   5IXY              
TITLE     LACTATE DEHYDROGENASE IN COMPLEX WITH HYDROXYLACTAM INHIBITOR COMPOUND
TITLE    2 31: (2~{S})-5-(2-CHLOROPHENYL)SULFANYL-2-(4-MORPHOLIN-4-YLPHENYL)-4- 
TITLE    3 OXIDANYL-2-THIOPHEN-3-YL-1,3-DIHYDROPYRIDIN-6-ONE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-LACTATE DEHYDROGENASE A CHAIN;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: LDH-A,CELL PROLIFERATION-INDUCING GENE 19 PROTEIN,LDH MUSCLE
COMPND   5 SUBUNIT,LDH-M,RENAL CARCINOMA ANTIGEN NY-REN-59;                     
COMPND   6 EC: 1.1.1.27;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LDHA, PIG19;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE TETRAMER, OXIREDUCTASE-OXIREDUCTASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHEN,C.EIGENBROT                                                    
REVDAT   2   09-NOV-16 5IXY    1       JRNL                                     
REVDAT   1   14-SEP-16 5IXY    0                                                
JRNL        AUTH   H.E.PURKEY,K.ROBARGE,J.CHEN,Z.CHEN,L.B.CORSON,C.Z.DING,      
JRNL        AUTH 2 A.G.DIPASQUALE,P.S.DRAGOVICH,C.EIGENBROT,M.EVANGELISTA,      
JRNL        AUTH 3 B.P.FAUBER,Z.GAO,H.GE,A.HITZ,Q.HO,S.S.LABADIE,K.W.LAI,W.LIU, 
JRNL        AUTH 4 Y.LIU,C.LI,S.MA,S.MALEK,T.O'BRIEN,J.PANG,D.PETERSON,         
JRNL        AUTH 5 L.SALPHATI,S.SIDERIS,M.ULTSCH,B.WEI,I.YEN,Q.YUE,H.ZHANG,     
JRNL        AUTH 6 A.ZHOU                                                       
JRNL        TITL   CELL ACTIVE HYDROXYLACTAM INHIBITORS OF HUMAN LACTATE        
JRNL        TITL 2 DEHYDROGENASE WITH ORAL BIOAVAILABILITY IN MICE.             
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   896 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   27774125                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00190                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22595                          
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)  : 0.237                          
REMARK   3   R VALUE            (WORKING SET)  : 0.236                          
REMARK   3   FREE R VALUE                      : 0.279                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.240                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 506                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.15                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 88.49                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2541                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2771                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2479                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2755                   
REMARK   3   BIN FREE R VALUE                        : 0.3451                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.44                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 62                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10245                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 343                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.18740                                              
REMARK   3    B22 (A**2) : -1.24830                                             
REMARK   3    B33 (A**2) : -0.93900                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.58360                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.464               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.573               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.876                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.816                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 10794  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 14653  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3783   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 256    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1572   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 10794  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1398   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 12268  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.10                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.73                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219634.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-SEP-13                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22595                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: 1I10                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM MALONATE, PH 7.0,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K                     
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       40.34800            
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: 28340 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -271.0 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 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 D   103                                                      
REMARK 465     SER D   104                                                      
REMARK 465     ARG D   105                                                      
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 D  13    O                                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS B   13   CG   CD   CE   NZ                                   
REMARK 480     GLU C   14   CG   CD   OE1  OE2                                  
REMARK 480     GLU C   15   CG   CD   OE1  OE2                                  
REMARK 480     LYS D   13   C    CG   CD   CE   NZ                              
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       66.24   -115.54                                   
REMARK 500    CYS A 162       31.20    -94.84                                   
REMARK 500    SER A 248      -64.53   -133.42                                   
REMARK 500    HIS B 214       81.29   -164.53                                   
REMARK 500    SER B 248      -64.69   -133.77                                   
REMARK 500    MET B 275      100.24    -57.74                                   
REMARK 500    CYS C 162       30.80    -91.09                                   
REMARK 500    SER C 248      -64.98   -133.82                                   
REMARK 500    THR C 306       99.84    -67.89                                   
REMARK 500    CYS D 162       31.39    -95.11                                   
REMARK 500    GLN D 225       73.64     43.88                                   
REMARK 500    SER D 248      -64.87   -133.79                                   
REMARK 500    LYS D 277       99.95    -57.04                                   
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 NAD A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GN2 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GN2 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GN2 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GN2 D 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IXS   RELATED DB: PDB                                   
DBREF  5IXY A    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  5IXY B    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  5IXY C    1   331  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  5IXY 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    NAD  A 401      44                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    GN2  A 404      33                                                       
HET    NAD  B 401      44                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    GN2  B 405      33                                                       
HET    NAD  C 401      44                                                       
HET    SO4  C 402       5                                                       
HET    SO4  C 403       5                                                       
HET    GN2  C 404      33                                                       
HET    NAD  D 401      44                                                       
HET    GN2  D 402      33                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GN2 (2~{S})-5-(2-CHLOROPHENYL)SULFANYL-2-(4-MORPHOLIN-4-             
HETNAM   2 GN2  YLPHENYL)-4-OXIDANYL-2-THIOPHEN-3-YL-1,3-                       
HETNAM   3 GN2  DIHYDROPYRIDIN-6-ONE                                            
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   6  SO4    7(O4 S 2-)                                                   
FORMUL   8  GN2    4(C25 H23 CL N2 O3 S2)                                       
HELIX    1 AA1 THR A    2  LEU A    7  1                                   6    
HELIX    2 AA2 GLY A   28  ASP A   42  1                                  15    
HELIX    3 AA3 ILE A   53  GLY A   67  1                                  15    
HELIX    4 AA4 SER A   68  LEU A   71  5                                   4    
HELIX    5 AA5 ASP A   81  ALA A   86  5                                   6    
HELIX    6 AA6 SER A  104  SER A  127  1                                  24    
HELIX    7 AA7 PRO A  138  GLY A  151  1                                  14    
HELIX    8 AA8 PRO A  153  ASN A  155  5                                   3    
HELIX    9 AA9 CYS A  162  GLY A  178  1                                  17    
HELIX   10 AB1 LEU A  210  HIS A  214  1                                   5    
HELIX   11 AB2 LYS A  227  LYS A  244  1                                  18    
HELIX   12 AB3 SER A  248  ASN A  265  1                                  18    
HELIX   13 AB4 THR A  308  LYS A  327  1                                  20    
HELIX   14 AB5 THR B    2  LEU B    7  1                                   6    
HELIX   15 AB6 GLY B   28  ASP B   42  1                                  15    
HELIX   16 AB7 ILE B   53  GLY B   67  1                                  15    
HELIX   17 AB8 SER B   68  LEU B   71  5                                   4    
HELIX   18 AB9 ASP B   81  ALA B   86  5                                   6    
HELIX   19 AC1 SER B  104  SER B  127  1                                  24    
HELIX   20 AC2 PRO B  138  GLY B  151  1                                  14    
HELIX   21 AC3 PRO B  153  ASN B  155  5                                   3    
HELIX   22 AC4 CYS B  162  GLY B  178  1                                  17    
HELIX   23 AC5 TRP B  226  LYS B  244  1                                  19    
HELIX   24 AC6 SER B  248  ASN B  265  1                                  18    
HELIX   25 AC7 THR B  308  LYS B  327  1                                  20    
HELIX   26 AC8 THR C    2  LEU C    7  1                                   6    
HELIX   27 AC9 GLY C   28  LYS C   41  1                                  14    
HELIX   28 AD1 ILE C   53  GLY C   67  1                                  15    
HELIX   29 AD2 SER C   68  LEU C   71  5                                   4    
HELIX   30 AD3 ASP C   81  ALA C   86  5                                   6    
HELIX   31 AD4 SER C  104  SER C  127  1                                  24    
HELIX   32 AD5 PRO C  138  GLY C  151  1                                  14    
HELIX   33 AD6 PRO C  153  ASN C  155  5                                   3    
HELIX   34 AD7 CYS C  162  GLY C  178  1                                  17    
HELIX   35 AD8 LEU C  210  HIS C  214  1                                   5    
HELIX   36 AD9 TRP C  226  LYS C  244  1                                  19    
HELIX   37 AE1 SER C  248  ASN C  265  1                                  18    
HELIX   38 AE2 THR C  308  LYS C  327  1                                  20    
HELIX   39 AE3 THR D    2  LEU D    7  1                                   6    
HELIX   40 AE4 GLY D   28  ASP D   42  1                                  15    
HELIX   41 AE5 ILE D   53  GLY D   67  1                                  15    
HELIX   42 AE6 SER D   68  LEU D   71  5                                   4    
HELIX   43 AE7 ASP D   81  ALA D   86  5                                   6    
HELIX   44 AE8 ASN D  107  SER D  127  1                                  21    
HELIX   45 AE9 PRO D  138  GLY D  151  1                                  14    
HELIX   46 AF1 PRO D  153  ASN D  155  5                                   3    
HELIX   47 AF2 CYS D  162  GLY D  178  1                                  17    
HELIX   48 AF3 LEU D  210  HIS D  214  1                                   5    
HELIX   49 AF4 TRP D  226  LYS D  244  1                                  19    
HELIX   50 AF5 SER D  248  ASN D  265  1                                  18    
HELIX   51 AF6 THR D  308  LYS D  327  1                                  20    
SHEET    1 AA1 4 ILE A   8  ASN A  10  0                                        
SHEET    2 AA1 4 GLY D 298  VAL D 303 -1  O  LEU D 302   N  TYR A   9           
SHEET    3 AA1 4 PHE D 287  GLY D 295 -1  N  PRO D 291   O  VAL D 303           
SHEET    4 AA1 4 ARG D 268  MET D 275 -1  N  THR D 274   O  LEU D 288           
SHEET    1 AA2 6 LYS A  75  SER A  78  0                                        
SHEET    2 AA2 6 GLU A  46  VAL A  50  1  N  LEU A  47   O  VAL A  77           
SHEET    3 AA2 6 LYS A  21  VAL A  25  1  N  ILE A  22   O  ALA A  48           
SHEET    4 AA2 6 LEU A  90  ILE A  93  1  O  ILE A  92   N  THR A  23           
SHEET    5 AA2 6 LYS A 131  ILE A 134  1  O  LEU A 133   N  VAL A  91           
SHEET    6 AA2 6 VAL A 157  GLY A 159  1  O  ILE A 158   N  LEU A 132           
SHEET    1 AA3 3 CYS A 184  GLY A 190  0                                        
SHEET    2 AA3 3 SER A 196  VAL A 205 -1  O  VAL A 197   N  LEU A 189           
SHEET    3 AA3 3 VAL A 208  SER A 209 -1  O  VAL A 208   N  VAL A 205           
SHEET    1 AA4 4 ARG A 268  MET A 275  0                                        
SHEET    2 AA4 4 PHE A 287  GLY A 295 -1  O  LEU A 288   N  THR A 274           
SHEET    3 AA4 4 GLY A 298  VAL A 303 -1  O  VAL A 303   N  PRO A 291           
SHEET    4 AA4 4 ILE D   8  ASN D  10 -1  O  TYR D   9   N  LEU A 302           
SHEET    1 AA5 4 ILE B   8  ASN B  10  0                                        
SHEET    2 AA5 4 GLY C 298  VAL C 303 -1  O  LEU C 302   N  TYR B   9           
SHEET    3 AA5 4 PHE C 287  GLY C 295 -1  N  PRO C 291   O  VAL C 303           
SHEET    4 AA5 4 ARG C 268  MET C 275 -1  N  THR C 274   O  LEU C 288           
SHEET    1 AA6 6 LYS B  75  SER B  78  0                                        
SHEET    2 AA6 6 GLU B  46  VAL B  50  1  N  LEU B  47   O  VAL B  77           
SHEET    3 AA6 6 LYS B  21  VAL B  25  1  N  VAL B  24   O  ALA B  48           
SHEET    4 AA6 6 LEU B  90  ILE B  93  1  O  ILE B  92   N  THR B  23           
SHEET    5 AA6 6 LYS B 131  ILE B 134  1  O  LEU B 133   N  VAL B  91           
SHEET    6 AA6 6 VAL B 157  GLY B 159  1  O  ILE B 158   N  LEU B 132           
SHEET    1 AA7 3 CYS B 184  GLY B 190  0                                        
SHEET    2 AA7 3 SER B 196  VAL B 205 -1  O  VAL B 197   N  LEU B 189           
SHEET    3 AA7 3 VAL B 208  SER B 209 -1  O  VAL B 208   N  VAL B 205           
SHEET    1 AA8 4 ARG B 268  MET B 275  0                                        
SHEET    2 AA8 4 PHE B 287  GLY B 295 -1  O  LEU B 288   N  THR B 274           
SHEET    3 AA8 4 GLY B 298  VAL B 303 -1  O  VAL B 303   N  PRO B 291           
SHEET    4 AA8 4 ILE C   8  ASN C  10 -1  O  TYR C   9   N  LEU B 302           
SHEET    1 AA9 6 LYS C  75  SER C  78  0                                        
SHEET    2 AA9 6 GLU C  46  VAL C  50  1  N  LEU C  47   O  VAL C  77           
SHEET    3 AA9 6 LYS C  21  VAL C  25  1  N  VAL C  24   O  ALA C  48           
SHEET    4 AA9 6 LEU C  90  ILE C  93  1  O  ILE C  92   N  THR C  23           
SHEET    5 AA9 6 LYS C 131  ILE C 134  1  O  LEU C 133   N  VAL C  91           
SHEET    6 AA9 6 VAL C 157  GLY C 159  1  O  ILE C 158   N  LEU C 132           
SHEET    1 AB1 3 CYS C 184  GLY C 190  0                                        
SHEET    2 AB1 3 SER C 196  VAL C 205 -1  O  VAL C 197   N  LEU C 189           
SHEET    3 AB1 3 VAL C 208  SER C 209 -1  O  VAL C 208   N  VAL C 205           
SHEET    1 AB2 6 LYS D  75  SER D  78  0                                        
SHEET    2 AB2 6 GLU D  46  VAL D  50  1  N  LEU D  47   O  VAL D  77           
SHEET    3 AB2 6 LYS D  21  VAL D  25  1  N  VAL D  24   O  ALA D  48           
SHEET    4 AB2 6 LEU D  90  ILE D  93  1  O  ILE D  92   N  THR D  23           
SHEET    5 AB2 6 LYS D 131  ILE D 134  1  O  LEU D 133   N  VAL D  91           
SHEET    6 AB2 6 VAL D 157  GLY D 159  1  O  ILE D 158   N  LEU D 132           
SHEET    1 AB3 3 CYS D 184  LEU D 189  0                                        
SHEET    2 AB3 3 VAL D 197  VAL D 205 -1  O  VAL D 197   N  LEU D 189           
SHEET    3 AB3 3 VAL D 208  SER D 209 -1  O  VAL D 208   N  VAL D 205           
CISPEP   1 ASN A  137    PRO A  138          0        -1.95                     
CISPEP   2 ASN B  137    PRO B  138          0        -2.13                     
CISPEP   3 ASN C  137    PRO C  138          0        -2.85                     
CISPEP   4 ASN D  137    PRO D  138          0        -1.42                     
SITE     1 AC1 20 GLY A  28  ALA A  29  VAL A  30  ASP A  51                    
SITE     2 AC1 20 VAL A  52  ILE A  53  LYS A  56  THR A  94                    
SITE     3 AC1 20 ALA A  95  GLY A  96  ARG A  98  ILE A 115                    
SITE     4 AC1 20 ILE A 119  VAL A 135  SER A 136  ASN A 137                    
SITE     5 AC1 20 LEU A 164  HIS A 192  ILE A 251  GN2 A 404                    
SITE     1 AC2  3 HIS A 185  ARG C 170  HIS C 185                               
SITE     1 AC3  3 TRP A 147  PRO A 153  LYS A 154                               
SITE     1 AC4 13 ARG A  98  ASN A 137  LEU A 164  ASP A 165                    
SITE     2 AC4 13 ARG A 168  HIS A 192  GLY A 193  ALA A 237                    
SITE     3 AC4 13 TYR A 238  ILE A 241  GLY A 245  THR A 247                    
SITE     4 AC4 13 NAD A 401                                                     
SITE     1 AC5 19 GLY B  28  ALA B  29  VAL B  30  ASP B  51                    
SITE     2 AC5 19 VAL B  52  ILE B  53  THR B  94  ALA B  95                    
SITE     3 AC5 19 GLY B  96  ARG B  98  ILE B 115  ILE B 119                    
SITE     4 AC5 19 VAL B 135  SER B 136  ASN B 137  LEU B 164                    
SITE     5 AC5 19 HIS B 192  ILE B 251  GN2 B 405                               
SITE     1 AC6  4 ARG B 170  HIS B 185  LEU D 182  HIS D 185                    
SITE     1 AC7  3 HIS B 185  ARG D 170  HIS D 185                               
SITE     1 AC8  3 LYS A 283  TRP B 147  LYS B 154                               
SITE     1 AC9 12 ARG B  98  ASN B 137  LEU B 164  ASP B 165                    
SITE     2 AC9 12 ARG B 168  HIS B 192  GLY B 193  ALA B 237                    
SITE     3 AC9 12 TYR B 238  ILE B 241  THR B 247  NAD B 401                    
SITE     1 AD1 19 GLY C  28  ALA C  29  VAL C  30  ASP C  51                    
SITE     2 AD1 19 VAL C  52  ILE C  53  THR C  94  ALA C  95                    
SITE     3 AD1 19 GLY C  96  ARG C  98  ILE C 115  ILE C 119                    
SITE     4 AD1 19 VAL C 135  SER C 136  ASN C 137  LEU C 164                    
SITE     5 AD1 19 HIS C 192  ILE C 251  GN2 C 404                               
SITE     1 AD2  5 ARG A 170  HIS A 185  LEU C 182  SER C 183                    
SITE     2 AD2  5 HIS C 185                                                     
SITE     1 AD3  3 TRP C 147  PRO C 153  LYS C 154                               
SITE     1 AD4 11 ARG C  98  ASN C 137  ASP C 165  ARG C 168                    
SITE     2 AD4 11 HIS C 192  GLY C 193  ALA C 237  TYR C 238                    
SITE     3 AD4 11 ILE C 241  THR C 247  NAD C 401                               
SITE     1 AD5 19 GLY D  28  ALA D  29  VAL D  30  ASP D  51                    
SITE     2 AD5 19 VAL D  52  ILE D  53  THR D  94  ALA D  95                    
SITE     3 AD5 19 GLY D  96  ILE D 115  PHE D 118  ILE D 119                    
SITE     4 AD5 19 VAL D 135  SER D 136  ASN D 137  LEU D 164                    
SITE     5 AD5 19 HIS D 192  ILE D 251  GN2 D 402                               
SITE     1 AD6 12 ASN D 137  LEU D 164  ASP D 165  ARG D 168                    
SITE     2 AD6 12 HIS D 192  GLY D 193  ALA D 237  TYR D 238                    
SITE     3 AD6 12 ILE D 241  GLY D 245  THR D 247  NAD D 401                    
CRYST1   78.452   80.696  102.236  90.00  97.90  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      0.012747  0.000000  0.001768        0.00000                         
SCALE2      0.000000  0.012392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009875        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system